Pubmed abstracts for Protein-Protein Interaction search result :

Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.72833103
The protein Max binds to c Myc and the heterodimer c Myc / Max seems to be the active form in vivo . 0.72833103^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.55575797
The small constitutively expressed bHLHZip protein Max is known to form sequence specific DNA binding heterodimers with members of both the Myc and Mad families of bHLHZip proteins . 0.55575797^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.6345051
The bHLHZip protein Max interacts with both the Myc and Mad family proteins forming heterodimers which specifically bind certain E box DNA recognition sequences , thereby regulating transcription . 0.6345051^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.97941578
The myc protein forms a sequence specific DNA binding complex with Max and may act as a transcription factor ; thus , it may be possible that myc family oncogenes are involved in DNA synthesis and repair processes mediating drug resistance . 0.97941578^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.61689584
Here we use Saccharomyces cerevisiae as an in vivo model system to show that the Myc protein is a sequence specific transcriptional activator whose DNA binding is strictly dependent on dimerization with Max . 0.61689584^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.61023457
We mutagenized the basic , HLH and LZ domains of Max and studied the ability of the normal and mutant proteins to bind to DNA as both homo and heterodimers and their ability to heterodimerize with Myc . 0.61023457^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.51227324
Although Max itself is a highly stable protein , Myc is rapidly degraded during or after its association with Max . 0.51227324^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :1.3305864
First , we show that Max can interact with c Myc intracellularly in a manner dependent on the integrity of the helix loop helix and leucine zipper motifs . 1.3305864^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.6311644
Finally , extracts prepared from NIH 3T3 cell lines that overexpress Max contained a phosphorylated Max protein which , following phosphatase treatment or heterodimerization with Myc , was capable of sequence specific DNA binding activity . 0.6311644^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.66123083
Max specifically associated with c Myc , N Myc , and L Myc proteins , but not with a number of other bHLH , bZip , or bHLH Zip proteins . 0.66123083^^^ Max : a helix loop helix zipper protein that forms a sequence specific DNA binding complex with Myc . 0.55133413^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.76924784
We suggest that the c Myc HLH / LZ domain induces apoptosis by specific interaction with cellular factors different to Max . . 0.76924784^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.58248081
Binding of AP 2 to Myc does not preclude association of Myc with Max , but impairs DNA binding of the Myc / Max complex and inhibits transactivation by Myc even in the absence of an overlapping AP 2 binding site . 0.58248081^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :1.114191
In most cell types , c Myc forms a sequence specific DNA binding complex with the stable , constitutively expressed Max . 1.114191^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.52410265
It appears that the interaction of Myc with its heterodimeric partner Max is essential for Myc function . 0.52410265^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :1.014754
In the undifferentiated U 937 monocyte cell line Max was found complexed with Myc but not Mad . 1.014754^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :1.0490751
Site specific modulation of c Myc cotransformation by residues phosphorylated in vivo . c Myc is a nuclear phosphoprotein which binds DNA as a heterodimer with Max . 1.0490751^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.84436741
Specific association of c Myc with Max was dictated by helices 1 and 2 of the HLH motif and by the LZ . 0.84436741^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.5222151
The recently identified max protein dimerizes with c myc to promote its sequence specific DNA binding . max exists in two forms ( long and short ) that differ by virtue of a 9 amino acid insertion / deletion at the N terminus . 0.5222151^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.72644817
In vivo , Myc proteins have been found associated with Max , another basic helix loop helix / leucine zipper protein . 0.72644817^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.59475894
Mxi 1 and Mad , novel Max associated proteins have been identified and shown to form heterodimers with Max which bind efficiently to the Myc / Max consensus recognition sequence , CACGTG , in vitro . 0.59475894^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :1.421186
Myc binds this sequence as a heterodimer with Max in the activation of both transcription and transformation . 1.421186^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.62991951
The c Myc protein activates transcription as part of a heteromeric complex with Max . 0.62991951^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.53845288
In contrast , incubation of U 937 cells with phorbol ester was associated with progressive down regulation of c myc protein . c myc can also form transcriptionally active heterodimeric complexes with the nuclear phosphoproteins p20 / p22 max : thus , TPA treatment resulted in down regulation of the p 20 form of max in TUR cells . 0.53845288^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.65452146
Members of the Mad family of transcription factors are thought to modulate the cell proliferative effects of the c myc proto oncogene by binding to Max , directly competing with the Myc protein for both heterodimerization and DNA binding . 0.65452146^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :1.1262271
The c Myc protein exhibits sequence specific DNA binding when dimerized with its partner Max , and DNA binding is mediated through the basic region , which recognizes the core sequence CACGTG ( Berberich et al . , 1992 ; Blackwell et al . , 1993 ; Blackwood and Eisenman , 1991 ; Prendergast and Ziff , 1991 ; Prendergast et al . , 1991 ) , but exhibits somewhat higher affinity for the more extended sequence ACCACGTGGT ( Berberich et al . , 1992 ; Blackwell et al . , 1993 ; Halazonetis and Kandil , 1991 ) . 1.1262271^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.53400342
Furthermore , p 73 stimulated the interaction of Max with c Myc and promoted binding of the c Myc Max complex to its target DNA . 0.53400342^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.64878182
The transcription factor Myc forms a complex with its partner Max and with the regulatory DNA sequences on its target genes . 0.64878182^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.5595717
The proto oncogene c Myc plays a central role in cell growth and the development of human tumors . c Myc interacts with Max and Myc Max complexes bind to E box and related sequences to activate transcription . 0.5595717^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max ( Myc associated factor 10 ) is a basic helix loop helix / leucine zipper protein that has been shown to play a central role in the functional activity of c Myc as a transcriptional activator . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
In addition , c , N and L Myc proteins heterodimerize , in vitro and in vivo , with the bHLH Z protein Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Remarkably , c Myc delta 7 , like wild type c Myc , retains the capacity to transform the growth phenotype of myoblasts , and associates with the b HLH LZ Myc partner protein Max in transformed cells . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The family of Myc proteins appears to function through heterodimerization with the bHLH Zip protein Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Here , we demonstrate that the placement of the specific Myc DNA binding site CACGTG upstream of a luciferase reporter gene conferred Myc stimulated expression that was inhibited by the overexpression of the basic helix loop helix / leucine zipper protein Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
To gain insight into the role of Myc family oncoproteins and their associated protein Max in vertebrate growth and development , we sought to identify homologs in the zebra fish ( Brachydanio rerio ) . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The basic helix loop helix leucine zipper ( bHLHZip ) protein Max associates with members of the Myc family , as well as with the related proteins Mad ( Mad 1 ) and Mxi 1 . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Transcriptional activation studies involving the human oncoprotein and transcription factor Myc and its helix loop helix partner protein Max in mammalian cells are critical due to the presence of endogenous Myc and Max proteins . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
This antagonism relates partly to their ability to compete with Myc for the protein Max and for consensus DNA binding sites and to recruit transcriptional co repressors . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Differential effects of the widely expressed dMax splice variant of Max on E box vs initiator element mediated regulation by c Myc . dMax , a naturally occurring splice variant of the Myc binding protein Max , lacks the DNA binding basic region and helix 1 of the Helix Loop Helix domain ; dMax interacts with c Myc in vitro and in vivo , and inhibits E box Myc site driven transcription in transient transfection assays . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
They interact with the bHLH ZIP protein max , compete for the same DNA binding sites as myc max heterodimers and down regulate myc responsive genes . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
For its oncogenic activity , Myc must dimerize with the ubiquitously expressed basic helix loop helix leucine zipper protein Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
N Myc is a transcription factor that forms heterodimers with the protein Max and binds gene promoters by recognizing a DNA sequence , CACGTG , called E box . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Regulation of Myc : Max complex formation and its potential role in cell proliferation . ^^^ Here we discuss the evidence for Myc ' s involvement in normal and abnormal cell proliferation and review recent information on Max , a novel protein that forms a sequence specific DNA binding complex with Myc . ^^^ The properties of the Myc : Max heterodimeric complex suggest a model for how Myc may function in the cell . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Basal levels of max are sufficient for the cotransformation of C3H10T1 / 2 cells by ras and myc . ^^^ In C3H10T1 / 2 cells overexpressing the 5 myc or H ras oncogenes , the levels of mRNA encoding max , the recently identified oligomerization partner of myc , remain unchanged , suggesting that the endogenous level of max in C3H10T1 / 2 cells is sufficient for a high frequency of transformation by ras and myc . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Heterodimerization of Myc with Max or Max like proteins could be a prerequisite for such inhibition . ^^^ It is , therefore , of interest to study the regulation of max in MEL cells expressing normal and deregulated myc genes . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Opposite orientations of DNA bending by c Myc and Max . ^^^ The recent discovery of Max , a basic helix loop helix leucine zipper partner protein for c Myc , suggests that the ability of c Myc to regulate transcription is modulated by the presence of Max . ^^^ By taking advantage of the altered mobility of protein bound DNA in the mobility shift assay , we demonstrate the homo and heterodimeric complexes of c Myc and Max are able to cause increased DNA flexure as measured by the circular permutation assay . ^^^ Based on phasing analysis , c Myc and Max homodimers bend DNA in opposite orientations , whereas c Myc Max heterodimers cause a smaller bend , in an orientation similar to that induced by Max homodimers . ^^^ To address the possibility that the apparent opposite orientation of bending was the result of DNA unwinding by one of the proteins , we measured the ability of c Myc and Max homodimers to affect DNA unwinding ; we were unable to show any specific unwinding caused by c Myc or Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The c Myc protein is a potential activator of transcription , with the ability to bind in a heterodimer form with Max to DNA sequences containing the core hexanucleotide sequence CAC ( G / A ) TG . ^^^ The data that have accumulated to date are consistent with a model in which a c Myc / Max heterodimer positively regulates the transcription of growth related genes , with Max homodimer functioning as a negative regulator of the same genes ( Fig . 4 ) [ 55 ] . ^^^ Max is expressed constitutively at low levels , whereas c Myc is expressed at low levels in quiescent cells , but high levels of c Myc are induced by mitogenic stimulation [ 56 ] . ^^^ Thus , in proliferating cells c Myc / Max heterodimers might bind to the regulatory elements of growth related genes , where the c Myc TAD might stimulate transcription . ^^^ Conversely , in quiescent cells with little c Myc present , Max homodimers might predominate . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Biphasic effect of Max on Myc cotransformation activity and dependence on amino and carboxy terminal Max functions . ^^^ In Ras cotransformation assays , Max exhibited a biphasic effect on Myc transformation activity . ^^^ Cotransfection of low levels of Max expression plasmid stimulated Myc transformation activity , but cotransfection of high levels suppressed it . ^^^ Our data suggest that both the ratio of Myc / Max hetero oligomers to Max homo oligomers and Max specific regulation can contribute to determining the biological activity of Myc in vivo . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc / Max and other helix loop helix / leucine zipper proteins bend DNA toward the minor groove . ^^^ Members of this family include the Myc oncoproteins , their binding partner Max , and the mammalian transcription factors USF , TFE 3 , and TFEB . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Similar overexpression of max results in a repression of reporter gene activity , an effect which is reversed by co expression with c myc . ^^^ Transcriptional activities of the Myc and Max proteins in mammalian cells . ^^^ We report here the direct testing of full length Myc and its dimerization partner , Max , on the transcriptional activity of reporter genes bearing Myc / Max binding sites . ^^^ Max repression is dependent on an intact DNA binding region , while Myc activation depends on both the N terminal activation and the C terminal dimerization domains . ^^^ These results suggest a model in which Max homodimers can act as as repressors , and Myc Max heterodimers as activators , of potential target genes . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc and Max : a putative transcriptional complex in search of a cellular target . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max and c Myc / Max DNA binding activities in cell extracts . ^^^ We have examined the interactions and DNA binding activities of the c Myc oncoprotein and its partner Max . ^^^ In cell extracts virtually all c Myc molecules are associated with Max in heterodimeric complexes . ^^^ Moreover , DNA binding studies with in vitro translated protein and cell extracts show that both Max alone and c Myc / Max bind the same DNA sequence . ^^^ Conversely , c Myc is unable to bind this sequence in the absence of Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Recently , the c Myc protein was found to heterodimerize with Max , a protein that cooperates with c Myc to bind specifically to a core DNA sequence , CAC ( G / A ) TG . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
It was recently reported that the c myc protein forms complexes with a novel helix loop helix leucine zipper protein ( Max ) , and that the Myc Max complex specifically recognizes a DNA sequence different from the sequence we have defined in the c myc gene . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Max gene encodes a protein that interacts specifically with the Myc protein to form a heterodimer with high affinity for the specific cognate DNA binding site of Myc . ^^^ Here we examine the expression of Max RNA in comparison to Myc RNA during cell growth and differentiation . ^^^ Unlike Myc , the steady state level of Max RNA is not significantly modulated with respect to proliferation or differentiation . ^^^ In contrast to Myc RNA , Max RNA does not decline immediately upon induction of differentiation of HL 60 cells by dimethyl sulfoxide , and only a modest decrease of Max RNA was observed 72 h after induction of differentiation . ^^^ Unlike Myc RNA , Max RNA is relatively stable with a half life of greater than 3 h and , therefore , does not exhibit the characteristic short half life of RNAs encoded by most immediate early genes . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max and c Myc proteins , produced in bacteria , were studied for DNA binding activity using the electrophoretic band shift assay ( EMSA ) . ^^^ Both Max homodimers and c Myc Max heterodimers selected the same sequence CA ( C / T ) GTG from an initial pool of 10 ( 6 ) DNA molecules . ^^^ Furthermore , max expression is constant in both confluent and serum stimulated A 31 fibroblasts , in contrast to c myc expression , which is barely detectable in confluent fibroblasts and induced 20 fold by serum growth factors . ^^^ Based on recognition of the same DNA sequence by Max and c Myc Max complexes and differential expression of the two genes , we propose that Max homodimers and c Myc Max heterodimers may bind to a common set of cellular target genes . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
This delta Max protein retained the ability to bind to the CACGTG motif in a complex with c Myc but lacks the nuclear localization signal and the putative regulatory domain of Max . ^^^ Thus , the max gene may encode both a negative and a positive regulator of c Myc function . . ^^^ Alternative forms of Max as enhancers or suppressors of Myc ras cotransformation . ^^^ Max is a basic helix loop helix leucine zipper protein capable of forming sequence specific DNA binding complexes with Myc proteins . ^^^ When tested in a myc ras cotransformation assay in rat embryo fibroblasts , Max suppressed , whereas delta Max enhanced , transformation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The protein encoded by the MAX gene is a member of the class of basic region helix loop helix zipper proteins and has been demonstrated to associate with N , L , and c Myc proteins both in vitro and in vivo . ^^^ Heterodimers formed between c Myc and Max proteins have been shown to possess sequence specific DNA binding activity . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
One such motif is a helix loop helix / leucine zipper like domain which shares some sequence similarity with these motifs in the Myc and Max proteins . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Partner proteins that oligomerize with c Myc have been identified in humans and mice ( Max and Myn ) . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We next determined that the interaction of the C terminal bHLH Zip region of L Myc or c Myc with that of a Myc partner protein , Max , was equivalent in transfected cells . ^^^ A Max expression vector was found to augment the cotransforming activity of L Myc as well as that of c Myc . ^^^ In addition , a bacterially synthesized DNA binding domain of L Myc , like that o c Myc , heterodimerizes with purified Max protein to bind the core DNA sequence CACGTG . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
This motif is found in protein sequences from many eukaryotic organisms and is contained in the protein sequence of the oncogene myc and its partner max , and a shortened version of the motif ( bHLH ) is found in the muscle determination factor myoD and its partner E 12 . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc , but not Max , possesses domains that function in both transcription activation and cellular transformation . ^^^ Similarly , we investigated whether Max , the protein binding partner of Myc , also possesses the potential to activate transcription . ^^^ Interestingly , chimeric GAL4 / Max proteins were not functional in our assays , suggesting that the potential of the Myc Max complex to influence gene expression and function in cellular transformation relies primarily on sequences found within the amino terminus of Myc . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc and Max function as a nucleoprotein complex . ^^^ Recent studies show that Myc proteins form sequence specific DNA binding complexes with Max , a new member of the helix loop helix leucine zipper protein class . ^^^ The properties of the Myc Max complex suggest a mechanism for Myc ' s function in both normal and neoplastic cell behavior . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Employing co immunoprecipitation with either anti Myc or anti Max antibodies , we show that the transfected normal c Myc , N Myc , and L Myc oncoproteins associate with the endogenous Max protein in REF transformants , indicating that the Max interaction represents at least one component common to Myc family function . ^^^ Myc family oncoproteins function through a common pathway to transform normal cells in culture : cross interference by Max and trans acting dominant mutants . ^^^ Current evidence indicates that Myc family proteins exist as biologically active heterodimeric complexes in association with another helix loop helix leucine zipper phosphoprotein , Max . ^^^ We have investigated the common and unique properties among the Myc family , as well as the physiological role of Max in the regulation of Myc family function . ^^^ In addition , we observed a striking reduction in Myc cotransformation activity when a Max expression construct was added to myc / ras co transfections . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc meets its Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
These two forms of Max can act either as enhancers or suppressors of cotransformation by c myc and ras . ^^^ Through their homologous helix loop helix and leucine zipper structures , Myc and Max proteins form heterodimers that bind to specific DNA sequences more efficiently than Myc or Max alone . ^^^ We have recently identified delta Max , a naturally occurring truncated version of Max , which is also able to dimerize with Myc in the nucleus , but is cytoplasmic in the absence of Myc . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
By dissecting the c Myc protein , a number of critical functional domains of c Myc have been identified and characterized ; these findings suggest a model for c Myc function and intracellular activity ( Fig . 4 ) . c Myc is synthesized in the cytoplasm and undergoes oligomerization another protein such as Max . ^^^ Continued studies of c Myc and its partner Max should further elucidate the mechanisms by which c Myc can contribute both to the regulation of normal cell growth and the alteration in that regulation in neoplasia . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Myc : Max protein complex and cell growth regulation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Association of Myn , the murine homolog of max , with c Myc stimulates methylation sensitive DNA binding and ras cotransformation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The N Myc oncoprotein is associated in vivo with the phosphoprotein Max ( p20 / 22 ) in human neuroblastoma cells . ^^^ By partial proteolytic maps we show that p 20 and p 22 are structurally related to each other and that p 20 is identical with Max , a recently described in vitro binding partner of myc proteins . ^^^ While the expression of N myc is restricted , expression of both Max ( p20 / 22 ) and the murine homolog Myn ( p20 / 22 ) was observed in cells of diverse human and murine embryonal lineages as detected by heterologous complex formation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We demonstrate that overexpression of c Myc results in efficient activation of the ODC promoter , whereas overexpression of Max exerts a repressive effect . ^^^ Transactivation of the ODC promoter also requires the dimerization of c Myc with Max . ^^^ Our data suggest that c Myc and Max are potential transcriptional regulators of the ODC promoter . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mxi 2 in yeast interacts with Max and with the C terminus of c Myc . ^^^ The Mxi 2 putative substrate recognition region has sequence similarity to the helix loop helix region in Max and c Myc , suggesting that substrate recognition might be mediated via this motif . ^^^ We describe Mxi 2 , a human protein that interacts with Max protein , the heterodimeric partner of the Myc oncoprotein . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Preferential heterodimeric parallel coiled coil formation by synthetic Max and c Myc leucine zippers : a description of putative electrostatic interactions responsible for the specificity of heterodimerization . ^^^ The oncoprotein c Myc must heterodimerize with Max to bind DNA and perform its oncogenic activity . ^^^ The c Myc Max heterodimer binds DNA through a basic helix loop helix leucine zipper ( b HLH zip ) motif and it is proposed that leucine zipper domains could , in concert with the HLH regions , provide the specificity and stability of the b HLH zip motif . ^^^ In this context , we have synthesized the peptides corresponding to the leucine zipper domains of Max and c Myc with a N terminal Cys Gly Gly linker and studied their dimerization behavior using reversed phase HPLC and CD spectroscopy . ^^^ The preferential formation of a fully helical parallel c Myc Max heterodimeric coiled coil was observed under air oxidation and redox conditions at neutral pH . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Differential expression of c myc , max and mxi 1 in human myeloid leukemia cells during retrodifferentiation and cell death . ^^^ Treatment of U 937 cells with 12 O tetradecanoyl phorbol 13 acetate ( TPA ) which is associated with the induction of a monocytic differentiation program and growth arrest , revealed an initial up regulation of c myc , c max , and mxi 1 mRNAs after 1 6 h . ^^^ After 48 72 h of serum starvation , expression of the c myc and c max genes were significantly down regulated by 4 fold and 3 fold , respectively , while there was little , if any , change in mxi 1 mRNA levels . ^^^ Synchronization of proliferating U 937 cells throughout distinct phases of the cell cycle exhibited little , if any , change in c myc , c max and mxi 1 mRNAs . ^^^ Furthermore , like c myc , c max and mxi 1 mRNA transcripts appeared to be regulated primarily by post transcriptional mechanisms , and c max and mxi 1 half lives exceeded 4 h in contrast to < 60 min for the c myc gene . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max is the recently discovered heterodimeric partner of the human myc oncogene product . ^^^ Previously published data have shown both myc and max to be highly conserved amongst species , and indeed there is a 100 % homology between feline max and max , while the murine equivalent myn is 98 % homologous at the amino acid level , with the nucleotide sequences showing a similarity of 98 % and 95 % respectively . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The small bHLHZip protein , Max , was originally identified through its interaction with Myc family proteins and appears to be an obligate partner for Myc function . ^^^ Mad : Max complexes are detected during differentiation and appear to replace the Myc : Max complexes present in proliferating cell populations . ^^^ Since these complexes appear to form even in the presence of Myc , there may exist mechanisms that act to inhibit Myc : Max , or to promote Mad : Max , complex formation . ^^^ We have also developed an approach to identification of the gene targets for Myc : Max complexes . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Determination of sequences responsible for the differential regulation of Myc function by delta Max and Max . ^^^ The DNA binding , transcriptional activation and transforming activities of the Myc protein require dimerization with Max . ^^^ Max can form also homodimers which are able to bind the same DNA sequence as Myc / Max heterodimers and suppress Myc induced transcription and transformation . ^^^ We have recently identified a naturally occurring truncated form of Max , delta Max , which in a rat embryo fibroblast enhances transformation by Myc and Ras . ^^^ Here we have dissected the regions responsible for the specific effects of Max and delta Max in Ras Myc cotransformation of rat embryo fibroblasts . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Differential effects by Mad and Max on transformation by cellular and viral oncoproteins . c Myc is an essential component of the regulatory mechanisms controlling cell growth . ^^^ Max is the obligatory partner of c Myc for all its biological functions analysed to date . ^^^ It has been suggested that these two proteins modulate c Myc function , in the simplest model by competing with c Myc for the interaction with Max . ^^^ Native Mad / Max heterodimers bound specifically to a c Myc / Max consensus DNA binding site . ^^^ In contrast to Mad , Max did not inhibit E1a / Ha Ras cotransformation but repressed c Myc / Ha Ras transformation efficiently . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc is glycosylated at threonine 58 , a known phosphorylation site and a mutational hot spot in lymphomas . c Myc is a helix loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation , cell differentiation , and programmed cell death . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
During early development , when the entire embryonic genome is transcriptionally inactive , c Myc does not exhibit a DNA binding activity with Max . ^^^ Moreover , embryonic nuclei not only prevent the formation of c Myc / Max complexes but also dissociate such preformed complexes . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mad : Max heterodimers recognize the same DNA binding sites as Myc : Max heterodimers . ^^^ However , Myc and Mad are thought to influence transcription and cell proliferation in opposite ways through interaction with Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max as an obligate heterodimeric partner for Myc mediates its functions as a specific transcriptional activator and a transforming protein . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Characterization of the mouse homolog of human mad on the structural level revealed that domains shown previously to be required in the human protein for anti Myc repression , sequence specific DNA binding activity , and dimerization with its partner Max are highly conserved . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mad is a bHLH / Zip protein that , as a heterodimer with Max , can repress Myc induced transcriptional transactivation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The level of transcripts for c jun , c fos , c myc , and transforming growth factor beta 1 were increased for an extended period of time in livers of deficient animals , whereas the expression of both p 53 and max were unchanged . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Because c Myc is known to bind to several cellular proteins , including Max , we further examined the effects of expression of a dominant negative Max on activation induced apoptosis . ^^^ We found that this Max mutant , which interferes with the function of the Myc / Max heterodimer , inhibits the induction of apoptosis by antigen receptor ligation . ^^^ Thus , both Myc and Max play roles in activation induced apoptosis , presumably via control of gene expression . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Analysis of c Myc and Max binding to the c myc promoter : evidence that autosuppression occurs via an indirect mechanism . c myc negatively autoregulates its expression at the level of transcriptional initiation , although the precise mechanism remains debated . ^^^ In an attempt to clarify this issue , sequences flanking the c myc gene were screened for c Myc or Max binding sites using a novel procedure to facilitate the detection of DNA binding dependent upon long distance interactions or DNA secondary structure . ^^^ Using conditions that gave strong binding to an internal control sequence , c Myc or Max binding elements were not detected in genomic sequences extending 5 . 4 kb upstream of the Xenopus c myc gene . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The TFEB protein is known to form homodimers . c Myc , on the other hand , does not homodimerize in vivo , but is mostly found in heterodimeric complexes with Max , another protein of the HLH LZ family . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Regulation of transcription factors c Myc , Max , and c Myb by casein kinase 2 . ^^^ We have identified CKII phosphorylation sites in c Myc , Max , and c Myb which are phosphorylated in the cell . ^^^ Whereas little evidence to any functional significance of the CKII sites in c Myc has been obtained , phosphorylation of its heterodimeric partner Max alters DNA binding properties . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Expression of c Myc mutants which have been shown to dominantly interfere with the function of c Myc and Max significantly inhibited cad transcription during S phase but had no effect on transcription from another G1 / S phase activated promoter , dhfr . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Specific c myc and max regulation in epithelial cells . ^^^ We have investigated c myc , max and c fos mRNA and protein expression in proliferating , quiescent and stimulated immortalized , SV 40 T antigen ( LT ) transformed and tumor derived epithelial cells as well in human primary keratinocytes and have compared them to their expression in fibroblasts . ^^^ In proliferating immortalized and tumor derived epithelial cells , the levels of c myc , max and c fos expression were comparable and much higher than in transformed fibroblasts . c myc and c fos mRNA and protein levels remained high even during quiescence , when cells stopped dividing . ^^^ Changing the medium to serum free medium of confluent epithelial cells induced a complete proliferative response which started with a transient increase in c fos and c myc mRNA , followed by the expression of max . ^^^ In fibroblasts , similar treatment induced the arrest of c myc expression and growth , but max expression was also induced in these cells by serum . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The c myc oncogene c Myc is commonly activated in cancer and transactivates gene expression by binding to CACGTG DNA sequences as a heterodimeric complex with Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The MXI 1 gene encodes a protein interacting with Max , a regulatory factor of the Myc oncogene , and is located on chromosome 10q25 , a region showing frequent loss of heterozygosity in malignant gliomas . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The nerve growth factor responsive PC 12 cell line does not express the Myc dimerization partner Max . ^^^ Heterodimerization of Max with the nuclear oncoprotein Myc and the differentiation associated proteins Mad and Mxi 1 enables these factors to bind E box sites in DNA and control genes implicated in cell proliferation and differentiation . ^^^ Finally , the ability of these cells to divide , differentiate , and apoptose in the absence of Max demonstrates for the first time that these processes can occur via Max and possibly Myc independent mechanisms . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Analysis of the Myc and Max interaction specificity with lambda repressor HLH domain fusions . ^^^ Myc and Max belong to a subset of HLH proteins , containing a leucine zipper ( LZ ) adjacent to the bHLH domain . ^^^ To analyze the interaction specificity of Myc and Max bHLH LZ domains , we developed a simple Escherichia coli genetic system , which uses the amino terminal lambda phage cI repressor as a reporter for dimerization and allows an easy detection of dimeric interactions . ^^^ By reciprocal exchanges of different Myc and Max subdomains ( helix 1 , helix 2 and leucine zipper ) , we showed that the recognition specificity of Max homodimers as well as of Myc / Max heterodimers is entirely determined by the helix 2 leucine zipper region , the major role being played by the leucine zipper . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Here we present evidence for O GlcNAc glycosylation of the oncoprotein c Myc , a helix loop helix / leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Cell density and paradoxical transcriptional properties of c Myc and Max in cultured mouse fibroblasts . ^^^ We found that endogenous c Myc protein levels vary inversely with the degree of cell confluency , such that at low cell confluency , where endogenous levels of c Myc are high and presumably endogenous levels of Max are limiting , exogenous c Myc fails to affect basal transcription . ^^^ In cells at high cell confluency , in which endogenous c Myc levels are low , exogenous c Myc augments transactivation by titrating the relative excess endogenous Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The B ' complexes of Inr lambda 5 : 1 and Inr lambda 5 : 2 each contained c myc and myn ( murine homologue of Max ) proteins . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Bitransgenic myc / max 41 mice developed pre B cell lymphoma . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mad is a basic region helix loop helix leucine zipper transcription factor which can dimerize with the Max protein and antagonize transcriptional activation by the Myc Max transcription factor heterodimer . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Regulation of human ornithine decarboxylase expression following prolonged quiescence : role for the c Myc / Max protein complex . ^^^ The presence of a CACGTG element within this fragment , studies with antibodies against c Myc and Max , the use of purified recombinant c Myc protein in the mobility shift assay , and antisense studies suggest that these proteins can specifically bind this portion of the human ODC promoter in a manner consistent with growth associated modulation of the expression of ODC and other early G 1 genes following prolonged quiescence . ^^^ These studies suggest a role for the c Myc / Max protein complex in regulating events involved in the progression of cells out of long term quiescence into G 1 and subsequently into S . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
In turn , mad max or mxi 1 max heterodimers or max homodimers can compete for DNA binding sites with dimers formed between max and myc oncoproteins and antagonize the transcriptional activities of this latter class of proteins . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Moreover , induction of apoptosis by c Myc requires association with c Myc ' s heterologous partner , Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
As a heterodimer with a structurally related protein , Max , Myc can bind DNA in a sequence specific manner . ^^^ These results suggest that the Myc / Max heterodimer functions as a transcriptional activator of genes that are critical for the regulation of cell growth . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mxi 1 , a protein that specifically interacts with Max to bind Myc Max recognition sites . ^^^ This protein , Mxi 1 ( for Max interactor 1 ) , contains a bHLH Zip motif that is similar to that found in Myc family proteins . ^^^ Mxi 1 interacts specifically with Max to form heterodimers that efficiently bind to the Myc Max consensus recognition site . ^^^ These facts are consistent with a model in which Mxi 1 Max heterodimers indirectly inhibit Myc function in two ways : first , by sequestering Max , thus preventing the formation of Myc Max heterodimers , and second , by competing with Myc Max heterodimers for binding to target sites . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The LIM bHLH interactions are highly specific in that RBTN 1 and RBTN 2 will associate with TAL 1 , TAL 2 and LYL 1 , but not with other bHLH proteins , including E 12 , E 47 , Id 1 , NHLH 1 , AP 4 , MAX , MYC and MyoD 1 . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Myc proteins , as heterodimers with Max protein , have been shown to function as activators of transcription through an E box DNA binding element , CACGTG . ^^^ In addition , Myc / Max heterodimers , but not Max homodimers , bind to the EFII enhancer sequence in vitro . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Overexpressed max is not oncogenic and attenuates myc induced lymphoproliferation and lymphomagenesis in transgenic mice . ^^^ The cellular growth promoting function of the Myc oncoprotein requires its heterodimerization with the Max protein , but Max can also form complexes that inhibit Myc action . ^^^ To determine whether max overexpression in vivo is oncogenic and whether it can modulate the action of Myc , we generated transgenic mice in which the max gene was directed to express in lymphoid cells by a linked immunoglobulin heavy chain enhancer ( E mu ) . ^^^ Moreover , analysis of bi transgenic E mu myc / E mu max mice revealed that max overexpression attenuated the premalignant B lymphoproliferative state induced by an E mu myc transgene and reduced the rate of lymphoma onset . ^^^ These results suggest that elevation of Max expression in vivo inhibits the function of Myc . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Within its C terminal sequence , a remarkable similarity to Myc and Max proteins can be found . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
EB 2 transformation in Rat 1 cells correlates with an increase in the steady state level of the cellular oncogenic protein c Myc , and cotransfection of a plasmid expressing Max suppresses the transformation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Coexpression of dominant negative c Myc or Max mutants with LTAg inhibited DNA synthesis , indicating that functional c Myc is necessary for induction of DNA synthesis by LTAg . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
This role for c Myc in apoptosis is now confirmed in studies using a dominant negative form of its heterodimeric binding partner , Max , which we show here inhibits activation induced apoptosis . ^^^ Functional Myc Max heterodimer is required for activation induced apoptosis in T cell hybridomas . ^^^ Further , coexpression of a reciprocally mutant Myc protein capable of forming functional heterodimers with the mutant Max can compensate for the dominant negative activity and restore activation induced apoptosis . ^^^ These results imply that Myc promotes activation induced apoptosis by obligatory heterodimerization with Max , and therefore , by regulating gene transcription . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Transactivation of the human p 53 tumor suppressor gene by c Myc / Max contributes to elevated mutant p 53 expression in some tumors . ^^^ Recent findings indicate that c Myc / Max heterodimers can bind to an essential CA ( C / T ) GTG containing site in the p 53 promoter and elevate its expression . ^^^ Here we demonstrate that the human p 53 promoter is transactivated by high c Myc expression and repressed by high Max expression . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Regulation of murine Max ( Myn ) parallels the regulation of c Myc in differentiating murine erythroleukemia cells . ^^^ We now demonstrate that N , N ' hexamethylene bisacetamide mediated differentiation of murine erythroleukemia cells leads to a pattern of biphasic down regulation of the 1 . 9 and the 2 . 3 kb myn ( murine max ) mRNAs that closely parallels that which occurs for myc mRNA . ^^^ Furthermore , unlike myc , the overexpression of which prevents differentiation , elevated max levels merely delay differentiation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max is a nuclear phosphoprotein that has a dose dependent role in regulation of Myc function . ^^^ The DNA binding activity of Max homodimers , but not of Myc / Max heterodimers , has been reported to be inhibited by NH 2 terminal phosphorylation . ( S . ^^^ A Max mutant deficient in the NH 2 terminal phosphorylation was found to inhibit both basal and Myc induced transcription of a reporter gene more efficiently than the wild type protein . ^^^ These results indicate that the NH 2 terminal phosphorylation diminishes the ability of Max to negatively interfere with Myc function . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The significance of the flanking bases was further demonstrated by showing that USF and the related proteins c Myc and Max discriminate between CACGTG type E boxes and that the primary means of discrimination appears to be the identity of the nucleotide at + / 4 , the presence of a T at 4 being inhibitory to binding by Myc but not by USF or Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc Max Mad : a transcription factor network controlling cell cycle progression , differentiation and death . ^^^ The Myc oncoprotein dimerizes with its partner , Max , to bind DNA , activate transcription , and promote cell proliferation , as well as programmed cell death . ^^^ These complexes behave as antagonists of Myc / Max through competition for common DNA targets , and perhaps permit cellular differentiation . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We have identified an enhancer element within the first intron that is sufficient to mediate a response to Myc and Max in transient transfection assays and to activation of estrogen receptor Myc chimeras in vivo . ^^^ Disruption of this site abolishes the response to Myc and Max in both transient and stable assays . ^^^ Mutants of either Myc or Max that are deficient for heterodimerization fail to regulate the prothymosin alpha gene , suggesting that a heterodimer between Myc and Max activates the prothymosin alpha gene . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
In particular , we found that association with Max is not required for repression of cyclin D 1 by MYC in vivo . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Differential binding of c Myc and Max to nucleosomal DNA . ^^^ We have used Max and derivatives of c Myc to characterize the effect of changes of dimerization partner on binding to nucleosomal DNA templates . ^^^ Although Max homodimers bind to nucleosomes , truncated c Myc homodimers do not . ^^^ Surprisingly , modifying the c Myc dimerization interface or changing its dimerization partner to Max enables nucleosomal DNA binding . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Lack of correlation between N myc and MAX expression in neuroblastoma tumors and in cell lines : implication for N myc MAX complex formation . ^^^ MAX mRNA levels were independent of tumor stage and N myc genomic amplification . ^^^ Immunoprecipitations with a specific antibody to MAX detected two proteins of M ( r ) 21 , 000 and 22 , 000 in approximately equal amounts in all neuroblastoma lines regardless of N myc amplification and / or expression . ^^^ Thus , N myc expression might be a limiting factor in the formation of the N myc MAX heterodimer in neuroblastomas . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The human max protein has been shown to form heterodimers with myc family proteins . ^^^ The ability of myc+max heterodimers to act as sequence specific transcriptional activators appears to be essential for the oncogenic activity of myc . max ( also called myn in murine cells ) can homodimerize to form a transcriptionally inactive complex . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Suppression of Myc , but not E1a , transformation activity by Max associated proteins , Mad and Mxi 1 . ^^^ Mad and Mxi 1 , two members of the Myc related basic region helix loop helix / leucine zipper family of proteins , associate directly with Max to form sequence specific DNA binding heterodimers that are transactivation incompetent . ^^^ Mad Max complexes have been shown to exert a strong repressive effect on Myc induced transactivation , perhaps through the competitive occupation of common promoter binding sites also recognized by active Myc Max heterodimers . ^^^ In contrast , mad and mxi 1 expression constructs bearing deletions in the basic region exerted only mild repressive effects on Myc transformation activity , suggesting that occupation of common DNA binding sites by transactivation incompetent Mad Max or Mxi 1 Max complexes appears to play a more dominant role in this suppression than titration of limited intracellular pools of Max away from active Myc Max complexes . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The effects of Myc on both gene expression and cell growth are differentially regulated by the recently described Max and delta Max proteins that can either cooperate or compete with Myc for sequence specific DNA binding . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Retinoid modulation of c myc and max gene expression in human breast carcinoma . ^^^ Retinoic acid ( RA ) modulation of c myc and max gene expression was investigated in human breast carcinoma ( HBC ) cell lines . ^^^ Our results demonstrate that c myc and max genes are differentially expressed in HBC cells which was accompanied by increases in [ 3H ] thymidine incorporation and percent of cells in the S phase of cell cycle . ^^^ We thus report for the first time that RA , during its growth inhibitory effects on MCF 7 HBC cells , positively regulates the gene expression of c myc and max . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Identification of casein kinase 2 phosphorylation sites in Max : effects on DNA binding kinetics of Max homo and Myc / Max heterodimers . ^^^ The identification of Max , a basic region / helix loop helix / leucine zipper protein , as a partner for Myc has provided insights into Myc ' s molecular function as a transcription factor . ^^^ Recent evidence indicates that the relative abundance of Myc and Max is important to determine the level of specific gene transcription . ^^^ Phosphorylation of these sites modulates DNA binding by increasing both the on and off rates of Max homo as well as Myc / Max heterodimers . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The c Myc protein induces cell cycle progression and apoptosis through dimerization with Max . ^^^ Myc and its partner protein , Max , dimerize and bind DNA in vitro and in vivo through basic / helix loop helix / leucine zipper motifs ( bHLH LZ ) . ^^^ By using complementary leucine zipper mutants ( termed MycEG and MaxEG ) , which dimerize efficiently with each other but not with their wild type partners , we demonstrate that both cell cycle progression and apoptosis in nontransformed rodent fibroblasts are induced by Myc Max dimers . ^^^ Thus , Myc can control two alternative cell fates through dimerization with a single partner , Max . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Also , use of antibodies against c Myc and Max and purified recombinant c Myc and Max protein in the electrophoretic mobility shift assay confirmed that these proteins can specifically bind this portion of the human ODC promoter . ^^^ Transient transfection studies showed that increase in the level of c Myc and / or Max led to a significant enhancement of expression of a human ODC promoter CAT reporter construct . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Distinct DNA binding preferences for the c Myc / Max and Max / Max dimers . ^^^ The transcription factor c Myc and its dimerisation partner Max are members of the basic / helix loop helix / leucine zipper ( bHLH Z ) family and bind to the DNA core sequence CACGTG . ^^^ Using a site selection protocol , we determined the complete 12 base pair consensus binding sites of c Myc / Max ( RACCACGTGGTY ) and Max / Max ( RANCACGTGNTY ) dimers . ^^^ We find that the c Myc / Max dimer fails to bind the core when it is flanked by a 5 ' T or a 3 ' A , while the Max / Max dimer readily binds such sequences . ^^^ In conclusion , Max / Max dimers are less discriminatory than c Myc / Max and may regulate other genes in addition to c Myc / Max targets . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Affinity chromatography confirmed that YY 1 associates with c Myc but not with Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Transcription activation by Myc and Max : flanking sequences target activation to a subset of CACGTG motifs in vivo . ^^^ Although Myc contains a bHLH LZ motif , it fails to bind DNA alone but can do so by forming heterodimers with an unrelated bHLH LZ protein , Max . ^^^ Max homodimers and Myc Max heterodimers share the ability to bind CACGTG or CATGTG elements . ^^^ Current models , based on experimentally induced overexpression of Myc and Max in mammalian cells , propose that Max Max homodimers repress while Myc Max heterodimers activate transcription through CACGTG binding sites . ^^^ Activation by Max requires DNA binding and amino acids outside the bHLH LZ domain but is reduced compared with activation by Myc Max heterodimers . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Our results strongly suggest that homologous amino acids of Myc and Max make equivalent contacts in the respective protein DNA complexes . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
This suggests that Myc may interact with transcription factors other than Max to transactivate the ODC gene . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We analysed the expression of c myc , N myc , L myc , max and RB 1 mRNAs in a panel of human gliomas and glioma cell lines and compared the findings with normal neural cells . ^^^ We conclude that ( 1 ) glioma cells in vivo may coexpress several myc genes , thus resembling fetal neural cells ; but ( 2 ) cultured glioma cells expression only c myc ; ( 3 ) myc , max and RB 1 are regulated independently in glioma cells ; and ( 4 ) alternative processing of max mRNA in some glioma cells results in delta Max encoding mRNAs not seen in normal fetal brain . . ^^^ Differential expression of myc , max and RB 1 genes in human gliomas and glioma cell lines . ^^^ The max and RB 1 genes were included in the study because their protein products can interact with the Myc proteins , being thus putative modulators of Myc activity . ^^^ The in situ hybridisations revealed mutually exclusive topographic distribution of myc and glial fibrillary acidic protein ( GFAP ) mRNAs , and a lack of correlation between myc expression and proliferative activity , max and RB 1 mRNAs were detected in most tumours and cell lines . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The recent identification of Max , a nuclear phosphoprotein that dimerizes with members of the Myc protein family , has provided an additional tool to examine the role of the Myc oncoprotein as a sequence specific DNA binding protein and a potential regulator of gene transcription . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Both the MAD and the MXI 1 genes encode basic helix loop helix leucine zipper ( bHLH Zip ) transcription factors which bind Max in vitro , forming a sequence specific DNA binding complex similar to the Myc Max heterodimer . ^^^ Mad and Myc compete for binding to Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Helix 1 ( H 1 ) and leucine zipper peptides from the basic helix loop helix zipper domain of c Myc and Max were assayed as potential inhibitors of c Myc 92 DNA binding . ^^^ In a partially hydrophobic environment , H 1 Mx ( from Max ) is a random coil , while H 1 WT , H 1 F8A , and H 1 F8A , S6A ( from c Myc ) display differing degrees of helicity . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max is a small helix loop helix protein which forms heterodimers with members of the Myc protein family . ^^^ Myc / Max heterodimers exhibit sequence specific DNA binding with much greater affinity than Myc homodimers . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Functional analysis of the carboxy terminal transforming region of 5 Myc : binding to Max is necessary , but not sufficient , for cellular transformation . ^^^ In this study , we have generated a series of deletion mutations within the MC 29 gag myc gene to define precisely the carboxy terminal transforming region using the co transformation of C3H10T1 / 2 cells as an assay . 5 Myc proteins encoded by selected deletion mutations were also examined for their intracellular location , the ability to interact with the Max protein and the potential to bind specifically to DNA . ^^^ In addition , while the binding of 5 Myc to Max is necessary for ras / myc co transformation , it is not sufficient , and also requires the integrity of Myc sequences specifying site specific DNA binding . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Opposite regulation of gene transcription and cell proliferation by c Myc and Max . c Myc and Max are nuclear phosphoproteins capable of forming DNA binding , homo and heteropolymeric complexes in vitro and in vivo . ^^^ Using a transient cotransfection assay involving c Myc and Max expression vectors and a reporter gene plasmid containing the Myc / Max binding site , we find that Max represses transcription , whereas a significant stimulation is obtained when Max is coexpressed with c Myc . ^^^ Analysis of specific mutants indicates that transcriptional activation requires both the c Myc and the Max dimerization and DNA binding domains , as well as the c Myc transactivation function ; transcriptional repression by Max requires both DNA binding and dimerization . ^^^ Analogously , in stably transfected human B lymphoblastoid cell lines , overexpressed c Myc and Max synergize to cause malignant transformation , whereas overexpression of Max alone leads to growth inhibition . ^^^ These results indicate that the c Myc and Max are transcriptional regulators with the ability to oppositely regulate target gene expression and cell proliferation , most likely as the result of the opposite effects of heterodimeric c Myc Max ( positive ) versus homodimeric Max ( negative ) complexes . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Sequence specific transcriptional activation by Myc and repression by Max . ^^^ The discovery of the specific cognate DNA binding site for Myc and its specific heterodimerization partner , Max , enabled the use of direct experiments to elucidate how Myc functions in vivo and how this function is modulated by Max . ^^^ In contrast to Myc , exogenously expressed Max elicited transcriptional repression and blocked transcriptional activation by Myc through the same DNA binding site . ^^^ Our results suggest a functional antagonism between Myc and Max which is mediated by their relative levels in the cells . ^^^ A model for the activity of Myc and Max in vivo is presented . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
N Myc , like c Myc , preferentially forms heterodimeric DNA binding complexes with Max protein . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max protein forms specific DNA binding dimeric complexes with itself and with proteins of the c myc gene family . ^^^ To elucidate the role of max in regulating c myc functions and the effect of both proteins on cell proliferation and differentiation , we transfected murine erythroleukemia ( MEL ) cells with a full length wild type ( wt ) human max gene and a mutant containing a double point mutation in the basic region ( bm ) , which abolishes specific DNA binding . ^^^ Our findings are consistent with a model in which a large excess of wt Max in the cells enhances the formation of Max Max growth suppressor complexes , while elevated bm Max deprives the cell of growth promoting Myc Max heterodimers in a dominant negative manner , presumably by inactivating endogenous Myc and Max . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mad : a heterodimeric partner for Max that antagonizes Myc transcriptional activity . ^^^ Myc family proteins appear to function through heterodimerization with the stable , constitutively expressed bHLH Zip protein , Max . ^^^ To determine whether Max mediates the function of regulatory proteins other than Myc , we screened a lambda gt 11 expression library with radiolabeled Max protein . ^^^ Human Mad protein homodimerizes poorly but binds Max in vitro , forming a sequence specific DNA binding complex with properties very similar to those of Myc Max . ^^^ Both Myc Max and Mad Max heterocomplexes are favored over Max homodimers , and , unlike Max homodimers , the DNA binding activity of the heterodimers is unaffected by CKII phosphorylation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Oncogenic activity of the c Myc protein requires dimerization with Max . c Myc ( Myc ) and Max proteins dimerize and bind DNA through basic helix loop helix leucine zipper motifs ( b HLH LZ ) . ^^^ Using a genetic approach , we demonstrate that binding to Max is essential for Myc transforming activity and that Myc homodimers are inactive . ^^^ Mutants of Myc and Max that bind efficiently to each other but not to their wild type partners were generated by either exchanging the HLH LZ domains or reciprocally modifying LZ dimerization specificities . ^^^ In addition , wild type max antagonizes myc function in a dose dependent manner , presumably through competition of Max Max and Myc Max dimers for common target DNA sites . ^^^ Therefore , Max can function as both suppressor and activator of Myc . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The max gene encodes a heterodimeric partner of Myc . ^^^ Like delta Max , this protein enhanced the number of transformed foci in the ras myc co transformation assay . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Recent experiments have established that the c myc oncogene encodes a sequence specific DNA binding protein that interacts with a specific intracellular partner , Max , and probably manifests its effects through transcriptional modulation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max heterodimerizes with Myc family proteins to form sequence specific DNA binding complexes . ^^^ In order to elucidate the potential role of Myc and Max during amphibian embryogenesis , we have isolated and analyzed the expression of two Xenopus Max complementary DNAs : XMax 1 and XMax 2 . ^^^ Our results demonstrate the presence of Xenopus Max throughout frog development , raising the possibility that Myc and Max could function as a complex even during early embryogenesis . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Overproduction of 5 Myc in the nucleus and its excess over Max are not required for avian fibroblast transformation . ^^^ Upon synthesis , 5 Gag Myc enters the nucleus , forms complexes with its heterodimeric partner Max , and in this complex binds to DNA in a sequence specific manner . ^^^ Consequently , only a small fraction of Max is associated with Myc . ^^^ However , cells infected with this mutant exhibit a completely transformed phenotype in vitro , suggesting that production of enough 5 Gag Myc to tie up all cellular Max is not needed for transformation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max is a basic helix loop helix / leucine zipper ( bHLH / LZ ) protein that forms sequence specific DNA binding complexes with the c Myc oncoprotein ( Myc ) . ^^^ Gene regulatory properties of Myc helix loop helix / leucine zipper mutants : Max dependent DNA binding and transcriptional activation in yeast correlates with transforming capacity . ^^^ Using Saccharomyces cerevisiae , we have shown that the Max bHLH / LZ domain enables Myc to activate transcription through CACGTG and CACATG sequences in vivo , and that the number and context of such sites determines the level of activation . ^^^ In addition , we have used yeast to investigate the role of the Myc helix loop helix ( HLH ) and leucine zipper ( LZ ) motifs in mediating Max dependent DNA binding and transcriptional activation in vivo using HLH / LZ mutants generated by site directed mutagenesis . ^^^ The results show that , while both motifs are essential for Myc to activate transcription , helix 2 of the HLH together with the contiguous LZ suffice to mediate complex formation with Max , whilst helix 1 is essential for sequence specific DNA binding of Myc Max complexes . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The levels of several mRNAs encoding cell cycle functions , including cyclin D 2 , cyclin D 3 , cyclin B 1 , c myc and max all declined at 1 . 5 3 h following IL 2 deprivation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Regulation of Myc and Mad during epidermal differentiation and HPV associated tumorigenesis . c Myc and Mad each form heterodimers with Max that bind the same E box related DNA sequences . ^^^ Whereas Myc : Max complexes activate transcription and promote cell proliferation and transformation , Mad : Max complexes repress transcription and block c Myc mediated cell transformation . ^^^ During differentiation of primary human keratinocytes , Mad is rapidly induced and c Myc is downregulated , resulting in a switch from c Myc : Max to Mad : Max heterodimers . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Neonatal deprivation of maternal touch may suppress ornithine decarboxylase via downregulation of the proto oncogenes c myc and max . ^^^ Prolactin ( PRL ) injected subcutaneously increased hepatic ODC activity as well as mRNA levels of ODC and the proto oncogenes c fos , c jun , junB , junD , c myc , and max . ^^^ MS significantly suppressed PRL induced increases in ODC enzyme activity and c myc , max , and ODC mRNAs but had little effect on expression of the other proto oncogenes . ^^^ PRL induced stimulation of ODC , c myc , and max mRNAs also was depressed in neonates placed with an anesthetized lactating dam ( touch deprived ) but not in pups placed with nipple ligated dams ( food deprived ) . ^^^ These findings indicate that suppression of ODC gene transcription in the neonatal pup during MS may be mediated by downregulation of the ODC gene transactivator proto oncogenes c myc and max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Blocking c Myc and Max expression inhibits proliferation and induces differentiation of normal and leukemic myeloid cells . ^^^ In this work we showed that blocking expression of either c Myc or Max , its molecular partner , in myeloblastic leukemia M 1 cells activated the differentiation program in the absence of an exogenous source of differentiation inducer ; the cells assumed an intermediate stage myeloid morphology . ^^^ Moreover , when both c Myc and Max expression was concommitantly blocked , many of the cells underwent terminal differentiation . ^^^ Finally , extending these studies to myeloblast enriched normal bone marrow ( BM ) cell has shown that blocking expression of either c Myc or Max accelerated GM CSF induced differentiation along both the granulocytic and monocytic lineages . ^^^ Thus , it can be concluded that blocking either c Myc or Max expression in myeloid cells at specific stages of development activates and accelerates the terminal differentiation program . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc heterodimerizes with a partner protein termed Max ; the heterodimeric complex binds to CAC ( G / A ) TG ( E box ) sequences and activates transcription from these sites . ^^^ As observed in transformation assays , Myc and Max strongly synergize in activation from a distal enhancer position . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Establishment of the novel B acute lymphoblastic leukemia ( FAB L 3 ) cell line KHM 10B with a 13q34 abnormality and constitutive expression of c myc and max during cell cycle . ^^^ The expression of c myc and max was observed throughout the cell cycle , as was found in the Burkitt ' s lymphoma cell in Raji . ^^^ Our findings indicate that FISH analysis is of diagnostic value in detecting obscure chromosomal translocations and that max , as well as c myc , is expressed constitutively in ALL L 3 and Burkitt ' s lymphoma cell lines . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mad 1 dimerizes with Max and recognizes the same DNA sequences as do Myc : Max dimers . ^^^ Myc : Max heterodimers activate transcription while Mad : Max heterodimers repress transcription from the same promoter . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mxi 1 is a basic region helix loop helix leucine zipper ( bHLH / LZ ) protein that , in association with Max , antagonizes Myc oncogenic activities . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The finding that the neuronal model cell line PC 12 lacks the Myc DNA binding partner , the Max protein , and the demonstration that Myc is a repressor of gene activity as well as a transactivator , lead to models for Myc action in regulating cell growth . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc and Max interactions in quiescent and mitogen stimulated primary hepatocytes . ^^^ Max was found to be associated in vivo with hepatocyte Myc species , with this association being independent of growth conditions and of the endogenous Myc or Max levels . ^^^ The unusually long half life of the endogenous Myc species was found to be independent of their association with the widely accepted as `` stable ' ' partner , Max . ^^^ We suggest that Myc and Max in hepatocytes are involved in the growth ( proliferation , cell death ) and differentiation program of these cells , acting independently or as a complex . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The product of the proto oncogene c myc , in partnership with Max , forms a transcription factor that can promote either oncogenic transformation or apoptosis . ^^^ The Myc / Max heterodimer binds to elements in the cdc25A gene and activates transcription . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Furthermore , electrophoretic mobility shift assays demonstrated quantitative binding to the E box motifs that correlated with myc levels in the electrophoretic mobility shift assay extracts ; supershift assays demonstrated max and USF binding to the same motif . cis mutations in the core or flank of the eIF4E E box simultaneously altered myc max and USF binding and inactivated the promoter . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max protein exerts a pivotal function with the Myc family , and Mxi1 / Mad proteins play a positive and negative activity , respectively , on transcription . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc inactivation by mutant Max alters growth and morphology of NCI H 630 colon cancer cells . ^^^ For its cellular growth promoting function , Myc must heterodimerize with Max . ^^^ To study the effect of Myc inactivation on the growth and differentiation properties of epithelial tumor cells , we transfected the H 630 human colon cancer cell line with bm max , a mutant Max protein in which DNA binding activity has been abolished . ^^^ The results of this study support a model in which sequestering of endogenous Myc and Max proteins into `` basic mutant ' ' dimers lacking DNA binding activity is sufficient both to inhibit proliferation and to induce changes in cell behavior consistent with differentiation . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc and Max homologs in Drosophila . ^^^ Myc acts through dimerization with Max to bind DNA and activate transcription . ^^^ Homologs of the myc and max genes were cloned from the fruit fly Drosophila melanogaster and their protein products ( dMyc and dMax ) were shown to heterodimerize , recognize the same DNA sequence as their vertebrate homologs , and activate transcription . ^^^ These findings indicate a potential role for Myc in germ cell development and set the stage for genetic analysis of Myc and Max . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Growth rescue by Myc required dimerization with Max , DNA binding and an intact transcriptional activation domain , as previously shown for cellular transformation . ^^^ We propose that this activity is mediated by the product of an as yet unknown Myc Max target gene ( s ) and represents an essential aspect of Myc ' s mitogenic and oncogenic functions . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Conversely , cyclin D 1 rescued cells were inhibited from forming CSF 1 dependent colonies in agar when challenged with either a dominant negative c myc mutant or mad , a transcription factor which competes with myc for max , its requisite heterodimeric partner . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max is a basic helix loop helix / leucine zipper protein that forms heterodimers with the Myc family of proteins to promote cell growth and with the Mad / Mxi1 family of proteins to inhibit cell growth . ^^^ Our data suggest that it is the persistence of this 90 kDa protein in vertebrate cells which drives max gene expression , insulates the max promoter from the dramatic changes in transcription that accompany cell growth and development , and ensures that adequate levels of Max will be available to facilitate the function of the Myc , Mad , and Mxi 1 families of proteins . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The c Myc protein is involved in cell proliferation , differentiation and apoptosis though heterodimerization with Max to form a transcriptionally active sequence specific DNA binding complex . ^^^ Myc Max heterodimers activate a DEAD box gene and interact with multiple E box related sites in vivo . ^^^ By means of sequential immunoprecipitation of chromatin using anti Max and anti Myc antibodies , we have identified a Myc regulated gene and genomic sites occupied by Myc Max in vivo . ^^^ The corresponding mRNA was induced following activation of a Myc estrogen receptor fusion protein ( Myc ER ) in the presence of a protein synthesis inhibitor , consistent with this helicase gene being a direct target of Myc Max . ^^^ Our results indicate that Myc Max heterodimers interact in vivo with a specific set of E box related DNA sequences and that Myc is likely to activate multiple target genes including a highly conserved DEAD box protein . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Based on the three dimensional structures , its DNA binding domain is structurally related to that of Max , the partner of Myc . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Biochemical and biological activities of Myc oncoproteins are highly dependent upon their association with another basic region helix loop helix / leucine zipper ( bHLH / LZ ) protein , Max . ^^^ Our previous observation that the DNA binding / dimerization region of Max is absolutely conserved throughout vertebrate evolution provided the basis for a yeast two hybrid interaction screen that led to the isolation of the Drosophila Myc ( dMyc 1 ) protein . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Using an in vivo UV cross linking and immunoprecipitation assay , we show that Myc , Max , and upstream stimulatory factor ( USF ) bind to the chromosomal cad promoter . ^^^ To determine whether binding of Myc Max or USF is critical for cad growth regulation , we analyzed promoter constructs which contain mutations in the nucleotides flanking the E box . ^^^ We demonstrate that altering nucleotides which flank the cad E box to sequences which decrease Myc Max binding in vitro correlates with a loss of cad G1 / S phase transcriptional activation . ^^^ This result supports the conclusion that binding of Myc Max , but not USF , is essential for cad regulation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max is able to form homodimers and heterodimers with other members of this family , which include Mad , Mxi 1 and Myc ; Myc is an oncoprotein implicated in cell proliferation , differentiation and apoptosis . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Expression and subcellular localization of the Myc superfamily proteins : c Myc , Max , Mad 1 and Mxi 1 in the epiphyseal plate cartilage chondrocytes of growing rats . ^^^ The changes in the expressions of the protooncogene protein c Myc , its dimerization partner Max and the competitive inhibitors Mad 1 and Mxi 1 during the terminal differentiation of chondrocytes in vivo were investigated by immunocytochemistry . ^^^ Immunoreactivity of the c Myc dimerization partner Max was mainly in the nucleus of proliferative chondrocytes and decreased as the chondrocytes matured . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Immunoaffinity purification and characterization of CACGTG sequence binding proteins from cultured mammalian cells using an anti c Myc monoclonal antibody recognizing the DNA binding domain . c Myc protein contains a basic helix loop helix and leucine zipper ( bHLHLZ ) structure in its carboxyl terminal region , forms heterodimers with Max , and binds to the CACGTG sequence in DNA . ^^^ The immunoaffinity purified fraction was found to contain not only c Myc but also other CACGTG sequence binding proteins , such as Max , Mad , and USF , indicating a wide cross reaction to CACGTG sequence binding proteins . ^^^ The immunoaffinity purified N Myc , Max , Mad , and , presumably , c Myc were highly phosphorylated , and phosphatase treatment increased the DNA binding activity of Myc , suggesting that the DNA binding activity of c Myc was regulated by phosphorylation in vivo . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The core of the conserved region is homologous to the basic helix loop helix ( bHLH ) motif of eukaryotic transcription factors , specifically to the human Myc and Max proteins . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
As a heterodimer with Max , the c Myc protein binds to the E box sequence ( CACGTG ) , which is also recognized by USF dimers . ^^^ In order to test differences in target gene recognition of c Myc / Max , Max and USF dimers , we compared the DNA binding characteristics of these proteins in vitro using vaccinia viruses expressing full length c Myc and Max proteins . ^^^ As expected , purified c Myc / max binds specifically to a consensus E box . ^^^ The optimal conditions for DNA binding by either c Myc / Max , Max or USF dimers differ with respect to ionic strength and Mg2+ ion concentration . ^^^ Most interestingly , the c Myc / Max complex binds with a high affinity to its natural target , the rat ODC gene , which contains two adjacent , consensus E boxes . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc proteins function as transcriptional activators through heterodimerization with Max , but might also act as negative regulators of transcription . ^^^ Identification of genes directly controlled by Myc Max has proved difficult , but recent work is producing a growing list of candidates . ^^^ Results to date suggest that Myc Max influences cell growth and proliferation through direct activation of genes involved in DNA synthesis , RNA metabolism and cell cycle progression . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max and inhibitory c Myc mutants induce erythroid differentiation and resistance to apoptosis in human myeloid leukemia cells . ^^^ We show here that In 373 is able to compete with c Myc for Max binding and to inhibit the transformation activity of c Myc . ^^^ Ectopic Max overexpression resulted in an increased erythroid differentiation , thus reproducing the effects of c myc inhibitory mutants . ^^^ We also studied the role of c myc mutants and max in apoptosis of K 562 induced by okadaic acid , a protein phosphatases inhibitor . ^^^ The expression of D 106 143 and In 373 c myc mutants and the overexpression of max reduced the apoptosis mediated by okadaic acid . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Gel retardation experiments suggest that c Myc with Max binds to the CACGTG elements in the context of the RCC 1 gene sequence in vitro . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The identification of a novel Max interacting protein adds an important piece to the puzzle of Myc / Max / Mad coordinated action and function in normal and pathological situations . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
It has been shown that the protein encoded by the MAX gene plays an important role in the physiological activity of Myc oncoproteins . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mammalian Sin 3 proteins interact with the Mad components of the Myc / Max / Mad network of cell growth regulators . ^^^ The finding that Mad / Max complexes interact with Sin 3 and HD 1 in vivo suggests a model for the role of Mad proteins in antagonizing the function of Myc proteins . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
In addition to the IFN regulated element , a myc max binding site is also present in this promoter . ^^^ Purified Myc and Max proteins interact with the Myc stimulated element of the p 48 promoter . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
In NIH3T3 cells , MAX ( L ) was able to repress a c Myc responsive reporter gene whereas MAX ( S ) either stimulated the reporter gene or had little effect on its expression . ^^^ In comparison to control cell lines or those stably over expressing MAX ( S ) , MAX ( L ) over expressing cell lines showed reduced expression of transiently expressed or endogenous c Myc responsive genes , grew more slowly , possessed a higher growth factor requirement , and showed accelerated apoptosis following growth factor deprivation . ^^^ MAX is a basic helix loop helix leucine zipper protein that plays a central role in the transcriptional control of Myc oncoproteins . ^^^ MYC MAX heterodimers stimulate transcription , whereas MAX homodimers , or heterodimers between MAX and members of the MAD family of basic helix loop helix leucine zipper proteins , repress transcription . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Several molecules have been isolated by expression cloning , including CRE BP 1 associating with Jun ( Macgregor et al . , 1990 ) ; Grb 1 , identical to p 85 PI3 kinase , with the EGF receptor ( Skolnik et al . , 1991 ) ; and Max with Myc ( Blackwood and Eisenman , 1991 ) . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Further analysis of these Mad containing complexes revealed that they were also unlikely to have the capacity to antagonize c Myc function , as they did not contain Max . ^^^ In addition , analysis of E box DNA binding revealed that , although Myc Max complexes were lost rapidly after differentiation induction , formation of Mad 1 containing complexes only occurred during the later stages of the differentiation programme . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Enforced c Myc expression promotes continuous , growth factor independent , cell cycle progression and activates expression of the ornithine decarboxylase ( ODC ) gene and its promoter . c Myc responsiveness of murine ODC is mediated by two conserved c Myc : Max E boxes in ODC intron 1 . c Myc and ODC are both required for cell growth and their expression is sequentially induced in G0 / G1 cells stimulated with mitogens , yet their expression is not modulated by the cell cycle in proliferating cells . ^^^ The first phase of this response was independent of the intronic c Myc : Max E boxes and de novo protein synthesis . ^^^ Sustained induction of the ODC promoter however required the c Myc : Max binding sites and protein synthesis . ^^^ Consistent with a two pathway model of ODC regulation , inducible overexpression of dominant negative form of c Myc ( In 373 Myc ) , which specifically inhibits the c Myc Max network , inhibited the delayed , but not immediate , induction of ODC promoter activity in response to IL 3 . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max is a basic region / helix loop helix / leucine zipper ( b / HLH / Z ) protein that forms a hetero complex with the Myc family proteins Myc , Mad , and Mxi 1 , and a homo complex with itself . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mnt : a novel Max interacting protein and Myc antagonist . ^^^ We have identified a novel Max binding protein , Mnt , which belongs to neither the Myc nor the Mad families ( Hurlin et al . 1997 ) . ^^^ Mnt : Max complexes also efficiently suppress Myc dependent activation from the same promoter . ^^^ Likewise , Mnt protein is expressed in many proliferating cell types in culture where both Myc : Max and Mnt : Max complexes are detected . ^^^ An exception is P 19 embryonal carcinoma cells , where Mnt is expressed and in a complex with Max , but Myc proteins are not detected . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Myc protein activates transcription as part of a complex with its partner protein , Max . ^^^ Myc transformed cells are also characterised by the loss of expression of a number of genes and this repressive effect of Myc on gene expression may not be mediated by the Myc / Max complex . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The procedure has been used to identify new ts alleles of cdc 2 and swi7 / poll , a ts mutant rescued by actin , and to identify a ts allele of cdc 11 which can be rescued by combined mammalian Myc and Max expression . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Protein expression of Fas / APO 1 or bcl 2 , and messenger RNA ( mRNA ) expression of bcl 2 , bcl xL , bax , bak , Fas / APO 1 , Fas ligand ( Fas L ) , c myc , mad , or max were determined . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
In quiescent LLC PK 1 renal epithelial cells , c myc but not max or mad mRNA is induced by the nephrotoxicant S ( 1 , 2 dichlorovinyl ) L cysteine ( DCVC ) . ^^^ Activation of the odc promoter by DCVC required consensus c Myc Max binding sites in odc intron 1 . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Thermal denaturation studies indicate that a heterodimer between a Myc B HLHZip domain and a D N consisting of a 12 amino acid sequence appended onto the Max dimerization domain ( A Max ) is 6 . 3 kcal . mol 1 more stable than the Myc : Max heterodimer . ^^^ One molar equivalent of A Max can totally abolish the DNA binding activity of a Myc : Max heterodimer . ^^^ A Max can inhibit Myc dependent foci formation twice as well as the Max dimerization domain ( HLHZip ) . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Use of a two hybrid system to identify mutations in Max that confer increased affinity for Myc . ^^^ A yeast two hybrid system was used to identify mutants of Max that exhibit an increased affinity for Myc . ^^^ Truncated forms of the Max helix loop helix / leucine zipper motif ( HLH / Zip ) were first expressed in a two hybrid system in which the bait protein was the HLH / Zip motif of Myc . ^^^ Deletion of amino acids both amino terminal and carboxy terminal to the leucine zipper of Max reduced Myc / Max heterodimer formation as evidenced by a 160 fold reduction in the expression of the lacZ gene . ^^^ Mutant forms of the Max leucine zipper were identified whose affinities for Myc , as measured by beta galactosidase activity in yeast lysates , were from 8 to 200 fold greater than the wild type Max zipper . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max mRNA , which encodes the partner protein for Myc , was constitutively expressed and levels did not change with treatment or with time . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Herein , the effects of SPC on DNA binding activity and transcription of the basic , helix loop helix , leucine zipper ( bHLH ZIP ) proteins Myc , Max , and USF were investigated because they regulate genes involved in mitogenesis . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The MAX protein is at the center of this network in that it associates with MYC as well as with the family of MAD proteins : MAD 1 , MXI 1 , MAD 3 and MAD 4 . ^^^ Whereas MYC MAX complexes activate transcription , MAD MAX complexes repress transcription through identical E box binding sites . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
C myc , a member of the basic helix loop helix leucine zipper ( bHLH ZIP ) protein family activates target genes in heterodimeric association with another bHLH ZIP protein , Max . ^^^ Max readily homodimerizes , competes with C myc Max heterodimers , and represses transcription . ^^^ Four additional bHLH ZIP proteins , Mad 1 , Mxi 1 , Mad 3 and Mad 4 , heterodimerize with Max and also repress transcription of c myc responsive genes . ^^^ We identified a novel ZIP containing protein , Mmip 1 ( Mad member interacting protein 1 ) that strongly dimerizes with all four Mad members , but not with c myc , Max , or with unrelated HLH proteins . ^^^ The Mmip 1 Mxi association is mediated by the ZIP domain of each polypeptide and is as strong or stronger than the associations between c myc and Max or Max and Mxi 1 . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
As expected , however , max ( USF ) was unable to heterodimerize with any of the tested max partner proteins and was incapable of suppressing c myc target genes . ^^^ Max , a basic helix loop helix leucine zipper ( bHLH ZIP ) protein , plays a central role in the transcriptional regulation of myc oncoprotein responsive genes . ^^^ Myc max heterodimers bind to consensus E box motifs near or within the promoters of these genes and activate gene expression , whereas heterodimers between max and members of the mad family of bHLH ZIP proteins promote transcriptional repression . ^^^ In contrast to all other members of the myc network , max readily homodimerizes and binds to identical E box sites in vitro . ^^^ Upstream stimulatory factor ( USF ) is a bHLH ZIP protein which does not interact with members of the myc max mad family . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
To test this hypothesis , a recently developed quantitative reverse transcriptase polymerase chain reaction method was used to assess simultaneously expression of 15 genes mechanistically associated with cell cycle control ( c myc , E2F 1 , p 21 , rb , PCNA , cyclin D 2 , cyclin D 3 , cyclin E , cdc 2 , CDK 2 , CDK 4 , mad , max p 21 , max p 22 , and p 53 ) in normal cell cultures from five individuals and in nine different malignant BEC lines . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
MXI 1 encodes a basic helix loop helix protein that suppresses the transcriptional activity of the MYC oncoprotein by competing for the common dimerization partner , MAX , and binding to identical DNA sites . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Distinct apoptotic responses imparted by c myc and max . ^^^ We have shown that max , the obligate c myc heterodimeric partner protein , also promotes apoptosis after serum withdrawal in NIH3T3 fibroblasts or cytokine deprivation in interleukin 3 ( IL 3 ) dependent 32D murine myeloid cells . ^^^ We now show that c myc and max overexpressing 32D cells differ in the nature of their apoptotic responses after IL 3 removal or treatment with chemotherapeutic compounds . ^^^ In the presence of IL 3 , c myc overexpression enhances the sensitivity of 32D cells to Etoposide ( Sigma , St Louis , MO ) , Adriamycin ( Pharmacia , Columbus , OH ) , and Camptothecin ( Sigma ) , whereas max overexpression increases sensitivity only to Camptothecin . ^^^ In contrast , whereas Bcl 2 blocked apoptosis in both cell lines in response to IL 3 withdrawal , Bcl XL blocked apoptosis in max overexpressing cells but not in c myc overexpressing cells . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Insights into the mechanism of heterodimerization from the 1H NMR solution structure of the c Myc Max heterodimeric leucine zipper . ^^^ The oncoprotein c Myc ( a member of the helix loop helix leucine zipper ( b HLH LZ ) family of transcription factors ) must heterodimerize with the b HLH LZ Max protein to bind DNA and activate transcription . ^^^ It has been shown that the LZ domains of the c Myc and Max proteins specifically form a heterodimeric LZ at 20 degreesC and neutral pH . ^^^ This suggests that the LZ domains of the c Myc and Max proteins are playing an important role in the heterodimerization of the corresponding gene products in vivo . ^^^ Initially , to gain an insight into the energetics of heterodimerization , we studied the stability of N terminal disulfide linked versions of the c Myc and Max homodimeric LZs and c Myc Max heterodimeric LZ by fitting the temperature induced denaturation curves monitored by circular dichroism spectroscopy . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The proto oncoprotein c Myc and the multifunctional transcriptional regulator YY 1 have been shown previously to interact directly in a manner that excludes Max from the complex ( Shrivastava et al . , 1993 ) . ^^^ As binding to Max is necessary for all known c Myc activities we have analysed the influence of YY 1 on c Myc function . ^^^ In addition YY 1 did not alter c Myc / Max DNA binding , further supporting an indirect mode of action . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Nmi interacts with c Myc , N Myc , Max , and fos , as demonstrated by yeast two hybrid and coimmunoprecipitation assays . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
This is accomplished by the downregulation of specific Immediate Early Genes ( c myc and max ) that normally promote the synthesis of this critical growth regulatory enzyme . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Efficient BRCA 1 Myc association requires the intact helix loop helix region of c Myc , a motif involved in Myc Max dimerization . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The expression of mRNAs for apoptosis regulating genes also remained unchanged , except for slight down regulation of Bax . c myc protein was not found later than 48 h , and Max mRNA was downregulated . c jun was immediately induced , followed by the fluctuated expression level along with treatment . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
A variety of functions of C MYC , the product of c myc , are attributed to protein protein interactions with various cellular factors including Max , YY 1 , p 107 , Bin 1 and TBP . ^^^ Max and YY 1 bind to the C terminal region of C MYC , while p 107 , Bin 1 and TBP bind to the N terminal region covering myc boxes . ^^^ AMY 1 by itself did not recognize the E box element , the MYC / Max binding sequence , nor did it transactivate via the element , but stimulated the activation of E box regulated transcription by MYC / Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc is a bHLHZip protein involved in growth control and cancer , which operates in a network with the structurally related proteins Max , Mad and Mnt . ^^^ Myc / Max dimers activate gene transcription , while Mad / Max and Mnt / Max complexes are Myc / Max antagonists and act as repressors . ^^^ We report that Myc recognition specificity is encoded in a short region within the leucine zipper ; mutation of four amino acids generates a protein , Omomyc , that homodimerizes efficiently and can still heterodimerize with wild type Myc and Max . ^^^ Omomyc sequestered Myc in complexes with low DNA binding efficiency , preventing binding to Max and inhibiting Myc transcriptional activator function . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Because the encoded MYC protein has transcriptional activity only when dimerized with MAX , it is possible that mutations of MAX also could have phenotypic consequences . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The basic region / helix loop helix / leucine zipper ( B HLH LZ ) oncoprotein c Myc is abundant in proliferating cells and forms heterodimers with Max protein that bind to E box sites in DNA and stimulate genes required for proliferation . ^^^ A second B HLH LZ protein , Mxi 1 , is induced during terminal differentiation , and forms heterodimers with Max that also bind E boxes but tether the mSin 3 transcriptional repressor protein along with histone deacetylase thereby antagonizing Myc dependent activation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The protein Mad 1 heterodimerizes with Max to form an E box binding complex able to interfere with the transcriptional and transforming activities of c Myc . ^^^ To do so , we utilized the leukemia derived B precursor cell line , Reh , and studied the expressions of Mad 1 , c Myc , Mxil , and Max during cAMP mediated growth inhibition of these cells . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The proapoptotic property of c Myc requires an intact N terminal transactivation domain and bHLHZip domain , as well as interaction with Max , thereby implicating c Myc target genes in this apoptotic process . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Expression of many mammalian genes is activated by the binding of heterodimers of the Myc and Max proteins to specific DNA sequences called the E boxes . ^^^ Max Mad / Mxi1 heterodimers , which bind to E boxes in absence of co repressors , do not inhibit gene expression simply by competition with Myc Max heterodimers , but require Sin 3 and Rpd 3 for efficient repression of transcription . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Consequently , the synergism between all trans retinoic acid and interferon alpha down regulated the expression of c Myc , but not its functional partner , Max . ^^^ Max heterodimers bound to their consensus DNA sequence were undetectable in cells treated with all trans retinoic acid and interferon alpha , indicating diminished c Myc functionality . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mad ( Mxi 1 ) proteins not only compete with Myc for dimerization to Max and binding to Myc / Max consensus sites but also recruit powerful repressors of gene expression . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Involvement of c myc and max in CNS beta endorphin modulation of hepatic ornithine decarboxylase responsiveness to insulin in rat pups . ^^^ We now report that insulin induced stimulation of hepatic ODC mRNA expression is accompanied by a concomitant increase in the expression of c myc and max mRNAs , and that this effect is also inhibited by pretreatment with i . c . v . beta endorphin . ^^^ These results suggest that CNS beta endorphin suppresses tissue ODC responsiveness to trophic hormones by downregulating the expression of c myc and max mRNAs , the encoded proteins of which are known to act physiologically as transcriptional activators of the ODC gene . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The latter effect was associated with an heightened expression of c myc and max mRNAs , the encoded proteins of which act as transactivators of the ODC gene . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Moreover , c Jun / c Fos stimulation was inhibited by co expression of c Myc and Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max interacting protein 1 ( MXI 1 ) , a negative regulator of myc oncoprotein with tumor suppressor properties , has been mapped to chromosome 10q24 25 . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
METHODS : Expression of the c myc , N myc , and L myc proto oncogenes and of the max gene was investigated in 46 supratentorial glioblastomas from adult patients using in situ hybridization . ^^^ RESULTS : Seventy eight percent of the tumors expressed c myc m RNA , 84 % max m RNA , 57 % N myc m RNA , and 57 % L myc m RNA . ^^^ A difference in postoperative survival , however , was found in the over 60 year age group between patients whose tumors expressed max to an equal or lesser extent than c myc and those whose tumors expressed max to a greater extent than c myc or neither max nor c myc . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
To understand the antiproliferative signaling of IFNgamma , we studied the effect of IFNgamma on expression of c Myc , Mad 1 , Max , cyclin D 1 , and cyclin D 2 genes in both a macrophage cell line and in primary bone marrow derived macrophages ( BMM ) in response to colony stimulating factor 1 ( CSF 1 ) . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Our results show that TPA + IFN gamma treatment led to an inhibition of 5 Myc and c Myc dependent transcription , and a specific reduction of 5 Myc : Max complexes and associated DNA binding activity , whereas the steady state level of the 5 Myc protein was only marginally affected . ^^^ The reduced amount of 5 Myc : Max heterodimers in response to treatment was accompanied by partial dephosphorylation of 5 Myc and c Myc . ^^^ The transcription factors of the Myc / Max / Mad network are important regulators of cell growth , differentiation , and apoptosis and are frequently involved in tumor development . ^^^ Phosphatase treatment of Myc : Max complexes lead to their dissociation , thus mimicking the effect of TPA + IFN gamma . ^^^ In addition to modulation of the expression of Myc / Max / Mad network proteins , posttranslational negative regulation of Myc by external signals may , therefore , be an alternative biologically important level of control with potential therapeutic relevance for hematopoietic and other tumors with deregulated Myc expression . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The C terminal domain ( CTD ) of c Myc mediates interaction with Max and physiological recognition of DNA target sequences , events needed for all biological actions . ^^^ Recently described interactions between the CTD and other cellular proteins , including YY 1 , AP 2 , BRCA 1 , TFII 1 , and Miz 1 , suggest levels of regulatory complexity beyond Max in controlling DNA recognition by c Myc . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Molecularly Myc functions as a transcriptional regulator that needs to heterodimerize with Max to exert the biological activities described above and to regulate gene transcription . ^^^ Myc and Max are just two members of a growing family of proteins referred to as the Myc / Max / Mad network . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
This repressive effect was mediated by the promoter region within 52 base pairs from the transcription start site but direct binding of N myc : Max to the promoter sequence was not demonstrated , which is analogous to the cases recently reported for transcriptional repression by c myc . c myc also repressed Ndr 1 promoter activity similarly to N myc . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Recent studies have demonstrated the presence of novel nuclear proteins that specifically recognize a Myc core element , in addition to c Myc , Max , Mad and Mxi 1 . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
In the present study , we show that adrenomedullin induces the expression of Max , a heterodimeric partner of c Myc , which may contribute to its ability to rescue endothelial cells from apoptosis . ^^^ The expression of Max is reported to be constitutive and more stable than c Myc , and serum induces immediate c Myc stimulation followed by modest Max up regulation . ^^^ In quiescent rat endothelial cells , adrenomedullin stimulated the expression of Max without affecting c Myc . ^^^ The negative regulation of E box driven transcription by adrenomedullin was demonstrated by using preproendothelin 1 promoter containing c Myc Max binding consensus sequence ; the promoter activity of preproendothelin 1 was reduced by cotransfecting Max and Mad expressing plasmids as well as addition of adrenomedullin and CGRP . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The c Myc protein , the product of the c myc protooncogene , is a nuclear phosphoprotein with DNA binding properties when heterodimerized with the Max protein . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We looked for the protooncogene protein , c Myc , its dimerization partner , Max , and the repressors of its transactivation activity , Mad 1 and Mxi 1 , in the epiphyseal plate cartilage matrix of growing rats by immunocytochemistry in the electron microscope . c Myc and Mxi 1 immunoreactivities were found in the calcifying areas of the cartilage matrix only . ^^^ The absence of Max immunoreactivity from the calcifying cartilage matrix raises the question of whether there are other c Myc and Mxi 1 dimerization partners . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
DNA binding of Myc / Max / Mad network complexes to oligonucleotides containing two E box elements : c Myc / Max heterodimers do not bind DNA cooperatively . ^^^ Myc proteins function in heterodimeric complexes with Max proteins as transcriptional regulators at least in part by binding to E box sequences with a 5 ' CACGTG core . ^^^ Since such E boxes are found frequently in the human genome and since other proteins besides Myc / Max can bind to similar or identical sequences it is unclear how the specificity of E box mediated gene transcription is determined . ^^^ Recent findings were interpreted to suggest that Myc / Max , but not Max / Max or USF complexes , bind cooperatively to DNA sequences that contain two E box elements . ^^^ To extend this finding we analyzed DNA binding of c Myc / Max complexes using a transient COS 7 expression system . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
These studies , in conjunction with mutational analysis and reporter gene assays with dominant negative Myc and Max expression vectors , showed that Myc and Max interaction with a Myc consensus site is required for androgen regulation of the 350 bp fragment . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Members of the Mad family of bHLHZip proteins heterodimerize with Max and function to repress the transcriptional and transforming activities of the Myc proto oncogene . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Regulation of c Myc and Max in megakaryocytic and monocytic macrophagic differentiation of K 562 cells induced by protein kinase C modifiers : c Myc is down regulated but does not inhibit differentiation . ^^^ We have studied the regulation and role of c Myc and Max in the differentiation pathways induced in K 562 cells by 12 O tetradecanoyl phorbol 13 acetate ( TPA ) and staurosporine , an activator and inhibitor , respectively , of protein kinase C ( PKC ) . ^^^ In contrast , TPA induced a differentiated phenotype that more closely resembled that of the monocyte macrophage lineage . c myc expression was down regulated in K 562 differentiated by both TPA and staurosporine , whereas max expression did not change in either case . ^^^ Similarly , both differentiation pathways were not affected by Max overexpression or by concomitant overexpression of c Myc and Max . ^^^ This result is in contrast with the inhibition of erythroid differentiation of K 562 exerted by c Myc , suggesting divergent roles for c Myc / Max , depending on the differentiation pathway . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The c Myc oncoprotein and its dimerization partner Max bind the DNA core consensus sequence CACGTG ( E box ) and activate gene transcription . ^^^ Here , we describe a computer based pre selection of candidate Myc / Max target genes , based on two restrictive criteria : an extended E box consensus sequence for Myc / Max binding and the occurrence of this sequence within a potential genomic CpG island . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
OBJECTIVE : To examine the expression of myc proto oncogenes ; c myc , L myc , and N myc , and their related genes max and mad , in the arthritic synovium . ^^^ RESULTS : As a novel finding , synovial cells were observed to express L myc , N myc as well as their related genes max and mad , in addition to the previously described presence of c myc proto oncogene in synovium . c myc , L myc , N myc , and mad were expressed in all patient samples studied , including the controls . ^^^ CONCLUSIONS : The L myc , N myc , max , and mad genes are expressed in synovial cells , in addition to c myc proto oncogene . ^^^ Expression of the myc family proto oncogenes and related genes max and mad in synovial tissue . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Nmi was initially identified through a yeast two hybrid interaction with N Myc but it also interacts with c Myc , Max , Fos , and several other transcription factors , including signal transducer and activator of transcription ( Stat ) proteins . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The c myc gene encodes the transcription factor c Myc , which heterodimerizes with a partner protein , termed Max , to regulate gene expression . ^^^ Max also heterodimerizes with the Mad family of proteins to repress transcription , antagonize c Myc , and promote cellular differentiation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mad : Max heterodimers oppose the growth promoting action of Myc : Max heterodimers by recruiting the mSin 3 histone deacetylase ( mSin 3 . ^^^ There are four known members of the Mad family that are indistinguishable in their abilities to interact with Max , bind DNA , repress transcription , and block Myc + Ras co transformation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
A number of interaction partners of Myc have been identified , such as Max , p 107 , TBP , YY 1 , Miz 1 , AP 2 and Nmi . ^^^ In contrast to the well defined binding of Max to Myc family proteins the interaction of Nmi with Myc or MycN is only poorly characterized . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We have identified a novel Max interacting protein , Mga , which contains a Myc like bHLHZip motif , but otherwise shows no relationship with Myc or other Max interacting proteins . ^^^ Like Myc , Mad and Mnt proteins , Mga requires heterodimerization with Max for binding to the preferred Myc Max binding site CACGTG . ^^^ Surprisingly , Mga is converted to a transcription activator of both Myc Max and Brachyury site containing reporters in a Max dependent manner . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The switch from MYC MAX complexes to MAD MAX complexes has been postulated to couple cell cycle arrest with differentiation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Of interest , Max overexpression attenuates aberrant growth of B cells triggered by c Myc . ^^^ In the present studies , we studied the expression of the c Myc and Max proteins in normal lymph nodes and in childhood LL . ^^^ In normal lymph nodes , c Myc protein was expressed by the majority of cells in germinal center and marginal zone , but Max protein was expressed only by some of them . ^^^ In contrast , c Myc and Max were absent in mantle zone . ^^^ Cells positive for c Myc and Max expression in LL were 70 . 6 + / 19 . 8 % and 47 . 3 + / 32 . 4 % , respectively , determined by immunohistochemical staining using paraffin blocks from 23 cases of childhood LL . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max and , by extension , the Myc superfamily , serve essential roles in early mammalian development and a maternal reservoir of Max exists in sufficient amount to sustain Myc superfamily function through preimplantation stages of development . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
RESULTS : We report that MSSP 1 and MSSP 2 bound directly to the C terminal portion of c Myc , along with Max , side by side . ^^^ MSSP , c Myc and Max formed a ternary complex in vivo , although MSSP did not directly associate with Max . ^^^ The MSSP / Myc / Max ternary complex lost the binding activity to the E box sequence the recognition sequence of c Myc / Max complex thereby abrogating the E box dependent transcription activity of c Myc . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
ATF 2 at Ser 69 / 71 , forming a complex with Myc for DNA binding at CRE motif ; 3 ) Max at Ser 62 to combine DNA of E Box motif . p 38 MAPK can be activated by LPS , inflammatory cytokines , such as TNF and IL 1 , osmolarity . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The transcription factor c Myc is important for the control of cell cycle progression , neoplasia , and apoptotic cell death . c Myc dimerizes with its partner Max to form an active transcription factor complex . ^^^ Further , FasL promoter activity in T cells is driven by overexpression of c Myc and inhibited by expression of dominant negative mutants of c Myc and Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mad 1 is a member of the Myc / Max / Mad network of transcriptional regulators that play a central role in the control of cellular behavior . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc and Mad are basic helix loop helix leucine zipper ( bHLH LZ ) proteins that heterodimerize with Max to bind DNA and thereby influence the transcription of Myc responsive genes . ^^^ Myc Max dimers transactivate whereas Mad Max mSin 3 complexes repress Myc mediated transcriptional activation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
In this study , we demonstrate that Myc in combination with Max can bind , albeit with low affinity , to an E box like element in the tsp 1 promoter . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Furthermore , chromatin immunoprecipitation assay showed that USF , c Myc , and Max proteins were associated with the FGF BP promoter in vivo . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
BACKGROUND : The c myc oncogene product ( c Myc ) is a transcription factor that forms a complex with Max and recognizes the E box sequence . c Myc plays key functions in cell proliferation , differentiation and apoptosis . ^^^ RESULTS : We found that c Myc directly bound to the N terminal region of origin recognition complex 1 ( ORC 1 ) , a region that is responsible for gene silencing , in a state of complex containing other ORC subunits and Max in vivo and in vitro . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
A c Myc Max consensus DNA binding site was identified as an element important in the serum stimulation of HMG I / Y . ^^^ The oncoprotein c Myc and its protein partner Max bind to this site in vitro and activate transcription in transfection experiments . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
CDC 6 interacts with c Myc to inhibit E box dependent transcription by abrogating c Myc / Max complex . ^^^ The c myc oncogene product ( c Myc ) is a transcription factor that dimerizes with Max and recognizes the E box sequence . ^^^ CDC 6 bound to the C proximal region of c Myc , thereby competing with Max on the E box sequence and changing c Myc / Max heterodimer to a Max / Max homodimer . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
In FR3T3 cells transfected with cmyc and Hras , influx 5 ( max ) for [ ( 3 ) H ] MTX is downregulated 4 fold and 9 fold , respectively . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Mads and Rox compete with Myc in heterodimerizing with Max and in binding to the same specific target sequences . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The transcription factor Max is the obligate dimerization partner of the Myc oncoprotein . ^^^ The pivotal role of Max within the Myc regulatory network is dependent upon its ability to dimerize via the helix loop helix leucine zipper domain . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The interferon and differentiation inducible p202a protein inhibits the transcriptional activity of c Myc by blocking its association with Max . p202a is a murine protein that is induced during the fusion of myoblasts to myotubes and can also be induced by interferon . ^^^ These effects of p202a are consistent with our finding that the binding of p202a to c Myc inhibited the binding of c Myc to Max in vitro and in vivo . p202a also inhibited the c Myc induced anchorage independent growth and apoptosis of Rat 1 cells . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The purpose of the present study was to examine the expression of the Myc network proteins c Myc , Mad 1 and Max in normal cells under different growth and differentiation conditions . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Myc / Max / Mad network and the transcriptional control of cell behavior . ^^^ The Myc / Max / Mad network comprises a group of transcription factors whose distinct interactions result in gene specific transcriptional activation or repression . ^^^ Both Myc and Mad , as well as the more recently described Mnt and Mga proteins , form heterodimers with Max , permitting binding to specific DNA sequences . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We investigated the early effects of oxLDL and alpha tocopherol on c Myc , its binding partner Max , and the carboxy terminal domain binding factors activator protein 2 and elongation 2 factor in human coronary SMCs . ^^^ METHODS AND RESULTS : OxLDL enhanced c Myc / Max expression and transcription by cotransfection assay and the nuclear activities of E2F and activator protein 2 by binding shift and supershift in coronary SMCs . alpha Tocopherol significantly reduced these molecular events . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The FasL promoter can be driven by c Myc overexpression , and functional inhibitors of Myc and its binding partner , Max , inhibit the transcriptional activity of the FasL promoter [ 9 , 10 ] . ^^^ We identified a non canonical binding site ( ATTCTCT ) for c Myc Max heterodimers in the FasL promoter , which , when mutated , abolished activity in response to c Myc . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max is a common dimerization partner for a family of transcription factors ( Myc , Mad [ or Mxi ] ) , and Mnt [ or Rox ] proteins ) that regulate cell growth , proliferation , and apoptosis . ^^^ MondoA forms homodimers weakly and does not interact with Max or members of the Myc or Mad families . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
From a family of 73 H 1 motifs belonging to ( H 1 Loop H 2 ) hu man sequences , the smallest evolutionary distance from our reference peptide was observed for the H 1 of N Myc , L Myc , c Myc , H 1 S6A , F8A of c Myc , and Max , in that order . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Immunoprecipitation assays showed that in HHV 6 infected cells association of c Myc with YY 1 was decreased and that of Max with c Myc was increased , whereas association of Mad with Max appeared to be decreased . ^^^ The amounts of each of YY 1 , c Myc , Max , and Mad proteins synthesized in cells were not altered by HHV 6 infection . ^^^ These data indicate that the decreased association of YY 1 with c Myc that is caused by impaired interaction in the c Myc / Max / Mad network results in increased binding activity of YY 1 to the CXCR 4 promoter , mediating down regulation of CXCR 4 production in HHV 6 infected cells . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The balance between Myc Max and Mad Max complexes has been postulated to influence cell proliferation and differentiation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mad 1 is a Myc antagonist that heterodimerizes with Max and functions as a transcriptional repressor . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc and Max form a complex with Miz 1 at the p 15 initiator and inhibit transcriptional activation by Miz 1 . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Using immunohistochemistry , we have investigated the patterns of c Myc , N Myc , Max , and Mad 1 4 expression at different stages of the human hair growth cycle . ^^^ N Myc , Max , Mad 1 , and Mad 3 immunoreactivity was detected in the epidermis and the epithelium of both anagen and telogen hair follicles . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Dissociation constants ( K ( d ) ) for the heterodimer formed with the recombinant bHLHZip domain of the Myc binding partner Max ( p 14 ( max ) ) and for the Myc Max DNA complex were estimated using circular dichroism ( CD ) spectroscopy and quantitative electrophoretic mobility shift assay ( EMSA ) . ^^^ The restricted conformational space of the 5 Myc bHLHZip domain reduces the entropy penalty associated with heterodimerization and allows rapid and accurate recognition by the authentic Myc binding partner Max . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Finally , binding of Max was shown to facilitate c Myc binding and repression of p 27 promoter activity . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
TGF beta 1 arrests growth by blocking the function of the c myc proto oncogene . c myc function is determined by the level of c myc expression relative to other Max interacting transcription factors , and TGF beta 1 has been shown to inhibit c myc expression by inhibiting c myc transcription . ^^^ However , whether TGF beta 1 might also increase the expression of a Max interacting factor that blocks myc function by competing with myc for Max binding is not known . ^^^ Mad 4 and Mxi 1 are novel targets of TGF beta 1 , known to inhibit cell growth by antagonizing the interaction of Myc with Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Our results show that the cytokine induced signals reduced Myc dependent transcription of an artificial target promoter / reporter gene construct , correlating in most , but not all , cases with decreased association of 5 and c Myc with its essential partner , Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Transcriptional activation by Myc is mediated through dimerization with Max and binding to the DNA consensus sequence CA ( C / T ) GTG ( the E box ) . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We observed that the mRNA levels of myc family genes , c myc and max , were markedly reduced in MG thymuses . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc is a member of the basic region helix loop helix leucine zipper ( b HLH Zip ) class of transcription factors , which heterodimerizes with the Max protein and recognizes a consensus Myc binding motif . ^^^ Stimulation of gene expression by Myc is thought to be mediated by direct binding of Myc Max heterodimers to specific target genes . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Microarray gene screening reveals that quiescent and senescent cells , in comparison with replicating ones , are characterized by downregulation of Pam , a protein associated with c Myc , and upregulation of Mad family genes , Max dimerization proteins . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Expression of oncogenic transcription factors , c Myc , B Myc , Max and Mad , and apoptotic genes , namely Bcl 2 , Bax and Bad , was increased after FB 1 treatment . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Treatment of mice with FB ( 1 ) increased the expression of B Myc , c Myc and Max , oncogenic transcription factors in the kidney . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
ICI 182 , 780 or doxycycline ( a tetracycline analog ) treatment did not alter the mRNA levels of Max , the c myc binding partner . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Members of the Myc oncoprotein network ( c Myc , Max , and Mad ) play important roles in proliferation , differentiation , and apoptosis . ^^^ We expressed chimeric green fluorescent protein ( GFP ) fusions of c Myc , Max , and three Mad proteins in fibroblasts . ^^^ Individually , c Myc and Mad proteins localized in subnuclear speckles , whereas Max assumed a homogeneous nuclear pattern . ^^^ However , in the presence of co expressed Max , c Myc , but not Mad , co localized to a subset of SC 35 loci . ^^^ In addition , c Myc Max heterodimers , but not Max Mad heterodimers , localize to foci actively engaged in pre mRNA transcription / processing . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max is the central component of the Myc / Max / Mad network of transcription factors that regulate growth , differentiation and apoptosis . ^^^ Whereas the Myc and Mad genes and proteins are highly regulated , Max expression is constitutive and no post translational regulation is known . ^^^ Taken together , our findings uncover three distinct processes , namely dephosphorylation and cleavage by caspase 5 and caspase 7 , that target Max during Fas mediated apoptosis , suggesting the regulation of the Myc / Max / Mad network through its central component . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The c myc oncogene product ( c Myc ) is a transcription factor that dimerizes with Max and recognizes the E box sequence , and it plays key functions in cell proliferation , differentiation , and apoptosis . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
While transactivation pathways of c Myc either from the N proximal or the C proximal region that is linked to the chromatin remodeling complex have been identified , a transrepression pathway had been identified only from the C proximal region via Max and Mad that recruit the histone deacetylase ( HDAC ) complex . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The opposing transcriptional activities of the basic helix loop helix leucine zipper proteins Myc and Mad , taken together with information related to their expression patterns and biological effects , have led to a model of the Myc / Max / Mad network in which Myc and Mad proteins function as antagonists . ^^^ This antagonism is presumed to operate at the level of genes targeted by these complexes , where Myc : Max activates and Mad : Max represses expression of the same set of genes . ^^^ Furthermore , the model does not address the findings that Myc : Max indirectly represses transcription of several regulatory genes . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mad 1 is a Myc antagonist that heterodimerizes with Max and functions as a transcriptional repressor . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Here we describe a protein , JLP ( c Jun NH 2 terminal kinase associated leucine zipper protein ) , which acts as a scaffolding protein to bring together Max and c Myc along with JNK ( c Jun NH 2 terminal kinase ) and p38MAPK , as well as their upstream kinases MKK 4 ( MAPK kinase 4 ) and MEKK 3 ( MAPK kinase kinase 3 ) . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Alterations in the expression and / or function of these transcription factors , or of the c Myc and Max interacting proteins , such as MM 1 and Mxi 1 , can influence the neoplastic process . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Modulation of c myc , max , and mad gene expression during neural differentiation of embryonic stem cells by all trans retinoic acid . c Myc regulates cellular proliferation , differentiation , and apoptosis . ^^^ Correlation to the modulation of dimerizing partners Max and Mad that may influence c Myc signaling and transcription regulation was elucidated for the first time in these cells . ^^^ Increases in max and mad gene transcription detected by RPA at times of elevated c Myc in RA treated ES cells suggest that a transient increase in c Myc protein expression may influence differential dimerization of Myc partners needed for signaling in the neural differentiation of ES cells . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Myc basic helix loop helix zipper domain determines dimerization with Max and binding to the DNA E box , both of which play a critical role in Myc regulation of growth , proliferation , tumorigenesis , and apoptosis . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
It is also a key regulator of cellular proliferation , embryonic differentiation and apoptosis . c MYC encodes a transcription factor that activates target genes in a sequence specific manner through heterodimerization with the ubiquitously expressed factor MAX . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Transcriptional regulation of the ornithine decarboxylase gene by c Myc / Max / Mad network and retinoblastoma protein interacting with c Myc . c Myc is an oncogenic transcription factor involved in the regulation of cell proliferation , differentiation and apoptosis . ^^^ Transient transfection studies with different c Myc , Max and Mad constructs in COS 7 cells showed that the balance between c Myc / Max , Max / Max and Max / Mad complexes is crucial for the regulation , resulting in either transactivation or transrepression of an ODC CAT reporter gene . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Interactions of the DNA mismatch repair proteins MLH 1 and MSH 2 with c MYC and MAX . ^^^ We further demonstrate that the heterodimeric partner of c MYC , MAX , interacts with a different MMR protein , MSH 2 , both in vitro and in vivo . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Unsaturated fatty acids bind Myc Max transcription factor and inhibit Myc Max DNA complex formation . ^^^ Oncoprotein Myc , hetero dimerized with Max through a b / HLH / Zip region , is a transcription factor that governs important cellular processes such as cell cycle entry , proliferation and differentiation . ^^^ We found that linoleic acid , isolated from Pollen Typhae , and other unsaturated fatty acids have strong inhibitory effects on the binding of Myc Max heterodimer to an E box DNA site ( CA ( C / T ) GTG ) . ^^^ The interaction of a fatty acid with a protein dimer , not with DNA , is assumed to block the entire Myc Max DNA complex formation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Entry of Myc into the stable pool is signaled by an element within the carboxy terminus of the protein , and is a cell specific process that is regulated during mitosis and by interaction with Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
In this study , the glucose mediated induction of L type pyruvate kinase and glucose 6 phosphatase mRNA levels was diminished by maneuvers involving recombinant adenoviral vectors that interfere with ( 1 ) c Myc protein levels by antisense expression or ( 2 ) c Myc function through a dominant negative Max protein . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
X ray structures of Myc Max and Mad Max recognizing DNA . ^^^ Molecular bases of regulation by proto oncogenic transcription factors . 10 ray structures of the basic / helix loop helix / leucine zipper ( bHLHZ ) domains of Myc Max and Mad Max heterodimers bound to their common DNA target ( Enhancer or E box hexanucleotide , 5 ' CACGTG 3 ' ) have been determined at 1 . 9 A and 2 . 0 A resolution , respectively . ^^^ E box recognition by these two structurally similar transcription factor pairs determines whether a cell will divide and proliferate ( Myc Max ) or differentiate and become quiescent ( Mad Max ) . ^^^ The Myc Max heterodimer , but not its Mad Max counterpart , dimerizes to form a bivalent heterotetramer , which explains how Myc can upregulate expression of genes with promoters bearing widely separated E boxes . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
While c Myc and Mad 1 require Max for DNA binding , Max itself can form a homodimer that recognizes E box DNA sequences ( CACGTG ) in gene promoters that are targeted by c Myc . ^^^ Evidence suggests that this mode of binding by Max may repress c Myc transcriptional activity , and this may have applications in the control of the aberrant activity of c Myc during certain oncogenic transformations . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Taking myc to the max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Although Bcr and Max have overlapping binding sites on c Myc , Bcr can not interact with Max , or with the c Myc . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Thus , luteinization of primate granulosa cells is preceded by a burst of proliferation that is regulated by changes in the relative levels of c Myc , Max , and Mad as well as p53 . . ^^^ Dynamics of Myc / Max / Mad expression during luteinization of primate granulosa cells in vitro : association with periovulatory proliferation . ^^^ Max , the common dimerization partner for Myc and Mad , is similarly repressed by hCG , suggesting that changes in the expression of this gene may further regulate the activity of Myc and Mad . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Among the early response genes analyzed , c myc , junB , junD , c jun , c fos , fosB , fra , as well as max , mad 1 4 , sin 3 , only c jun and fra 2 mRNAs were up regulated after 1 , 25 ( OH ) ( 2 ) D ( 3 ) exposure . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Genomic binding by the Drosophila Myc , Max , Mad / Mnt transcription factor network . ^^^ The Myc / Max / Mad transcription factor network is critically involved in cell behavior ; however , there is relatively little information on its genomic binding sites . ^^^ We have employed the DamID method to carry out global genomic mapping of the Drosophila Myc , Max , and Mad / Mnt proteins . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The consensus binding sequence ( T / C ) GCGCA ( C / T ) GCGC ( A / G ) of NRF 1 includes a noncanonical CA ( C / T ) GCG Myc : MAX binding site . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Our results demonstrate that the absence of specific tactile stimuli provided by the mother limits PRL evoked stimulation of ODC biosynthesis by interfering with sn 1 , 2 diacylglycerol ' s ( DAG ) ability to activate protein kinase Calpha ( PKCalpha ) and consequently c myc mRNA and max mRNA expression . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Analysis of Myc bound loci identified by CpG island arrays shows that Max is essential for Myc dependent repression . ^^^ Analyzing a cohort of known and novel Myc target genes showed that Myc associated protein 10 , Max , also bound to these regulatory regions . ^^^ Indeed , Max is bound to these loci in the presence or absence of Myc . ^^^ The Myc : Max interaction is essential for Myc dependent transcriptional activation ; however , we show that Max bound targets also include Myc repressed genes . ^^^ Moreover , we show that the interaction between Myc and Max is essential for gene repression to occur . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We analyzed telomerase activities and gene expressions of telomerase components : hTERT , hTR , hTEP 1 , telomeric repeat binding factors : TRF 1 , TRF 2 , and c myc , Max and Mad in human normal oral and ectocervical epithelial keratinocytes , comparing with those of squamous carcinoma cells and HPV 16 or SV 40 immortalized cells . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We find that c Myc together with its heterodimeric partner , Max , occupy > 15 % of gene promoters tested in these cancer cells . ^^^ The DNA binding of c Myc and Max correlates extensively with gene expression throughout the genome , a hallmark attribute of general transcription factors . ^^^ The c Myc / Max heterodimer complexes also colocalize with transcription factor IID in these cells , further supporting a general role for overexpressed c Myc in global gene regulation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
MYCN is a member of the myc family of proto oncogenes which encode nuclear proteins that form heterodimers with MAX protein through their conserved HLHZip domains . ^^^ The MYC / MAX complexes transactivate a number of MYC target genes in a sequence specific manner . ^^^ MYC MAX interaction is essential for MYC induced cell cycle progression , cellular transformation , and transcriptional activation . ^^^ Inhibition of MYC MAX dimerisation by small molecule antagonists has recently been shown to interfere with MYC induced transformation of chick embryo fibroblasts , indicating that functional inhibitors of the MYC family of oncoproteins have potential as therapeutic agents . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Low molecular weight inhibitors of Myc Max interaction and function . c Myc is helix loop helix leucine zipper ( HLH ZIP ) oncoprotein that is frequently deregulated in human cancers . ^^^ In order to bind DNA , regulate target gene expression , and function in a biological context , c Myc must dimerize with another HLH ZIP protein , Max . ^^^ We have used a yeast two hybrid approach to identify low molecular weight compounds that inhibit c Myc Max association . ^^^ All of the compounds prevented transactivation by c Myc Max heterodimers , inhibited cell cycle progression , and prevented the in vitro growth of fibroblasts in a c Myc dependent manner . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Examples of specific , highly expressed , cancer associated genes in amplified loci include SERPINB 10 , MYC , TYMS , HEC , and EPB41L3 , while CD 14 , GZMK , TCF 7 , FOS , MLH 3 , CTNNA 1 , IRF 1 , VIM , CRK , MAP3K1 , STAM , MAX , SFRG 5 , ENC 1 , PURA , MNT , RASA 1 , GLRX , UBE2B , NR3C1 , PTENP 1 , BS 69 , COPEB , SKIP , PIM 2 , and MIC 2 represent cancer associated genes in deleted loci with decreased expression . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
In addition to the CD 95 and TNFalpha systems , the expression of apoptotic molecules bcl 2 , b myc , c myc , bax , max , mad and IL1alpha was induced by FB 1 in TKO mice to a greater extent than in WT animals ; many of these factors also had a higher constitutive expression in TKO animals than WT mice . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Max interaction with Myc is required for DNA binding at so called E box sequences and Myc dependent transcriptional activation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The curcuminoid 004 showed an inhibitory effect on the binding of myc max protein to the E box element in SNU 16 cells , and suppressed the expression of myc target genes including ornithine decarboxylase ( ODC ) , cdc25a and c myc in myc over expressed human stomach cancer cell line SNU16 . . ^^^ Determination of binding constant of transcription factor myc max / max max and E box DNA : the effect of inhibitors on the binding . ^^^ The truncated myc and max proteins , only containing basic regions and helix loop helix / zipper ( b / HLH / Zip ) regions were over expressed in E . coli and used for the determination of the binding constant and of the inhibitory mechanism on myc max ( or max max ) DNA complex formation . ^^^ The equilibrium binding constant ( K ( 1 ) ) was determined using these kinetic parameters [ K ( XXD ) = ( 7 . 8+ / 2 . 6 ) x 10 ( 6 ) M ( 1 ) for max max and DNA or K ( XYD ) = ( 6 . 9+ / 2 . 2 ) x 10 ( 6 ) M ( 1 ) for myc max and DNA ] . ^^^ The binding constants of myc max or max max dimer formation were K ( 20 ) = ( 2 . 6+ / 0 . 9 ) x 10 ( 5 ) M ( 1 ) or K ( XY ) = ( 1 . 3+ / 0 . 4 ) x 10 ( 4 ) M ( 1 ) , respectively . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
All of the effects of Myc require its function as a transcription factor that dimerizes with Max . ^^^ Here we report that in quiescent cells the Odc E boxes are occupied by Max and Mnt , a putative Myc antagonist , and that this complex is displaced by Myc Max complexes in proliferating cells . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Phosphorylation at all three residues reduces the binding of Myc to DNA , either by blocking the requisite dimerization with Max ( through phosphorylation at S 373 and T 400 ) or by interfering directly with binding to DNA ( through phosphorylation at T 358 ) . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Kinetics of myc max mad gene expression during hepatocyte proliferation in vivo : Differential regulation of mad family and stress mediated induction of c myc . ^^^ Despite the critical role of Max and Mad proteins as modulators of c Myc functions , there are no comparative data on their regulation in vivo . ^^^ We carried out a systematic analysis of c myc , max , and mad family expression in a model of synchronized cell proliferation in vivo in adult tissues , that is , rat hepatocytes after partial hepatectomy . ^^^ No such expression was detected in sham operated rat quiescent hepatocytes . max expression increased around 4 16 h after hepatectomy , before the peaks of c myc and DNA synthesis . mxi 1 and mad 4 were slightly downregulated during liver regeneration . mnt / rox expression did not change . ^^^ Expression of c Myc and Max increased clonogenic growth , whereas the reduction of c Myc levels by an antisense vector decreased growth . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Reconstitution of an E box binding Myc : Max complex with recombinant full length proteins expressed in Escherichia coli . ^^^ Myc has an N terminal transcription activation domain ( TAD ) that interacts with various coactivators and a C terminal basic helix loop helix leucine zipper ( bHLHZip ) domain required for E box specific DNA binding and heterodimerization with its obligatory bHLHZip protein partner Max . ^^^ The analysis of the mechanisms by which the Myc : Max complex regulates transcription at the molecular level in vitro has been hampered by the difficulty in obtaining highly pure recombinant Myc : Max heterodimers that contain full length Myc with its complete TAD domain and that have sequence specific DNA binding activity . ^^^ Here , we describe a simple method to reconstitute recombinant Myc : Max complexes from highly purified full length proteins expressed in Escherichia coli that are soluble and highly active in E box specific DNA binding in vitro . ^^^ The reconstituted Myc : Max complexes are stable and lack Max : Max homodimers . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mnt can inhibit Myc dependent cell transformation and is hypothesized to counterbalance the effects of c Myc on growth and proliferation in vivo by competing with Myc for binding to Max and by repressing target genes activated by Myc : Max heterodimers . ^^^ Unlike the related Mad family members , Mnt is expressed ubiquitously and Mnt / Max heterodimers are found in proliferating cells that contain Myc / Max heterodimers , suggesting a unique role for Mnt during proliferation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Visualization of Myc / Max / Mad family dimers and the competition for dimerization in living cells . ^^^ We have visualized the subcellular locations of complexes formed by Myc / Max / Mad family proteins using bimolecular fluorescence complementation ( BiFC ) analysis . ^^^ Max was recruited to different subnuclear locations by interactions with Myc versus Mad family members . ^^^ Complexes formed by Max with Mxi 1 , Mad 3 , or Mad 4 were enriched in nuclear foci , whereas complexes formed with Myc were more uniformly distributed in the nucleoplasm . ^^^ We compared the relative efficiencies of complex formation among Myc , Max , and Mad family proteins in living cells using multicolor BiFC analysis . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Activation induced Fas ligand expression in T cells is under the stringent control of various transcription factors , including nuclear factor kappaB ( NFkappaB ) and c Myc / Max . ^^^ In this study , we have analyzed the regulation of the Fas ligand gene promoter induction in two non small cell lung cancer cell lines , with a major focus on the role of the c Myc / Max transcription factor . ^^^ Our results revealed that inhibition of c Myc / Max did not substantially reduce basal levels of Fas ligand promoter activity , nor did overexpression of c Myc significantly induce promoter activity . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We were able to confirm key findings using antibodies to the endogenous c Myc and / or its partner , Max . ^^^ Evidence of Max concentration within PML bodies is shown both with and without proteasome inhibition , strengthening the relationship between PML bodies and Myc / Max . ^^^ Some accumulation of Myc and Max in nucleoli upon proteasome inhibition is also observed , although co localization of ubiquitin was only seen with PML bodies . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
However , mutational analysis of the p 21 promoter and the use of a Gal 4 Sp1 chimeric protein strongly suggest that c Myc affects Sp 1 transcriptional activity but not the binding of Sp 1 to the p 21 promoter . c Myc mediated impairment of Ras activity on p 21 expression required a transactivation domain , a DNA binding region , and a Max binding region . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Molecular modeling and biochemical analysis define a PARP domain that is capable of ADP ribosylating PARP 10 itself and core histones , but neither Myc nor Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Here we show that the proteins c Myc and Max interact in nucleoli and are associated with ribosomal DNA . ^^^ Using small interfering RNAs ( siRNAs ) against c Myc and an inhibitor of Myc Max interactions , we demonstrate that c Myc is required for activating rDNA transcription in response to mitogenic signals . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
They share a common obligatory dimerization partner , Max , with the oncoprotein c Myc and antagonize the function of Myc to activate transcription . ^^^ The Myc / Max / Mad network has therefore been suggested to function as a molecular switch that regulates cell growth and differentiation by controlling a common set of genes . ^^^ The elevated expression of Mad 1 in these cells resulted in increased Mad1 / Max heterodimer formation correlating with reduced expression of the Myc / Mad target gene ODC . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
These heterodimers specifically bind E box DNA sequence ( CACGTG ) to activate ( e . g . c Myc / Max ) and repress ( e . g . ^^^ Max can also homodimerize and bind E box sequences in c Myc target gene promoters . ^^^ Max , a b / H ( 1 ) LH ( 2 ) / LZ transcription factor , is the obligate heterodimeric partner of the related b / H ( 1 ) LH ( 2 ) / LZ proteins of the Myc and Mad families . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Increased c Myc protein formed heterodimers with its binding partner , Max , and specifically bound to the Myc / Max binding site , which was associated with an increase in DNA synthesis . ^^^ These results indicate that polyamine induced nuclear c Myc interacts with Max , binds to the specific DNA sequence , and plays an important role in stimulation of normal intestinal epithelial cell proliferation . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Functions of myc : max in the control of cell proliferation and tumorigenesis . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
A recent study identified , on a genomic scale , human genes whose promoters are bound by c Myc and its heterodimer partner Max in Burkitt ' s lymphoma cells . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Myc / Max / Mad network of transcription factors regulates cell proliferation , differentiation , and transformation . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Whereas CHK had no significant effects on the expression of YY 1 , c Myc , Max , and other YY 1 binding proteins , CHK was found to modulate the YY1 / c Myc association . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
On the other hand , c Myc protein is also a bHLHZIP protein that dimerizes with Max , binds the identical E box sequence but activates transcription of the target genes . ^^^ In summary , Mxi D may play an important role in the c Myc family protein network acting as a dominant negative isoform of Mxi F since : 1 ) Mxi D can dimerize with Max in vitro ; 2 ) Mxi D / Max heterodimers can not bind E box in vitro , 3 ) Mxi D can not suppress clonal growth stimulated by c Myc . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We confirmed that Wnt signaling was maximal in the proliferative compartment and observed a decrease in MYC and an increase in MAD and MAX expression during the maturation program . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Here , we show that c Myc induction during cell cycle entry leads to a transient decrease in Mnt Max complexes and a transient switch in the ratio of Mnt Max to c Myc Max on shared target genes . ^^^ Mnt overexpression suppressed cell cycle entry and cell proliferation , suggesting that the ratio of Mnt Max to c Myc Max is critical for cell cycle entry . ^^^ Mnt Max to Myc Max complex switching regulates cell cycle entry . ^^^ Mnt and Myc require interaction with Max for specific DNA binding at E box sites , but have opposing transcriptional activities . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
BACKGROUND : The c Myc oncogenic transcription factor heterodimerizes with Max , binds specific DNA sites and regulates transcription . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Myc Max Mad network of transcription factors plays an essential role in many cellular processes such as proliferation , differentiation , and apoptosis . ^^^ The Mad proteins heterodimerize with Max , function as transcriptional repressors , and are capable of antagonizing the transforming activity of Myc . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Determination of the dissociation constants for recombinant c Myc , Max , and DNA complexes : the inhibitory effect of linoleic acid on the DNA binding step . c Myc , the protein product of protooncogene c myc , functions in cell proliferation , differentiation , and neoplastic disease . ^^^ In this study , recombinant c Myc and Max proteins , encompassing DNA binding ( basic region ) and dimerization ( helix loop helix / leucine zipper ) domain of human origin , were expressed in bacteria as Myc 87 and Max 85 . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Myc Max Mad / Mnt network of transcription factors has been implicated in oncogenesis and the regulation of proliferation in vertebrate cells . ^^^ The identification of Myc and Max homologs in Drosophila melanogaster has demonstrated a critical role for dMyc in cell growth control . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The c Myc oncoprotein ( Myc ) functions as a transcription regulator in association with an obligatory partner , Max , to control cell growth and differentiation . ^^^ The Myc : Max complex regulates specific genes by recognizing `` E box ' ' DNA sequences and promoter bound factors such as Miz 1 . ^^^ Here , we have analyzed the acetylation of recombinant Myc : Max complexes by purified p 300 HAT in vitro by using MALDI TOF and LC ESI MS / MS mass spectrometry . ^^^ Our results further indicate that p 300 can acetylate DNA bound Myc : Max complexes and that acetylated Myc : Max heterodimers efficiently interact with Miz 1 . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Assembly of b / HLH / z proteins c Myc , Max , and Mad 1 with cognate DNA : importance of protein protein and protein DNA interactions . ^^^ Among the best characterized of the transcription factors are the b / HLH / z proteins : USF , Max , Myc , and Mad . ^^^ Max and Myc form a heterodimer that has strong oncogenic potential but can also repress transcription , while Mad and Max form a heterodimer that acts as a transcription repressor . ^^^ Looked at from the perspective of the Max protein , the binding of DNA to Max significantly reduces the affinity of the Max protein for the second monomer , whether the second monomer is Myc , Mad , or Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We have now generated a fusion protein ( designated Max U ) that is composed both of Max , which forms a heterodimer with c Myc , and of CHIP , which is a U box type ubiquitin ligase ( E 3 ) . ^^^ Max U physically interacted with c Myc in transfected cells and promoted the ubiquitylation of c Myc in vitro . ^^^ Expression of Max U reduced both the abundance of endogenous c Myc in and the proliferation rate of a Burkitt lymphoma cell line . ^^^ Furthermore , expression of Max U but not that of a catalytically inactive mutant thereof markedly inhibited both the anchorage independent growth in vitro of NIH 3T3 cells that overexpress c Myc as well as tumor formation by these cells in nude mice . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Coordinated regulation of c Myc and Max in rat liver development . ^^^ The processes of liver development and regeneration involve regulation of a key network of transcription factors , the c myc / max / mad network . ^^^ Nucleolar localization of c Myc coincided with changes in Max content . ^^^ High levels of Max resulted in a shift in c Myc localization from nucleolar to diffuse nuclear . ^^^ In contrast , liver regeneration was associated with an increase in c Myc content but no change in Max content . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The c Myc oncoprotein ( Myc ) controls cell fate by regulating gene transcription in association with a DNA binding partner , Max . ^^^ While Max lacks a transcription regulatory domain , the N terminus of Myc contains a transcription activation domain ( TAD ) that recruits cofactor complexes containing the histone acetyltransferases ( HATs ) GCN 5 and Tip 60 . ^^^ Moreover , the Myc : Max complex is differentially acetylated by p 300 and GCN 5 and is not acetylated by Tip 60 in vitro , suggesting distinct functions for these acetyltransferases . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Inhibition of c Myc and Max dimerization by this polypeptide leads to as much as a 2 fold reduction in the doxorubicin and etoposide IC ( 50 ) in three different cell lines tested . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
From a 285 membered library , several hits were obtained that disrupted the c Myc Max interaction and cellular functions of c Myc . ^^^ The IC 50 values determined for this small focused library for the disruption of Myc Max dimerization are quite potent , especially since small molecule antagonists of protein protein interactions are notoriously difficult to find . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Like Myc family proteins , Mxd and Mnt proteins use Max as a cofactor for DNA binding . ^^^ But Mnt Max and Mxd Max complexes are transcriptional repressors and can antagonize the transcriptional activation function of Myc Max . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
We now show that vMyc can sustain longer deletions in the LZ domain than cMyc before complete loss in transforming activity , implicating the viral mutations in contributing to Myc : Max complex formation . ^^^ Interaction with Max via the helix loop helix / leucine zipper ( HLH LZ ) domain is essential for Myc to function as a transcription factor . ^^^ We confirmed this both in vitro and in vivo , with loss of Max binding correlating with a loss in the biological activity of Myc . ^^^ Significantly , introduction of I 383 > L into a Myc mutant that is defective for Max binding substantially restored its ability to complex with Max in vitro and in vivo . ^^^ We therefore propose that this virally derived mutation is functional by significantly contributing to establishing a more hydrophobic interface between the LZs of Myc and Max . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Our results indicate that Max could homodimerize , bind DNA , and repress transcription in vivo and that its mutant could be more efficient at repressing the expression of c Myc target genes . . ^^^ Max is the only protein in this network that recognizes and binds E Box DNA sequences as a homodimer in vitro and represses transcription of Myc target genes in vivo . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Mad 1 forms a specific heterodimer with Max and acts as a transcriptional repressor when bound to an E box sequence ( CACGTG ) found in the promoter of c Myc target genes . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Myc oncoprotein forms a binary activating complex with its partner protein , Max , and a ternary repressive complex that , in addition to Max , contains the zinc finger protein Miz 1 . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Mad side of the Max network : antagonizing the function of Myc and more . ^^^ A significant body of evidence has been accumulated that demonstrates decisive roles of members of the Myc / Max / Mad network in the control of various aspects of cell behavior , including proliferation , differentiation , and apoptosis . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Structural aspects of interactions within the Myc / Max / Mad network . ^^^ In this review , we focus on the lessons provided by these structures toward understanding ( 1 ) interactions that govern transcriptional repression by Mad via the Sin 3 pathway , ( 2 ) homodimerization of Max , ( 3 ) heterodimerization of Myc Max and Mad Max , and ( 4 ) DNA recognition by each of the Max Max , Myc Max , and Mad Max dimers . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Although the molecular mechanisms by which c Myc and its obligate partner , Max , regulate gene expression are becoming better defined , genes or transcriptomes that c Myc regulate are just emerging from a variety of different experimental approaches . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Here we summarize the findings obtained from the myc / max / mad knockout mice generated to date , namely those in which the N myc , c myc , L myc , mad 1 , mxi 1 , mad 3 , mnt , or max genes have been targeted . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
The Myc Max Mad network of proteins activates or represses gene transcription depending on whether the dimerization partner of Max is c Myc or Mad . ^^^ The binding affinities and thermodynamics of dimerization of the Max Max homodimer and c Myc Max and Mad Max heterodimers were determined . ^^^ Our results indicate that c Myc and Max form the most stable heterodimer . ^^^ In the presence of PLG , entropy became more negative with the effect being largest for c Myc Max heterodimers . ^^^ Thermodynamics of protein protein interactions of cMyc , Max , and Mad : effect of polyions on protein dimerization . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
LZ family members Myc and Max , could not replace the PAS domains for either dimerization or DNA binding in the DR / Arnt heterodimer . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Since the participation of c Myc protein in transcription requires its dimerization with Max protein , we examined the Myc Max association in Cpd 5 treated cells and found that Cpd 5 suppressed Myc Max dimerization . ^^^ Transfection of Hep3B cells with mutated ERK ( T188A / Y190F ) , which has lost its dual phosphorylation sites , attenuated the actions of Cpd 5 on Myc Max association . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Myc / Max / Mad in invertebrates : the evolution of the Max network . ^^^ The Myc proto oncogenes , their binding partner Max and their antagonists from the Mad family of transcriptional repressors have been extensively analysed in vertebrates . ^^^ This review describes the structure of invertebrate Myc / Max / Mad genes and it discusses their regulation and physiological functions , with special emphasis on their essential role in the control of cellular growth and proliferation . . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
Recent experiments suggest the existence of a transcriptional network that functions in parallel to the canonical Myc / Max / Mad transcriptional network . ^^^ Unlike the Myc / Max / Mad network , our understanding of this network is still in its infancy . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
MAX serves as a cofactor for DNA binding by the various members of this network , which include the MYC family of oncoproteins and a group of putative MYC antagonists that include MNT , MXD 1 4 ( formerly MAD 1 , MXI 1 , MAD 3 and MAD 4 ) and MGA . ^^^
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA
Interacting proteins: P61244 and P01106	Pubmed	SVM Score :0.0
NA