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

EMBO Reports

Volumn 2, Issue 12, 2001, Pages 1133-1138

  Murata, Shigeo ^a   Minami, Yasufumi ^b   Minami, Michiko ^c   Chiba, Tomoki ^a   Tanaka, Keiji ^a  

^a JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^b OITA UNIVERSITY   (Japan)

^c Showagakuin Junior College   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

C TERMINUS OF HSC70 INTERACTING PROTEIN; CELL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 90; LUCIFERASE; PROTEASOME; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELL FUNCTION; IN VITRO STUDY; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; THERMAL EXPOSURE;

ANIMALS; BEETLES; BLOTTING, WESTERN; CATTLE; HEAT; HEAT-SHOCK PROTEINS; HSC70 HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; LIGASES; LUCIFERASES; MICE; MOLECULAR CHAPERONES; PROTEIN DENATURATION; PROTEIN FOLDING; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES;

EID: 0035684430     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1093/embo-reports/kve246     Document Type: Article

References (26)

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