Results 151 to 160 of about 558,213 (199)
Novel Electrophilic Scaffold for Imaging of Essential Penicillin-Binding Proteins in Streptococcus pneumoniae. [PDF]
ACS Chem Biol, 2017 Sharifzadeh S +7 more
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Copper inhibits peptidoglycan LD-transpeptidases suppressing β-lactam resistance due to bypass of penicillin-binding proteins. [PDF]
Proc Natl Acad Sci U S A, 2018 Peters K +8 more
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Peptidoglycan Cross-Linking Preferences of Staphylococcus aureus Penicillin-Binding Proteins Have Implications for Treating MRSA Infections. [PDF]
J Am Chem Soc, 2017 Srisuknimit V +4 more
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Resistant penicillin-binding proteins
Cellular and Molecular Life Sciences CMLS, 1998Low-affinity penicillin-binding proteins (PBPs), which participate in the beta-lactam resistance of several pathogenic bacteria, have different origins. Natural transformation and recombination events with DNA acquired from neighbouring intrinsically resistant organisms are responsible for the appearance of mosaic genes encoding two or three low ...
R, Hakenbeck, J, Coyette
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Penicillin binding proteins of Vibriocholerae
Biochemical and Biophysical Research Communications, 1990Eleven penicillin binding proteins (PBPs) of Vibrio cholerae have been identified using [125I] labelled p-hydroxybenzyl penicillin (PenX). These proteins are localised in the inner membrane and have molecular weights ranging from 97,000 to 22,000.
T K, Sengupta, A N, Chatterjee, J, Das
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Penicillin-Binding Proteins inFusobacteriumSpecies
Anaerobe, 1996Abstract PBPs were identified in four species ofFusobacterium. Each species had a distinctive PBP pattern, although some intra-species variation was noted. Most species had five or six PBPs, ranging in molecular weight from ∼100 kDa to ∼40 kDa. The two strains ofF. nucleatumtested had characteristic “wavy” PBP patterns.F. mortiferumwas distinctive in
K. Tunér +3 more
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Penicillin-Binding Proteins of Bacteria
1977The penicillin-binding components of bacteria are presumably enzymes of cell wall peptidoglycan synthesis, and one or more of these is a presumed killing site for penicillins. All organisms which have so far been examined contain multiple penicillin-binding components, e.g., there are five in Bacillus subtilis, six in Escherichia coli, and four in ...
J W, Kozarich +4 more
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Penicillin-Binding Proteins in Bacteria
Annals of Internal Medicine, 1982The 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
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Penicillin-binding proteins: evergreen drug targets
Current Opinion in Pharmacology, 2014The penicillin-binding proteins (PBPs) are well known targets for the β-lactam antibiotics. They continue to be a focus of interest for pharmaceutical design, as exemplified by the number of new agents under clinical investigation as well as novel experimental molecules.
Frère, Jean-Marie, Page, Malcolm G. P.
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Penicillin‐binding proteins in Listeria monocytogenes
APMIS, 1989The Penicillin‐Binding Proteins (PBP) of Listeria monocytogenes 29‐CCM‐A: 454 (ATCC 15313) are described by the use of 125I‐Penicillin X as radiotracer. The membranes of this tolerant bacilli contained at least five proteins with different affinities for the radiotracer or Dicloxacillin. The molecular weights of these proteins were estimated as 76, 74,
G O, Gutkind +2 more
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