CHIP is a chaperone‐dependent E3 ligase that ubiquitylates unfolded protein-Reference-Cited by-同舟云学术

CHIP is a chaperone‐dependent E3 ligase that ubiquitylates unfolded protein

Published:2001-12 Issue:12 Volume:2 Page:1133-1138
ISSN:1469-221X
Container-title:EMBO reports
language:en
Short-container-title:EMBO Rep

Author:

Murata Shigeo¹,Minami Yasufumi²,Minami Michiko³,Chiba Tomoki¹,Tanaka Keiji¹

Affiliation:

1. Department of Molecular Oncology, Tokyo Metropolitan Institute of Medical Science, and CREST, Japan Science and Technology Corporation (JST) 3–18–22 Honkomagome, Bunkyo‐ku Tokyo 113‐8613 Japan

2. Department of Biochemistry, Oita Medical University 1–1 Idaigaoka, Hasama‐machi Oita 879‐5593 Japan

3. Showa Gakuin Junior College 2–17–1, Higashi‐Sugano, Ichikawa Chiba 272‐0823 Japan

Publisher

EMBO

Subject

Genetics,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1093/embo-reports/kve246

Reference26 articles.

1. The U box is a modified RING finger — a common domain in ubiquitination

2. Identification of CHIP, a Novel Tetratricopeptide Repeat-Containing Protein That Interacts with Heat Shock Proteins and Negatively Regulates Chaperone Functions

3. Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

4. Ubiquitin-dependent Degradation of Certain Protein Substrates in Vitro Requires the Molecular Chaperone Hsc70

5. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

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