SecB is a bona fide generalized chaperone in Escherichia coli

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

Volumn 101, Issue 20, 2004, Pages 7583-7588

  Ullers, Ronald S ^a   Luirink, Joen ^a   Harms, Nellie ^a   Schwager, Françoise ^b   Georgopoulos, Costa ^b   Genevaux, Pierre ^b  

^a VU UNIVERSITY AMSTERDAM   (Netherlands)

^b UNIVERSITY OF GENEVA MEDICAL SCHOOL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CELL PROTEIN; CHAPERONE; PROTEIN DNAK; PROTEIN SECA; PROTEIN SECB; SECRETORY PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; CROSS LINKING; ESCHERICHIA COLI; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SYNTHESIS; TEMPERATURE SENSITIVITY;

BACTERIAL PROTEINS; DNA-DIRECTED RNA POLYMERASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; PEPTIDYLPROLYL ISOMERASE; PROTEIN FOLDING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 2442707856     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0402398101     Document Type: Article

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