194 related articles for article (PubMed ID: 29337688)
21. Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.
Biebl MM; Lopez A; Rehn A; Freiburger L; Lawatscheck J; Blank B; Sattler M; Buchner J
Nat Commun; 2021 Feb; 12(1):828. PubMed ID: 33547294
[TBL] [Abstract][Full Text] [Related]
22. Gambogic acid identifies an isoform-specific druggable pocket in the middle domain of Hsp90β.
Yim KH; Prince TL; Qu S; Bai F; Jennings PA; Onuchic JN; Theodorakis EA; Neckers L
Proc Natl Acad Sci U S A; 2016 Aug; 113(33):E4801-9. PubMed ID: 27466407
[TBL] [Abstract][Full Text] [Related]
23. 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]
24. Structures of Hsp90α and Hsp90β bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity.
Huck JD; Que NLS; Sharma S; Taldone T; Chiosis G; Gewirth DT
Proteins; 2019 Oct; 87(10):869-877. PubMed ID: 31141217
[TBL] [Abstract][Full Text] [Related]
25. p23 and Aha1.
Rehn AB; Buchner J
Subcell Biochem; 2015; 78():113-31. PubMed ID: 25487019
[TBL] [Abstract][Full Text] [Related]
26. Oligomeric forms of the 90-kDa heat shock protein.
Nemoto T; Sato N
Biochem J; 1998 Mar; 330 ( Pt 2)(Pt 2):989-95. PubMed ID: 9480920
[TBL] [Abstract][Full Text] [Related]
27. 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]
28. Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome.
Silva NSM; Seraphim TV; Minari K; Barbosa LRS; Borges JC
Int J Biol Macromol; 2018 Mar; 108():193-204. PubMed ID: 29191421
[TBL] [Abstract][Full Text] [Related]
29. Differential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.
Blacklock K; Verkhivker GM
PLoS One; 2013; 8(8):e71936. PubMed ID: 23977182
[TBL] [Abstract][Full Text] [Related]
30. Blind cavefish and heat shock protein chaperones: a novel role for hsp90alpha in lens apoptosis.
Hooven TA; Yamamoto Y; Jeffery WR
Int J Dev Biol; 2004; 48(8-9):731-8. PubMed ID: 15558465
[TBL] [Abstract][Full Text] [Related]
31. 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]
32. Molecular basis of the interaction of Hsp90 with its co-chaperone Hop.
Lott A; Oroz J; Zweckstetter M
Protein Sci; 2020 Dec; 29(12):2422-2432. PubMed ID: 33040396
[TBL] [Abstract][Full Text] [Related]
33. Mutations in the Hsp90 N Domain Identify a Site that Controls Dimer Opening and Expand Human Hsp90α Function in Yeast.
Reidy M; Masison DC
J Mol Biol; 2020 Jul; 432(16):4673-4689. PubMed ID: 32565117
[TBL] [Abstract][Full Text] [Related]
34. Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism.
Noddings CM; Wang RY; Johnson JL; Agard DA
Nature; 2022 Jan; 601(7893):465-469. PubMed ID: 34937936
[TBL] [Abstract][Full Text] [Related]
35. Cytosolic Hsp90 Isoform-Specific Functions and Clinical Significance.
Maiti S; Picard D
Biomolecules; 2022 Aug; 12(9):. PubMed ID: 36139005
[TBL] [Abstract][Full Text] [Related]
36. 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]
37. Protein-selective capture to analyze electrophile adduction of hsp90 by 4-hydroxynonenal.
Connor RE; Marnett LJ; Liebler DC
Chem Res Toxicol; 2011 Aug; 24(8):1275-82. PubMed ID: 21749116
[TBL] [Abstract][Full Text] [Related]
38. Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.
Dittmar KD; Demady DR; Stancato LF; Krishna P; Pratt WB
J Biol Chem; 1997 Aug; 272(34):21213-20. PubMed ID: 9261129
[TBL] [Abstract][Full Text] [Related]
39. Domain-mediated dimerization of the Hsp90 cochaperones Harc and Cdc37.
Roiniotis J; Masendycz P; Ho S; Scholz GM
Biochemistry; 2005 May; 44(17):6662-9. PubMed ID: 15850399
[TBL] [Abstract][Full Text] [Related]
40. Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions.
Yun BG; Huang W; Leach N; Hartson SD; Matts RL
Biochemistry; 2004 Jun; 43(25):8217-29. PubMed ID: 15209518
[TBL] [Abstract][Full Text] [Related]
[Previous] [Next] [New Search]