233 related articles for article (PubMed ID: 31189925)
1. Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1.
Xu W; Beebe K; Chavez JD; Boysen M; Lu Y; Zuehlke AD; Keramisanou D; Trepel JB; Prodromou C; Mayer MP; Bruce JE; Gelis I; Neckers L
Nat Commun; 2019 Jun; 10(1):2574. PubMed ID: 31189925
[TBL] [Abstract][Full Text] [Related]
2. Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine.
Xu W; Mollapour M; Prodromou C; Wang S; Scroggins BT; Palchick Z; Beebe K; Siderius M; Lee MJ; Couvillon A; Trepel JB; Miyata Y; Matts R; Neckers L
Mol Cell; 2012 Aug; 47(3):434-43. PubMed ID: 22727666
[TBL] [Abstract][Full Text] [Related]
3. Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle.
Siligardi G; Hu B; Panaretou B; Piper PW; Pearl LH; Prodromou C
J Biol Chem; 2004 Dec; 279(50):51989-98. PubMed ID: 15466438
[TBL] [Abstract][Full Text] [Related]
4. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.
Meyer P; Prodromou C; Liao C; Hu B; Roe SM; Vaughan CK; Vlasic I; Panaretou B; Piper PW; Pearl LH
EMBO J; 2004 Mar; 23(6):1402-10. PubMed ID: 15039704
[TBL] [Abstract][Full Text] [Related]
5. An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans.
Zuehlke AD; Reidy M; Lin C; LaPointe P; Alsomairy S; Lee DJ; Rivera-Marquez GM; Beebe K; Prince T; Lee S; Trepel JB; Xu W; Johnson J; Masison D; Neckers L
Nat Commun; 2017 May; 8():15328. PubMed ID: 28537252
[TBL] [Abstract][Full Text] [Related]
6. Asymmetric activation of the hsp90 dimer by its cochaperone aha1.
Retzlaff M; Hagn F; Mitschke L; Hessling M; Gugel F; Kessler H; Richter K; Buchner J
Mol Cell; 2010 Feb; 37(3):344-54. PubMed ID: 20159554
[TBL] [Abstract][Full Text] [Related]
7. A primate specific extra domain in the molecular chaperone Hsp90.
Tripathi V; Obermann WM
PLoS One; 2013; 8(8):e71856. PubMed ID: 23951259
[TBL] [Abstract][Full Text] [Related]
8. A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.
Stiegler SC; Rübbelke M; Korotkov VS; Weiwad M; John C; Fischer G; Sieber SA; Sattler M; Buchner J
J Biol Chem; 2017 Oct; 292(41):17073-17083. PubMed ID: 28851842
[TBL] [Abstract][Full Text] [Related]
9. p23 and Aha1: Distinct Functions Promote Client Maturation.
Biebl MM; Buchner J
Subcell Biochem; 2023; 101():159-187. PubMed ID: 36520307
[TBL] [Abstract][Full Text] [Related]
10. Aha1 regulates Hsp90's conformation and function in a stoichiometry-dependent way.
Mondol T; Silbermann LM; Schimpf J; Vollmar L; Hermann B; Tych KK; Hugel T
Biophys J; 2023 Sep; 122(17):3458-3468. PubMed ID: 37515325
[TBL] [Abstract][Full Text] [Related]
11. A novel C-terminal homologue of Aha1 co-chaperone binds to heat shock protein 90 and stimulates its ATPase activity in Entamoeba histolytica.
Singh M; Shah V; Tatu U
J Mol Biol; 2014 Apr; 426(8):1786-98. PubMed ID: 24486610
[TBL] [Abstract][Full Text] [Related]
12. Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.
Ran F; Gadura N; Michels CA
J Biol Chem; 2010 Apr; 285(18):13850-62. PubMed ID: 20177068
[TBL] [Abstract][Full Text] [Related]
13. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.
Panaretou B; Siligardi G; Meyer P; Maloney A; Sullivan JK; Singh S; Millson SH; Clarke PA; Naaby-Hansen S; Stein R; Cramer R; Mollapour M; Workman P; Piper PW; Pearl LH; Prodromou C
Mol Cell; 2002 Dec; 10(6):1307-18. PubMed ID: 12504007
[TBL] [Abstract][Full Text] [Related]
14. Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis.
Koulov AV; LaPointe P; Lu B; Razvi A; Coppinger J; Dong MQ; Matteson J; Laister R; Arrowsmith C; Yates JR; Balch WE
Mol Biol Cell; 2010 Mar; 21(6):871-84. PubMed ID: 20089831
[TBL] [Abstract][Full Text] [Related]
15. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.
Meyer P; Prodromou C; Liao C; Hu B; Mark Roe S; Vaughan CK; Vlasic I; Panaretou B; Piper PW; Pearl LH
EMBO J; 2004 Feb; 23(3):511-9. PubMed ID: 14739935
[TBL] [Abstract][Full Text] [Related]
16. c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells.
Dunn DM; Woodford MR; Truman AW; Jensen SM; Schulman J; Caza T; Remillard TC; Loiselle D; Wolfgeher D; Blagg BS; Franco L; Haystead TA; Daturpalli S; Mayer MP; Trepel JB; Morgan RM; Prodromou C; Kron SJ; Panaretou B; Stetler-Stevenson WG; Landas SK; Neckers L; Bratslavsky G; Bourboulia D; Mollapour M
Cell Rep; 2015 Aug; 12(6):1006-18. PubMed ID: 26235616
[TBL] [Abstract][Full Text] [Related]
17. Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone.
Lotz GP; Lin H; Harst A; Obermann WM
J Biol Chem; 2003 May; 278(19):17228-35. PubMed ID: 12604615
[TBL] [Abstract][Full Text] [Related]
18. Dynamic Aha1 co-chaperone binding to human Hsp90.
Oroz J; Blair LJ; Zweckstetter M
Protein Sci; 2019 Sep; 28(9):1545-1551. PubMed ID: 31299134
[TBL] [Abstract][Full Text] [Related]
19. Aha-type co-chaperones: the alpha or the omega of the Hsp90 ATPase cycle?
LaPointe P; Mercier R; Wolmarans A
Biol Chem; 2020 Mar; 401(4):423-434. PubMed ID: 31782942
[TBL] [Abstract][Full Text] [Related]
20. Structure and mechanism of the Hsp90 molecular chaperone machinery.
Pearl LH; Prodromou C
Annu Rev Biochem; 2006; 75():271-94. PubMed ID: 16756493
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
