Coupled Unfolding and Dimerization by the PAH2 Domain of the Mammalian Sin3A Corepressor
- 1 June 2006
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 360 (1) , 7-14
- https://doi.org/10.1016/j.jmb.2006.04.069
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Role of Structural and Dynamical Plasticity in Sin3: The Free PAH2 Domain is a Folded Module in mSin3BJournal of Molecular Biology, 2006
- mSin3A corepressor regulates diverse transcriptional networks governing normal and neoplastic growth and survivalGenes & Development, 2005
- HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientationsNature Structural & Molecular Biology, 2004
- Extension of the Binding Motif of the Sin3 Interacting Domain of the Mad Family Proteins,Biochemistry, 2003
- A Conserved α-Helical Motif Mediates the Interaction of Sp1-Like Transcriptional Repressors with the Corepressor mSin3AMolecular and Cellular Biology, 2001
- Pf1, a Novel PHD Zinc Finger Protein That Links the TLE Corepressor to the mSin3A-Histone Deacetylase ComplexMolecular and Cellular Biology, 2001
- Identification of the Sin3-Binding Site in Ume6 Defines a Two-Step Process for Conversion of Ume6 from a Transcriptional Repressor to an Activator in YeastMolecular and Cellular Biology, 2001
- Solution Structure of the Interacting Domains of the Mad–Sin3 Complex: Implications for Recruitment of a Chromatin-Modifying ComplexCell, 2000
- A 13-Amino Acid Amphipathic α-Helix Is Required for the Functional Interaction between the Transcriptional Repressor Mad1 and mSin3AJournal of Biological Chemistry, 1999
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995