Results 51 to 60 of about 1,672,197 (320)

Complete sequence of the IncA/C 1 plasmid pCf587 carrying bla PER-2 from citrobacter freundii [PDF]

open access: yes, 2018
The bla PER-2 -harboring plasmid pCf587 (191,541 bp) belongs to lineage IncA/C 1 and is closely related to pRA1. It contains a large resistance island including the bla PER-2 gene between two copies of ISKox2-like elements, the toxin-antitoxin module ...
Dabos, Laura   +5 more
core   +1 more source

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

open access: yesFEMS 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   +4 more
openaire   +1 more source

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

open access: yesClinical 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   +4 more
openaire   +1 more source

β-Lactamases and β-Lactamase Inhibitors in the 21st Century

open access: yesJournal of Molecular Biology, 2019
The β-lactams retain a central place in the antibacterial armamentarium. In Gram-negative bacteria, β-lactamase enzymes that hydrolyze the amide bond of the four-membered β-lactam ring are the primary resistance mechanism, with multiple enzymes ...
C. L. Tooke   +6 more
semanticscholar   +1 more source

Distribution and classification of Serine β-lactamases in Brazilian Hospital Sewage and Other Environmental Metagenomes deposited in Public Databases

open access: yesFrontiers in Microbiology, 2016
β-lactam is the most used antibiotic class in the clinical area and it acts on blocking the bacteria cell wall synthesis, causing cell death. However, some bacteria have evolved resistance to these antibiotics mainly due the production of enzymes known ...
Adriana Fróes   +3 more
doaj   +1 more source

Resistance to carbapenems in non-typhoidal Salmonella enterica serovars from humans, animals and food [PDF]

open access: yes, 2018
Non-typhoidal serovars of Salmonella enterica (NTS) are a leading cause of food-borne disease in animals and humans worldwide. Like other zoonotic bacteria, NTS have the potential to act as reservoirs and vehicles for the transmission of antimicrobial ...
Fernández, J.   +2 more
core   +3 more sources

Identification of Family Specific Fingerprints in β-Lactamase Families

open access: yesThe Scientific World Journal, 2014
Beta-lactamases are a superfamily of enzymes which degrade the β-lactam class of antibiotics. They are produced endogenously by the bacterial cells, which when exposed to the β-lactam class of antibiotics inactivate them by cleaving the β-lactam ring ...
Abhishikha Srivastava   +4 more
doaj   +1 more source

Metallo-β-Lactamases: Structure, Function, Epidemiology, Treatment Options, and the Development Pipeline

open access: yesAntimicrobial Agents and Chemotherapy, 2020
Modern medicine is threatened by the global rise of antibiotic resistance, especially among Gram-negative bacteria. Metallo-β-lactamase (MBL) enzymes are a particular concern and are increasingly disseminated worldwide, though particularly in Asia.
S. Boyd   +3 more
semanticscholar   +1 more source

Some aspects of general characteristic and classification of bacterial β-lactamases

open access: yesVìsnik Dnìpropetrovsʹkogo Unìversitetu: Serìâ Bìologìâ, Ekologìâ, 2009
Main structural and functional groups of bacterial β-lactamases are cited in the data review. Modern systems of classification, which was based on spectra of activity, sensitivity to inhibitors and peculiarities of molecular structure are described.
A. V. Krysenko   +2 more
doaj   +1 more source

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

open access: yesFEMS 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   +7 more
openaire   +1 more source

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