Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins

Biochemical Journal

Volumn 359, Issue 2, 2001, Pages 419-426

  Wu, S J ^a   Liu, F H ^a   Hu, S M ^a   Wang, C ^a  

^a INSTITUTE OF MOLECULAR BIOLOGY   (Taiwan)

Author keywords

Heat shock proteins; Luciferase refolding; Molecular chaperones; Protein protein interaction; Tetratricopeptide repeats

Indexed keywords

CHEMICAL ACTIVATION; MUTAGENESIS; PROTEINS;

CHAPERONES;

BIOCHEMISTRY;

CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; TRIPEPTIDE;

ARTICLE; NONHUMAN; NUCLEOTIDE SEQUENCE; PEPTIDE ANALYSIS; PLASMID; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; YEAST;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BASE SEQUENCE; CARRIER PROTEINS; DNA PRIMERS; HSC70 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; LUCIFERASES; MOLECULAR SEQUENCE DATA; NUCLEAR PROTEINS; PEPTIDES; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; RATS; RECOMBINANT FUSION PROTEINS; REPETITIVE SEQUENCES, AMINO ACID; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; UBIQUITIN-PROTEIN LIGASES;

EID: 0035887167     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3590419     Document Type: Article

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