These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
4. Dual Roles for Yeast Sti1/Hop in Regulating the Hsp90 Chaperone Cycle. Reidy M; Kumar S; Anderson DE; Masison DC Genetics; 2018 Aug; 209(4):1139-1154. PubMed ID: 29930177 [TBL] [Abstract][Full Text] [Related]
5. 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]
6. 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]
7. Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules. Röhl A; Wengler D; Madl T; Lagleder S; Tippel F; Herrmann M; Hendrix J; Richter K; Hack G; Schmid AB; Kessler H; Lamb DC; Buchner J Nat Commun; 2015 Apr; 6():6655. PubMed ID: 25851214 [TBL] [Abstract][Full Text] [Related]
9. Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1. Johnson JL; Halas A; Flom G Mol Cell Biol; 2007 Jan; 27(2):768-76. PubMed ID: 17101799 [TBL] [Abstract][Full Text] [Related]
10. Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. Richter K; Muschler P; Hainzl O; Reinstein J; Buchner J J Biol Chem; 2003 Mar; 278(12):10328-33. PubMed ID: 12525481 [TBL] [Abstract][Full Text] [Related]
11. Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. Siligardi G; Panaretou B; Meyer P; Singh S; Woolfson DN; Piper PW; Pearl LH; Prodromou C J Biol Chem; 2002 Jun; 277(23):20151-9. PubMed ID: 11916974 [TBL] [Abstract][Full Text] [Related]
12. Ydj1 interaction at nucleotide-binding-domain of yeast Ssa1 impacts Hsp90 collaboration and client maturation. Gaur D; Kumar N; Ghosh A; Singh P; Kumar P; Guleria J; Kaur S; Malik N; Saha S; Nystrom T; Sharma D PLoS Genet; 2022 Nov; 18(11):e1010442. PubMed ID: 36350833 [TBL] [Abstract][Full Text] [Related]
13. Cns1 is an activator of the Ssa1 ATPase activity. Hainzl O; Wegele H; Richter K; Buchner J J Biol Chem; 2004 May; 279(22):23267-73. PubMed ID: 15044454 [TBL] [Abstract][Full Text] [Related]
14. Functional and physical interaction between yeast Hsp90 and Hsp70. Kravats AN; Hoskins JR; Reidy M; Johnson JL; Doyle SM; Genest O; Masison DC; Wickner S Proc Natl Acad Sci U S A; 2018 Mar; 115(10):E2210-E2219. PubMed ID: 29463764 [TBL] [Abstract][Full Text] [Related]
16. Large Rotation of the N-terminal Domain of Hsp90 Is Important for Interaction with Some but Not All Client Proteins. Daturpalli S; Knieß RA; Lee CT; Mayer MP J Mol Biol; 2017 May; 429(9):1406-1423. PubMed ID: 28363677 [TBL] [Abstract][Full Text] [Related]
17. Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects. Hohrman K; Gonçalves D; Morano KA; Johnson JL Genetics; 2021 Mar; 217(3):. PubMed ID: 33789348 [TBL] [Abstract][Full Text] [Related]
18. Hsp90/Hsp70 chaperone machine regulation of the Saccharomyces MAL-activator as determined in vivo using noninducible and constitutive mutant alleles. Ran F; Bali M; Michels CA Genetics; 2008 May; 179(1):331-43. PubMed ID: 18458105 [TBL] [Abstract][Full Text] [Related]
19. Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites. Eckl JM; Rutz DA; Haslbeck V; Zierer BK; Reinstein J; Richter K J Biol Chem; 2013 May; 288(22):16032-42. PubMed ID: 23569206 [TBL] [Abstract][Full Text] [Related]
20. Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Li J; Richter K; Reinstein J; Buchner J Nat Struct Mol Biol; 2013 Mar; 20(3):326-31. PubMed ID: 23396352 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]