705 related articles for article (PubMed ID: 25487024)
1. 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]
2. 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]
3. 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]
4. Chaperone-dependent E3 ligase CHIP ubiquitinates and mediates proteasomal degradation of soluble guanylyl cyclase.
Xia T; Dimitropoulou C; Zeng J; Antonova GN; Snead C; Venema RC; Fulton D; Qian S; Patterson C; Papapetropoulos A; Catravas JD
Am J Physiol Heart Circ Physiol; 2007 Nov; 293(5):H3080-7. PubMed ID: 17873020
[TBL] [Abstract][Full Text] [Related]
5. 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]
6. CHIP: a link between the chaperone and proteasome systems.
McDonough H; Patterson C
Cell Stress Chaperones; 2003; 8(4):303-8. PubMed ID: 15115282
[TBL] [Abstract][Full Text] [Related]
7. Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling.
Demand J; Alberti S; Patterson C; Höhfeld J
Curr Biol; 2001 Oct; 11(20):1569-77. PubMed ID: 11676916
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances.
Muller P; Ruckova E; Halada P; Coates PJ; Hrstka R; Lane DP; Vojtesek B
Oncogene; 2013 Jun; 32(25):3101-10. PubMed ID: 22824801
[TBL] [Abstract][Full Text] [Related]
10. Protein quality control: U-box-containing E3 ubiquitin ligases join the fold.
Cyr DM; Höhfeld J; Patterson C
Trends Biochem Sci; 2002 Jul; 27(7):368-75. PubMed ID: 12114026
[TBL] [Abstract][Full Text] [Related]
11. 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]
12. 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]
13. CHIP: a quality-control E3 ligase collaborating with molecular chaperones.
Murata S; Chiba T; Tanaka K
Int J Biochem Cell Biol; 2003 May; 35(5):572-8. PubMed ID: 12672450
[TBL] [Abstract][Full Text] [Related]
14. Protein-Protein Interactions Modulate the Docking-Dependent E3-Ubiquitin Ligase Activity of Carboxy-Terminus of Hsc70-Interacting Protein (CHIP).
Narayan V; Landré V; Ning J; Hernychova L; Muller P; Verma C; Walkinshaw MD; Blackburn EA; Ball KL
Mol Cell Proteomics; 2015 Nov; 14(11):2973-87. PubMed ID: 26330542
[TBL] [Abstract][Full Text] [Related]
15. The chaperone-assisted E3 ligase C terminus of Hsc70-interacting protein (CHIP) targets PTEN for proteasomal degradation.
Ahmed SF; Deb S; Paul I; Chatterjee A; Mandal T; Chatterjee U; Ghosh MK
J Biol Chem; 2012 May; 287(19):15996-6006. PubMed ID: 22427670
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. C-terminal Hsp-interacting protein slows androgen receptor synthesis and reduces its rate of degradation.
Cardozo CP; Michaud C; Ost MC; Fliss AE; Yang E; Patterson C; Hall SJ; Caplan AJ
Arch Biochem Biophys; 2003 Feb; 410(1):134-40. PubMed ID: 12559985
[TBL] [Abstract][Full Text] [Related]
18. Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase.
Matsumura Y; Sakai J; Skach WR
J Biol Chem; 2013 Oct; 288(43):31069-79. PubMed ID: 23990462
[TBL] [Abstract][Full Text] [Related]
19. The triage of damaged proteins: degradation by the ubiquitin-proteasome pathway or repair by molecular chaperones.
Marques C; Guo W; Pereira P; Taylor A; Patterson C; Evans PC; Shang F
FASEB J; 2006 Apr; 20(6):741-3. PubMed ID: 16469848
[TBL] [Abstract][Full Text] [Related]
20. Curcumin-induced degradation of ErbB2: A role for the E3 ubiquitin ligase CHIP and the Michael reaction acceptor activity of curcumin.
Jung Y; Xu W; Kim H; Ha N; Neckers L
Biochim Biophys Acta; 2007 Mar; 1773(3):383-90. PubMed ID: 17239458
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
