The unfolded protein response supports cellular robustness as a broad-spectrum compensatory pathway

Proceedings of the National Academy of Sciences of the United States of America

Volumn 108, Issue 51, 2011, Pages 20597-20602

  Thibault, Guillaume ^a   Ismail, Nurzian ^a,b   Ng, Davis T W ^a  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

Chaperones; Glycosylation; Protein degradation; Protein folding; Signal transduction

Indexed keywords

AMPLITUDE MODULATION; ARTICLE; ENDOPLASMIC RETICULUM STRESS; GENE EXPRESSION PROFILING; GENE FUNCTION; GENE TARGETING; NONHUMAN; PRIORITY JOURNAL; UNFOLDED PROTEIN RESPONSE; YEAST CELL;

ALLELES; BETA-GALACTOSIDASE; ENDOPLASMIC RETICULUM; FUNGAL PROTEINS; GENE DELETION; GLYCOSYLATION; MODELS, GENETIC; MOLECULAR CONFORMATION; MUTATION; PHENOTYPE; PROTEIN DENATURATION; PROTEIN FOLDING; SIGNAL TRANSDUCTION; TEMPERATURE; TRANSCRIPTION, GENETIC; UNFOLDED PROTEIN RESPONSE;

EID: 84855496731     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1117184109     Document Type: Article

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