These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
3. A 13-amino acid amphipathic alpha-helix is required for the functional interaction between the transcriptional repressor Mad1 and mSin3A. Eilers AL; Billin AN; Liu J; Ayer DE J Biol Chem; 1999 Nov; 274(46):32750-6. PubMed ID: 10551834 [TBL] [Abstract][Full Text] [Related]
4. Conserved themes in target recognition by the PAH1 and PAH2 domains of the Sin3 transcriptional corepressor. Sahu SC; Swanson KA; Kang RS; Huang K; Brubaker K; Ratcliff K; Radhakrishnan I J Mol Biol; 2008 Feb; 375(5):1444-56. PubMed ID: 18089292 [TBL] [Abstract][Full Text] [Related]
5. The neural repressor NRSF/REST binds the PAH1 domain of the Sin3 corepressor by using its distinct short hydrophobic helix. Nomura M; Uda-Tochio H; Murai K; Mori N; Nishimura Y J Mol Biol; 2005 Dec; 354(4):903-15. PubMed ID: 16288918 [TBL] [Abstract][Full Text] [Related]
6. Solution structure of the mSin3A PAH2-Pf1 SID1 complex: a Mad1/Mxd1-like interaction disrupted by MRG15 in the Rpd3S/Sin3S complex. Kumar GS; Xie T; Zhang Y; Radhakrishnan I J Mol Biol; 2011 May; 408(5):987-1000. PubMed ID: 21440557 [TBL] [Abstract][Full Text] [Related]
7. Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex. Yochum GS; Ayer DE Mol Cell Biol; 2001 Jul; 21(13):4110-8. PubMed ID: 11390640 [TBL] [Abstract][Full Text] [Related]
8. HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations. Swanson KA; Knoepfler PS; Huang K; Kang RS; Cowley SM; Laherty CD; Eisenman RN; Radhakrishnan I Nat Struct Mol Biol; 2004 Aug; 11(8):738-46. PubMed ID: 15235594 [TBL] [Abstract][Full Text] [Related]
9. A conserved alpha-helical motif mediates the interaction of Sp1-like transcriptional repressors with the corepressor mSin3A. Zhang JS; Moncrieffe MC; Kaczynski J; Ellenrieder V; Prendergast FG; Urrutia R Mol Cell Biol; 2001 Aug; 21(15):5041-9. PubMed ID: 11438660 [TBL] [Abstract][Full Text] [Related]
10. The Mad1-Sin3B interaction involves a novel helical fold. Spronk CA; Tessari M; Kaan AM; Jansen JF; Vermeulen M; Stunnenberg HG; Vuister GW Nat Struct Biol; 2000 Dec; 7(12):1100-4. PubMed ID: 11101889 [TBL] [Abstract][Full Text] [Related]
11. SIN3-dependent transcriptional repression by interaction with the Mad1 DNA-binding protein. Kasten MM; Ayer DE; Stillman DJ Mol Cell Biol; 1996 Aug; 16(8):4215-21. PubMed ID: 8754821 [TBL] [Abstract][Full Text] [Related]
12. Molecular characterization of Sin3 PAH-domain interactor specificity and identification of PAH partners. Le Guezennec X; Vermeulen M; Stunnenberg HG Nucleic Acids Res; 2006; 34(14):3929-37. PubMed ID: 16914451 [TBL] [Abstract][Full Text] [Related]
13. Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex. Brubaker K; Cowley SM; Huang K; Loo L; Yochum GS; Ayer DE; Eisenman RN; Radhakrishnan I Cell; 2000 Nov; 103(4):655-65. PubMed ID: 11106735 [TBL] [Abstract][Full Text] [Related]
14. Molecular determinants of the interaction of Mad with the PAH2 domain of mSin3. Le Guezennec X; Vriend G; Stunnenberg HG J Biol Chem; 2004 Jun; 279(24):25823-9. PubMed ID: 15047710 [TBL] [Abstract][Full Text] [Related]
15. The Sin3A/MAD1 Complex, through Its PAH2 Domain, Acts as a Second Repressor of Retinoic Acid Receptor Beta Expression in Breast Cancer Cells. Dahiya NR; Leibovitch BA; Kadamb R; Bansal N; Waxman S Cells; 2022 Mar; 11(7):. PubMed ID: 35406744 [TBL] [Abstract][Full Text] [Related]
16. Signaling disrupts mSin3A binding to the Mad1-like Sin3-interacting domain of TIEG2, an Sp1-like repressor. Ellenrieder V; Zhang JS; Kaczynski J; Urrutia R EMBO J; 2002 May; 21(10):2451-60. PubMed ID: 12006497 [TBL] [Abstract][Full Text] [Related]
17. Role of structural and dynamical plasticity in Sin3: the free PAH2 domain is a folded module in mSin3B. van Ingen H; Baltussen MA; Aelen J; Vuister GW J Mol Biol; 2006 Apr; 358(2):485-97. PubMed ID: 16519900 [TBL] [Abstract][Full Text] [Related]
18. Sin3A recruits Tet1 to the PAH1 domain via a highly conserved Sin3-Interaction Domain. Chandru A; Bate N; Vuister GW; Cowley SM Sci Rep; 2018 Oct; 8(1):14689. PubMed ID: 30279502 [TBL] [Abstract][Full Text] [Related]
19. Solution NMR studies of apo-mSin3A and -mSin3B reveal that the PAH1 and PAH2 domains are structurally independent. He Y; Radhakrishnan I Protein Sci; 2008 Jan; 17(1):171-5. PubMed ID: 18042683 [TBL] [Abstract][Full Text] [Related]
20. Identification and characterization of three new components of the mSin3A corepressor complex. Fleischer TC; Yun UJ; Ayer DE Mol Cell Biol; 2003 May; 23(10):3456-67. PubMed ID: 12724404 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]