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Volumn 269, Issue 10, 1994, Pages 7464-7472
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Chaperone function of calnexin for the folding intermediate of gp80, the major secretory protein in MDCK cells. Regulation by redox state and ATP
a
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Author keywords
[No Author keywords available]
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Indexed keywords
CALNEXIN;
CHAPERONE;
DIAMIDE;
DITHIOTHREITOL;
MEMBRANE PROTEIN;
PROTEIN PRECURSOR;
SECRETORY PROTEIN;
ANIMAL CELL;
ARTICLE;
CONTROLLED STUDY;
DISSOCIATION;
DOG;
ENDOPLASMIC RETICULUM;
KIDNEY CELL;
NONHUMAN;
OXIDATION REDUCTION REACTION;
PRIORITY JOURNAL;
PROTEIN ASSEMBLY;
PROTEIN FOLDING;
PROTEIN PROCESSING;
ADENOSINE TRIPHOSPHATE;
ANIMAL;
BINDING SITES;
CALCIUM-BINDING PROTEINS;
CALNEXIN;
CELLS, CULTURED;
CHAPERONINS;
DOGS;
ENDOPLASMIC RETICULUM;
MEMBRANE GLYCOPROTEINS;
MEMBRANE PROTEINS;
OXIDATION-REDUCTION;
PROTEIN FOLDING;
PROTEIN PRECURSORS;
PROTEINS;
SUPPORT, NON-U.S. GOV'T;
EUKARYOTA;
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EID: 0028235984
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: None Document Type: Article |
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Times cited : (60)
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References (0)
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