A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery

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

Volumn 100, Issue 22, 2003, Pages 12735-12740

  Hitchcock, Amy L ^a,b,c   Auld, Kathryn ^a,b   Gygi, Steven P ^a   Silver, Pamela A ^a,b  

^a HARVARD MEDICAL SCHOOL   (United States)

^b DANA FARBER CANCER INSTITUTE   (United States)

^c MOUNT HOLYOKE COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL ENZYME; MEMBRANE PROTEIN; MEMBRANE RECEPTOR; PERMEASE; PROTEASOME; TRANSCRIPTION FACTOR;

ACTIN FILAMENT; ARTICLE; BIOACCUMULATION; CELL MEMBRANE; CELLULAR DISTRIBUTION; CHEMICAL REACTION; CONTROLLED STUDY; ENDOCYTOSIS; ENDOPLASMIC RETICULUM; ENZYME LOCALIZATION; ENZYME MECHANISM; ENZYME SUBSTRATE; FUNGAL STRAIN; FUNGUS MUTANT; GENE MAPPING; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN INDUCTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTEIN TARGETING; PROTEIN TRANSPORT; PROTEOMICS; SACCHAROMYCES CEREVISIAE; UBIQUITINATION; YEAST;

ENDOPLASMIC RETICULUM; GENES, FUNGAL; GENES, SUPPRESSOR; MEMBRANE PROTEINS; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUBCELLULAR FRACTIONS; SUBSTRATE SPECIFICITY; UBIQUITIN;

FUNGI; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0242300110     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.2135500100     Document Type: Article

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