ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load

Journal of Cell Biology

Volumn 198, Issue 3, 2012, Pages 371-385

  Chambers, Joseph E ^a   Petrova, Kseniya ^b   Tomba, Giulia ^a   Vendruscolo, Michele ^a   Ron, David ^a,b  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GLUCOSE REGULATED PROTEIN 78;

ADENOSINE DIPHOSPHATE RIBOSYLATION; ALLOSTERISM; ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; BINDING SITE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM STRESS; ENZYME INACTIVATION; ENZYME KINETICS; HAMSTER; MOUSE; NONHUMAN; PANCREAS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN PROCESSING;

ADENOSINE DIPHOSPHATE; ALLOSTERIC SITE; ANIMALS; ANISOTROPY; CATALYTIC DOMAIN; CELL LINE; CRICETINAE; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; HOMEOSTASIS; HUMANS; KINETICS; MICE; MOLECULAR CHAPERONES; MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; RIBOSE;

CRICETINAE; MUS;

EID: 84866455655     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201202005     Document Type: Article

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