Binding of Ceftobiprole and Comparators to the Penicillin-Binding Proteins of Escherichia coli , Pseudomonas aeruginosa , Staphylococcus aureus , and Streptococcus pneumoniae
Author:
Affiliation:
1. Johnson & Johnson Pharmaceutical Research and Development, LLC, Raritan, New Jersey
2. Basilea Pharmaceutica AG, Grenzacherstrasse 487, P.O. Box CH-4005, Basel, Switzerland
Abstract
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Link
https://journals.asm.org/doi/pdf/10.1128/AAC.00029-07
Reference30 articles.
1. Diversity of Substitutions within or Adjacent to Conserved Amino Acid Motifs of Penicillin-Binding Protein 2X in Cephalosporin-Resistant Streptococcus pneumoniae Isolates
2. Association of a Thr-371 Substitution in a Conserved Amino Acid Motif of Penicillin-Binding Protein 1A with Penicillin Resistance of Streptococcus pneumoniae
3. Activities of Ceftobiprole, a Novel Broad-Spectrum Cephalosporin, against Haemophilus influenzae and Moraxella catarrhalis
4. Antistaphylococcal Activity of Ceftobiprole, a New Broad-Spectrum Cephalosporin
5. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically. 2006
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