Results 31 to 40 of about 87,683 (298)

Pharmacokinetics of β-Lactam Antibiotics:Clues from the Past to Help Discover Long-Acting Oral Drugs in the Future [PDF]

, 2018
β-Lactams represent perhaps the most important class of antibiotics yet discovered. However, despite many years of active research, none of the currently approved drugs in this class combine oral activity with long duration of action. Recent developments
Bates, Robert H., Epemolu, Ola, Martinez-Martinez, Maria Santos, Peet, Caroline, Read, Kevin D., Smith, Paul W., Zuccotto, Fabio   +6 more
core   +3 more sources

β-Lactam induction of colanic acid gene expression inEscherichia coli [PDF]

FEMS Microbiology Letters, 2003
An unexpected observation led us to examine the relationship between beta-lactam exposure and synthesis of colonic acid capsular polysaccharide in Escherichia coli. Strains containing a cps-lacZ transcriptional fusion were challenged with antibiotics having various modes of action, and gene expression was detected by a disk-diffusion assay and in broth
Frances C, Sailer, Bernadette M, Meberg, Kevin D, Young   +2 more
openaire   +2 more sources

A degenerate PCR-based strategy as a means of identifying homologues of aminoglycoside and ß-lactam resistance genes in the gut microbiota [PDF]

, 2014
peer-reviewedBackground: The potential for the human gut microbiota to serve as a reservoir for antibiotic resistance genes has been the subject of recent discussion. However, this has yet to be investigated using a rapid PCR-based approach.
Cotter, Paul D., Fitzgerald, Gerald F, Fouhy, Fiona, Ross, R Paul, STANTON, CATHERINE   +4 more
core   +1 more source

Synergistic Combinations of FDA-Approved Drugs with Ceftobiprole against Methicillin-Resistant Staphylococcus aureus

Microbiology Spectrum, 2023
New strategies are urgently needed to address the public health threat of antimicrobial resistance. Synergistic agent combinations provide one possible pathway toward addressing this need and are also of fundamental mechanistic interest.
Amar Deep Sharma, William G. Gutheil
doaj   +1 more source

The porin and the permeating antibiotic: A selective diffusion barrier in gram-negative bacteria [PDF]

, 2008
Gram-negative bacteria are responsible for a large proportion of antibiotic resistant bacterial diseases. These bacteria have a complex cell envelope that comprises an outer membrane and an inner membrane that delimit the periplasm.
A Baslé, A Baslé, A Bryskier, A Davin-Regli, A Davin-Régli, A Doménech-Sánchez, A Doménech-Sánchez, A Loli, A Mena, A Mena, A Prilipov, A Thiolas, A Thiolas, AA Medeiros, AH Delcour, AM Berezhkovskii, AM Giuliodori, AS Low, C Bornet, C Bornet, C Bosi, C Danelon, C Danelon, C Rodrigues, C Sheridan, Chloë E. James, D Jeanteur, D Szabó, DJ Wolter, E Dé, E Elliott, E Sugawara, EM Nestorovich, EM Nestorovich, F Yoshimura, FM Kaczmarek, G Schwarz, GA Jacoby, GE Schulz, H Nikaido, H Nikaido, H Nikaido, H Samartzidou, H Samartzidou, J Bredin, J Chevalier, J Chevalier, J-M Pagès, JC Cai, Jean-Marie Pagès, JM Bower, K Poole, L Kullman, L Martínez-Martínez, LB Rice, LJ Piddock, LP Randall, M Ceccarelli, M Guillier, M Luckey, M Malléa, M Olesky, M Olesky, M Viveiros, MA Kohanski, Mathias Winterhalter, MM Ochs, N El Amin, P Valentin-Hansen, R Dutzler, R Iyer, R Iyer, R Koebnik, RE Hancock, RN Charrel, S Biswas, S Blot, S Hernández-Allés, S Hernández-Allés, S Nekolla, S Vidal, S Vidal, SF Epp, SM Bezrukov, SM Bezrukov, SR Norrby, SW Cowan, T Ferenci, T Mach, UO Hasdemir, V Simonet, V Simonet, WL Veal, WM Shafer, WR Bauer, XZ Li   +95 more
core   +1 more source

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

FEMS 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

Detection of an IS21 insertion sequence in the mexR gene of Pseudomonas aeruginosa increasing β-lactam resistance [PDF]

FEMS Microbiology Letters, 2004
To understand the regulation of the MexAB OprM efflux system in a clinical strain of Pseudomonas aeruginosa presenting a decreased susceptibility to ticarcillin and aztreonam, the mexR repressor gene was amplified by polymerase chain reaction (PCR) and was shown to be disrupted by an insertion sequence of more than 2 kb, with characteristic direct and ...
Boutoille, David, Corvec, Stéphane, Caroff, Nathalie, Giraudeau, Cécile, Espaze, Eric, Caillon, Jocelyne, Plesiat, Patrick, Reynaud, Alain   +7 more
openaire   +2 more sources

Reversible inactivation of a peptidoglycan transpeptidase by a β-lactam antibiotic mediated by β-lactam-ring recyclization in the enzyme active site

Scientific Reports, 2017
β-lactam antibiotics act as suicide substrates of transpeptidases responsible for the last cross-linking step of peptidoglycan synthesis in the bacterial cell wall.
Zainab Edoo, Michel Arthur, Jean-Emmanuel Hugonnet   +2 more
doaj   +1 more source

FtsH Sensitizes Methicillin-Resistant Staphylococcus aureus to β-Lactam Antibiotics by Degrading YpfP, a Lipoteichoic Acid Synthesis Enzyme

Antibiotics, 2021
In the Gram-positive pathogen Staphylococcus aureus, FtsH, a membrane-bound metalloprotease, plays a critical role in bacterial virulence and stress resistance.
Won-Sik Yeo, Bohyun Jeong, Nimat Ullah, Majid Ali Shah, Amjad Ali, Kyeong Kyu Kim, Taeok Bae   +6 more
doaj   +1 more source

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