Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum

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

Volumn 92, Issue 5, 1995, Pages 1764-1768

  Knittler, M R ^a   Dirks, S ^a   Haas, I G ^a  

^a UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

folding intermediates; half life; substrate specificity; subunit assembly; temperature sensitivity

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; IMMUNOGLOBULIN LIGHT CHAIN;

ANIMAL CELL; ARTICLE; CELL CULTURE; ENDOPLASMIC RETICULUM; ENZYME SPECIFICITY; GENE EXPRESSION; GENE REARRANGEMENT; GENETIC TRANSFECTION; HALF LIFE TIME; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; TEMPERATURE SENSITIVITY;

ANIMAL; CARRIER PROTEINS; CELL LINE; ENDOPLASMIC RETICULUM; IMMUNOGLOBULINS, LIGHT-CHAIN; MICE; MOLECULAR CHAPERONES; MONENSIN; OXIDATION-REDUCTION; PROTEIN FOLDING; SUPPORT, NON-U.S. GOV'T; TEMPERATURE;

ANIMALIA; MURINAE;

EID: 0028928021     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.92.5.1764     Document Type: Article

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