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Volumn 15, Issue 3, 2002, Pages 113-125
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Conformational analysis of bacterial cell wall peptides indicates how particular conformations have influenced the evolution of penicillin-binding proteins, β-lactam antibiotics and antibiotic resistance mechanisms
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Author keywords
Lactamase; Antibiotic resistance; Conformational analysis; Ligand binding; Molecular recognition; Peptide backbone torsions; Peptide conformers; Peptide transporters; Serine protease; Vancomycin
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Indexed keywords
AMINO ACID SEQUENCE;
ANTIBIOTICS, LACTAM;
BACTERIA;
BACTERIAL PROTEINS;
CARRIER PROTEINS;
CELL WALL;
DRUG DESIGN;
DRUG RESISTANCE, BACTERIAL;
EVOLUTION, MOLECULAR;
MODELS, MOLECULAR;
MOLECULAR STRUCTURE;
MURAMOYLPENTAPEPTIDE CARBOXYPEPTIDASE;
PEPTIDES;
PROTEIN CONFORMATION;
SUBSTRATE SPECIFICITY;
SUPPORT, NON-U.S. GOV'T;
VANCOMYCIN;
ANTI-BACTERIAL AGENTS;
BETA-LACTAMS;
HEXOSYLTRANSFERASES;
PENICILLIN-BINDING PROTEINS;
PEPTIDYL TRANSFERASES;
BACTERIA (MICROORGANISMS);
ANTIINFECTIVE AGENT;
BACTERIAL PROTEIN;
BETA LACTAM;
CARBOXYPEPTIDASE TRANSPEPTIDASE;
CARRIER PROTEIN;
GLYCOSYLTRANSFERASE;
PENICILLIN BINDING PROTEIN;
PEPTIDE;
PEPTIDYLTRANSFERASE;
VANCOMYCIN;
AMINO ACID SEQUENCE;
ANTIBIOTIC RESISTANCE;
ARTICLE;
BACTERIUM;
CELL WALL;
CHEMICAL STRUCTURE;
CHEMISTRY;
CYTOLOGY;
DRUG DESIGN;
ENZYME SPECIFICITY;
GENETICS;
MOLECULAR EVOLUTION;
PROTEIN CONFORMATION;
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EID: 0035994076
PISSN: 09523499
EISSN: None
Source Type: Journal
DOI: 10.1002/jmr.566 Document Type: Article |
Times cited : (9)
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References (42)
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