Multiple molecules of Hsc70 and a dimer of DjA1 independently bind to an unfolded protein

Journal of Biological Chemistry

Volumn 285, Issue 22, 2010, Pages 16789-16797

  Terada, Kazutoyo ^a   Oike, Yuichi ^a  

^a KUMAMOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION RATES; CHAPERONE FUNCTIONS; CONFORMATIONAL CHANGE; GEL FILTRATION; NUCLEOTIDE-EXCHANGE FACTOR; PEPTIDE ARRAYS; REFOLDING; SUBSTRATE RECOGNITION; SURFACE PLASMONS; TRYPTIC DIGESTION; UNFOLDED PROTEINS;

GELS; PROTEIN FOLDING; SURFACE PLASMON RESONANCE;

CONFORMATIONS;

DIMER; HEAT SHOCK COGNATE PROTEIN 70; PEPTIDE; PROTEIN DJA1; PROTEIN DNAJ; TRYPSIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN TARGETING; STOICHIOMETRY;

ANIMALS; CELLULOSE; CROSS-LINKING REAGENTS; DIMERIZATION; HSC70 HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; KINETICS; LIVER; MICE; MOLECULAR CHAPERONES; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; RATS; SURFACE PLASMON RESONANCE;

EID: 77952773873     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.101501     Document Type: Article

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