Results 41 to 50 of about 564,515 (340)
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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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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Perturbed cholesterol and vesicular trafficking associated with dengue blocking in Wolbachia-infected Aedes aegypti cells [PDF]
, 2017 Wolbachia are intracellular maternally inherited bacteria that can spread through insect populations and block virus transmission by mosquitoes, providing an important approach to dengue control.
Ant, Thomas H. +9 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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Allosteric p97 inhibitors can overcome resistance to ATP-competitive p97 inhibitors for potential anti-cancer therapy [PDF]
, 2020 A major challenge of targeted cancer therapy is the selection for drug‐resistant mutations in tumor cells leading to loss of treatment effectiveness. p97/VCP is a central regulator of protein homeostasis and a promising anti‐cancer target because of its ...
Chou, Tsui-Fen +5 more
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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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Surfactant-free purification of membrane protein complexes from bacteria: application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a [PDF]
, 2014 Surfactant-mediated removal of proteins from biomembranes invariably results in partial or complete loss of function and disassembly of multi-protein complexes. We determined the capacity of styrene-co-maleic acid (SMA) co-polymer to remove components of
Dafforn, Timothy R +8 more
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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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