Results 111 to 120 of about 893,574 (181)

Investigation of the prevalence and role of mobile genetic elements associated with an aminoglycoside resistance gene, aacC2a, in Acinetobacter baumannii [PDF]

, 2009
Includes abstract. Includes bibliographical references (leaves 115-141)
Jongwe, Tsungai Ivai
core   +1 more source

High in vitro activity of aztreonam/avibactam against NDM-producing Enterobacterales with emerging resistance in Escherichia coli in the United States Mid-Atlantic region

Microbiology Spectrum
New Delhi metallo-β-lactamase (NDM)-producing Enterobacterales represent a critical antimicrobial resistance threat with limited therapeutic options. Aztreonam/avibactam, which combines the stability of aztreonam against metallo-β-lactamases with the ...
Eetu Eklund, Tyler Maruca, Kate Kruczynski, Heather Critchfield, Robert Murphy, Eric Keller, Benjamin Lee, Ami Patel, Liore Klein, David A. Torpey, Robert A. Myers, Victoria L. Campodónico   +11 more
doaj   +1 more source

Poster Sessions

HemaSphere, Volume 10, Issue S1, June 2026.
wiley   +1 more source

An Evaluation of Beta-Lactamase Prevalence and the Increasing Incidence of MBL in Gram-Negative Bacteria

Online Journal of Health & Allied Sciences
Purpose: β-lactamase mediated resistance mechanisms in gram-negative bacteria play a pivotal role in spreading antimicrobial resistance. We conducted this study to understand the prevalence of β-lactamases in Gram-negative bacteria in our region ...
Amrita Joshi, Suhas Nirkhiwale, Sheetal Bhasin, Aparna Tripathi   +3 more
doaj  

Structure, function, and evolution of metallo-β-lactamases from the B3 subgroup-emerging targets to combat antibiotic resistance. [PDF]

Front Chem, 2023
Krco S, Davis SJ, Joshi P, Wilson LA, Monteiro Pedroso M, Douw A, Schofield CJ, Hugenholtz P, Schenk G, Morris MT.   +9 more
europepmc   +1 more source

Resistance of Gram-Negative Bacteria to Cefepime-Enmetazobactam: A Systematic Review

Pathogens
Cefepime-enmetazobactam is a novel β-lactam/β-lactamase inhibitor combination showing good activity against multidrug-resistant (MDR) Gram-negative bacteria producing a variety of β-lactamases.
Matthew E. Falagas, Laura T. Romanos, Dimitrios S. Kontogiannis, Katerina Tsiara, Stylianos A. Kakoullis   +4 more
doaj   +1 more source

Correction: 2-Mercaptomethyl-thiazolidines use conserved aromatic-S interactions to achieve broad-range inhibition of metallo-β-lactamases. [PDF]

Chem Sci, 2023
Rossi MA, Martinez V, Hinchliffe P, Mojica MF, Castillo V, Moreno DM, Smith R, Spellberg B, Drusano GL, Banchio C, Bonomo RA, Spencer J, Vila AJ, Mahler G.   +13 more
europepmc   +1 more source

Structural insights into the substrate specificity of IMP-6 and IMP-1 metallo-β-lactamases. [PDF]

J Biochem, 2022
Yamamoto K, Tanaka H, Kurisu G, Nakano R, Yano H, Sakai H.   +5 more
europepmc   +1 more source

Metallo-β-lactamases immobilized by magnetic zeolitic imidazolate frameworks-8 for degradation of β-lactam antibiotics in an aqueous environment. [PDF]

RSC Adv, 2023
Wang Q, Sun Y, Zhao S, Bai C, Cong Z, Dong Y, Wang T.   +6 more
europepmc   +1 more source

Probing the Role of Asn 152 in the Class C β-lactamase AmpC [PDF]

, 2012
AmpC, a class C β-lactamase, is a main cause of antibiotic resistance to cephalosporins in many species of bacteria. The current proposed mechanism of action involves an acyl-intermediate, where the enzyme becomes covalently attached to the drug at ...
Powers, Rachel, Leonard, David, Anwar, Mujahid, Docter, Brianne, Wallar, Bradley   +4 more
core