Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone

EMBO Journal

Volumn 20, Issue 5, 2001, Pages 1042-1050

  Rüdiger, Stefan ^a,b   Schneider Mergener, Jens ^c   Bukau, Bernd ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

^b MEDICAL RESEARCH COUNCIL   (United Kingdom)

^c CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

Heat shock proteins; Hsp40; Hsp70; Protein folding; Spot synthesis

Indexed keywords

AMINO ACID; ARGININE; BINDING PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; PEPTIDE DERIVATIVE; PROTEIN DNAJ; PROTEIN DNAK;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACIDS; BACTERIAL PROTEINS; BINDING, COMPETITIVE; CELLULOSE; CONSENSUS SEQUENCE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; LUCIFERASES; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PEPTIDE LIBRARY; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0035283043     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.5.1042     Document Type: Article

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