Pubmed abstracts for Protein-Protein Interaction search result :

Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.92036883
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 . 0.92036883^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.73149834
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 . 0.73149834^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.5072258
Cotransfection of a constitutive c myc with a zinc inducible mad 1 results in clones expressing both genes , whereby a switch from proliferation to differentiation can be modulated . 0.5072258^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Regional differences in expression were more striking on the cellular level , particularly in the mouse and human gastrointestinal system , wherein c Myc protein was readily detected in immature proliferating cells at the base of the colonic crypts , while Mad protein distribution was restricted to the postmitotic differentiated cells in the apex of the crypts . ^^^
Interacting proteins: Q05195 and P01106	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 P01106	Pubmed	SVM Score :0.0
Mad protein has been shown as an antagonist of c Myc protein in some cell lines . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
In this review we focus on the Myc and Mad protein families and attempt to relate their biological functions to their transcriptional activities and gene targets . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Mad protein , a specific antagonist of Myc , repressed E 6 mediated transactivation of the hTERT promoter and this repression was relieved by Myc overexpression . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
When certain cells differentiate , Myc in Myc Max heterodimers is replaced by Mad or Mxi , generating heterodimers that suppress transcription by interacting with the repressor Sin3 . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Effects of the MYC oncogene antagonist , MAD , on proliferation , cell cycling and the malignant phenotype of human brain tumour cells . ^^^ To investigate how overexpression of MAD , an antagonist of MYC oncogenes influences the malignant phenotype of human cancer cells , an adenovirus vector system was used to transfer the human MAD gene ( AdMAD ) into human astrocytoma cells . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Mad has been shown to abrogate the positive transcriptional activity of Myc and to inhibit Myc in co transformation assays . ^^^ This suggests that Mad may antagonize Myc function . ^^^ Mad is rapidly induced upon differentiation , a time when Myc is frequently down regulated . ^^^ 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 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 . ^^^ While Myc activates transcription and cell proliferation Mad represses these activities ( Ayer et . al . , Cell 72 , 211 222 , 1993 ) . ^^^
Interacting proteins: Q05195 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 . ^^^ Native Mad / Max heterodimers bound specifically to a c Myc / Max consensus DNA binding site . ^^^ Furthermore Mad inhibited efficiently c Myc , mutant p 53 , adenovirus E1a , or human papilloma virus type 16 transformation of rat embryo cells in cooperation with activated Ha Ras . ^^^ In contrast to Mad , Max did not inhibit E1a / Ha Ras cotransformation but repressed c Myc / Ha Ras transformation efficiently . ^^^ Mad delta N , an N terminal deletion mutant of Mad , was as efficient in repressing c Myc / Ha Ras cotransformation as full length Mad but showed little inhibitory activity when assayed on E1a / Ha Ras . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Transcriptional activation by Myc can be suppressed by increasing the amount of Mad or Mxi 1 . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Here we show that Mad also blocks transformation of primary rat embryo fibroblasts by c Myc and the activated c Ha Ras oncoproteins . ^^^ Repression of Myc Ras cotransformation by Mad is mediated by multiple protein protein interactions . ^^^ Mad is a bHLH / Zip protein that , as a heterodimer with Max , can repress Myc induced transcriptional transactivation . ^^^ Expression of Mad is induced upon terminal differentiation of several cell types , where it has been postulated to down regulate Myc induced genes that drive cell proliferation . ^^^ Mad mutants lacking either the basic region , the leucine zipper , or an intact NH 2 terminal protein interaction domain fail to inhibit Myc Ras cotransformation . ^^^
Interacting proteins: Q05195 and P01106	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 P01106	Pubmed	SVM Score :0.0
We also studied the expression of the other two described members of the c Myc network : mxi 1 and mad . mxi 1 expression increased during erythroid differentiation but was strongly down regulated during myelomonocytic differentiation of K 562 . mad was constitutively expressed during K 562 erythroid differentiation and slightly increased during induction of the myelomonocytic pathway . ^^^
Interacting proteins: Q05195 and P01106	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 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: Q05195 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 . ^^^ While the expression of Myc is necessary for cell proliferation , the expression of Mad is induced upon differentiation of at least some leukemia cell lines . ^^^ In cell culture , Mad inhibited colony formation of a mouse keratinocyte cell line and rat embryo fibroblast transformation by Myc and Ras . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
In mammals , current evidence supports the view that Myc responsive activities are regulated in part through an intracellular balance between levels of transcriptionally active Myc / Max heterodimers and those of transcriptionally inert Max / Max , Mad / Max and Mxi1 / Max complexes . ^^^
Interacting proteins: Q05195 and P01106	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 . ^^^ 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 . ^^^ These analysis thus suggest that the expression of mad and c myc is inversely regulated during induced hematopoietic differentiation . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Myc Max Mad : a transcription factor network controlling cell cycle progression , differentiation and death . ^^^
Interacting proteins: Q05195 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 . ^^^ To place these recent biochemical observations in a biological context , mad and mxi 1 expression vectors were tested for their ability to influence Myc transformation activity in the rat embryo fibroblast cooperation assay . ^^^ Addition of an equimolar amount of mad or mxi 1 expression vector to mouse c myc / ras cotransfections resulted in a dramatic reduction in both the number of foci generated and the severity of the malignant phenotype . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
A switch from Myc : Max to Mad : Max heterocomplexes accompanies monocyte / macrophage differentiation . ^^^ Mad : Max heterodimers recognize the same E box related DNA binding sites as Myc : Max heterodimers . ^^^ However , in transient transfection assays Myc and Mad influence transcription in opposite ways through interaction with Max ; Myc activates while Mad represses transcription . ^^^ In the undifferentiated U 937 monocyte cell line Max was found complexed with Myc but not Mad . ^^^
Interacting proteins: Q05195 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 . ^^^ In addition , Mad has been shown to act as a transcriptional repressor while Myc appears to function as an activator . ^^^ Therefore , Mxi 1 and Mad might antagonize Myc function and are candidate tumor suppressor genes . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Expression of Mad , an antagonist of Myc oncoprotein function , in differentiating keratinocytes during tumorigenesis of the skin . ^^^ The related Mad transcription factor , which antagonises Myc activity , is highly expressed in epidermal keratinocytes . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Mad 1 dimerizes with Max and recognizes the same DNA sequences as do Myc : Max dimers . ^^^ However , Mad 1 and Myc appear to have opposing functions . ^^^ Myc : Max heterodimers activate transcription while Mad : Max heterodimers repress transcription from the same promoter . ^^^ In addition Mad 1 has been shown to block the oncogenic activity of Myc . ^^^ The ability of over expressed Myc and cyclin D 1 to complement the mutant CSF 1 receptor Y809F ( containing a Y to F mutation at position 809 ) is also inhibited by Mad 1 . ^^^
Interacting proteins: Q05195 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 . ^^^ In normal epidermis and colonic mucosa c myc expression is restricted to proliferating cell layers , while mad expression is restricted to differentiating cell layers . ^^^ These results indicate that c Myc and Mad expression are tightly coupled to the transition from proliferation to differentiation of epithelial cells and that restriction of Mad expression may be associated with loss of normal differentiation capability and with tumorigenesis . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Mad 3 and Mad 4 : novel Max interacting transcriptional repressors that suppress c myc dependent transformation and are expressed during neural and epidermal differentiation . ^^^ Using a rat embryo fibroblast transformation assay , we show that both Mad 3 and Mad 4 inhibit c Myc dependent cell transformation . ^^^ An examination of the expression patterns of all mad genes during murine embryogenesis reveals that mad 1 , mad 3 and mad 4 are expressed primarily in growth arrested differentiating cells . mxi 1 is also expressed in differentiating cells , but is co expressed with either c myc , N myc , or both in proliferating cells of the developing central nervous system and the epidermis . ^^^ 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 . ^^^ Whereas both Myc : Max and Mad : Max heterodimers bind related E box sequences , Myc : Max activates transcription and promotes proliferation while Mad : Max represses transcription and suppresses Myc dependent transformation . ^^^
Interacting proteins: Q05195 and P01106	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 ) . ^^^ However , transfer of a 25 to 36 aa region from Mad or Mxi 1 , which interacts with mSin 3 , to the b HLH LZ of TFEB , mediated profound suppression of Myc induced transcription and transformation . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
When fused to a full length c Myc protein , the Mad 1 SID specifically represses both c Myc ' s transcriptional and transforming activities . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	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 . ^^^ 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 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: Q05195 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: Q05195 and P01106	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 P01106	Pubmed	SVM Score :0.0
Proteins of the Myc and Mad family are involved in transcriptional regulation and mediate cell differentiation and proliferation . ^^^ 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 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: Q05195 and P01106	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 P01106	Pubmed	SVM Score :0.0
In general , the DNA binding activity of c Myc and Mad 1 correlate with their expression . ^^^ 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 . ^^^ Whereas Myc proteins actively promote cell proliferation , Mad complexes have the opposite function . ^^^ Although the main regulation of this network seems to be the control of myc and mad family gene expression , regulation at the level of DNA binding and transactivation may also be in operation . ^^^
Interacting proteins: Q05195 and P01106	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 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: Q05195 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 ) . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Targeted disruption of the MYC antagonist MAD 1 inhibits cell cycle exit during granulocyte differentiation . ^^^ The switch from transcriptionally activating MYC MAX to transcriptionally repressing MAD 1 MAX protein heterodimers has been correlated with the initiation of terminal differentiation in many cell types . ^^^ These findings demonstrate that MAD 1 regulates cell cycle withdrawal during a late stage of granulocyte differentiation , and suggest that the relative levels of MYC versus MAD 1 mediate a balance between cell proliferation and terminal differentiation . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
To define whether viral receptor up regulation by itself increased gene transfer , cell cycling was inhibited by a recombinant adenovirus expressing the Mad transcription factor ( AdMad ) , which is a dominant negative c Myc regulator . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Mxi 1 belongs to the Mad ( Mxi 1 ) family of proteins , which function as potent antagonists of Myc oncoproteins . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Activities of Myc are countered by those of Mad and Mxi 1 , two related members of the Myc superfamily . ^^^ Mad and Mxi 1 compete with Myc for common elements and interact with putative transcriptional repressors . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
The functions of Myc in transformation and transactivation are countered by the suppressive actions of the Mad ( Mxi 1 ) family . ^^^ 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 . ^^^ A prediction of the yin yang relationship between Myc and Mad ( Mxi 1 ) families would be that the latter constitutes a new class of tumor suppressors . ^^^ Here , we review the current literature on the Mad ( Mxi 1 ) family , with particular attention paid to the molecular mechanisms by which these proteins antagonize the actions of Myc in normal and neoplastic cells . . ^^^
Interacting proteins: Q05195 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 . ^^^ MAD proteins therefore act as antagonists of MYC . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Mmip 1 : a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c myc . ^^^ 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 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: Q05195 and P01106	Pubmed	SVM Score :0.0
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 P01106	Pubmed	SVM Score :0.0
MXI 1 , a member of the MAD family of Myc antagonists , encodes a transcription factor whose expression must be tightly regulated to maintain normal cell growth and differentiation . ^^^
Interacting proteins: Q05195 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: Q05195 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: Q05195 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 . ^^^
Interacting proteins: Q05195 and P01106	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 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: Q05195 and P01106	Pubmed	SVM Score :0.0
The basic helix loop helix leucine zipper ( bHLHZip ) proteins Myc , Mad and Mnt are part of a transcription activation / repression system involved in the regulation of cell proliferation . ^^^ 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 P01106	Pubmed	SVM Score :0.0
Since c Myc function is inhibited by recruitment of histone deacetylase activity through Mad family proteins , these opposing biochemical activities are likely to be responsible for the antagonistic biological effects of c Myc and Mad on target genes and ultimately on cellular transformation . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Dwarfism and dysregulated proliferation in mice overexpressing the MYC antagonist MAD 1 . ^^^ The switch from MYC MAX complexes to MAD MAX complexes has been postulated to couple cell cycle arrest with differentiation . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Myc and Mad family proteins regulate multiple biological processes through their capacity to influence gene expression directly . ^^^ Here we show that the basic regions of Myc and Mad proteins are not functionally equivalent in oncogenesis , have separable E box binding activities and engage both common and distinct gene targets . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
This Mad mediated repression of the hTERT promoter in mortal cells was counteracted by ectopic expression of Myc . ^^^ The antagonism between Mad and Myc was also observed with an endogenous hTERT promoter . ^^^ Their potential roles in differential hTERT promoter activities were further supported by the relative amounts of Mad and Myc proteins detected in immortal and mortal cells . ^^^ Thus , Mad may be a direct negative regulator of hTERT in mortal cells and this repression mechanism can be inhibited by induction of Myc in immortal cells . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
In contrast , mad 3 expression was associated with progression through S phase and the proliferative burst of differentiating preadipocytes , overlapping in part c myc expression . ^^^ Analysis of Myc / Max / Mad network members in adipogenesis : inhibition of the proliferative burst and differentiation by ectopically expressed Mad 1 . ^^^ Transcription factors of the Myc / Max / Mad network affect multiple aspects of cellular behavior , including proliferation , differentiation , and apoptosis . ^^^ Recent studies have shown that Mad proteins can inhibit cellular growth and transformation and thus antagonize the function of Myc proteins . ^^^ Our findings suggest that the precise temporal regulation of Myc / Max / Mad network proteins is critical for determining cellular behavior . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
METHODS : To perturb the activity of c Myc , which regulates G0 / G1 transitions , we overexpressed Mad 1 protein with an adenoviral vector , AdMad . ^^^
Interacting proteins: Q05195 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 . ^^^ We show that removal of the last 18 amino acids of Mad 1 ( region 5 ) abolishes the growth inhibitory function of the protein and the ability to reverse a Myc imposed differentiation block . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Members of the Mad / Mxi family of repressors play important roles in the transition between proliferation and differentiation by down regulating the expression of genes that are activated by the proto oncogene product Myc . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Targeted deletion of the S phase specific Myc antagonist Mad 3 sensitizes neuronal and lymphoid cells to radiation induced apoptosis . ^^^ The balance between Myc Max and Mad Max complexes has been postulated to influence cell proliferation and differentiation . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
C myc expression in prostate cells is well established but to our knowledge that of several recently discovered mad / mxi genes is completely uncharacterized . ^^^ Novel expression patterns of the myc / max / mad transcription factor network in developing murine prostate gland . ^^^ PURPOSE : Expression of myc proto oncogenes and myc antagonizing mad / mxi genes typically predominate in proliferating versus differentiating cells , respectively . ^^^ C myc expression in prostate cells is well established but to our knowledge that of several recently discovered mad / mxi genes is completely uncharacterized . ^^^ The expression patterns of the 3 myc genes c , L and N myc , and the mad 1 , mxi 1 and mad 4 genes were studied in most detail with nonradioactive in situ and immunohistochemical analyses . ^^^
Interacting proteins: Q05195 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: Q05195 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: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Function and regulation of the transcription factors of the Myc / Max / Mad network . ^^^ The members of the Myc / Max / Mad network function as transcriptional regulators . ^^^ Substantial evidence has been accumulated over the last years that support the model that Myc / Max / Mad proteins affect different aspects of cell behavior , including proliferation , differentiation , and apoptosis , by modulating distinct target genes . ^^^ Myc and Mad proteins affect target gene expression by recruiting chromatin remodeling activities . ^^^ Mad proteins , that antagonize Myc function , recruit an mSin 3 repressor complex with histone deacetylase activity . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
The interplay between Mad and Myc in proliferation and differentiation . ^^^ Mad family proteins are related to Myc , but they antagonize the oncogenic activity of Myc in cell culture assays . ^^^ Here , we examine current models of Mad function and the relationship between Mad and Myc in cell proliferation , differentiation and tumorigenesis . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
It has been shown in several in vitro systems that Mad proteins antagonize c Myc functions . ^^^ Repression of in vivo growth of Myc / Ras transformed tumor cells by Mad 1 . ^^^ The Myc / Max / Mad network of transcriptional regulatory proteins plays an essential role in cell proliferation , growth , apoptosis , and differentiation . ^^^ Whereas Myc proteins affect cell cycle progression positively , Mad proteins are negative regulators of cell proliferation . ^^^ These data demonstrate that Mad 1 is able to suppress Myc / Ras mediated transformation under in vivo conditions . . ^^^
Interacting proteins: Q05195 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: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Modulation of T lymphocyte development , growth and cell size by the Myc antagonist and transcriptional repressor Mad 1 . ^^^ Here , we utilized transgenesis to provide evidence suggesting that the basic helix loop helix zipper ( bHLHZ ) transcriptional repressor Mad 1 , considered to be an antagonist of Myc function , inhibits lymphocyte expansion , maturation and growth following pre T cell receptor ( pre TCR ) and TCR stimulation . ^^^ Over 80 % of the genes repressed by Mad 1 have previously been found to be induced by Myc . ^^^ These results suggest that a balance between Myc and Mad levels may normally modulate lymphocyte proliferation and development in part by controlling expression of growth regulating genes . . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
To examine these issues relating to DNA binding specificity and biological responses , we have determined the DNA binding preferences of Mad 1 by using selection and amplification of randomized oligonucleotides and demonstrated that its intrinsic specificity is identical with that of c Myc . ^^^ Myc and Mad bHLHZ domains possess identical DNA binding specificities but only partially overlapping functions in vivo . ^^^ 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 . ^^^ We have also used a chimeric Myc protein , containing a substitution of the entire Mad basic helix loop helix leucine zipper motif , and shown that it can reproduce the growth promoting activities of Myc , but not its apoptotic function . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
In this study , we found that the basic helix loop helix transcription factor Mad , which usually acts as a repressor to c Myc , enhances insulin gene transcription . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Mad 4 is regulated by a transcriptional repressor complex that contains Miz 1 and c Myc . ^^^ We demonstrate that the initiator element is required for Mad 4 activation , and show that induction is associated with the loss from the initiator of a complex that contains Miz 1 and c Myc . ^^^ Miz 1 activates the Mad 4 promoter in transient transfection assays , and this effect is antagonized by c Myc . ^^^ We therefore identify Mad 4 as a novel target of transcriptional repression by c Myc . ^^^ These data suggest that the expression of Mad 4 in proliferating undifferentiated cells is suppressed by the binding of a c Myc Miz 1 repressor complex at the initiator , and that the activation of Mad 4 during differentiation results , at least in part , from a decrease in c Myc mediated repression . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Wild type c Myc was then compared with c Myc ( Mad BR ) in oncogenic transformation , regulation of cell proliferation , induction of apoptosis , activation of chromosomal gene expression , and direct binding to chromosomal sites by chromatin immunoprecipitation . ^^^ The Mad and Myc basic domains are functionally equivalent . ^^^ The Myc / Max / Mad family of transcription factors plays a fundamental role in the regulation of cell proliferation , oncogenic transformation , and cell differentiation . ^^^ However , it remains unclear whether different heterodimers , such as Myc / Max and Mad / Max , recognize the same or different target genes in vivo . ^^^ We show by chromatin immunoprecipitation that Myc target genes are also recognized by Mad 1 in differentiated HL 60 cells . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
In contrast , the c Myc antagonists Mad 1 , Mad 4 , and Mxi 1 are transiently repressed by hCG . ^^^ 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Ectopic expression of the E box binding factors c Myc and Mad did influence promoter activity in these cells ; indeed , the presence of endogenous c Myc protein was altered after differentiation . ^^^
Interacting proteins: Q05195 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 . ^^^ Expression of c myc was slightly decreased , whereas Mad was expressed in parallel with that of hTERT during passages . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Mad 4 , c Myc endogenous inhibitor , induces a replicative senescence like state when overexpressed in human fibroblasts . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
However , sustained Id 2 repression in these cells and in human keratinocytes coincides with induction of the Myc antagonistic repressors Mad 2 and Mad 4 , decreased formation of Myc Max heterodimers and the replacement of Myc Max complexes with Mad Max complexes on the Id 2 promoter . ^^^
Interacting proteins: Q05195 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: Q05195 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 . ^^^ Mad proteins ( Mad 1 , Mxi 1 , Mad 3 , Mad 4 , Mnt / Rox ) are biochemical and biological antagonists of c Myc oncoprotein . ^^^ 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 P01106	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 P01106	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 P01106	Pubmed	SVM Score :0.0
As MAD 4 is a member of the MAD family , which antagonizes the functions of MYC and promotes cell differentiation , the biological function of the interaction between TCP10L and MAD 4 may be to maintain the differentiation state in liver cells . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Mxi 1 , a member of the Mad family , represses transcription of c Myc regulated genes by mediating chromatin condensation via histone deacetylase and the Sin 3 corepressor . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Two negative regulators of growth control [ antagonizer of myc transcriptional activity ( Mad ) and p27kip1 ] were induced 68 and 3 fold , respectively . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Microarray analysis by ATRA treatment for 48 hr in peripheral blood mononuclear cells ( in vivo ) and in cultured bone marrow mononuclear cells ( in vitro ) from a patient with APL revealed upregulation of CD11b , CD11c , CCAAT enhancer binding protein epsilon , Rb 1 , Mad , and tumor necrosis factor related genes ; and downregulation of hTERT , c Myc , WT 1 , bcl 2 , and eukaryotic translation elongation factor 1alpha2 . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Isolation and comparative expression analysis of the Myc regulatory proteins Mad 1 , Mad 3 , and Mnt during Xenopus development . ^^^ 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 P01106	Pubmed	SVM Score :0.0
Visualization of Myc / Max / Mad family dimers and the competition for dimerization in living cells . ^^^ Myc and Mad family proteins play opposing roles in the control of cell growth and proliferation . ^^^ 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 . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Immunoprecipitation ( IP ) and immunoblotting ( IB ) analysis reveal that the suppression of hTERT by USF was not through the interaction of USF with c myc or mad , nor disturbed the cellular protein levels of those . ^^^
Interacting proteins: Q05195 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 . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	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 . ^^^ 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 P01106	Pubmed	SVM Score :0.0
Myc creates an activation loop by transcriptionally repressing its own functional inhibitor , hMad 4 , in young fibroblasts , a loop lost in replicatively senescent fibroblasts . c Myc transcriptional activity in cells is dampened by the Mad family of transcriptional repressors . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
The b HLH LZ family of transcription factors contains numerous proteins including the Myc and Mad families of proteins . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Myc activities appear also to be constrained and fine tuned by a set of proteins that include the Mxd ( formerly named Mad ) family and the related protein Mnt . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Terminal B cell differentiation is associated with down regulation of Bcl 6 , activation of Blimp 1 , modulation of Myc , and specifically with the up regulation of the Mad 1 and Mad 4 transcription factors , which play a critical role in cell differentiation and cell cycle regulation . ^^^
Interacting proteins: Q05195 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 . ^^^ Thermodynamics of protein protein interactions of cMyc , Max , and Mad : effect of polyions on protein dimerization . ^^^
Interacting proteins: Q05195 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 . ^^^ Mad family members , including Mad 1 , Mxi 1 , Mad 3 , Mad 4 , Mnt , and Mga , function in part as antagonists of Myc oncoproteins . ^^^ At the molecular level this antagonism is reflected by the different cofactor / chromatin remodeling complexes that are recruited by Myc and Mad family members . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
To fully appreciate the differences between physiological c Myc function in normal cells and deregulated c Myc function in tumors , the challenge now is to determine how the authenticated transcriptomes effect the various phenotypes induced by c Myc and to define how c Myc transcriptomes are altered by the Mad family of proteins . . ^^^
Interacting proteins: Q05195 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: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Myc / Max / Mad often play pivotal roles in the proliferation , apoptosis , differentiation and cell cycle progress of leukemia cells . ^^^ Myc and Mad are known to be unstable proteins and their expression is tightly regulated throughout cell cycle progression and differentiation . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Myc proteins are transcription factors that function within a network of transcriptional activators ( Myc ) and repressors ( Mxd / Mad and Mnt ) , all of which heterodimerize with the bHLHZ protein Mad and bind E box sequences in DNA . ^^^ Our results support the view that the Myc / Max / Mad network influences transcription on a global scale . . ^^^
Interacting proteins: Q05195 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 . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Analysis of this line during growth arrest revealed that , although the expression of the Myc target gene , ornithine decarboxylase ( ODC ) was down regulated , the cells differed from those of the parental line in that they continued to express high levels of c Myc protein , but did not maintain high levels of expression of the Myc antagonists , mad 1 and mxi 1 . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
It has been shown that during myeloid differentiation the levels of mad 1 mRNA are induced before the loss of c Myc protein . ^^^ This suggests that inactivation of the differentiation blocking activity of c Myc might not occur primarily through the loss of Myc protein , but through an increase in the levels of its antagonist , Mad 1 . ^^^ 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Regulated expression and function of the c Myc antagonist , Mad 1 , during a molecular switch from proliferation to differentiation . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Another regulatory factor in the myc family , mad 1 , was expressed unaltered in U 937 and in TUR cells regardless of TPA stimulation . . ^^^
Interacting proteins: Q05195 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 . ^^^ Downregulation of c Myc accompanied by induction of Mad 1 upon differentiation has fueled the notion that Mad 1 may play a role in the cessation of proliferation associated with the differentiation process . ^^^ 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 . ^^^ This growth inhibition was associated with transient increased expression of Mad 1 concomitant with transient downregulation of c Myc . ^^^ By continually treating Reh cells with forskolin for 72 h , we observed a sustained elevated expression of Mad 1 concomitant with downregulated c Myc expression , still without changing the differentiation profile of the Reh cells . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Furthermore , apoptosis of WEHI 231 cells ensued following enhanced expression of Mad 1 , which has been found to reduce functional c Myc levels . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Expression of Mad 1 protein inhibits proliferation of cancer cells and inversely correlated with Myc protein expression in primary gastric cancer . ^^^ We performed immunohistochemical assay for Mad 1 and Myc protein in 76 gastric cancer tissues . ^^^ Cancers with reduced Mad 1 expression had high proliferative index ( S and G2 / M phase ) and there was inverse correlation between Mad 1 and Myc expression in the same cancer cells . ^^^ Mad 1 may influence biologic behavior of cancer cell by inhibiting transcriptional activity of Myc and reduced levels of Mad 1 expression seem to be associated with carcinogenesis in human gastric cancer . . ^^^
Interacting proteins: Q05195 and P01106	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 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 . ^^^
Interacting proteins: Q05195 and P01106	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 P01106	Pubmed	SVM Score :0.0
For both genes , mutation of the E boxes abolishes transcriptional activation by Myc as well as repression by Mad 1 . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
BACKGROUND : Mad 1 protein is known to repress Myc target genes and antagonize Myc function . ^^^ METHODS : The authors performed immunohistochemical assays for Mad 1 and Myc proteins in human breast carcinoma , along with tissues from normal breast and benign diseases . ^^^ The authors did not observe any correlation between S phase and expression status of Myc or Mad 1 . ^^^ Mad 1 expression was closely linked to differentiation of the cancer cells and inversely correlated with Myc expression ( P = 0 . 042 ) . ^^^ CONCLUSIONS : In human breast carcinoma cells , expression of Mad 1 seems to be down regulated , whereas expression of Myc is amplified . ^^^
Interacting proteins: Q05195 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 ) . ^^^ We found that whereas IFNgamma inhibits CSF 1 stimulated c Myc gene expression , it induces Mad 1 expression . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Furthermore , microinjection of Mad 1 expressing plasmids into fibroblasts inhibited apoptosis induced by the oncoproteins c Myc and E1A . ^^^ 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Co induction of Mad 1 and c Myc in activated normal B lymphocytes . ^^^ 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 . ^^^ A dominant view has been that Mad 1 as a c Myc antagonist plays a role in growth inhibition linked to differentiation . ^^^ The most intriguing observation we made using this cell system was a pronounced coinduction of Mad 1 and c Myc . ^^^ The levels of c Myc and Mad 1 mRNAs and proteins increased within 3 h of anti mu stimulation , and the levels were further enhanced by TPA . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
A third gene encoded for the transcriptional repressor and c Myc antagonist Mad 1 . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
Recent evidence suggests that the Myc and Mad 1 proteins are implicated in the regulation of the gene encoding the human telomerase reverse transcriptase ( hTERT ) , the catalytic subunit of telomerase . ^^^ We have analyzed the in vivo interaction between endogenous c Myc and Mad 1 proteins and the hTERT promoter in HL 60 cells with the use of the chromatin immunoprecipitation assay . ^^^ These data suggest that the reciprocal E box occupancy by c Myc and Mad 1 is responsible for activation and repression of the hTERT gene in proliferating and differentiated HL 60 cells , respectively . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
An at least 30 fold reduction of immature intron containing hTERT RNA was observed after the introduction of a normal chromosome 3 , but expression levels of c Myc , Mad 1 , and other c Myc target genes were unchanged . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
In this study , we demonstrate that activin A and TGF beta 1 directly induce the expression and activity of Mad 1 , an antagonist of the c Myc transcription factor , in the human HaCaT keratinocyte cell line . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Conditional expression of Mad 1 , a Myc antagonist , represses proliferation of different cell types including U2OS cells . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Expression of mad 1 mRNA was rapidly increased in response to expression of MEnT resulting in a shift from predominantly c Myc / Max complexes to predominantly Mad / Max containing complexes . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
MAD 1 and p 27 ( KIP 1 ) cooperate to promote terminal differentiation of granulocytes and to inhibit Myc expression and cyclin E CDK 2 activity . ^^^ To understand how cellular differentiation is coupled to withdrawal from the cell cycle , we have focused on two negative regulators of the cell cycle , the MYC antagonist MAD 1 and the cyclin dependent kinase inhibitor p 27 ( KIP 1 ) . ^^^ By contrast , similar treatment of granulocytes from Mad 1 or p 27 ( KIP 1 ) single null mice resulted in differentiation accompanied by downregulation of both Myc expression and cyclin E CDK 2 kinase activity . ^^^ We conclude that Mad 1 and p 27 ( KIP 1 ) operate , at least in part , by distinct mechanisms to downregulate CDK 2 activity and Myc expression in order to promote cell cycle exit during differentiation . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
The addition of ZnCl ( 2 ) to HT 29 APC cells increased wild type APC protein and Mad 1 RNA and protein and decreased levels of c myc and ODC RNA and protein , relative to these parameters in HT 29 cells transfected with the same plasmid containing the beta galactosidase gene in place of APC . ^^^ These results demonstrated that wild type APC suppressed c myc and activated Mad 1 expression in HT 29 colon derived cells . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
In keeping with the role of PML in transcriptional repression , pRB also promoted PML dependent transcriptional repression by the c Myc antagonist Mad 1 . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Endogenous expression levels of c Myc or Mad 1 , which could activate or repress hTERT transcription when overexpressed , did not account for the differential hTERT transcription . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
To perturb the activity of c Myc , which is involved in the progression of melanoma , we overexpressed Mad 1 protein with liposomal mediated transfection of cytomegalovirus promoter driven expression vector containing the human Mad 1 gene , pcMad 1 . ^^^ Mad 1 is a Myc antagonist that heterodimerizes with Max and functions as a transcriptional repressor . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
It is the obligate partner of the related b HLH LZ proteins , c Myc and Mad 1 , with which it forms heterodimers on target DNA . ^^^ 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 P01106	Pubmed	SVM Score :0.0
APC influences the expression of several genes , including the c myc oncogene and its antagonist Mad 1 . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
We show that this regulation may involve the suppression of c Myc and an increased production of Mad 1 . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Recent studies have shown that the transcription factors c Myc and Mad 1 activate and repress hTERT , respectively . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Using primary cells from mice deficient for either the cyclin dependent kinase inhibitor ( CDKi ) p 27 ( Kip 1 ) , the Myc antagonist Mad 1 , or both Mad 1 and p 27 ( Kip 1 ) , we observed that signals mediated through retinoic acid receptor alpha ( RAR alpha ) , but not RAR beta or gamma , required both Mad 1 and p 27 ( Kip 1 ) to induce cell cycle arrest and to accelerate terminal differentiation of granulocytes . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
By using PCR based and gel shift assays we demonstrated specific binding to a core hTERT promoter of Ets 2 , Fli 1 , Id 2 , c Myc , Mad 1 , and Sp 1 in lysates from subclones of U 937 cells . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
The expression of Mad 1 , a competitor of c Myc , was increased . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
MAD 1 and c MYC regulate UBF and rDNA transcription during granulocyte differentiation . ^^^ Here we show that granulocytic cells deficient in the c MYC antagonist MAD 1 display increased cell volume , rDNA transcription and protein synthesis . ^^^ MAD 1 repressed and c MYC activated rDNA transcription in nuclear run on assays . ^^^ These data demonstrate that MAD 1 and c MYC reciprocally regulate rDNA transcription , providing a mechanism for coordination of ribosome biogenesis and cell growth under conditions of sustained growth inhibition such as granulocyte differentiation . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Transcript regulation of human telomerase reverse transcriptase by c myc and mad 1 . ^^^ Among the transcript regulation factors of hTERT , c myc and mad 1 are well known . ^^^ Here , we constructed c myc and mad 1 eukaryotic expression vectors , then co transfected them with the wild type ( Tw ) or mutant hTERT promoter ( Td ) luciferase reporter plasmid , which were double mutated in the E box sequences from CACGTG to CACCTG of Tw . ^^^ The results showed that Tw was obviously activated in T 24 and EJ bladder cancer cells , but not in normal fibrocytes . c myc and mad 1 had positive and negative effects respectively on the Tw transcript in a dose dependent manner , while the roles of c myc and mad 1 in regulating the Td transcript were reversed . c myc combined with mad 1 can down regulate Tw but not Td . ^^^ These observations indicate that c myc and mad 1 can regulate the hTERT transcript in a different manner in hTERT positive cells , but not in normal cells . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
METHODS : Methyl thiazolyl tetrazolium ( MTT ) analysis , flow cytometry , polymerase chain reaction ( PCR ) enzyme linked immunosorbent assay ( ELISA ) and RT PCR methods were used respectively to determine the killing effects of OM and its influence on cell cycle distribution , telomerase activity and the expressions of hTERT , c myc , p 53 and mad 1 in SW 1116 cells . ^^^ After OM administration , the expression of hTERT in the SW 1116 cells decreased , those of p 53 and mad 1 increased , and the expression of c myc was unchanged . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
RT PCR method was employed to detect the influence of EGCG on the expressions of hTERT , c myc , p 53 and mad 1 genes in sensitive cancer cell line . ^^^ After EGCG administration , the expression of hTERT and c myc genes in MKN 45 cells was decreased , that of the mad 1 gene increased , and that of the p 53 gene unchanged . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
To investigate the molecular mechanism involved in hTERT down regulation by HNE , the expression of several transcription factors was also studied : in all these cell lines , c Myc was inhibited , Mad 1 was up regulated , and Sp 1 was not affected . ^^^ In HL 60 cells , DNA binding activity of c Myc and Mad 1 to the E box sequence of the hTERT promoter was inhibited and up regulated , respectively . ^^^ In summary , HNE inhibits telomerase activity via decreased hTERT promoter activity , by modulating c Myc / Mad 1 transcription factor expression . . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
These effects are largely reversed by exogenous Myc as well as by differentiation and are mimicked by the Myc antagonist Mad 1 . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
Consistent with the gene expression profile , DNA binding activity of c myc and the nuclear protein concentration of its coactivator , upstream binding factor ( UBF ) , increased in the atrophied heart whereas protein levels of the c myc inhibitor MAD 1 decreased . ^^^
Interacting proteins: Q05195 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: Q05195 and P01106	Pubmed	SVM Score :0.0
We then investigated the sequential changes in cellular growth , expression of telomerase subunits and transcription factors ( c Myc , Mad 1 ) , telomerase activity and telomere length . ^^^ Of the telomerase subunits , telomerase reverse transcriptase ( hTERT ) and c Myc were the first to show a reduction in activity after AZT treatment , followed by changes in hTER , Mad 1 and hTEP 1 . ^^^ CONCLUSION : Cyclic treatment with AZT initially suppressed hTERT and c Myc , followed by suppression of hTER , Mad 1 and hTEP 1 . ^^^
Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: Q05195 and P01106	Pubmed	SVM Score :0.0
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