Results 31 to 40 of about 905,435 (191)

Epidemiology of extended-spectrum β-lactamase and metallo-β-lactamase-producing Escherichia coli in South Asia

open access: yes, 2021
Aim: To determine the prevalence of extended-spectrum β-lactamase (ESBL) and metallo-β-lactamase (MBL)-producing Escherichia coli in South Asia. Methodology: A systematic review and meta-analysis of data published in PubMed, EMBASE, Web of Science and ...
Hassen Chowdhury, Mohammed Abdul   +6 more
core   +1 more source

Phenotypic Characterization of Multidrug-resistant Escherichia Coli with Special Reference to Extended-spectrum-beta-lactamases and Metallo-beta-lactamases in a Tertiary Care Center

open access: yesJournal of Nepal Medical Association, 2015
Introduction: The increasing reports on extended-spectrum-beta-lactamase and metallo-betalactamase producing Escherichia coli have addressed a potential threat to global health since it is found to be highly resistance to most of the currently available ...
Basudha Shrestha   +9 more
doaj   +3 more sources

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

open access: yesFEMS 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   +7 more
openaire   +3 more sources

Isothermal Titration Calorimetric Studies of Complexation Reactions [PDF]

open access: yes
The objective of this work has been to study the binding of metal ions to complex ligands expressing two or more metal binding sites, in terms of the thermodynamics of the binding events, and to use this information to contribute to the understanding of ...
Motara, Hasina
core   +3 more sources

Molecular heterogeneity ofblaVIM-2-containing integrons fromPseudomonas aeruginosaplasmids encoding the VIM-2 metallo-β-lactamase [PDF]

open access: yesFEMS Microbiology Letters, 2001
A bla(VIM-2) metallo-beta-lactamase determinant, identical to that previously identified in Pseudomonas aeruginosa COL-1 isolate from a French hospital, was detected on a 28-kb plasmid carried by a nosocomial isolate of P. aeruginosa from Verona, Italy.
PALLECCHI L.   +4 more
openaire   +4 more sources

Table_5_Increased zinc levels facilitate phenotypic detection of ceftazidime-avibactam resistance in metallo-β-lactamase-producing Gram-negative bacteria.docx

open access: yes, 2022
Ceftazidime-avibactam is one of the last resort antimicrobial agents for the treatment of carbapenem-resistant, Gram-negative bacteria. Metallo-β-lactamase-producing bacteria are considered to be ceftazidime-avibactam resistant. Here, we evaluated a semi-
Niels Pfennigwerth (5244080)   +10 more
core   +1 more source

Table_3_Increased zinc levels facilitate phenotypic detection of ceftazidime-avibactam resistance in metallo-β-lactamase-producing Gram-negative bacteria.docx

open access: yes, 2022
Ceftazidime-avibactam is one of the last resort antimicrobial agents for the treatment of carbapenem-resistant, Gram-negative bacteria. Metallo-β-lactamase-producing bacteria are considered to be ceftazidime-avibactam resistant. Here, we evaluated a semi-
Niels Pfennigwerth (5244080)   +10 more
core   +1 more source

Table_2_Increased zinc levels facilitate phenotypic detection of ceftazidime-avibactam resistance in metallo-β-lactamase-producing Gram-negative bacteria.docx

open access: yes, 2022
Ceftazidime-avibactam is one of the last resort antimicrobial agents for the treatment of carbapenem-resistant, Gram-negative bacteria. Metallo-β-lactamase-producing bacteria are considered to be ceftazidime-avibactam resistant. Here, we evaluated a semi-
Niels Pfennigwerth (5244080)   +10 more
core   +1 more source

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

open access: yesMicrobiome, 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   +7 more
doaj   +1 more source

Additional file 2: of Mortality related to Verona Integron-encoded Metallo-β-lactamase-positive Pseudomonas aeruginosa: assessment by a novel clinical tool

open access: yes, 2019
Updated Charlson index score. (DOCX 14 kb)
Persoon, Marjolein   +6 more
openaire   +1 more source

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