Penicillin-binding proteins 2b and 2x of Streptococcus pneumoniae are primary resistance determinants for difierent classes of β-lactam antibiotics

Antimicrobial Agents and Chemotherapy

Volumn 40, Issue 4, 1996, Pages 829-834

  Grebe, Thorsten ^a,b   Hakenbeck, Regine ^a  

^a MAX PLANCK INSTITUTE FOR MOLECULAR GENETICS   (Germany)

^b PFIZER GLOBAL RESEARCH AND DEVELOPMENT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BETA LACTAM ANTIBIOTIC; CEFOTAXIME; OXACILLIN; PENICILLIN BINDING PROTEIN; PIPERACILLIN;

AMINO ACID SUBSTITUTION; ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIUM TRANSFORMATION; DRUG PROTEIN BINDING; GENE ISOLATION; POINT MUTATION; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; STREPTOCOCCUS PNEUMONIAE;

AMINO ACID SEQUENCE; AMINOACYLTRANSFERASES; BACTERIAL PROTEINS; BASE SEQUENCE; BETA-LACTAM RESISTANCE; BETA-LACTAMS; CARRIER PROTEINS; CEFOTAXIME; DOSE-RESPONSE RELATIONSHIP, DRUG; HEXOSYLTRANSFERASES; MOLECULAR SEQUENCE DATA; MURAMOYLPENTAPEPTIDE CARBOXYPEPTIDASE; OXACILLIN; PENICILLIN-BINDING PROTEINS; PEPTIDYL TRANSFERASES; PIPERACILLIN; POLYMERASE CHAIN REACTION; STREPTOCOCCUS PNEUMONIAE;

EID: 0030003591     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.40.4.829     Document Type: Article

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