447 related articles for article (PubMed ID: 20404045)
1. 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]
2. Dynamic cycling with Hsp90 stabilizes neuronal nitric oxide synthase through calmodulin-dependent inhibition of ubiquitination.
Peng HM; Morishima Y; Clapp KM; Lau M; Pratt WB; Osawa Y
Biochemistry; 2009 Sep; 48(35):8483-90. PubMed ID: 19642705
[TBL] [Abstract][Full Text] [Related]
3. Modulation of heme/substrate binding cleft of neuronal nitric-oxide synthase (nNOS) regulates binding of Hsp90 and Hsp70 proteins and nNOS ubiquitination.
Peng HM; Morishima Y; Pratt WB; Osawa Y
J Biol Chem; 2012 Jan; 287(2):1556-65. PubMed ID: 22128174
[TBL] [Abstract][Full Text] [Related]
4. Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradation.
Wang AM; Morishima Y; Clapp KM; Peng HM; Pratt WB; Gestwicki JE; Osawa Y; Lieberman AP
J Biol Chem; 2010 May; 285(21):15714-23. PubMed ID: 20348093
[TBL] [Abstract][Full Text] [Related]
5. CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates.
Stankiewicz M; Nikolay R; Rybin V; Mayer MP
FEBS J; 2010 Aug; 277(16):3353-67. PubMed ID: 20618441
[TBL] [Abstract][Full Text] [Related]
6. CHIP: A Co-chaperone for Degradation by the Proteasome and Lysosome.
Chakraborty A; Edkins AL
Subcell Biochem; 2023; 101():351-387. PubMed ID: 36520313
[TBL] [Abstract][Full Text] [Related]
7. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery.
Pratt WB; Toft DO
Exp Biol Med (Maywood); 2003 Feb; 228(2):111-33. PubMed ID: 12563018
[TBL] [Abstract][Full Text] [Related]
8. C331A mutant of neuronal nitric-oxide synthase is labilized for Hsp70/CHIP (C terminus of HSC70-interacting protein)-dependent ubiquitination.
Clapp KM; Peng HM; Morishima Y; Lau M; Walker VJ; Pratt WB; Osawa Y
J Biol Chem; 2010 Oct; 285(44):33642-51. PubMed ID: 20729196
[TBL] [Abstract][Full Text] [Related]
9. Ca2+/S100 proteins act as upstream regulators of the chaperone-associated ubiquitin ligase CHIP (C terminus of Hsc70-interacting protein).
Shimamoto S; Kubota Y; Yamaguchi F; Tokumitsu H; Kobayashi R
J Biol Chem; 2013 Mar; 288(10):7158-68. PubMed ID: 23344957
[TBL] [Abstract][Full Text] [Related]
10. Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP in complex with chaperones and E2 enzymes.
Graf C; Stankiewicz M; Nikolay R; Mayer MP
Biochemistry; 2010 Mar; 49(10):2121-9. PubMed ID: 20146531
[TBL] [Abstract][Full Text] [Related]
11. Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP.
Kundrat L; Regan L
J Mol Biol; 2010 Jan; 395(3):587-94. PubMed ID: 19913553
[TBL] [Abstract][Full Text] [Related]
12. Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase.
Peng HM; Morishima Y; Jenkins GJ; Dunbar AY; Lau M; Patterson C; Pratt WB; Osawa Y
J Biol Chem; 2004 Dec; 279(51):52970-7. PubMed ID: 15466472
[TBL] [Abstract][Full Text] [Related]
13. Chaperoning of glucocorticoid receptors.
Pratt WB; Morishima Y; Murphy M; Harrell M
Handb Exp Pharmacol; 2006; (172):111-38. PubMed ID: 16610357
[TBL] [Abstract][Full Text] [Related]
14. Functional inactivation of endogenous MDM2 and CHIP by HSP90 causes aberrant stabilization of mutant p53 in human cancer cells.
Li D; Marchenko ND; Schulz R; Fischer V; Velasco-Hernandez T; Talos F; Moll UM
Mol Cancer Res; 2011 May; 9(5):577-88. PubMed ID: 21478269
[TBL] [Abstract][Full Text] [Related]
15. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins.
Connell P; Ballinger CA; Jiang J; Wu Y; Thompson LJ; Höhfeld J; Patterson C
Nat Cell Biol; 2001 Jan; 3(1):93-6. PubMed ID: 11146632
[TBL] [Abstract][Full Text] [Related]
16. CHIP: a co-chaperone for degradation by the proteasome.
Edkins AL
Subcell Biochem; 2015; 78():219-42. PubMed ID: 25487024
[TBL] [Abstract][Full Text] [Related]
17. 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]
18. Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases.
Pratt WB; Gestwicki JE; Osawa Y; Lieberman AP
Annu Rev Pharmacol Toxicol; 2015; 55():353-71. PubMed ID: 25292434
[TBL] [Abstract][Full Text] [Related]
19. Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP.
Kundrat L; Regan L
Biochemistry; 2010 Sep; 49(35):7428-38. PubMed ID: 20704274
[TBL] [Abstract][Full Text] [Related]
20. Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubiquitin ligase CHIP.
Jiang J; Cyr D; Babbitt RW; Sessa WC; Patterson C
J Biol Chem; 2003 Dec; 278(49):49332-41. PubMed ID: 14507928
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]