Results 51 to 60 of about 58,396 (229)

Spectroscopic and Mechanistic Studies of Heterodimetallic Forms of Metallo-β-lactamase NDM-1 [PDF]

, 2014
In an effort to characterize the roles of each metal ion in metallo-β-lactamase NDM-1, heterodimetallic analogues (CoCo-, ZnCo-, and CoCd-) of the enzyme were generated and characterized. UV–vis, 1H NMR, EPR, and EXAFS spectroscopies were used to confirm
Alyssa Hetrick, Ambler R. P., Amy R. Marts, Ankudinov A. L., Badarau A., Banci L., Bebrone C., Bennett B., Bertini I., Bertini I., Bertini I., Bertini I., Bicknell R., Bienvenue D. L., Bonomo R. A., Breece R. M., Brian Bennett, Carfi A., Copick A. J., Cricco J. A., Crisp J., Crowder M. W., Crowder M. W., David L. Tierney, Dennison C., Dennison C., deSeny D., Docobo-Perez F., Docquier J. D., Doi Y., Donaire A., Donaire A., Drawz S. M., Fernandez C. O., Fisher J. F., Garcia-Saez I., Garmer D. R., Garrity J. D., Garrity J. D., González J. M., Griffin D. H., Hao Yang, Hawk M. J., Hernandez V., Hu Z., Huang C. C., Huntington K. M., Kim Y., King D., Koh T. H., Kumarasamy K. K., Li T., Lisa M. N., Livermore D. M., Llarrull L. I., Llarrull L. I., Mahesh Aitha, McManus-Munoz S., Michael W. Crowder, Momb J., Orellano E. G., Papp-Wallace K. M., Park H., Periyannan G., Piccioli M., Prescott J. M., Reid T. S., Renault J. P., Riley E. A., Saini A., Salgado J., Sharma N., Sharma N. P., Spencer J., Stamper C., Strynadka N. C. J., Thakur P. K., Thomas P. W., Thomas P. W., Tioni M. F., Toney J. H., Ullah J. H., Vila A. J., Vila A. J., Wang Z., Wang Z., Worthington R. J., Xu D., Yamaguchi Y., Yang H., Yong D., Yuan Q., Zhang H., Zheng B., Zhu K.   +94 more
core   +3 more sources

New Delhi Metallo-β-Lactamase–producing Enterobacteriaceae, United States

Emerging Infectious Diseases, 2013
We characterized 9 New Delhi metallo-β-lactamase–producing Enterobacteriaceae (5 Klebsiella pneumoniae, 2 Escherichia coli, 1 Enterobacter cloacae, 1 Salmonella enterica serovar Senftenberg) isolates identified in the United States and cultured from 8 ...
J. Kamile Rasheed, Brandon Kitchel, Wenming Zhu, Karen F. Anderson, Nancye C. Clark, Mary Jane Ferraro, Patrice Savard, Romney M. Humphries, Alexander J. Kallen, Brandi M. Limbago   +9 more
doaj   +1 more source

New Delhi Metallo-β-Lactamase-5–Producing Escherichia coli in Companion Animals, United States

Emerging Infectious Diseases, 2020
We report isolation of a New Delhi metallo-β-lactamase-5–producing carbapenem-resistant Escherichia coli sequence type 167 from companion animals in the United States. Reports of carbapenem-resistant Enterobacteriaceae in companion animals are rare.
S. Cole, Laura Peak, G. Tyson, R. Reimschuessel, O. Ceric, S. Rankin   +5 more
semanticscholar   +1 more source

Conformational Dynamics of metallo-β-lactamase CcrA during Catalysis Investigated by Using DEER Spectroscopy [PDF]

, 2015
Previous crystallographic and mutagenesis studies have implicated the role of a position-conserved hairpin loop in the metallo-β-lactamases in substrate binding and catalysis.
Aitha, Mahesh, Bennett, Brian, Crowder, Michael W., Lorigan, Gary A., McCarrick, Robert, Moritz, Lindsay, Roche, Zahilyn, Sahu, Indra D., Sanyurah, Omar   +8 more
core   +2 more sources

Identification of 76 novel B1 metallo-β-lactamases through large-scale screening of genomic and metagenomic data

Microbiome, 2017
Background Metallo-β-lactamases are bacterial enzymes that provide resistance to carbapenems, the most potent class of antibiotics. These enzymes are commonly encoded on mobile genetic elements, which, together with their broad substrate spectrum and ...
Fanny Berglund, Nachiket P. Marathe, Tobias Österlund, Johan Bengtsson-Palme, Stathis Kotsakis, Carl-Fredrik Flach, D G Joakim Larsson, Erik Kristiansson   +7 more
doaj   +1 more source

In vitro activity of cefiderocol, a siderophore cephalosporin, against a recent collection of clinically relevant carbapenem-non-susceptible Gram-negative bacilli, including serine carbapenemase- and metallo-β-lactamase-producing isolates (SIDERO-WT-2014 Study).

International Journal of Antimicrobial Agents, 2019
Cefiderocol is a siderophore cephalosporin in development for treatment of infections caused by Gram-negative bacilli, including carbapenem-resistant and multidrug-resistant isolates.
K. Kazmierczak, M. Tsuji, M. Wise, M. Hackel, Y. Yamano, R. Echols, D. Sahm   +6 more
semanticscholar   +1 more source

Clinical Features and Outcomes of Bloodstream Infections Caused by New Delhi Metallo-β-Lactamase–Producing Enterobacterales During a Regional Outbreak

Open Forum Infectious Diseases, 2020
Limited data about New Delhi metallo-β-lactamase (NDM) bacteremia are available. Blood isolates from 40 patients with NDM bacteremia were studied for antibiotic susceptibility and whole-genomic sequencing. NDM bacteremia has high 30-day mortality.
M. Falcone, G. Tiseo, Alberto Antonelli, Cesira Giordano, V. di Pilato, Pietro Bertolucci, E. Parisio, A. Leonildi, N. Aiezza, Ilaria Baccani, E. Tagliaferri, L. Righi, S. Forni, S. Sani, M. T. Mechi, F. Pieralli, S. Barnini, G. Rossolini, F. Menichetti   +18 more
semanticscholar   +1 more source

Escherichia coli of sequence type 3835 carrying blaNDM-1, blaCTX-M-15, blaCMY-42 and blaSHV-12 [PDF]

, 2015
New Delhi metallo-β-lactamase (NDM) represents a serious challenge for treatment and public health. A carbapenem-resistant Escherichia coli clinical strain WCHEC13-8 was subjected to antimicrobial susceptibility tests, whole genome sequencing and ...
Feng, Y, McNally, A, Wang, X, Xie, Y, Yang, P, Zong, Z   +5 more
core   +1 more source

Prevalence of Imipenemase and Verona Integron-Encoded Metallo-β-Lactamase in Imipenem-Resistant Pseudomonas aeruginosa

Journal of Health Science and Medical Research (JHSMR), 2021
Objective: To determine the prevalence of metallo-β-lactamase (MBL) including imipenemase (IMP) and Verona integronencoded metallo-β-lactamase (VIM) in imipenem-resistant Pseudomonas aeruginosa (IRPA) isolates and investigate the in vitro activities of 9
Wanutsanun Tunyapanit, Pornpimol Pruekprasert, Kamolwish Laoprasopwattana, Sureerat Chelae   +3 more
doaj   +1 more source

Aztreonam plus Clavulanate, Tazobactam, or Avibactam for Treatment of Infections Caused by Metallo-β-Lactamase-Producing Gram-Negative Bacteria

Antimicrobial Agents and Chemotherapy, 2019
Metallo-β-lactamase (MBL)-producing Gram-negative bacteria are often extremely resistant, leading to a real therapeutic dead end. Here, we evaluated the in vitro and in vivo efficacy of aztreonam in combination with ceftazidime-avibactam, ceftolozane ...
C. Emeraud, L. Escaut, A. Boucly, N. Fortineau, R. Bonnin, T. Naas, L. Dortet   +6 more
semanticscholar   +1 more source