Results 21 to 30 of about 61,324 (269)

β-lactam antibiotics induce metabolic perturbations linked to ROS generation leads to bacterial impairment [PDF]

Frontiers in Microbiology
Understanding the impact of antibiotics on bacterial metabolism is crucial for elucidating their mechanisms of action and developing more effective therapeutic strategies.
Dongyang Ye, Dongyang Ye, Dongyang Ye, Jing Sun, Jing Sun, Ran Jiang, Jiashen Chang, Yiming Liu, Xiangzheng Wu, Luqi Li, Yihan Luo, Juan Wang, Juan Wang, Juan Wang, Kangkang Guo, Kangkang Guo, Kangkang Guo, Zengqi Yang, Zengqi Yang, Zengqi Yang   +19 more
doaj   +2 more sources

Mutations in ampD cause hyperproduction of AmpC and CmcB β-lactamases and high resistance to β-lactam antibiotics in Chromobacterium violaceum [PDF]

Microbiology Spectrum
Bacterial resistance to β-lactam antibiotics mediated by β-lactamase enzymes is widespread worldwide. Chromobacterium violaceum, an environmental Gram-negative bacterial pathogen, is intrinsically resistant to some β-lactam antibiotics.
Luís Gustavo Laranjeiro, Carlos Eduardo M. Neme, Maristela Previato-Mello, Bianca B. Batista, Isabel Henriques, José F. da Silva Neto   +5 more
doaj   +2 more sources

The barrier function of the outer membrane ofPseudomonas maltophiliain the diffusion of saccharides and β-lactam antibiotics [PDF]

FEMS Microbiology Letters, 1989
This paper reports that the efficiency of solute diffusion through the outer membrane of Pseudomonas maltophilia is roughly 3 to 5% of that of Escherichia coli. This is despite the fact that the outer membrane pore(s) is only a little smaller than that of E. coli. These results suggest that P. maltophilia has a low copy number of porin(s).
E, Yamazaki, J, Ishii, K, Sato, T, Nakae
openaire   +2 more sources

Characterization of the membrane sensor PenJ for β-lactam antibodies fromBacillus licheniformisby amino acid substitution [PDF]

FEMS Microbiology Letters, 1993
The PenJ protein of the penicillinase gene (penP) expression system from Bacillus licheniformis is an antirepressor and membrane receptor for beta-lactam antibiotics. A putative beta-lactam antibiotic binding site including Ser402 and Lys405, which are homologous to the conserved sequence for the beta-lactam binding site (Ser-X-X-Lys) is present.
M, Takagi, T, Ohta, S, Johki, T, Imanaka
openaire   +2 more sources

Commonly prescribed β-lactam antibiotics induce C. trachomatis persistence/stress in culture at physiologically relevant concentrations [PDF]

Frontiers in Cellular and Infection Microbiology, 2014
Chlamydia trachomatis, the most common bacterial sexually transmitted disease agent worldwide, enters a viable, non-dividing and non-infectious state (historically termed persistence and more recently referred to as the chlamydial stress response) when exposed to penicillin G in culture.
Kintner, Jennifer, Lajoie, Dawn, Hall, Jennifer, Whittimore, Judy, Schoborg, Robert V.   +4 more
openaire   +4 more sources

The Mechanisms of Catalysis by Metallo β-Lactamases [PDF]

, 2008
Class B β-lactamases or metallo-β-lactamases (MBLs) require zinc ions to catalyse the hydrolysis of β-lactam antibiotics such as penicillins, cephalosporins, carbapenems, and cephamycins.
Michael I. Page, Page, Michael I., Badarau, Adriana, Adriana Badarau   +3 more
core   +1 more source

Efficacy of Non-Beta-lactam Antibiotics for Prevention of Cesarean Delivery Surgical Site Infections

American Journal of Perinatology Reports, 2019
Objective To examine the association between perioperative Beta (β))-lactam versus non-β-lactam antibiotics and cesarean delivery surgical site infection (SSI).
Benjamin S. Harris, Maeve K. Hopkins, Margaret S. Villers, Jeremy M. Weber, Carl Pieper, Chad A. Grotegut, Geeta K. Swamy, Brenna L. Hughes, R Phillips Heine   +8 more
doaj   +1 more source

Trimeric Tobramycin/Nebramine Synergizes β‑Lactam Antibiotics against Pseudomonas aeruginosa

, 2023
β-Lactam antibiotics remain one of the most effective therapeutics to treat infections caused by Gram-negative bacteria (GNB). However, since ancient times, bacteria have developed multiple resistance mechanisms toward this class of antibiotics including
Shiv Dhiman, Gilbert Arthur (2274238), Ayush Kumar (199516), Danyel Ramirez (8812073), Rajat Arora, Ruwani Wimalasekara (16726167), Frank Schweizer (148473), Rajat Arora (16726161), Ayush Kumar, Frank Schweizer, Karan Gandhi, Shiv Dhiman (1763281), Karan Gandhi (16726164), Danyel Ramirez, Gilbert Arthur, Ruwani Wimalasekara   +15 more
core   +1 more source

Resistance to β-lactam antibiotics conferred by point mutations in penicillin-binding proteins PBP3, PBP4 and PBP6 in Salmonella enterica. [PDF]

PLoS ONE, 2014
Penicillin-binding proteins (PBPs) are enzymes responsible for the polymerization of the glycan strand and the cross-linking between glycan chains as well as the target proteins for β-lactam antibiotics.
Song Sun, Maria Selmer, Dan I Andersson
doaj   +1 more source

Bacterial Resistance to β-Lactam Antibiotics in Municipal Wastewater: Insights from a Full-Scale Treatment Plant in Poland

Microorganisms, 2022
This study investigated enzymatic and genetic determinants of bacterial resistance to β-lactam antibiotics in the biocenosis involved in the process of biological treatment of wastewater by activated sludge.
Natalia Jendrzejewska, Ewa Karwowska
doaj   +1 more source