| Interacting proteins: Q05195 and Q13547 |
Pubmed |
SVM Score :0.0 |
| RESULTS : We report the identification of a tetrameric complex composed of Max , Mad 1 , Sin3B and HD 1 . ^^^ The inhibition of cell growth by Mad 1 is enhanced by Sin3B and HD 1 , as measured by colony formation assays . ^^^ 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 . . ^^^ Mad / Max complexes may recruit mammalian Rpd 3 like enzymes , therefore , directing histone deacetylase activity to promoters and negatively regulating cell growth . ^^^ |
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| Interacting proteins: Q05195 and Q13547 |
Pubmed |
SVM Score :0.0 |
| Here we show that PLZF associates in vitro and in vivo with the Mad co repressor mSin3A and the histone deacetylase HDAC 1 . ^^^ |
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| Interacting proteins: Q05195 and Q13547 |
Pubmed |
SVM Score :0.0 |
| Mad : Max heterodimers repress transcription by recruiting a large multi protein complex containing the histone deacetylases , HDAC 1 and HDAC 2 , to DNA . ^^^ |
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| Interacting proteins: Q05195 and Q13547 |
Pubmed |
SVM Score :0.0 |
| Chromatin immunoprecipitation assay revealed that p 53 , histone deacetylase 1 , and co repressor mSin3a associated with the MAD 1 promoter in vivo . ^^^ |
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| Interacting proteins: Q05195 and Q13547 |
Pubmed |
SVM Score :0.0 |
| This was the result of cyclin E / CDK2 interfering with the interaction of Mad 1 with HDAC 1 and reducing HDAC activity . ^^^ |
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| Interacting proteins: Q05195 and Q13547 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q05195 and Q13547 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q05195 and Q13547 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q05195 and Q13547 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q05195 and Q13547 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q05195 and Q13547 |
Pubmed |
SVM Score :0.0 |
| NA |
|