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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 16;276(46):42938-44. Epub 2001 Sep 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. Epub 2001 Nov 21.


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 16;11(20):1569-77.


The U-box ligase carboxyl-terminus of Hsc 70-interacting protein ubiquitylates Epsin.

Timsit YE, Miller SL, Mohney RP, O'Bryan JP.

Biochem Biophys Res Commun. 2005 Mar 11;328(2):550-9.


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 25;288(43):31069-79. doi: 10.1074/jbc.M113.479345. Epub 2013 Aug 29.


U-box protein carboxyl terminus of Hsc70-interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and is involved in neurodegeneration of tauopathy.

Hatakeyama S, Matsumoto M, Kamura T, Murayama M, Chui DH, Planel E, Takahashi R, Nakayama KI, Takashima A.

J Neurochem. 2004 Oct;91(2):299-307.


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 17;279(51):52970-7. Epub 2004 Oct 4.


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 May 26;10(5):e0128240. doi: 10.1371/journal.pone.0128240. eCollection 2015.


ErbB2 degradation mediated by the co-chaperone protein CHIP.

Zhou P, Fernandes N, Dodge IL, Reddi AL, Rao N, Safran H, DiPetrillo TA, Wazer DE, Band V, Band H.

J Biol Chem. 2003 Apr 18;278(16):13829-37. Epub 2003 Feb 6.


Notch-induced E2A degradation requires CHIP and Hsc70 as novel facilitators of ubiquitination.

Huang Z, Nie L, Xu M, Sun XH.

Mol Cell Biol. 2004 Oct;24(20):8951-62.


Regulation of the cytoplasmic quality control protein degradation pathway by BAG2.

Dai Q, Qian SB, Li HH, McDonough H, Borchers C, Huang D, Takayama S, Younger JM, Ren HY, Cyr DM, Patterson C.

J Biol Chem. 2005 Nov 18;280(46):38673-81. Epub 2005 Sep 16.


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.


Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP, mediate plastid-destined precursor degradation through the ubiquitin-26S proteasome system in Arabidopsis.

Lee S, Lee DW, Lee Y, Mayer U, Stierhof YD, Lee S, Jürgens G, Hwang I.

Plant Cell. 2009 Dec;21(12):3984-4001. doi: 10.1105/tpc.109.071548. Epub 2009 Dec 22.


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. Review.


A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase.

Younger JM, Ren HY, Chen L, Fan CY, Fields A, Patterson C, Cyr DM.

J Cell Biol. 2004 Dec 20;167(6):1075-85.


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. Epub 2007 Sep 14.


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