Results 31 to 40 of about 109,585 (312)

Detection of cfxA2, cfxA3, and cfxA6 genes in beta-lactamase producing oral anaerobes

Journal of Applied Oral Science, 2016
Purpose The aim of this study was to identify β-lactamase-producing oral anaerobic bacteria and screen them for the presence of cfxA and BlaTEM genes that are responsible for β-lactamase production and resistance to β-lactam antibiotics.
Buhle BINTA, Mrudula PATEL
doaj   +1 more source

Old and New Beta-Lactamase Inhibitors: Molecular Structure, Mechanism of Action, and Clinical Use

Antibiotics, 2021
The β-lactams have a central place in the antibacterial armamentarium, but the increasing resistance to these drugs, especially among Gram-negative bacteria, is becoming one of the major threats to public health worldwide.
Davide Carcione, Claudia Siracusa, Adela Sulejmani, Valerio Leoni, Jari Intra   +4 more
doaj   +1 more source

Mutation of serine residue 318 in the class C β-lactamase ofEnterobacter cloacae908R [PDF]

FEMS Microbiology Letters, 1992
The involvement of the serine residue 318 in the specificity of a class C β-lactamase was investigated. Multiple site-directed mutants at this position were generated using a polymerase chain reaction technique. These mutants were then probed for their activity towards various β-lactam compounds.
Christine Jacobs, Alain Dubus, Didier Monnaie, Staffan Normark, Jean-Marie Frère   +4 more
openaire   +1 more source

Molecular Docking Approach of Viscosin as Antibacterial for Methicillin-resistant Staphylococcus Aureus Via β-Lactamase Inhibitor Mechanism

Clinical and Research Journal in Internal Medicine, 2021
Background: β-lactamase is an enzyme that plays a role in the occurrence of antibiotic resistance against Methicillin-resistant Staphylococcus aureus (MRSA) bacteria. Viscosin is a lipopeptide biosurfactant produced by the Pseudomonas group bacteria.
Mokhamad Fahmi Rizki Syaban, Nabila Erina Erwan, Muhammad Rafif Raihan Syamsuddin, Fatimah Az Zahra, Faradilah Lukmana Sabila   +4 more
openaire   +1 more source

Draft Genome Sequences of Four NDM-1-Producing Klebsiella pneumoniae Strains from a Health Care Facility in Northern California. [PDF]

, 2015
We report the draft genome sequences of Klebsiella pneumoniae strains from four patients at a northern California health care facility. All strains contained the New Delhi metallo-β-lactamase (NDM1) carbapenemase with extended antibiotic resistance ...
Chaturvedi, Vishnu, Chorny, Ilya, Greninger, Alexander L, Knowles, Susan, Ng, Valerie L   +4 more
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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
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Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea

Life, 2020
β-lactam antibiotics have a well-known activity which disturbs the bacterial cell wall biosynthesis and may be cleaved by β-lactamases. However, these drugs are not active on archaea microorganisms, which are naturally resistant because of the lack of β ...
Seydina M. Diene, Lucile Pinault, Nicholas Armstrong, Said Azza, Vivek Keshri, Saber Khelaifia, Eric Chabrière, Gustavo Caetano-Anolles, Jean-Marc Rolain, Pierre Pontarotti, Didier Raoult   +10 more
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In Silico Assigned Resistance Genes Confer Bifidobacterium with Partial Resistance to Aminoglycosides but Not to Β-Lactams [PDF]

, 2013
peer-reviewedBifidobacteria have received significant attention due to their contribution to human gut health and the use of specific strains as probiotics.
Cotter, Paul D., Fitzgerald, Gerald F, Fouhy, Fiona, O'Connell-Motherway, Mary, Ross, R Paul, STANTON, CATHERINE, van Sinderen, Douwe   +6 more
core   +3 more sources

Genotypic detection of β-lactamase-producing Escherichia coli isolates obtained from Seven Crater Lakes of San Pablo, Laguna, Philippines

Journal of Water and Health, 2023
The extended-spectrum β-lactamase (ESBL)-producing Escherichia coli is becoming a global public health concern. More comprehensive surveillance of β-lactam resistance in E.
Diana Rose D. Mamawal, Jonah David V. Calayo, Kherson P. Gandola, Mae Ashley G. Nacario, Mark Raymond A. Vejano, Laurice Beatrice Raphaelle O. dela Peña, Windell L. Rivera   +6 more
doaj   +1 more source

Nucleotide sequence of the gene encoding the active-site serine β-lactamase fromStreptomyces cacaoi [PDF]

FEMS Microbiology Letters, 1988
Abstract The gene encoding the extracellular active-site serine β-lactamase of Streptomyces cacaoi previously cloned into Streptomyces lividans , has the information for the synthesis of a 303 amino-acid precursor. The β-lactamase as excreted by the host S.
Mauro V. Lenzini, Hiroshi Ishihara, Jean Dusart, Hiroshi Ogawara, Bernard Joris, Jozef Beeumen, Jean-Marie Frère, Jean-Marie Ghuysen   +7 more
openaire   +1 more source