Literature DB >> 7039448

Penicillin-binding proteins in bacteria.

A Tomasz.   

Abstract

The last 5 to 6 years have witnessed an outburst of renewed interest in the beta-lactam antibiotics. One of the main factors contributing to this was the introduction of the simple and powerful technique of sodium dodecyl sulphate electrophoresis for the identification of bacterial membrane components--penicillin binding proteins--that bind radioactive penicillin and most likely represent the primary biochemical targets of penicillin action in the bacterial cell. Application of this technique has led to a remarkable number of novel observations that have substantially modified our view of the mode of action of beta-lactam antibiotics.

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Year:  1982        PMID: 7039448     DOI: 10.7326/0003-4819-96-4-502

Source DB:  PubMed          Journal:  Ann Intern Med        ISSN: 0003-4819            Impact factor:   25.391


  9 in total

1.  Identification of two new cell division genes that affect a high-molecular-weight penicillin-binding protein in Caulobacter crescentus.

Authors:  P Nathan; A Newton
Journal:  J Bacteriol       Date:  1988-05       Impact factor: 3.490

2.  Effect of human serum on inhibition of growth of Staphylococcus aureus by antimicrobial agents.

Authors:  C W Stratton; M E Evans; D J Burch; H B Hawley; T A Horsman; K K Tu; L B Reller
Journal:  Eur J Clin Microbiol       Date:  1986-06       Impact factor: 3.267

3.  Different staphylococcal species contain various numbers of penicillin-binding proteins ranging from four (Staphylococcus aureus) to only one (Staphylococcus hyicus).

Authors:  P Canepari; P E Varaldo; R Fontana; G Satta
Journal:  J Bacteriol       Date:  1985-08       Impact factor: 3.490

4.  Identification of Treponema pallidum penicillin-binding proteins.

Authors:  T M Cunningham; J N Miller; M A Lovett
Journal:  J Bacteriol       Date:  1987-11       Impact factor: 3.490

5.  Selective release of the Treponema pallidum outer membrane and associated polypeptides with Triton X-114.

Authors:  T M Cunningham; E M Walker; J N Miller; M A Lovett
Journal:  J Bacteriol       Date:  1988-12       Impact factor: 3.490

6.  Characterization of nutritionally variant streptococci by biochemical tests and penicillin-binding proteins.

Authors:  A Bouvet; F Villeroy; F Cheng; C Lamesch; R Williamson; L Gutmann
Journal:  J Clin Microbiol       Date:  1985-12       Impact factor: 5.948

7.  Multiply resistant viridans streptococci: susceptibility to beta-lactam antibiotics and comparison of penicillin-binding protein patterns.

Authors:  B F Farber; G M Eliopoulos; J I Ward; K L Ruoff; V Syriopoulou; R C Moellering
Journal:  Antimicrob Agents Chemother       Date:  1983-11       Impact factor: 5.191

8.  Streptococcus faecium mutants that are temperature sensitive for cell growth and show alterations in penicillin-binding proteins.

Authors:  P Canepari; M M Lleò; R Fontana; G Satta
Journal:  J Bacteriol       Date:  1987-06       Impact factor: 3.490

9.  Bacteriostatic and bactericidal activities of beta-lactams against Streptococcus (Enterococcus) faecium are associated with saturation of different penicillin-binding proteins.

Authors:  M M Lleó; P Canepari; G Cornaglia; R Fontana; G Satta
Journal:  Antimicrob Agents Chemother       Date:  1987-10       Impact factor: 5.191

  9 in total

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