Results 121 to 130 of about 905,435 (191)

Functional dynamics of water in New Delhi metallo-β-lactamase catalysis. [PDF]

Protein Sci
Kandhan P, Xiong C, Palzkill T, Tao P.
europepmc   +1 more source

Rising Incidence of New Delhi Metallo-β-Lactamase-Producing Carbapenem-Resistant Enterobacterales, 10 US Sites, 2018-2023. [PDF]

Open Forum Infect Dis
Duffy N, Campbell D, Li R, Brandenburg J, Ansari U, Kent AG, Nadle J, Hoetzer K, Johnston H, Driscoll J, Czaja C, Maloney M, Jacob JT, Smith G, Vaeth E, Wilson LE, Tourdot L, Gross A, Malley SO, Lynfield R, Dumyati G, Looi HC, Tellerman J, Hoffman MR, Flores KG, Hertzel H, Muleta D, Wilson CD, Karlsson M, Gargis AS, Guh AY.   +30 more
europepmc   +1 more source

Molecular Detection of Metallo-β-Lactamase-Encoding Genes in the Clinical Isolates of Acinetobacter baumannii: A Prospective Cross-Sectional Study at a Tertiary Care Center. [PDF]

Cureus
Gupta A, Chintala N, Lakshmi J.
europepmc   +1 more source

Development of novel phosphonic acid-type metallo-β-lactamase inhibitors

The Global Antibiotic Research & Development Partnership (GARDP) estimates that antibiotic resistance claims one life in every 6 seconds. Antibiotic resistance is already associated with 5 million deaths annually, and this number continues to rise. A
Rosenström, Ulrika,, Erdélyi, Máté,, Gulyás, Kinga Virág,   +2 more
core  

Beyond β-Lactams: Defining the Role of Eravacycline in Multidrug-Resistant and Metallo-β-Lactamase-Producing Infections. [PDF]

Antibiotics (Basel)
Keck JM.
europepmc   +1 more source

Phase I dose-ascending, safety, and pharmacokinetics study of APC148, a novel metallo-β-lactamase inhibitor, in healthy volunteers. [PDF]

Antimicrob Agents Chemother
Bolstad B, Hovland R, Bylund J, Rein-Hedin E, Kuusk S, Klem B, Rongved P.   +6 more
europepmc   +1 more source

Structure based drug design: the discovery of novel inhibitors active against New Delhi Metallo-β-lactamase-1

, 2017
Background. The emergence of bacterial strains resistant to available antibiotic armamentarium is nowadays a pressing issue in clinical therapy. Among the several mechanisms of bacterial resistance, the rapid evolution and spread of carbapenemases, β ...
Cross, Simon, Perilli, Mariagrazia, Celenza, Giuseppe, Cendron, Laura, TONDI, Donatella, Bellio, Pierangelo, SPYRAKIS, FRANCESCA, Marcoccia, Francesca   +7 more
core  

Management of metallo-β-lactamase-producing Enterobacterales infections: a modified Delphi study. [PDF]

JAC Antimicrob Resist
Carmeli Y, Price M, Daikos GL, Falcone M, Gales AC, Hagel S, Omrani AS, Ramirez P, Todi S, Wang M, Gheorghe M, Hauber B, Little CJ, Townsend A.   +13 more
europepmc   +1 more source

Chelate-conjugated β-lactams resensitize metallo-β-lactamase IMP-1-producing gram-negative bacteria against carbapenem antibiotics. [PDF]

Microbiol Spectr
Toyomoto T, Ono K, Honda H, Zhang T, Tsutsuki H, Uegama A, Fukushima R, Yamamoto K, Tanaka Y, Nakburee K, Kaewkong W, Tsugawa H, Sawa T.   +12 more
europepmc   +1 more source

Lanthipeptides from <i>Chitinophaga pinensis</i> re-potentiating β-lactams against metallo-β-lactamase-producing Enterobacterales <i>in vitro</i>. [PDF]

Microbiol Spectr
Lambropoulou A, Herrmann J, Deschner F, Müller R, Kotsakis SD.   +4 more
europepmc   +1 more source