170 related articles for article (PubMed ID: 37352720)
1. Discovery of a highly potent NPAS3 heterodimer inhibitor by covalently modifying ARNT.
Li P; Tian Y; Shang Q; Tang C; Hou Z; Li Y; Cao L; Xue S; Bian J; Luo C; Wu D; Li Z; Ding H
Bioorg Chem; 2023 Oct; 139():106676. PubMed ID: 37352720
[TBL] [Abstract][Full Text] [Related]
2. NPAS1-ARNT and NPAS3-ARNT crystal structures implicate the bHLH-PAS family as multi-ligand binding transcription factors.
Wu D; Su X; Potluri N; Kim Y; Rastinejad F
Elife; 2016 Oct; 5():. PubMed ID: 27782878
[TBL] [Abstract][Full Text] [Related]
3. Identification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR.
Hao N; Whitelaw ML; Shearwin KE; Dodd IB; Chapman-Smith A
Nucleic Acids Res; 2011 May; 39(9):3695-709. PubMed ID: 21245039
[TBL] [Abstract][Full Text] [Related]
4. Structures of NPAS4-ARNT and NPAS4-ARNT2 heterodimers reveal new dimerization modalities in the bHLH-PAS transcription factor family.
Sun X; Jing L; Li F; Zhang M; Diao X; Zhuang J; Rastinejad F; Wu D
Proc Natl Acad Sci U S A; 2022 Nov; 119(46):e2208804119. PubMed ID: 36343253
[TBL] [Abstract][Full Text] [Related]
5. The crystal structure of the AhRR-ARNT heterodimer reveals the structural basis of the repression of AhR-mediated transcription.
Sakurai S; Shimizu T; Ohto U
J Biol Chem; 2017 Oct; 292(43):17609-17616. PubMed ID: 28904176
[TBL] [Abstract][Full Text] [Related]
6. Coactivators necessary for transcriptional output of the hypoxia inducible factor, HIF, are directly recruited by ARNT PAS-B.
Partch CL; Gardner KH
Proc Natl Acad Sci U S A; 2011 May; 108(19):7739-44. PubMed ID: 21512126
[TBL] [Abstract][Full Text] [Related]
7. Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT).
Reisz-Porszasz S; Probst MR; Fukunaga BN; Hankinson O
Mol Cell Biol; 1994 Sep; 14(9):6075-86. PubMed ID: 8065341
[TBL] [Abstract][Full Text] [Related]
8. Molecular basis of coiled coil coactivator recruitment by the aryl hydrocarbon receptor nuclear translocator (ARNT).
Partch CL; Card PB; Amezcua CA; Gardner KH
J Biol Chem; 2009 May; 284(22):15184-92. PubMed ID: 19324882
[TBL] [Abstract][Full Text] [Related]
9. Novel DNA binding by a basic helix-loop-helix protein. The role of the dioxin receptor PAS domain.
Chapman-Smith A; Whitelaw ML
J Biol Chem; 2006 May; 281(18):12535-45. PubMed ID: 16520375
[TBL] [Abstract][Full Text] [Related]
10. Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex.
Lindebro MC; Poellinger L; Whitelaw ML
EMBO J; 1995 Jul; 14(14):3528-39. PubMed ID: 7628454
[TBL] [Abstract][Full Text] [Related]
11. cDNA cloning and tissue-specific expression of a novel basic helix-loop-helix/PAS factor (Arnt2) with close sequence similarity to the aryl hydrocarbon receptor nuclear translocator (Arnt).
Hirose K; Morita M; Ema M; Mimura J; Hamada H; Fujii H; Saijo Y; Gotoh O; Sogawa K; Fujii-Kuriyama Y
Mol Cell Biol; 1996 Apr; 16(4):1706-13. PubMed ID: 8657146
[TBL] [Abstract][Full Text] [Related]
12. Isolation and expression of cDNAs from rainbow trout (Oncorhynchus mykiss) that encode two novel basic helix-loop-Helix/PER-ARNT-SIM (bHLH/PAS) proteins with distinct functions in the presence of the aryl hydrocarbon receptor. Evidence for alternative mRNA splicing and dominant negative activity in the bHLH/PAS family.
Pollenz RS; Sullivan HR; Holmes J; Necela B; Peterson RE
J Biol Chem; 1996 Nov; 271(48):30886-96. PubMed ID: 8940073
[TBL] [Abstract][Full Text] [Related]
13. Binding studies using Pichia pastoris expressed human aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator proteins.
Zheng Y; Xie J; Huang X; Dong J; Park MS; Chan WK
Protein Expr Purif; 2016 Jun; 122():72-81. PubMed ID: 26923060
[TBL] [Abstract][Full Text] [Related]
14. The evolution and structure/function of bHLH-PAS transcription factor family.
Edwards HE; Gorelick DA
Biochem Soc Trans; 2022 Jun; 50(3):1227-1243. PubMed ID: 35695677
[TBL] [Abstract][Full Text] [Related]
15. Structural insight into the ligand binding mechanism of aryl hydrocarbon receptor.
Dai S; Qu L; Li J; Zhang Y; Jiang L; Wei H; Guo M; Chen X; Chen Y
Nat Commun; 2022 Oct; 13(1):6234. PubMed ID: 36266304
[TBL] [Abstract][Full Text] [Related]
16. Deciphering Dimerization Modes of PAS Domains: Computational and Experimental Analyses of the AhR:ARNT Complex Reveal New Insights Into the Mechanisms of AhR Transformation.
Corrada D; Soshilov AA; Denison MS; Bonati L
PLoS Comput Biol; 2016 Jun; 12(6):e1004981. PubMed ID: 27295348
[TBL] [Abstract][Full Text] [Related]
17. Structural basis of ARNT PAS-B dimerization: use of a common beta-sheet interface for hetero- and homodimerization.
Card PB; Erbel PJ; Gardner KH
J Mol Biol; 2005 Oct; 353(3):664-77. PubMed ID: 16181639
[TBL] [Abstract][Full Text] [Related]
18. Role of the PAS domain in regulation of dimerization and DNA binding specificity of the dioxin receptor.
Pongratz I; Antonsson C; Whitelaw ML; Poellinger L
Mol Cell Biol; 1998 Jul; 18(7):4079-88. PubMed ID: 9632792
[TBL] [Abstract][Full Text] [Related]
19. The basic helix-loop-helix-PAS protein ARNT functions as a potent coactivator of estrogen receptor-dependent transcription.
Brunnberg S; Pettersson K; Rydin E; Matthews J; Hanberg A; Pongratz I
Proc Natl Acad Sci U S A; 2003 May; 100(11):6517-22. PubMed ID: 12754377
[TBL] [Abstract][Full Text] [Related]
20. The basic helix-loop-helix domain of the aryl hydrocarbon receptor nuclear transporter (ARNT) can oligomerize and bind E-box DNA specifically.
Huffman JL; Mokashi A; Bächinger HP; Brennan RG
J Biol Chem; 2001 Nov; 276(44):40537-44. PubMed ID: 11502749
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]