Results 21 to 30 of about 144,498 (294)

Spherical and rod shaped protoplasts from β-lactam antibiotic treated cultures of Bacillus subtilis [PDF]

open access: yesFEMS Microbiology Letters, 1988
Addition of β-lactams to exponentially growing cultures of an autolytically deficient Bacillus subtilis metc3 lyt-2 strain FJ6 caused increase in optical density to stop after 1 h when it had about doubled, and thereafter to remain constant for at least 6 h.
G. Wright, H.J. Rogers
openaire   +1 more source

Initiation of murein biosynthesis inEscherichia colicells treated with β-lactam antibiotics [PDF]

open access: yesFEMS Microbiology Letters, 1987
The study of the synthesis and accumulation of murein in cells initiating growth in the presence of β-lactam antibiotics indicated: (i) Murein rearrangement contributes substantially to cell enlargement during the first doubling in cell mass; (ii) Penicillin-binding protein 2 has the potential capability to synthesize most, if not all, the new murein ...
Antonio G. Pisabarro   +3 more
openaire   +1 more source

Purine Nucleosides Interfere with c-di-AMP Levels and Act as Adjuvants To Re-Sensitize MRSA To β-Lactam Antibiotics

open access: yesbioRxiv, 2022
The clinical burden of infections caused by antimicrobial resistant (AMR) pathogens is a leading threat to public health. Maintaining the effectiveness of existing antimicrobial drugs or finding ways to reintroduce drugs to which resistance is widespread
Aaron C Nolan   +7 more
semanticscholar   +1 more source

NMR spectrometric assay for determining enzymatic hydrolysis of β-lactam antibiotics with bacteria in aqueous solution [PDF]

open access: yesFEMS Microbiology Letters, 1984
An application of a nuclear magnetic resonance (NMR) spectrometer for the measurement of β-lactamase activity in clinical material containing bacteria is presented. By means of proton (1H)-NMR, it was easy to measure quantitatively β-lactamase activity in human bacteriuria, without performing any such pretreatment as isolation of bacteria or extraction
Koji O'hara, Yoko Shiomi, Megumi Kono
openaire   +1 more source

High potency of sequential therapy with only β-lactam antibiotics

open access: yesbioRxiv, 2021
Evolutionary adaptation is a major source of antibiotic resistance in bacterial pathogens. Evolution- informed therapy aims to constrain resistance by accounting for bacterial evolvability.
Aditi Batra   +5 more
semanticscholar   +1 more source

Characterization of the antibacterial activity from ethanolic extracts of the botanical, Larrea tridentata

open access: yesBMC Complementary Medicine and Therapies, 2021
Background β-lactam antibiotics are a class of broad-spectrum antibiotics consisting of all antibiotic agents that contain a β-lactam ring in their molecular structures. β-lactam antibiotics are only known to be isolated from fungi (e.g.
Tiffany Turner   +3 more
doaj   +1 more source

Involvement of O8-antigen in altering β-lactam antibiotic susceptibilities inEscherichia coli [PDF]

open access: yesFEMS Microbiology Letters, 2008
In spite of being dispensable, O-antigens are believed to facilitate various cellular processes and alter antibiotic sensitivities. Escherichia coli K-12 (CS109) strains are lacking in O-antigens and are reported to be sensitive to antibiotics. To our surprise, E. coli 2443 (expressing O8-antigen) manifested two- to fourfold higher sensitivities toward
Sujoy K, Sarkar, Anindya S, Ghosh
openaire   +2 more sources

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

open access: yesFrontiers 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   +4 more
openaire   +4 more sources

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

open access: yesFEMS 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

Image-based dynamic phenotyping reveals genetic determinants of filamentation-mediated beta-lactam tolerance [PDF]

open access: yes, 2020
Antibiotic tolerance characterized by slow killing of bacteria in response to a drug can lead to treatment failure and promote the emergence of resistance.
Camacho, Rafael   +8 more
core   +2 more sources

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