Molecular Determinants of the Interaction of Mad with the PAH2 Domain of mSin3

This publication has 40 references indexed in Scilit:

• In Vitro Targeting Reveals Intrinsic Histone Tail Specificity of the Sin3/Histone Deacetylase and N-CoR/SMRT Corepressor Complexes
  Molecular and Cellular Biology, 2004
• Identification and Characterization of Three New Components of the mSin3A Corepressor Complex
  Molecular and Cellular Biology, 2003
• X-Ray Structures of Myc-Max and Mad-Max Recognizing DNA
  Cell, 2003
• Identification of Mammalian Sds3 as an Integral Component of the Sin3/Histone Deacetylase Corepressor Complex
  Molecular and Cellular Biology, 2002
• A Conserved α-Helical Motif Mediates the Interaction of Sp1-Like Transcriptional Repressors with the Corepressor mSin3A
  Molecular and Cellular Biology, 2001
• Pf1, a Novel PHD Zinc Finger Protein That Links the TLE Corepressor to the mSin3A-Histone Deacetylase Complex
  Molecular and Cellular Biology, 2001
• RBP1 Recruits the mSIN3-Histone Deacetylase Complex to the Pocket of Retinoblastoma Tumor Suppressor Family Proteins Found in Limited Discrete Regions of the Nucleus at Growth Arrest
  Molecular and Cellular Biology, 2001
• Solution Structure of the Interacting Domains of the Mad–Sin3 Complex: Implications for Recruitment of a Chromatin-Modifying Complex
  Cell, 2000
• A 13-Amino Acid Amphipathic α-Helix Is Required for the Functional Interaction between the Transcriptional Repressor Mad1 and mSin3A
  Journal of Biological Chemistry, 1999
• Mad: A heterodimeric partner for Max that antagonizes Myc transcriptional activity
  Cell, 1993