Results 191 to 200 of about 17,864 (222)
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Carbapenemases: a worldwide threat

Expert Review of Anti-infective Therapy, 2013
β-lactam antibiotics remain one of our workhorse classes for serious infection due to their usually broad activity and attractive safety profile.
openaire   +2 more sources

Rapid LC–MS/MS detection of different carbapenemase types in carbapenemase-producing Enterobacterales

European Journal of Clinical Microbiology & Infectious Diseases, 2022
Klebsiella pneumoniae carbapenemase (KPC)-2, metallo-beta-lactamases (MBL), and oxacillinase (OXA)-48-like carbapenemases are considered the most important carbapenemases. In vitro studies have demonstrated that the carbapenemase activity of KPC-2 and MBL can be inhibited by 3-aminophenylboronic acid and ethylenediaminetetraacetic acid (EDTA ...
Gen Li   +8 more
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Detection systems for carbapenemase gene identification should include the SME serine carbapenemase

International Journal of Antimicrobial Agents, 2013
Carbapenemase detection has become a major problem in hospitals that encounter outbreaks of infections caused by carbapenem-resistant Gram-negative bacteria. Rapid detection systems have been reported using multiplex PCR analyses and DNA microarray assays.
Karen, Bush   +7 more
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Development and evaluation of the method for detecting metallo-carbapenemases among carbapenemase-producing Enterobacteriaceae

Journal of Microbiological Methods, 2019
A simple EDTA synergistic carbapenem inactivation method (esCIM) based on the simplified carbapenem inactivation method (sCIM) and EDTA synergistic carbapenem inactivation test (eCIM) detected the levels of metallo-β-lactamases (MBLs) carbapenemase.
Quanfeng, Liao   +9 more
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Clinically significant carbapenemases: an update

Current Opinion in Infectious Diseases, 2008
To provide a brief synopsis of studies which have extended our understanding of carbapenem resistance in clinical isolates in terms of epidemiology, mechanism of action and genetic factors affecting their carriage and spread.Studies published in the last 18 months continue to confirm that VIM-2 is the dominant metallo-beta-lactamase in Pseudomonas ...
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Carbapenemases: a problem in waiting?

Current Opinion in Microbiology, 2000
Carbapenems are stable to most prevalent beta-lactamases, and chromosomal carbapenemases are restricted to Stenotrophomonas maltophilia, to a few Bacteroides fragilis, and to rare pathogens. Nevertheless, an acquired metallo-beta-lactamase called IMP-1 is beginning to emerge in Pseudomonas aeruginosa and Enterobacteriaceae isolates in Japan, and has ...
D M, Livermore, N, Woodford
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[Carbapenemases in enterobacteriaceae].

Archives de pediatrie : organe officiel de la Societe francaise de pediatrie, 2011
Carbapenem-hydrolyzing beta-lactamases are the most powerful mechanism of resistance to carbapenems. Carbapenemases have been reported extensively worldwide now in Enterobacteriaceae. Carbapenemases of the KPC type have been reported first from the USA in Klebsiella pneumoniae, then worldwide with a marked endemicity in Israel and Greece.
P, Nordmann, A, Carrer
openaire   +1 more source

[Carbapenemases in Pseudomonas spp].

Enfermedades infecciosas y microbiologia clinica, 2010
Pseudomonas aeruginosa is one of the most relevant nosocomial pathogens, as well as one of the main causes of chronic respiratory infections in patients with underlying diseases such as cystic fibrosis or chronic obstructive pulmonary disease. The high intrinsic antibiotic resistance of this pathogen, together with its extraordinary capacity for ...
Carlos, Juan Nicolau, Antonio, Oliver
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[ESBL and carbapenemases in Enterobacteriaceae].

Revue medicale suisse, 2015
Carbapenemase-producing enterobacteria (CPE) spread all over the world during the last years, causing serious infections with increasing frequency. Very few new drugs active against CPE are expected to be clinically available. Studies summarized in this review show that there is yet room to improve our therapeutic approaches, in the treatment of ...
A, Cherkaoui   +5 more
openaire   +1 more source

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