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Volumn 153, Issue 5, 2001, Pages 1061-1069
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Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
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Author keywords
BiP; ERAD; Jem1p; Molecular chaperone; Protein translocation
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Indexed keywords
CARBOXYPEPTIDASE C;
CHAPERONE;
FUNGAL PROTEIN;
HEAT SHOCK PROTEIN 70;
PROTEASOME;
PROTEIN JEM1;
PROTEIN SCJIP;
UNCLASSIFIED DRUG;
ARTICLE;
CONTROLLED STUDY;
CYTOSOL;
ENDOPLASMIC RETICULUM;
GENE DELETION;
GENE MUTATION;
GENETIC CODE;
IN VITRO STUDY;
IN VIVO STUDY;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
PROTEIN DOMAIN;
PROTEIN INTERACTION;
PROTEIN TRANSPORT;
SOLUBILITY;
TEMPERATURE DEPENDENCE;
YEAST;
CARBOXYPEPTIDASE C;
CARBOXYPEPTIDASES;
ENDOPLASMIC RETICULUM;
FUNGAL PROTEINS;
HEAT-SHOCK PROTEINS;
HSP40 HEAT-SHOCK PROTEINS;
HSP70 HEAT-SHOCK PROTEINS;
MEMBRANE PROTEINS;
MEMBRANE TRANSPORT PROTEINS;
MUTATION;
PEPTIDES;
PROTEIN BINDING;
PROTEIN PRECURSORS;
PROTEIN PROCESSING, POST-TRANSLATIONAL;
PROTEIN STRUCTURE, TERTIARY;
PROTEIN TRANSPORT;
SACCHAROMYCES CEREVISIAE PROTEINS;
SOLUBILITY;
TEMPERATURE;
THERMODYNAMICS;
YEASTS;
FUNGI;
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EID: 0035947773
PISSN: 00219525
EISSN: None
Source Type: Journal
DOI: 10.1083/jcb.153.5.1061 Document Type: Article |
Times cited : (271)
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References (70)
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