Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase

Journal of Cell Biology

Volumn 147, Issue 7, 1999, Pages 1443-1456

  Gillece, Pauline ^a   Luz, José Manuel ^c   Lennarz, William J ^c   De La Cruz, Francisco Javier ^b   Römisch, Karin ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY COLLEGE LONDON   (United Kingdom)

^c STONY BROOK UNIVERSITY   (United States)

Author keywords

BiP; Endoplasmic reticulum quality control; Endoplasmic reticulum associated degradation; Protein disulfide isomerase; Yeast

Indexed keywords

CHAPERONE; CYSTEINE; MUTANT PROTEIN; PROTEIN DISULFIDE ISOMERASE; SECRETORY PROTEIN; THIOL;

ARTICLE; CYTOSOL; ENDOPLASMIC RETICULUM; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING;

BIOLOGICAL TRANSPORT; CYSTEINE; CYTOSOL; ENDOPLASMIC RETICULUM; FUNGAL PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MEMBRANE PROTEINS; MICROSOMES; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; PROTEIN BINDING; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE DELETION; SUBSTRATE SPECIFICITY;

EID: 0033611127     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.147.7.1443     Document Type: Article

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