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Inactivated pbp4 in highly glycopeptide-resistant laboratory mutants of Staphylococcus aureus.

author

Mariana Gomes de Pinho

Alexander Tomasz

published in: Journal of Biological Chemistry

date of publication: 1999-07-01

language: English

main subject: Staphylococcus aureus

Cites articles 13

Date

Title

Authors

1999-02-01

The development of vancomycin resistance in a patient with methicillin-resistant Staphylococcus aureus infection.

Alexander Tomasz
1997-07-01

Methicillin-resistant Staphylococcus aureus clinical strain with reduced vancomycin susceptibility.
1997-04

Inhibition of cell wall turnover and autolysis by vancomycin in a highly vancomycin-resistant mutant of Staphylococcus aureus

Alexander Tomasz
1997-05-01

Structural characterization of peptidoglycan muropeptides by matrix-assisted laser desorption ionization mass spectrometry and postsource decay analysis
1997-04-01

Transcription analysis of the Staphylococcus aureus gene encoding penicillin-binding protein 4
1994-08-01

The structure of an asymmetric dimer relevant to the mode of action of the glycopeptide antibiotics

Mark S. Searle
1994-06

Glycopeptide Antibiotic Activity and the Possible Role of Dimerization: A Model for Biological Signaling
1990-07-01

Emergence of teicoplanin resistance during therapy of Staphylococcus aureus endocarditis
1990-03-01

Cloning and nucleotide sequence of the N-acetylmuramidase M1-encoding gene from Streptomyces globisporus.

R. Dwayne Elmore
1989-02-01

Involvement of multiple genetic determinants in high-level methicillin resistance in Staphylococcus aureus

Alexander Tomasz
1989-11-01

Structure, biochemistry and mechanism of action of glycopeptide antibiotics
1971-08-01

Modifications of the acyl-D-alanyl-D-alanine terminus affecting complex-formation with vancomycin,Modifications of the acyl-d-alanyl-d-alanine terminus affecting complex-formation with vancomycin
1970-08-15

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

Ulrich Karl Lämmli

Article - wd:Q54090832

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