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.
314 related articles for article (PubMed ID: 24868554)
1. The E3 ligase CHIP: insights into its structure and regulation. Paul I; Ghosh MK Biomed Res Int; 2014; 2014():918183. PubMed ID: 24868554 [TBL] [Abstract][Full Text] [Related]
2. 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]
3. 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]
4. Molecular mechanism of the negative regulation of Smad1/5 protein by carboxyl terminus of Hsc70-interacting protein (CHIP). Wang L; Liu YT; Hao R; Chen L; Chang Z; Wang HR; Wang ZX; Wu JW J Biol Chem; 2011 May; 286(18):15883-94. PubMed ID: 21454478 [TBL] [Abstract][Full Text] [Related]
5. 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]
6. E3 ligase CHIP and Hsc70 regulate Kv1.5 protein expression and function in mammalian cells. Li P; Kurata Y; Maharani N; Mahati E; Higaki K; Hasegawa A; Shirayoshi Y; Yoshida A; Kondo T; Kurozawa Y; Yamamoto K; Ninomiya H; Hisatome I J Mol Cell Cardiol; 2015 Sep; 86():138-46. PubMed ID: 26232501 [TBL] [Abstract][Full Text] [Related]
7. The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex. Smith MC; Scaglione KM; Assimon VA; Patury S; Thompson AD; Dickey CA; Southworth DR; Paulson HL; Gestwicki JE; Zuiderweg ER Biochemistry; 2013 Aug; 52(32):5354-64. PubMed ID: 23865999 [TBL] [Abstract][Full Text] [Related]
8. 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]
9. 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]
10. 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]
11. CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. Jiang J; Ballinger CA; Wu Y; Dai Q; Cyr DM; Höhfeld J; Patterson C J Biol Chem; 2001 Nov; 276(46):42938-44. PubMed ID: 11557750 [TBL] [Abstract][Full Text] [Related]
12. 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]
13. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. Murata S; Minami Y; Minami M; Chiba T; Tanaka K EMBO Rep; 2001 Dec; 2(12):1133-8. PubMed ID: 11743028 [TBL] [Abstract][Full Text] [Related]
14. 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]
18. Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins. Wu SJ; Liu FH; Hu SM; Wang C Biochem J; 2001 Oct; 359(Pt 2):419-26. PubMed ID: 11583590 [TBL] [Abstract][Full Text] [Related]
19. Chemical Regulation of the Protein Quality Control E3 Ubiquitin Ligase C-Terminus of Hsc70 Interacting Protein (CHIP). Kanack AJ; Olp MD; Newsom OJ; Scaglione JB; Gooden DM; McMahon K; Smith BC; Scaglione KM Chembiochem; 2022 Mar; 23(6):e202100633. PubMed ID: 35061295 [TBL] [Abstract][Full Text] [Related]