Results 21 to 30 of about 19,930 (199)

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

Production of metallo-β-lactamase among Pseudomonas aeruginosa strains isolated in the State of Sergipe, Brazil

Revista da Sociedade Brasileira de Medicina Tropical, 2015
INTRODUCTION: Acquired production of metallo-β-lactamases is an important mechanism of resistance in Pseudomonas aeruginosa. The objective of this study was to investigate the production of metallo-β-lactamase and the genetic diversity among ceftazidime ...
Lívia Maria do Amorim Costa, Maria Emília de Castro Kling Fleming, Geraldo Renato de Paula, Lenise Arneiro Teixeira, Pedro Juan José Mondino, Sílvia Susana Bona de Mondino, Cláudia Rezende de Vieira Mendonça-Souza   +6 more
doaj   +1 more source

Detection of bla NDM-1 Encoding Imepenemase among the Imipenem-Resistant Gram-Negative Bacilli Isolated from Various Clinical Samples at a Tertiary Care Hospital of Eastern Nepal: A Descriptive Cross-Sectional Study

International Journal of Microbiology, 2020
Background. Carbapenem resistance among Gram-negative isolates caused by the production of the metallo-β-lactamase (MBL) enzyme is being increasingly reported worldwide. One of the newly emerged metallo-β-lactamases is New Delhi metallo-β-lactamase. Data
S. Gautam, N. R. Bhattarai, K. Rai, A. Poudyal, B. Khanal   +4 more
doaj   +1 more source

Occurrence of a new metallo-β-lactamase IMP-4 carried on a conjugative plasmid inCitrobacter youngaefrom the People's Republic of China [PDF]

FEMS Microbiology Letters, 2001
During the course of an antimicrobial resistance surveillance programme in Guangzhou, the People's Republic of China, single strains of Citrobacter youngae and Pseudomonas aeruginosa were identified which were resistant to imipenem and found to carry the carbapenemase gene bla(IMP).
P M, Hawkey, J, Xiong, H, Ye, H, Li, F H, M'Zali   +4 more
openaire   +2 more sources

Biochemical characterization of the carbapenem-hydrolyzing β-lactamase AsbM1 fromAeromonas sobriaAER 14M: a member of a novel subgroup of metallo-β-lactamases [PDF]

FEMS Microbiology Letters, 1996
AsbM1, a carbapenem-hydrolyzing beta-lactamase produced by Aeromonas sobria AER 14M, was purified chromatographically, with anion exchange chromatography performed in the absence of Zn2+. The molecular mass of AsbM1 was approximately 34,000; the isoelectric point was 9.1.
Y, Yang, K, Bush
openaire   +2 more sources

antimicrobial effects of aztreonam, colistin, and the 3-drug combination of aztreonam, ceftazidime and amikacin on metallo--lactamase-producing [PDF]

, 2009
Background There are limited choice of antimicrobial agents to treat infection with metallo-β-lactamase-producing Pseudomonas aeruginosa. We evaluate the antimicrobial effects of aztreonam alone, colistin alone and the 3-drug combination of aztreonam ...
Shigeharu Oie, Yumi Fukui, Masaya Yamamoto, Yuki Masuda, Akira Kamiya, M Thuong, SR Lockhart, GM Rossolini, JA Karlowsky, DM Livermore, J Garberding, D Sofianou, S Oie, S Oie, K Maeda, TR Walsh, N Sibata, BE Murray, National Committee for Clinical Laboratory Standards, CJ Soussy, EJ Giamarellos-Bourboulis, S Rochon-Edouard, EJ Giamarellos-Bourboulis, HO Hallander, BA Rasmussen, S Bellais, H Horimoto, M Mizuta, L Drago, YH Chen, EJ Giamarellos-Bourboulis, AA Gerceker, D Berlana, F Timurkaynak, PK Linden, AS Levin, ME Evans   +36 more
core   +1 more source

Prevalence and detection of Stenotrophomonas maltophilia carrying metallo-β-lactamase blaL1 in Beijing, China [PDF]

Frontiers in Microbiology, 2014
Intrinsic β-lactam resistance in Stenotrophomonas maltophilia is caused by bla L1 and/or bla L2, a kind of metallo-β-lactamase with a broad substrate spectrum including carbapenems. A rapid and sensitive molecular method for the detection of bla L1 in clinical samples is needed to guide therapeutic treatment. In present study, we first described a loop-
Zhan eYang, Wei eLiu, Qian eCui, Qian eCui, Wen Kai Niu, Huan eLi, Xiang Na Zhao, Xiao eWei, Xue Song Wang, Si Mo Huang, De Rong Dong, Si Jing Lu, Chang Qing Bai, Yan eLi, Liu Yu Huang, Jing eYuan   +15 more
openaire   +3 more sources

\u3cem\u3eArabidopsis thaliana\u3c/em\u3e GLX2-1 Contains a Dinuclear Metal Binding Site, but Is Not a Glyoxalase 2 [PDF]

, 2009
In an effort to probe the structure and function of a predicted mitochondrial glyoxalase 2, GLX2-1, from Arabidopsis thaliana, GLX2-1 was cloned, overexpressed, purified and characterized using metal analyses, kinetics, and UV–visible, EPR, and 1H-NMR ...
Bennett, Brian, Crowder, Michael W., Limphong, Pattraranee, Makaroff, Christopher A.   +3 more
core   +2 more sources

Detection of metallo-β-lactamase gene blaIMP of Escherichia coli clinical isolates in Sanglah General Hospital Bali

Indonesia Journal of Biomedical Science, 2019
Background: Escherichia coli belong to the family of Enterobacteriaceae that are responsible as one of the leading cause of nosocomial infections. The emergence of Carbapenem-resistant Enterobacteriaceae presents therapeutic challenges for clinicians on choosing the correct type of antibiotics to prescribe.
Muhammad Ardi Afriansyah, Ni Nyoman Sri Budayanti, Komang Januartha Putra Pinatih   +2 more
openaire   +1 more source

Molecular characterization ofbla_IMP-5, a new integron-borne metallo-β-lactamase gene from anAcinetobacter baumanniinosocomial isolate in Portugal [PDF]

FEMS Microbiology Letters, 2002
Acinetobacter baumannii 65FFC, an imipenem-resistant clinical strain, isolated from the urine of a patient at the Coimbra University Hospital, Portugal, in 1998, produced a metallo-beta-lactamase with a calculated pI 9.3. The isolate was highly resistant to penicillins, broad-spectrum cephalosporins, including ceftazidime, ceftriaxone, cefepime ...
Da Silva, GJ, Correia, M, Vital, C, Ribeiro, G, Sousa, JC, Leitao, R, Peixe, L, Duarte, A   +7 more
openaire   +3 more sources