Pubmed abstracts for Protein-Protein Interaction search result :

Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.62067436
Mad 3 and Mad 4 interact with both Max and mSin 3 and repress transcription from a promoter containing CACGTG binding sites . 0.62067436^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.64819877
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 . 0.64819877^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.51061673
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 . 0.51061673^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.78744716
Mad 1 was induced rapidly and efficiently , localized to the nucleus , and bound to DNA as a heterodimer with Max . 0.78744716^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.81630952
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 . 0.81630952^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
The Mad protein is synthesized in human cells as a 35 kD nuclear phosphoprotein with an extremely short half life ( t1 / 2 = 15 30 min ) and can be detected in vivo in a complex with Max . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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 . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
The Max transcription factor network : involvement of Mad in differentiation and an approach to identification of target genes . ^^^ Max has now been found to interact with at least two other proteins , Mad and Mxi 1 . ^^^ 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 . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Mad is a basic helix loop helix leucine zipper protein that heterodimerizes with Max . ^^^ 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: Q05195 and P61244	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 . ^^^ Recently two Max interacting proteins , Mad and Mxi 1 , have been identified . ^^^ We have analysed different aspects of Mad function in comparison to Max . ^^^ Native Mad / Max heterodimers bound specifically to a c Myc / Max consensus DNA binding site . ^^^ Myc transformed clones showed an increased cell cycle time and a reduced immortalization frequency after cotransfection with either mad or max . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Mad and Mxi 1 proteins both heterodimerize with Max and compete with each other for limiting amounts of Max . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
The second mechanism involves a specific interaction between C terminal domains of AP 2 and the BR / HLH / LZ domain of Myc , but not Max or Mad . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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 . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
MAD and MXI 1 , two recently described members of the basic helix loop helix ( bHLH ) gene family , encode proteins that dimerize with and modulate the DNA binding of max . ^^^ 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: Q05195 and P61244	Pubmed	SVM Score :0.0
Mad Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin 3 . ^^^ The bHLH ZIP protein Mad heterodimerizes with Max as a sequence specific transcriptional repressor . ^^^ Mad is rapidly induced upon differentiation , and the associated switch from Myc Max to Mad Max heterocomplexes seem to repress genes normally activated by Myc Max . ^^^ Mad Max and mSin 3 form ternary complexes in solution that specifically recognize the Mad Max E box binding site . ^^^ We suggest that Mad Max represses transcription by tethering mSin 3 to DNA as corepressors and that a transcriptional repression mechanism is conserved from yeast to mammals . . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
The interpretation of the results using mammalian cells is complicated by the presence of numerous unrelated CACGTG binding transcription activators and the existence of two alternative Max dimerization partners , Mad and Mxi 1 . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Mapping of two genes encoding members of a distinct subfamily of MAX interacting proteins : MAD to human chromosome 2 and mouse chromosome 6 , and MXI 1 to human chromosome 10 and mouse chromosome 19 . ^^^ 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: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
Expression of mad , mxi 1 , max and c myc during induced differentiation of hematopoietic cells : opposite regulation of mad and c myc . ^^^ Recently two other partners of Max , called Mad and Mxi 1 , have been identified . ^^^ In an effort to gain insight into the network of these four proteins we have started to analyse the expression of the c myc , max , mad and mxi 1 genes at the mRNA level during hematopoietic cell growth and differentiation . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Myc Max Mad : a transcription factor network controlling cell cycle progression , differentiation and death . ^^^ Max also forms homodimers or heterodimers with its alternative partners , Mad and Mxi 1 . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Transcription repression by the basic region helix loop helix zipper ( bHLHZip ) protein Mad 1 requires DNA binding as a ternary complex with Max and mSin3A or mSin3B , the mammalian orthologs of the Saccharomyces cerevisiae transcriptional corepressor SIN 3 . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
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 . ^^^ In contrast , Mad : Max heterodimers act as transcriptional repressors , have an antiproliferative effect , and are induced upon differentiation in a wide variety of cell types . ^^^ We have identified a novel bHLHZip Max binding protein , Mnt , which belongs to neither the Myc nor the Mad families and which is coexpressed with Myc in a number of proliferating cell types . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
The Myc family members Mad and Mxi 1 are known to suppress Myc induced transcription and transformation and to dimerize with Max to form ternary complexes with the mammalian Sin 3 transcriptional corepressor ( mSin 3 ) . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
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: Q05195 and P61244	Pubmed	SVM Score :0.0
Members of the Mad family of bHLH Zip proteins heterodimerize with Max to repress transcription in a sequence specific manner . ^^^ Transcriptional repression by Mad : Max heterodimers is mediated by ternary complex formation with either of the corepressors mSin3A or mSin3B . ^^^ The mSin3A immunocomplexes possess histone deacetylase activity that is sensitive to the specific deacetylase inhibitor trapoxin . mSin3A targeted repression of a reporter gene is reduced by trapoxin treatment , suggesting that histone deacetylation mediates transcriptional repression through Mad Max mSin3A multimeric complexes . . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
Cell growth inhibition by the Mad / Max complex through recruitment of histone deacetylase activity . ^^^ Mammalian Sin 3 proteins interact with the Mad components of the Myc / Max / Mad network of cell growth regulators . ^^^ Mad / Max complexes may recruit mammalian Rpd 3 like enzymes , therefore , directing histone deacetylase activity to promoters and negatively regulating cell growth . ^^^ RESULTS : We report the identification of a tetrameric complex composed of Max , Mad 1 , Sin3B and HD 1 . ^^^ 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: Q05195 and P61244	Pubmed	SVM Score :0.0
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: Q05195 and P61244	Pubmed	SVM Score :0.0
Analysis of the DNA binding activities of Myc / Max / Mad network complexes during induced differentiation of U 937 monoblasts and F 9 teratocarcinoma cells . ^^^ 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 . ^^^ Few studies on the DNA binding activity of native Myc : Max or Max : Mad complexes have been reported mainly due to technical difficulties . ^^^ To overcome these problems we have developed a specific and sensitive solid phase DNA binding assay based on partial purification of native Myc , Max and Mad 1 complexes by immunological methods . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
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 . ^^^ In vitro , Mmip 1 can inhibit DNA binding by Max Mad heterodimers and , in vivo , can reverse the suppressive effects of Mad proteins on c myc functions . ^^^ By interfering with the dimerization between Max and Mad family member proteins , Mmip 1 can indirectly up regulate the transcriptional activity of c myc and suppress the antiproliferative actions of Mad proteins . . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
The C . elegans MDL 1 and MXL 1 proteins can functionally substitute for vertebrate MAD and MAX . ^^^ The genes of the myc / max / mad family play an important role in controlling cell proliferation and differentiation . ^^^ We have identified the first homologues of the mad and max genes in the nematode C . elegans , which we have named mdl 1 and mxl 1 respectively . ^^^ The coexpression in the posterior intestinal cells occurs before their final division at the end of the L 1 stage and persists afterwards , demonstrating that mad and max expression can be correlated directly to the cell cycle state of an individual cell type . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
We have identified a novel Max binding protein , Mnt , which belongs to neither the Myc nor the Mad families ( Hurlin et al . 1997 ) . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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 ) . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Two MAD tails : what the recent knockouts of Mad 1 and Mxi 1 tell us about the MYC / MAX / MAD network . ^^^ Members of the MAD / MXI protein family heterodimerize with MAX and repress transcription by recruiting a chromatin modifying co repressor complex to specific DNA target genes . ^^^ Repression mediated by MAD is thought to antagonize the transcriptional activation and proliferation promoting functions of MYC MAX heterodimers . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
Max is a basic helix loop helix leucine zipper protein that forms heterodimers with its alternative partners , Mad and Mxi 1 , to behave as an antagonist for Myc Max heterodimer through competition for common DNA targets . ^^^ 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: Q05195 and P61244	Pubmed	SVM Score :0.0
Mad : Max dimers ) of genes linked to prostate cancer progression . ^^^
Interacting proteins: Q05195 and P61244	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 . ^^^ Mad : Max heterodimers repress transcription by recruiting a large multi protein complex containing the histone deacetylases , HDAC 1 and HDAC 2 , to DNA . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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 . ^^^ It does not form homodimers , working as a heterodimer with Max ; Max , instead , forms homodimers and heterodimers with Mad and Mnt . ^^^ Myc / Max dimers activate gene transcription , while Mad / Max and Mnt / Max complexes are Myc / Max antagonists and act as repressors . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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 . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
Expression of the myc family proto oncogenes and related genes max and mad in synovial tissue . ^^^ 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 . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Max also heterodimerizes with the Mad family of proteins to repress transcription , antagonize c Myc , and promote cellular differentiation . ^^^
Interacting proteins: Q05195 and P61244	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 . ^^^ The similarities between Mlx and Max include 1 ) broad expression in many tissues , 2 ) long protein half life , and 3 ) formation of heterodimers with Mad family proteins that are capable of specific CACGTG binding . ^^^ In contrast with Max , Mlx interacts only with Mad 1 and Mad 4 . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Like Myc , Mad and Mnt proteins , Mga requires heterodimerization with Max for binding to the preferred Myc Max binding site CACGTG . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
The four members of the MAD family are bHLHZip proteins that heterodimerize with MAX and act as transcriptional repressors . ^^^ The switch from MYC MAX complexes to MAD MAX complexes has been postulated to couple cell cycle arrest with differentiation . ^^^
Interacting proteins: Q05195 and P61244	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 . ^^^ We recently characterized a novel Max like protein , Mlx , which interacts with Mad 1 and Mad 4 . ^^^ MondoA forms homodimers weakly and does not interact with Max or members of the Myc or Mad families . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
The Mad family comprises four basic helix loop helix / leucine zipper proteins , Mad 1 , Mxi 1 , Mad 3 , and Mad 4 , which heterodimerize with Max and function as transcriptional repressors . ^^^ The balance between Myc Max and Mad Max complexes has been postulated to influence cell proliferation and differentiation . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
In utero RA treatment resulted in decreased expression of max , mad , caspases , bax , and bad genes at 48 h . ^^^
Interacting proteins: Q05195 and P61244	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 . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
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 . ^^^ Similar to Mad and Max , p 53 and wip 1 are transiently repressed by hCG , suggesting that the p 53 and Mad pathways have either parallel or cooperative roles in luteinization . ^^^ 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 . . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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 . ^^^ Mad 4 was localized to the cytoplasm when it was expressed separately , and Mad 4 was recruited to the nucleus through dimerization with Max . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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: Q05195 and P61244	Pubmed	SVM Score :0.0
RESULTS : 95 genes , such as the genes of thrombospondin 1 ( THBS 1 ) , phosphatase and tensin homolog ( PTEN ) , MAX dimerization protein ( MAD ) , DNA damage inducible transcript 3 ( DDIT 3 ) , ets variant gene 1 ( ETV 1 ) , G 1 to S phase transition 1 ( GSPT 1 ) , were shown to be abnormally expressed in at least 5 MDS patients compared to the normal controls , involving cell growth and differentiation regulation , cell cycle control , signaling , and redox . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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 . ^^^ Mad Max dimers repress the transcription of the same target genes activated by Myc Max dimers . ^^^ 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 . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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: Q05195 and P61244	Pubmed	SVM Score :0.0
Proteins studied included cell surface receptors ( Ephrins and Eph receptors , CD 44 ) , kinases ( EGFR cytoplasmic domain , CDK 2 and 4 ) , proteases ( MMP 1 , CASP 2 ) , signal transduction proteins ( GRB 2 , RAF 1 , HRAS ) and transcription factors ( GATA 2 , Fli 1 , Trp 53 , Mdm 2 , JUN , FOS , MAD , MAX ) . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	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 . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
The processes of liver development and regeneration involve regulation of a key network of transcription factors , the c myc / max / mad network . ^^^ On the basis of this finding , we went on to characterize the expression patterns of the other members of the network , max and mad , comparing their regulation during late fetal development with the proliferation of mature hepatocytes that is seen in liver regeneration . ^^^ We conclude that the regulation of Max content during liver development and its potential role in determining c Myc localization are means by which Max may control the biological activity of the c Myc / Max / Mad network during liver development . . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Thermodynamics of protein protein interactions of cMyc , Max , and Mad : effect of polyions on protein dimerization . ^^^ 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 . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	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: Q05195 and P61244	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 . ^^^ Like Max , Mix interacts with transcriptional repressors and transcriptional activators , namely the Mad family and the Mondo family , respectively . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Although Mad 1 ( a basic helix loop helix leucine zipper [ bHLH Zip ) protein ) forms a heterodimer with the Max bHLH Zip protein , LexA Mad 1 and VP 16 Max do not activate transcription of a reporter gene in a two hybrid assay . ^^^ This failure in activation is due to direct repression by ySin 3 , as LexA Mad 1 and VP 16 Max are able to activate the two hybrid reporter in a sin 3 mutant . ^^^ This inhibition of activation by LexA Mad 1 and VP 16 Max requires the PAH 2 domain of ySin 3 and the N terminal interaction region of Mad 1 . ^^^
Interacting proteins: Q05195 and P61244	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 . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
In in vitro protein : protein association assays , dMax interacted with c Myc , N Myc , L Myc , Mad 1 , Mxi 1 , Mad 3 and Mad 4 , but not with itself or wild type Max . ^^^
Interacting proteins: Q05195 and P61244	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 . ^^^ There was no immunolabeling in response to anti Max or anti Mad 1 antibodies . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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 . ^^^ Therefore these data suggest that an increase in the levels of mad 1 mRNA or the formation of a Mad Max complex are unlikely to be essential or determining events for myeloid differentiation . ^^^ In addition , the discovery of DNA binding complexes that contain Mad 1 , but not Max , opens up this transcription factor network to include other Max like proteins or proteins of an unrelated nature . . ^^^
Interacting proteins: Q05195 and P61244	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 . ^^^ By coimmunoprecipitation we detected increased binding of Mad 1 to Max in forskolin treated cells , indicating that the changes in Mad 1 protein levels had functional implications . ^^^
Interacting proteins: Q05195 and P61244	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 ) . ^^^ These results suggest that IFNgamma treatment could shift the Myc Max complex to the Mad 1 Max complex in cells . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Silencing of the Epstein Barr virus latent membrane protein 1 gene by the Max Mad 1 mSin3A modulator of chromatin structure . ^^^ Gel retardation assays showed that members of the basic helix loop helix transcription factor family , including Max , Mad 1 , USF , E 12 , and E 47 , and the corepressor mSin3A bound to the E box containing sequence . ^^^ Moreover , the activity of the LMP 1 promoter in reporter constructs was upregulated by overexpression of USF 1 and USF2a , and the transactivation was inhibited by the concurrent expression of Max and Mad 1 . ^^^ This suggests that Max Mad 1 mediated anchorage of a multiprotein complex including mSin3A and histone deacetylases to the E box site constitutes the basis for the repression . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
OBJECTIVES : To study the effects and possible mechanisms of mitosis arrest deficiency 1 ( Mad 1 ) , the heterodimerizer of Max and a transcriptional repressor , on cell proliferation of bladder cancer in vitro and in vivo . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Using the bHLH ZIP domain of mad 1 as a yeast two hybrid ' bait ' , we identified Mmip 2 , a novel RING finger protein that interacts with all mad members , but weakly or not at all with c myc , max or unrelated bHLH or bZIP proteins . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
Mad 1 is a Myc antagonist that heterodimerizes with Max and functions as a transcriptional repressor . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Like Max , Mlx has no intrinsic transcriptional activity , but its association with Mad 1 , Mad 4 , Mnt or WBSCR 14 can repress E box dependent transcription . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
Mad 1 is a Myc antagonist that heterodimerizes with Max and functions as a transcriptional repressor . ^^^
Interacting proteins: Q05195 and P61244	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 . ^^^
Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
Here we demonstrate that Mad 1 is a potent inhibitor of the G ( 1 ) to S phase transition , a function that requires Mad 1 to heterodimerize with Max and to bind to the corepressor complex . ^^^
Interacting proteins: Q05195 and P61244	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: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P61244	Pubmed	SVM Score :0.0
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