Results 91 to 100 of about 9,673 (155)

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

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  

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

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

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

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

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

Phenotypic and genotypic investigation of metallo-β-lactamases in Pseudomonas aeruginosa clinical isolates in Bushehr, Iran. [PDF]

Iran J Basic Med Sci, 2022
Seyedi M, Yousefi F, Naeimi B, Tajbakhsh S.   +3 more
europepmc   +1 more source

First report of SPM metallo-β-lactamases producing Acinetobacter baumannii isolates in Morocco. [PDF]

Iran J Microbiol, 2022
Massik A, Hibaoui L, Moussa B, Yahyaoui G, Oumokhtar B, Mahmoud M.   +5 more
europepmc   +1 more source

A STUDY OF METALLO-BETA-LACTATAMASE PRODUCING PSEUDOMONAS AERUGINOSA IN CLINICAL SAMPLES OF S.S.G. HOSPITAL

National Journal of Medical Research, 2011
Introduction: Pseudomonas spp. is common pathogen causing nosocomial infection. Acquired drug resistance is frequent in nosocomial isolates of Pseudomonas spp. Acquired metallo-β-lactamases (MBL) in pseudomonas spp.
Mehul S Chaudhari, Tanuja B Javadekar, Govind Ninama, Govind Ninama, Jivraj Damor   +4 more
doaj