Results 31 to 40 of about 400,542 (252)
mSystems, 2017 Penicillin binding proteins (PBPs) are involved in peptidoglycan synthesis, and their inactivation is linked to β-lactamase expression in ampR–β-lactamase module–harboring Gram-negative bacteria.
Yi-Wei Huang +6 more
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mBio, 2018 Enterococcus faecalis strains resistant to penicillin and ampicillin are rare and have been associated with increases in quantities of low-affinity penicillin-binding protein 4 (PBP4) or with amino acid substitutions in PBP4. We report an E.
Louis B. Rice +8 more
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Penicillin‐Binding Protein Imaging Probes [PDF]
Current Protocols in Chemical Biology, 2013 ABSTRACTPenicillin‐binding proteins (PBPs) are membrane‐associated proteins involved in the biosynthesis of peptidoglycan (PG), the main component of bacterial cell walls. These proteins were discovered and named for their affinity to bind the β‐lactam antibiotic penicillin.
Ozden, Kocaoglu, Erin E, Carlson
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PLoS ONE, 2011 Neisseria meningitidis is a human pathogen responsible for life-threatening inflammatory diseases. Meningococcal penicillin-binding proteins (PBPs) and particularly PBP2 are involved in bacterial resistance to β-lactams. Here we describe a novel function
Marcelo Hill +15 more
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Al-Mustansiriyah Journal of Pharmaceutical Sciences, 2020 Carbapenems are considered as the most effective antibiotic against Acinetobacter baumannii infections, as the pathogen has a resistance to the most of the other beta-lactam antibiotics; however, recent studies proved that this pathogen has developed
Twana Salih, Hawzhin A. Salih
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Penicillin-binding proteins in Actinobacteria [PDF]
The Journal of Antibiotics, 2014 Because some Actinobacteria, especially Streptomyces species, are β-lactam-producing bacteria, they have to have some self-resistant mechanism. The β-lactam biosynthetic gene clusters include genes for β-lactamases and penicillin-binding proteins (PBPs), suggesting that these are involved in self-resistance. However, direct evidence for the involvement
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Affinity of cefoperazone for penicillin-binding proteins [PDF]
Antimicrobial Agents and Chemotherapy, 1980 Cefoperazone (T-1551, CFP) a new semisynthetic cephalosporin, has a broad spectrum of antibacterial activity. We investigated the affinity of CFP to penicillin-binding proteins (PBPs) and the inhibition of peptidoglycan synthesis by CFP. CFP had high affinities for Escherichia coli PBP-3, -1Bs, -2, and -1A, in descending order, and low affinities for ...
N, Matsubara +4 more
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Hfq mutation confers increased cephalosporin resistance in Klebsiella pneumoniae [PDF]
Archives of Biological Sciences, 2017 Klebsiella pneumoniae (K. pneumoniae), is an opportunistic pathogen raising significant public health concerns owing to its multi-drug resistance. Hfq, one of the main RNA-binding proteins, is a key post-transcriptional regulator.
Li Xinran +7 more
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Penicillin-binding proteins in Haemophilus influenzae [PDF]
Antimicrobial Agents and Chemotherapy, 1981 The penicillin-binding proteins (PBPs) of Haemophilus influenzae were studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. Eight major PBPs, ranging in molecular weights from 90,000 to 27,000, were detected. The pattern of molecular weights was different from that determined fro Escherichia coli or Pseudomonas ...
S D, Makover, R, Wright, E, Telep
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mSphere, 2019 Penicillin-binding proteins (PBPs) are essential for bacterial cell wall biosynthesis, and several are clinically validated antibacterial targets of β-lactam antibiotics.
Srijan Ranjitkar +6 more
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