275 related articles for article (PubMed ID: 18515355)
1. The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.
Pratt WB; Morishima Y; Osawa Y
J Biol Chem; 2008 Aug; 283(34):22885-9. PubMed ID: 18515355
[No Abstract] [Full Text] [Related]
2. Heat-shock protein 90, a chaperone for folding and regulation.
Picard D
Cell Mol Life Sci; 2002 Oct; 59(10):1640-8. PubMed ID: 12475174
[TBL] [Abstract][Full Text] [Related]
3. Stimulation of the weak ATPase activity of human hsp90 by a client protein.
McLaughlin SH; Smith HW; Jackson SE
J Mol Biol; 2002 Jan; 315(4):787-98. PubMed ID: 11812147
[TBL] [Abstract][Full Text] [Related]
4. Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery.
Chen S; Smith DF
J Biol Chem; 1998 Dec; 273(52):35194-200. PubMed ID: 9857057
[TBL] [Abstract][Full Text] [Related]
5. Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage.
Pratt WB; Morishima Y; Peng HM; Osawa Y
Exp Biol Med (Maywood); 2010 Mar; 235(3):278-89. PubMed ID: 20404045
[TBL] [Abstract][Full Text] [Related]
6. The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones.
Li J; Soroka J; Buchner J
Biochim Biophys Acta; 2012 Mar; 1823(3):624-35. PubMed ID: 21951723
[TBL] [Abstract][Full Text] [Related]
7. The HSP90 chaperone machinery.
Schopf FH; Biebl MM; Buchner J
Nat Rev Mol Cell Biol; 2017 Jun; 18(6):345-360. PubMed ID: 28429788
[TBL] [Abstract][Full Text] [Related]
8. Both the N- and C-terminal chaperone sites of Hsp90 participate in protein refolding.
Minami M; Nakamura M; Emori Y; Minami Y
Eur J Biochem; 2001 Apr; 268(8):2520-4. PubMed ID: 11298772
[TBL] [Abstract][Full Text] [Related]
9. Hsp90: a chaperone for protein folding and gene regulation.
Zhao R; Houry WA
Biochem Cell Biol; 2005 Dec; 83(6):703-10. PubMed ID: 16333321
[TBL] [Abstract][Full Text] [Related]
10. The Hsp70-Hsp90 Chaperone Cascade in Protein Folding.
Morán Luengo T; Mayer MP; Rüdiger SGD
Trends Cell Biol; 2019 Feb; 29(2):164-177. PubMed ID: 30502916
[TBL] [Abstract][Full Text] [Related]
11. Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70.
Carrello A; Allan RK; Morgan SL; Owen BA; Mok D; Ward BK; Minchin RF; Toft DO; Ratajczak T
Cell Stress Chaperones; 2004; 9(2):167-81. PubMed ID: 15497503
[TBL] [Abstract][Full Text] [Related]
12. Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.
Brychzy A; Rein T; Winklhofer KF; Hartl FU; Young JC; Obermann WM
EMBO J; 2003 Jul; 22(14):3613-23. PubMed ID: 12853476
[TBL] [Abstract][Full Text] [Related]
13. An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function.
Weikl T; Abelmann K; Buchner J
J Mol Biol; 1999 Oct; 293(3):685-91. PubMed ID: 10543959
[TBL] [Abstract][Full Text] [Related]
14. Thr90 phosphorylation of Hsp90α by protein kinase A regulates its chaperone machinery.
Wang X; Lu XA; Song X; Zhuo W; Jia L; Jiang Y; Luo Y
Biochem J; 2012 Jan; 441(1):387-97. PubMed ID: 21919888
[TBL] [Abstract][Full Text] [Related]
15. A specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand.
Backe SJ; Sager RA; Regan BR; Sit J; Major LA; Bratslavsky G; Woodford MR; Bourboulia D; Mollapour M
Cell Rep; 2022 Jul; 40(2):111039. PubMed ID: 35830801
[TBL] [Abstract][Full Text] [Related]
16. Hsp90 interaction with clients.
Karagöz GE; Rüdiger SG
Trends Biochem Sci; 2015 Feb; 40(2):117-25. PubMed ID: 25579468
[TBL] [Abstract][Full Text] [Related]
17. Nox5 stability and superoxide production is regulated by C-terminal binding of Hsp90 and CO-chaperones.
Chen F; Haigh S; Yu Y; Benson T; Wang Y; Li X; Dou H; Bagi Z; Verin AD; Stepp DW; Csanyi G; Chadli A; Weintraub NL; Smith SM; Fulton DJ
Free Radic Biol Med; 2015 Dec; 89():793-805. PubMed ID: 26456056
[TBL] [Abstract][Full Text] [Related]
18. Cdc37 goes beyond Hsp90 and kinases.
MacLean M; Picard D
Cell Stress Chaperones; 2003; 8(2):114-9. PubMed ID: 14627196
[TBL] [Abstract][Full Text] [Related]
19. Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.
Cox MB; Johnson JL
Methods Mol Biol; 2018; 1709():397-422. PubMed ID: 29177674
[TBL] [Abstract][Full Text] [Related]
20. The switch from client holding to folding in the Hsp70/Hsp90 chaperone machineries is regulated by a direct interplay between co-chaperones.
Dahiya V; Rutz DA; Moessmer P; Mühlhofer M; Lawatscheck J; Rief M; Buchner J
Mol Cell; 2022 Apr; 82(8):1543-1556.e6. PubMed ID: 35176233
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]