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Volumn 342, Issue 3, 1994, Pages 242-248
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Structural similarities between chaperone molecules of the HSP60 and HSP70 families deduced from hydrophobic cluster analysis
a,b
c
b
b
c
a
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Author keywords
Heat shock protein; Hydrophobic cluster analysis; Molecular chaperone; Nucleotide binding
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Indexed keywords
ADENOSINE TRIPHOSPHATE;
CHAPERONE;
HEAT SHOCK PROTEIN;
HEAT SHOCK PROTEIN 60;
NUCLEOTIDE;
AMINO ACID SEQUENCE;
ARTICLE;
GENETIC CONSERVATION;
LIGAND BINDING;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN STRUCTURE;
ADENOSINE TRIPHOSPHATE;
ADENOSINETRIPHOSPHATASE;
AMINO ACID SEQUENCE;
ANIMAL;
BACTERIAL PROTEINS;
BINDING SITES;
CHAPERONINS;
COMPARATIVE STUDY;
HEAT-SHOCK PROTEINS;
MOLECULAR SEQUENCE DATA;
PROTEIN STRUCTURE, TERTIARY;
PROTEINS;
SEQUENCE ALIGNMENT;
SEQUENCE HOMOLOGY, AMINO ACID;
SUPPORT, NON-U.S. GOV'T;
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EID: 0028204274
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/0014-5793(94)80510-5 Document Type: Article |
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Times cited : (8)
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References (18)
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