621 related articles for article (PubMed ID: 36157498)
1. Chaperone-assisted E3 ligase CHIP: A double agent in cancer.
Kumar S; Basu M; Ghosh MK
Genes Dis; 2022 Nov; 9(6):1521-1555. PubMed ID: 36157498
[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. 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]
4. 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]
5. 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]
6. The ubiquitin ligase CHIP regulates c-Myc stability and transcriptional activity.
Paul I; Ahmed SF; Bhowmik A; Deb S; Ghosh MK
Oncogene; 2013 Mar; 32(10):1284-95. PubMed ID: 22543587
[TBL] [Abstract][Full Text] [Related]
7. 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]
8. 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]
9. 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]
10. 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]
11. 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]
12. Biochemical and Proteomic Analysis of Ubiquitination of Hsc70 and Hsp70 by the E3 Ligase CHIP.
Soss SE; Rose KL; Hill S; Jouan S; Chazin WJ
PLoS One; 2015; 10(5):e0128240. PubMed ID: 26010904
[TBL] [Abstract][Full Text] [Related]
13. 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]
14. A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins.
Zhang H; Amick J; Chakravarti R; Santarriaga S; Schlanger S; McGlone C; Dare M; Nix JC; Scaglione KM; Stuehr DJ; Misra S; Page RC
Structure; 2015 Mar; 23(3):472-482. PubMed ID: 25684577
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. Purification and assay of the chaperone-dependent ubiquitin ligase of the carboxyl terminus of Hsc70-interacting protein.
Murata S; Minami M; Minami Y
Methods Enzymol; 2005; 398():271-9. PubMed ID: 16275335
[TBL] [Abstract][Full Text] [Related]
17. 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]
18. 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]
19. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.
Ballinger CA; Connell P; Wu Y; Hu Z; Thompson LJ; Yin LY; Patterson C
Mol Cell Biol; 1999 Jun; 19(6):4535-45. PubMed ID: 10330192
[TBL] [Abstract][Full Text] [Related]
20. E3 ubiquitin ligase CHIP interacts with C-type lectin-like receptor CLEC-2 and promotes its ubiquitin-proteasome degradation.
Shao M; Li L; Song S; Wu W; Peng P; Yang C; Zhang M; Duan F; Jia D; Zhang J; Wu H; Zhao R; Wang L; Ruan Y; Gu J
Cell Signal; 2016 Oct; 28(10):1530-6. PubMed ID: 27443248
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]