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.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

623 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]
    of 32.