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Volumn 576, Issue 3, 2004, Pages 381-386
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Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity
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Author keywords
C terminal helical lid; Heat shock protein 70; Peptide binding; Substrate mass; Truncation variant
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Indexed keywords
CARBOXYMETHYL ALPHA LACTALBUMIN;
CHAPERONE;
CYSTEINYLLEUCYLLEUCYLLEUCYLSERYLALANYLPROLYLARGINYLARGININE;
HEAT SHOCK PROTEIN 70;
HEAT SHOCK PROTEIN 72;
PEPTIDE;
UNCLASSIFIED DRUG;
ALPHA HELIX;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
COMPLEX FORMATION;
GEL FILTRATION;
MOLECULAR BIOLOGY;
MOLECULAR RECOGNITION;
MOLECULAR WEIGHT;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN BINDING;
PROTEIN DOMAIN;
PROTEIN FUNCTION;
PROTEIN STRUCTURE;
REGULATORY MECHANISM;
STRUCTURE ANALYSIS;
ANIMALS;
BASE SEQUENCE;
BINDING SITES;
CHAPERONINS;
CHROMATOGRAPHY, GEL;
DNA PRIMERS;
HEAT-SHOCK PROTEINS;
HSP72 HEAT-SHOCK PROTEINS;
LACTALBUMIN;
MICE;
MODELS, MOLECULAR;
PROTEIN CONFORMATION;
RECOMBINANT PROTEINS;
SEQUENCE DELETION;
THERMODYNAMICS;
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EID: 6344241182
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/j.febslet.2004.09.044 Document Type: Article |
Times cited : (14)
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References (40)
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