Penicillin Resistance and Autolysis in Enterococci
Author:
Publisher
Mary Ann Liebert Inc
Subject
Microbiology (medical),Pharmacology,Immunology,Microbiology
Link
http://www.liebertpub.com/doi/pdf/10.1089/mdr.1996.2.159
Reference9 articles.
1. Release of autolytic enzyme from Streptococcus, faecium cell walls by treatment with dilute alkali
2. A SPECIFIC COLOR REACTION OF METHYLPENTOSES AND A SPECTROPHOTOMETRIC MICROMETHOD FOR THEIR DETERMINATION
3. The Enterococcus hirae R40 penicillin-binding protein 5 and the methicillin-resistant Staphylococcus aureus penicillin-binding protein 2′ are similar
4. Identification of a streptococcal penicillin-binding protein that reacts very slowly with penicillin
5. Transition from resistance to hypersusceptibility to beta-lactam antibiotics associated with loss of a low-affinity penicillin-binding protein in a Streptococcus faecium mutant highly resistant to penicillin
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1. Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site;BMC Microbiology;2016-10-12
2. The role of bacteriolysis in the pathophysiology of inflammation, infection and post-infectious sequelae;APMIS;2002-11
3. The PBP 5 synthesis repressor (psr) gene ofEnterococcus hiraeATCC 9790 is substantially longer than previously reported;FEMS Microbiology Letters;1998-09
4. Bacterial Walls, Peptidoglycan Hydrolases, Autolysins, and Autolysis;Microbial Drug Resistance;1996-01
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