126 related articles for article (PubMed ID: 15173105)
1. Evolutionary epitopes of Hsp90 and p23: implications for their interaction.
Zhu S; Tytgat J
FASEB J; 2004 Jun; 18(9):940-7. PubMed ID: 15173105
[TBL] [Abstract][Full Text] [Related]
2. Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90.
Chadli A; Bouhouche I; Sullivan W; Stensgard B; McMahon N; Catelli MG; Toft DO
Proc Natl Acad Sci U S A; 2000 Nov; 97(23):12524-9. PubMed ID: 11050175
[TBL] [Abstract][Full Text] [Related]
3. The influence of ATP and p23 on the conformation of hsp90.
Sullivan WP; Owen BA; Toft DO
J Biol Chem; 2002 Nov; 277(48):45942-8. PubMed ID: 12324468
[TBL] [Abstract][Full Text] [Related]
4. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.
Young JC; Hartl FU
EMBO J; 2000 Nov; 19(21):5930-40. PubMed ID: 11060043
[TBL] [Abstract][Full Text] [Related]
5. Interaction of the middle domains stabilizes Hsp90α dimer in a closed conformation with high affinity for p23.
Synoradzki K; Miszta P; Kazlauskas E; Mickevičiūtė A; Michailovienė V; Matulis D; Filipek S; Bieganowski P
Biol Chem; 2018 Mar; 399(4):337-345. PubMed ID: 29337688
[TBL] [Abstract][Full Text] [Related]
6. Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone.
Weaver AJ; Sullivan WP; Felts SJ; Owen BA; Toft DO
J Biol Chem; 2000 Jul; 275(30):23045-52. PubMed ID: 10811660
[TBL] [Abstract][Full Text] [Related]
7. N-terminal domain of human Hsp90 triggers binding to the cochaperone p23.
Karagöz GE; Duarte AM; Ippel H; Uetrecht C; Sinnige T; van Rosmalen M; Hausmann J; Heck AJ; Boelens R; Rüdiger SG
Proc Natl Acad Sci U S A; 2011 Jan; 108(2):580-5. PubMed ID: 21183720
[TBL] [Abstract][Full Text] [Related]
8. A motif in HSP90 and P23 that links molecular chaperones to efficient estrogen receptor α methylation by the lysine methyltransferase SMYD2.
Obermann WMJ
J Biol Chem; 2018 Oct; 293(42):16479-16487. PubMed ID: 30190324
[TBL] [Abstract][Full Text] [Related]
9. 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]
10. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex.
Ali MM; Roe SM; Vaughan CK; Meyer P; Panaretou B; Piper PW; Prodromou C; Pearl LH
Nature; 2006 Apr; 440(7087):1013-7. PubMed ID: 16625188
[TBL] [Abstract][Full Text] [Related]
11. Localization of sites of interaction between p23 and Hsp90 in solution.
Martinez-Yamout MA; Venkitakrishnan RP; Preece NE; Kroon G; Wright PE; Dyson HJ
J Biol Chem; 2006 May; 281(20):14457-64. PubMed ID: 16565516
[TBL] [Abstract][Full Text] [Related]
12. Evidence for iterative ratcheting of receptor-bound hsp70 between its ATP and ADP conformations during assembly of glucocorticoid receptor.hsp90 heterocomplexes.
Morishima Y; Kanelakis KC; Murphy PJ; Shewach DS; Pratt WB
Biochemistry; 2001 Jan; 40(4):1109-16. PubMed ID: 11170435
[TBL] [Abstract][Full Text] [Related]
13. 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]
14. Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling.
Oxelmark E; Knoblauch R; Arnal S; Su LF; Schapira M; Garabedian MJ
J Biol Chem; 2003 Sep; 278(38):36547-55. PubMed ID: 12835317
[TBL] [Abstract][Full Text] [Related]
15. The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains.
Prodromou C; Panaretou B; Chohan S; Siligardi G; O'Brien R; Ladbury JE; Roe SM; Piper PW; Pearl LH
EMBO J; 2000 Aug; 19(16):4383-92. PubMed ID: 10944121
[TBL] [Abstract][Full Text] [Related]
16. N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
Richter K; Reinstein J; Buchner J
J Biol Chem; 2002 Nov; 277(47):44905-10. PubMed ID: 12235160
[TBL] [Abstract][Full Text] [Related]
17. The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins.
McLaughlin SH; Sobott F; Yao ZP; Zhang W; Nielsen PR; Grossmann JG; Laue ED; Robinson CV; Jackson SE
J Mol Biol; 2006 Feb; 356(3):746-58. PubMed ID: 16403413
[TBL] [Abstract][Full Text] [Related]
18. The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes.
Johnson J; Corbisier R; Stensgard B; Toft D
J Steroid Biochem Mol Biol; 1996 Jan; 56(1-6 Spec No):31-7. PubMed ID: 8603045
[TBL] [Abstract][Full Text] [Related]
19. The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle.
Richter K; Walter S; Buchner J
J Mol Biol; 2004 Oct; 342(5):1403-13. PubMed ID: 15364569
[TBL] [Abstract][Full Text] [Related]
20. The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state.
Lee K; Thwin AC; Nadel CM; Tse E; Gates SN; Gestwicki JE; Southworth DR
Mol Cell; 2021 Sep; 81(17):3496-3508.e5. PubMed ID: 34380015
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
