213 related articles for article (PubMed ID: 15024060)
1. Functional analysis of the Mad1-mSin3A repressor-corepressor interaction reveals determinants of specificity, affinity, and transcriptional response.
Cowley SM; Kang RS; Frangioni JV; Yada JJ; DeGrand AM; Radhakrishnan I; Eisenman RN
Mol Cell Biol; 2004 Apr; 24(7):2698-709. PubMed ID: 15024060
[TBL] [Abstract][Full Text] [Related]
2. Mad proteins contain a dominant transcription repression domain.
Ayer DE; Laherty CD; Lawrence QA; Armstrong AP; Eisenman RN
Mol Cell Biol; 1996 Oct; 16(10):5772-81. PubMed ID: 8816491
[TBL] [Abstract][Full Text] [Related]
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]
