Mutations in Streptococcus pneumoniae Penicillin-Binding Protein 2x: Importance of the C-Terminal Penicillin-Binding Protein and Serine/Threonine Kinase-Associated Domains for Beta-Lactam Binding-Reference-Cited by-同舟云学术

Mutations in Streptococcus pneumoniae Penicillin-Binding Protein 2x: Importance of the C-Terminal Penicillin-Binding Protein and Serine/Threonine Kinase-Associated Domains for Beta-Lactam Binding

Published:2012-06 Issue:3 Volume:18 Page:314-321
ISSN:1076-6294
Container-title:Microbial Drug Resistance
language:en
Short-container-title:Microbial Drug Resistance

Author:

Maurer Patrick¹,Todorova Katya¹,Sauerbier Julia¹,Hakenbeck Regine¹

Affiliation:

1. Department of Microbiology, University of Kaiserslautern, Kaiserslautern, Germany.

Publisher

Mary Ann Liebert Inc

Subject

Microbiology (medical),Pharmacology,Immunology,Microbiology

Link

http://www.liebertpub.com/doi/pdf/10.1089/mdr.2012.0022

Reference24 articles.

1. Development of an optical biosensor assay for detection of β-lactam antibiotics in milk using the penicillin-binding protein 2x*

2. Fluorescent Bocillins: Synthesis and application in the detection of penicillin-binding proteins

3. Biochemistry and Comparative Genomics of SxxK Superfamily Acyltransferases Offer a Clue to the Mycobacterial Paradox: Presence of Penicillin-Susceptible Target Proteins versus Lack of Efficiency of Penicillin as Therapeutic Agent

4. The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance 1 1Edited by R. Huber

5. SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling

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