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Volumn 9, Issue 5, 2001, Pages 367-375
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The 2.2 å crystal structure of Hsp33: A heat shock protein with redox-regulated chaperone activity
a a a a a,b |
Author keywords
Crystal structure; Dimerization; Heat shock protein; Hsp33; Oxidative stress; Zinc
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Indexed keywords
CHAPERONE;
DIMER;
GLUTAMIC ACID;
HEAT SHOCK PROTEIN;
HEAT SHOCK PROTEIN 33;
MONOMER;
PROTEIN SUBUNIT;
UNCLASSIFIED DRUG;
ZINC;
BACTERIAL PROTEIN;
ESCHERICHIA COLI PROTEIN;
HSP33 PROTEIN, BACTERIA;
HSP33 PROTEIN, E COLI;
ARTICLE;
BETA SHEET;
BINDING SITE;
CARBOXY TERMINAL SEQUENCE;
CRYSTAL STRUCTURE;
ESCHERICHIA COLI;
HYDROGEN BOND;
NUCLEOTIDE SEQUENCE;
OXIDATION REDUCTION REACTION;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN BINDING;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PROTEIN STRUCTURE;
AMINO ACID SEQUENCE;
CHEMICAL STRUCTURE;
CHEMISTRY;
DIMERIZATION;
MOLECULAR GENETICS;
PROTEIN TERTIARY STRUCTURE;
X RAY CRYSTALLOGRAPHY;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
AMINO ACID SEQUENCE;
BACTERIAL PROTEINS;
CRYSTALLOGRAPHY, X-RAY;
DIMERIZATION;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
HEAT-SHOCK PROTEINS;
MODELS, MOLECULAR;
MOLECULAR CHAPERONES;
MOLECULAR SEQUENCE DATA;
OXIDATION-REDUCTION;
PROTEIN STRUCTURE, TERTIARY;
ZINC;
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EID: 0034990115
PISSN: 09692126
EISSN: None
Source Type: Journal
DOI: 10.1016/S0969-2126(01)00597-4 Document Type: Article |
Times cited : (50)
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References (27)
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