Academic literature on the topic 'METALLO-beta-LACTAMASE'

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Journal articles on the topic "METALLO-beta-LACTAMASE"

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Senda, K., Y. Arakawa, K. Nakashima, et al. "Multifocal outbreaks of metallo-beta-lactamase-producing Pseudomonas aeruginosa resistant to broad-spectrum beta-lactams, including carbapenems." Antimicrobial Agents and Chemotherapy 40, no. 2 (1996): 349–53. http://dx.doi.org/10.1128/aac.40.2.349.

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A total of 3,700 Pseudomonas aeruginosa isolates were collected from 17 general hospitals in Japan from 1992 to 1994. Of these isolates, 132 carbapenem-resistant strains were subjected to DNA hybridization analysis with the metallo-beta-lactamase gene (blaIMP)-specific probe. Fifteen strains carrying the metallo-beta-lactamase gene were identified in five hospitals in different geographical areas. Three strains of P. aeruginosa demonstrated high-level imipenem resistance (MIC, > or = 128 micrograms/ml), two strains exhibited low-level imipenem resistance (MIC, < or = 4 micrograms/ml), and the rest of the strains were in between. These results revealed that the acquisition of a metallo-beta-lactamase gene alone does not necessarily confer elevated resistance to carbapenems. In several strains, the metallo-beta-lactamase gene was carried by large plasmids, and carbapenem resistance was transferred from P. aeruginosa to Escherichia coli by electroporation in association with the acquisition of the large plasmid. Southern hybridization analysis and genomic DNA fingerprinting profiles revealed different genetic backgrounds for these 15 isolates, although considerable similarity was observed for the strains isolated from the same hospital. These findings suggest that the metallo-beta-lactamase-producing P. aeruginosa strains are not confined to a unique clonal lineage but proliferated multifocally by plasmid-mediated dissemination of the metallo-beta-lactamase gene in strains of different genetic backgrounds. Thus, further proliferation of metallo-beta-lactamase-producing strains with resistance to various beta-lactams may well be inevitable in the future, which emphasizes the need for early recognition of metallo-beta-lactamase-producing strains, rigorous infection control, and restricted clinical use of broad-spectrum beta-lactams including carbapenems.
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Shrestha, Basudha, Shovita Shrestha, Shyam Kumar Mishra, et al. "Phenotypic Characterization of Multidrug-resistant Escherichia Coli with Special Reference to Extended-spectrum-beta-lactamases and Metallo-beta-lactamases in a Tertiary Care Center." Journal of Nepal Medical Association 53, no. 198 (2015): 83–88. http://dx.doi.org/10.31729/jnma.2768.

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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 antibiotics including carbapenems. The present study was aimed to determine the antibiogram of extended-spectrum-beta-lactamase and metallo-beta-lactamase producing MDR E. coli isolates from various clinical samples.
 Methods: This was a cross-sectional study conducted over a period of seven months (December 2013 to July 2014) at bacteriology laboratory of Tribhuvan University Teaching Hospital. A total of 250 clinical specimens (urine, pus, sputum, blood, body fluid, bile, tissue and central venous pressure line tip) were processed from inpatients, with multidrug-resistant Escherichia coli infections. Standard microbiological techniques were used for isolation and identification of the isolates. The presence of extended-spectrum-beta-lactamase was detected by phenotypic confirmatory test recommended by Clinical and Laboratory Standards Institute and imipenem (IMP) /EDTA combined disc method was performed to detect metallo-beta-lactamase mediated resistance mechanism.
 Results: We found high level of beta lactamase mediated resistance mechanism as part of multidrug resistance. Among 250 MDR isolates, 60% isolates were extended-spectrum-beta-lactamase producers and 17.2% isolates were metallo-beta-lactamase producers. Co-existence of extended-spectrum-betalactamase and metallo-beta-lactamase identified in 6.8% isolates.
 Conclusions: Beta-lactamase mediated resistance mechanisms are accounting very high in the multidrug resistant isolates of E. coli. Therefore, early detection of beta lactamase mediated resistant strains and their current antibiotic susceptibility pattern is necessary to avoid treatment failure and prevent the spread of MDR. 
 Keywords: e. coli; extended-spectrum-β-lactamase; metallo-β-lactamase; multidrug-resistance.
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Smail, Sakar Bakr, and Kamal I. AL-OTRACHI. "Phenotypic Characterization of Extended-Spectrum Beta-Lactamases and Metallo-Beta-Lactamase of Multi Drug Resistant Acinetobacter baumannii Causing Nosocomial Infections in Erbil City." Al-Mustansiriyah Journal of Science 30, no. 4 (2020): 51. http://dx.doi.org/10.23851/mjs.v30i4.671.

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Background: Resistance to broad‑spectrum beta‑lactams, mediated by extended‑spectrum beta‑lactamases, and metallo‑beta‑lactamase enzymes, is an increasing problem worldwide. The main aim is to study phenotypic characterization of extended‑spectrum beta‑lactamases and metallo‑beta‑lactamase multidrug resistant Acinetobacter baumannii in Erbil City. Materials and Methods: A total of 112 Acinetobacter baumannii isolations were collected from patients of all age groups from clinical specimens sputum, blood, pus, wound swab, urine and body fluids (Pleural fluid and cerebrospinal fluid) collected from different medical wards and intensive care unit departments of hospitals in Erbil City for a period of one year from march 2018--march 2019. Isolates were tested for the presence of extended‑spectrum beta‑lactamases and metallo‑beta‑lactamase. Detection of extended‑spectrum beta‑lactamases was done by the combined disk diffusion method according to Clinical and Laboratory Standards Institute guidelines, while metallo‑beta‑lactamase was detected by meropenem and imipenem combined with ethylenediaminetetraacetic acid disk method. Results: 25% (28) Acinetobacter baumannii isolates were positive for extended‑spectrum beta‑lactamases, while 100 % (112) were metallo‑beta‑lactamase producers. Conclusion: Acinetobacter baumannii is becoming a global medical challenge due to the emergence of multi-drug resistance. Newer beta lactamase is a matter of concern as they are developing rapidly and lead to treatment failure. Carbapenems are known to be effective therapeutic agents for Acinetobacter baumannii infections and its resistance limits the use to polymyxins and colistin. Several new medicines are still in research and combination of drug therapy is being currently used in the hospitals together with ours to treat multidrug resistant Acinetobacter baumannii infections.
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Osipov, V. A., and D. V. Tapalskiy. "LOCAL FEATURES AND PHENOTYPES OF ANTIBIOTIC RESISTANCE OF <i>PSEUDOMONAS AERUGINOSA</i>." Health and Ecology Issues, no. 3 (September 28, 2012): 102–7. http://dx.doi.org/10.51523/2708-6011.2012-9-3-19.

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Objective : to estimate the resistance prevalence of P. aeruginosa to antipseudomonal antibiotics and reveal metallo-beta-lactamases producers among carbapenem resistant clinical isolates. Materials and methods. The subject of the study is clinical isolates of P. aeruginosa resistant to antibacterial drugs. The resistance of P. aeruginosa clinical isolates to antipseudomonal antibiotics was estimated, antimicrobial resistance phenotypes and associated resistance variants were analyzed, and production of metallo-beta-lactamases was detected using phenotypical screening method. Results. High levels of P. aeruginosa resistance to the most of antibacterial drugs, except carbapenems, were revealed. The local features of antimicrobial resistance in different hospitals were established. A total of 19 metallo-beta-lactamase producers were isolated in 6 hospitals of three republican regions. All metallo-beta-lactamase producers have the same phenotype, indicating of clonal prevalence. No carbapenem resistant isolates was resistant to colistin. Conclusion. It is necessary to carry out multi-facet research aimed at the detection of carbapenem resistance mechanisms and epidemiological marking of resistant isolates in order to reveal epidemically significant P.aeruginosa metallo-beta-lactamase producing clones in time and to develop the infection control measures to restrain its circulation.
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Upadhyay, Supriya, Malay Ranjan Sen, and Amitabha Bhattacharjee. "Presence of different beta-lactamase classes among clinical isolates of Pseudomonas aeruginosa expressing AmpC beta-lactamase enzyme." Journal of Infection in Developing Countries 4, no. 04 (2010): 239–42. http://dx.doi.org/10.3855/jidc.497.

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Introduction: Infections caused by Pseudomonas aeruginosa are difficult to treat as the majority of isolates exhibit varying degrees of beta-lactamase mediated resistance to most of the beta-lactam antibiotics. It is also not unusual to find a single isolate that expresses multiple β-lactamase enzymes, further complicating the treatment options. Thus the present study was designed to investigate the coexistence of different beta-lactamase enzymes in clinical isolates of P. aeruginosa. Methodology: A total of 202 clinical isolates of P. aeruginosa were tested for the presence of AmpC beta-lactamase, extended spectrum beta-lactamase (ESBL) and metallo beta-lactamase (MBL) enzyme. Detection of AmpC beta-lactamase was performed by disk antagonism test and a modified three-dimensional method, whereas detection of ESBL was done by the combined disk diffusion method per Clinical and Laboratory Standards Institute (CLSI) guidelines and MBL were detected by the Imipenem EDTA disk potentiation test. Results: A total of 120 (59.4%) isolates were confirmed to be positive for AmpC beta-lactamase. Among them, 14 strains (7%) were inducible AmpC producers. Co-production of AmpC along with extended spectrum beta-lactamase and metallo beta-lactamase was reported in 3.3% and 46.6% isolates respectively. Conclusion: The study emphasizes the high prevalence of multidrug resistant P. aeruginosa producing beta-lactamase enzymes of diverse mechanisms. Thus proper antibiotic policy and measures to restrict the indiscriminative use of cephalosporins and carbapenems should be taken to minimize the emergence of this multiple beta-lactamase producing pathogens.
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Poonam Loomba, Ashna Bhasin, Abha Sharma Bibhabati Mishra та Ashish Bajaj. "Coproduction of Extended Spectrum, AmpC and Metallo β- Lactamases in Pseudomonas aeruginosa Isolates from a Super Speciality Center". International Journal of Current Microbiology and Applied Sciences 10, № 10 (2021): 176–84. http://dx.doi.org/10.20546/ijcmas.2021.1010.020.

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Pseudomonas aeruginosa (P. aeruginosa) is one of the leading causes of hospital as well as community acquired infections. They’re strenuous to treat as most of isolates exhibit various degrees of beta- lactamase mediated resistance to majority of the beta-lactam antibiotics. Single isolate can express multiple β- lactamase enzymes, further limiting the treatment options. Therefore, this study was outlined to research the coexistence of various beta-lactamase enzymes in clinical isolates of P. aeruginosa. The aim of the study was to detect the co-prevalence of Extended Spectrum Beta lactmases (ESBL), AmpC and Metallo β-Lactamases (MBL) in Pseudomonas aeruginosa isolates from a superspeciality center. Fifty clinical isolates of P. aeruginosa were tested for the presence of AmpC beta-lactamase, extended spectrum beta- lactamase (ESBL) and metallo beta-lactamase (MBL) enzyme. Discernment of AmpC beta-lactamase was performed by disk antagonism while ESBL detection was done by the combined disk diffusion method as per Clinical and Laboratory Standards Institute (CLSI) guidelines and MBL were detected by the Imipenem EDTA disk potentiation test. Eleven of 50 (22%) isolates were confirmed to be positive for AmpC and Extended spectrum beta lactamases. Co-production of AmpC along side ESBL and MBL was reported in 12 % isolates. The study shows the high prevalence of multidrug resistant P. aeruginosa producing beta-lactamase enzymes of diverse mechanisms. Consequently, formulation of a correct antibiotic policy and taking measures to restrict the indiscriminative use of cephalosporins and carbapenems should be taken to mitigate the emergence of this multiple beta-lactamase producing pathogens.
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Ahsan, Sunjukta, and Riajul Islam. "Beta‐lactamase‐producing Escherichia coli in Bangladesh: Their phenotypic and molecular characteristics." Dhaka University Journal of Biological Sciences 28, no. 1 (2019): 71–81. http://dx.doi.org/10.3329/dujbs.v28i1.46494.

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The emergence and rapid dissemination of beta-lactamase-producing E. coli is now a worldwide problem. A total of 45 E. coli obtained from clinical specimens from a medical service centre in Dhaka were selected for this study. Test E. coli exhibited variable resistance to 3rd (71.7 - 97.8%, n = 48) and 4th (78%, n = 48) generation beta-lactam antibiotics, with 72% sensitivity to Carbapenem. Analysis of co-resistance indicated that 33.3% of E. coli (n = 48) were co-resistant to beta-lactams and ciprofloxacin. ESBL producers were predominant comprising of 84.7% E. coli. Among them, 22.7% contained blaTEM, 24.2% contained blaCTX-M, 4.3% contained blaSHV and 9.1% contained blaOXA-1 genes. A total of 25.75% isolates were metallo beta-lactamase producers. Of these, 1.5% of E. coli strains contained New Delhi metallo beta-lactamase gene and 6% contained AmpC gene. Multiple beta-lactamase genes were detected in some test isolates; 6.7% isolates contained 4, 20% contained 3 and 73.3% contained 2 beta lactamase genes. Fifty per cent of the E. coli contained plasmids of variable sizes. In addition, a total of 39% of the E. coli contained Class 1 integron. The increasing trend in beta-lactam resistance is of public health concern as it limits treatment regime and indicates to the need of continuous monitoring of resistance pattern.&#x0D; Dhaka Univ. J. Biol. Sci. 28(1): 71-81, 2019 (January)
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Ozer, Burcin, Muserref Tatman-Otkun, Dilek Memis, and Metin Otkun. "Characteristics of Pseudomonas aeruginosa isolates from intensive care unit." Open Medicine 4, no. 2 (2009): 156–63. http://dx.doi.org/10.2478/s11536-008-0090-2.

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AbstractThe study looked at the antimicrobial resistance patterns, serotypes, molecular types, metallo beta-lactamase, and chromosomal betalactamase enzymes of P. aeruginosa strains isolated from the patients and the staffs of the intensive care unit. P. aeruginosa isolates from the patients as nosocomial pathogens and from the staffs were evaluated for their susceptibilities to the antimicrobials by the disk diffusion and E-test methods. Metallo beta-lactamase enzymes were investigated by E-test, the inducibility of β - lactamase enzymes were detected by the disk antagonism test. Serotyping was performed by slide agglutination method. The P. aeruginosa isolates were typed by pulsed field gel electrophoresis. Twenty-five P. aeruginosa strains from the patients and three from the staffs were isolated. Fifteen P. aeruginosa, eleven of which composed of MDR bacteria, were found in serogroup E, 7 strains in G, 4 strains in B, and 1 strain in serogroup A. In all 12 bacteria in the MDR and serogroup E, metallo beta-lactamase enzyme was found to be positive. And in other 15 strains, except the bacterium which could not be serotyped, chromosomal beta-lactamase was found to be positive. The result of the molecular typing showed PFGE A pattern. In conclusion, a pattern in PFGE which included bacteria from MDR and serogroup E, G which was observed in the P. aeruginosa strains which was isolated from the staff’s hands and from the 5 patients, and PFGE F pattern were found to be observed the most. Finally, the two different clonal strains were found to be established in the intensive care.
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Felici, A., M. Perilli, N. Franceschini, et al. "Sensitivity of Aeromonas hydrophila carbapenemase to delta3-cephems: comparative study with other metallo-beta-lactamases." Antimicrobial Agents and Chemotherapy 41, no. 4 (1997): 866–68. http://dx.doi.org/10.1128/aac.41.4.866.

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Ceftriaxone and ceftriaxone S-oxide behaved as inactivators against the metallo-beta-lactamase of Aeromonas hydrophila AE036 and as substrates for the zinc beta-lactamase produced by Bacillus cereus (569/H/9) and Stenotrophomonas maltophilia ULA 511. Moreover, RO 09-1428, a catechol-cephalosporin, was not recognized by the A. hydrophila enzyme. Panipenem, cephalosporin C, cephalosporin C-gamma-lactone, and loracarbef were substrates for the three studied beta-lactamases.
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Payne, D. J., J. H. Bateson, B. C. Gasson, et al. "Inhibition of metallo-beta-lactamases by a series of mercaptoacetic acid thiol ester derivatives." Antimicrobial Agents and Chemotherapy 41, no. 1 (1997): 135–40. http://dx.doi.org/10.1128/aac.41.1.135.

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A series of mercaptoacetic acid thiol esters have been identified as metallo-beta-lactamase inhibitors. Electrospray mass spectrometry (ESMS) has shown that irreversible inhibition of the Bacillus cereus II metallo-beta-lactamase by SB214751, SB214752, and SB213079 was concomitant with a 90-Da increase in mass of the enzyme. Tryptic digestion of the B. cereus II inhibited with SB214751 illustrated that the peptide fragment, containing the only cysteine of the enzyme, had undergone a mass increment of 90 Da. It was further demonstrated that B. cereus II hydrolyzed this type of compound across the thiol ester bond to yield mercaptoacetic acid. Mercaptoacetic acid is the only molecular fragment common to SB214751, SB214752, and SB213079, and free mercaptoacetic acid does not bind covalently to B. cereus II. Therefore, it is concluded that these compounds inhibit B. cereus II by the mechanism-based delivery of mercaptoacetic acid, forming a disulfide linkage with the active sites cysteine (predicted mass shift = +90 Da) under the aerobic conditions of the assay. The different thiol esters examined had a broad range of potencies against the metallo-beta-lactamases tested. For example SB214751, SB214752, and SB213079 all had 50% inhibitory concentrations of &lt; 10 and &gt; 1,000 microM for the Stenotrophomonas maltophilia L-1 and Bacteroides fragilis CfiA enzymes, respectively. SB216968 was particularly active against the Aeromonas hydrophila CphA metallo-beta-lactamase and was found to be an uncompetitive inhibitor of this enzyme (Ki = 3.9 microM), whereas it exhibited irreversible inhibition of the L-1 enzyme. These observations with this series of compounds have revealed subtle differences between the active sites of different metallo-beta-lactamases. Finally, a novel application for isothermal titration calorimetry for assessing the zinc chelating activity of candidate inhibitors is also presented.
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Dissertations / Theses on the topic "METALLO-beta-LACTAMASE"

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Walter, Magnus Wilhelm. "Synthesis of metallo-#beta#-lactamase inhibitors." Thesis, University of Oxford, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.360013.

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Pauff, James. "Fluorescence properties of metallo-beta-lactamase L1." Miami University Honors Theses / OhioLINK, 2004. http://rave.ohiolink.edu/etdc/view?acc_num=muhonors1111003051.

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Bergstrom, Alexander R. "SPECTROSCOPIC AND MECHANISTIC STUDIES OF METALLO-BETA-LACTAMASE INHIBITORS AND THE STRUCTURE-FUNCTION RELATIONSHIP OF NEW DELHI METALLO-BETA-LACTAMASE VARIANTS." Miami University / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=miami1524154064246174.

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Periyannan, Gopal Raj. "Characterization of the metallo-[beta]-lactamase L1 from Stenotrophomonas maltophilia." Oxford, Ohio : Miami University, 2004. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=miami1099689034.

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Higgins, Catherine. "Analysis of the tetrameric metallo-#beta#-lactamase, L1, from Stenotrophomonas maltophilia." Thesis, University of Bristol, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.393011.

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Crawford, Patrick Anthony. "Characterization of ImiS, the metallo-[beta]-lactamase from Aeromonas veronii bv. sobria." Oxford, Ohio : Miami University, 2003. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=miami1069106986.

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Thesis (Ph. D.)--Miami University, Dept. of Chemistry and Biochemistry, 2003.<br>Title from first page of PDF document. Document formatted into pages; contains xi, 150 p. : ill. Includes bibliographical references.
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Hawk, Megan J. "Spectrocopic [sic] and mechanistic studies on metallo-[Beta]-lactamase Bla2 from Bacillus anthracis." Oxford, Ohio : Miami University, 2008. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=miami1229053358.

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Hu, Zhenxin. "Kinetic and spectroscopic studies of L1, the metallo-[beta]-lactamase from Stenotrophomonas maltophilia." Oxford, Ohio : Miami University, 2008. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=miami1218136291.

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Murphy, Deirdre M. "STUDIES OF THE METALLO BETA LACTAMASE CCrA FROM BACTERIODES FRAGILIS AND A DANSYLATED MONOCYCLIC BETA LACTAM (1-(5-DIMETHYLAMINO-1-NAPTHALENESULFONYL HYDRAZIDO)-3-ACETAMIDO-4-METHOXY-2-AZETIDINONE." University of Cincinnati / OhioLINK, 2001. http://rave.ohiolink.edu/etdc/view?acc_num=ucin990561318.

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Herron, Lissa. "Determining Which Tryptophan Residues Give Rise to Fluorescence Properties in the Metallo-Beta-Lactamase L1." Miami University Honors Theses / OhioLINK, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=muhonors1110916836.

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Books on the topic "METALLO-beta-LACTAMASE"

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Carenbauer, Anne Lynn. Site-directed mutagenesis of metallo- -lactamase L1 from Stenotrophomonas maltophilia. 2000.

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Carenbauer, Anne Lynn. Site-directed mutagenesis of metallo- -lactamase L1 from Stenotrophomonas maltophilia. 2000.

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Book chapters on the topic "METALLO-beta-LACTAMASE"

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McIntosh-Morgan, Venise, Karen Judith Roye-Green, Jasneth Mullings, Eberechi Patrick Akpaka, and Camille-Ann Thoms Rodriguez. "A Comprehensive Look at Carbapenemase-Producing Enterobacterales (CPE): An Urgent and Emerging Threat Posed by Carbapenemase Production." In Antimicrobial Resistance - New Insights [Working Title]. IntechOpen, 2025. https://doi.org/10.5772/intechopen.115305.

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In this chapter, we will explore and review published data on carbapenemase-producing Enterobacterales. Since the first published report of Klebsiella pneumoniae carbapenemase (KPC), other reports of carbapenemase enzymes have been reported globally and, by extension, from the English-speaking Caribbean. Several enzymes have been reported since the detection of KPC including oxacillinase (OXA)-48 like carbapenemase, Guiana extended-spectrum (GES) carbapenemase, New Delhi metallo-beta-lactamase (NDM), Verona integron-encoded metallo-beta-lactamase (VIM), and others. The ability to detect the carbapenemase enzyme is largely dependent on available infrastructure. Due to resource limitations, most centres have to rely on phenotypic tests and often are unable to describe at a molecular level the nature of the underlying carbapenemase genes. Regardless, in this report, we will do an extensive review of the literature to see what current reports are of these enzymes. This review will address the epidemiology and etiology of carbapenemase-producing Enterobacterales (CPE), a subset of carbapenem-resistant Enterobacterales (CRE); detection methods; management; and recommended treatments of CP-CRE and infection prevention and control (IPC) strategies for managing CP-CRE. The primary source of information will be through a review of published literature to date.
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Picoli, S. U., and A. L. S. Gonçalves. "Metallo-beta-lactamase producer Pseudomonas aeruginosa: an opportunistic pathogen in lungs." In The Microbiology of Respiratory System Infections. Elsevier, 2016. http://dx.doi.org/10.1016/b978-0-12-804543-5.00010-5.

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Qureshi, Mohammed Ansar. "Metallo Beta-Lactamase Resistance Mechanisms among Multi-Drug Resistant Pseudomonas aeruginosa (MDRPA)." In Research Advances in Microbiology and Biotechnology Vol. 9. B P International, 2024. http://dx.doi.org/10.9734/bpi/ramb/v9/8570a.

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J, Francisco, Miguel Lopez-Estepa, and M. Cristina. "Nucleases of Metallo-Beta-Lactamase and Protein Phosphatase Families in DNA Repair." In DNA Repair - On the Pathways to Fixing DNA Damage and Errors. InTech, 2011. http://dx.doi.org/10.5772/20884.

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MELO, DANDARA CAROLINE PINHEIRO, DÁLIA SAMARA GUIMARÃES FERREIRA, ALEXANDRE MELO DE LIMA, et al. "PROPAGAÇÃO DE NEW DELHI METALLO-BETA-LACTAMASE (NDM) EM AMBIENTES AQUÁTICOS: REVISÃO DE ESCOPO." In IMPACTO MULTIDISCIPLINAR NOS CUIDADOS DE SAÚDE DE CRIANÇAS E RECÉM-NASCIDOS. EDITORA SCISAUDE, 2024. http://dx.doi.org/10.56161/sci.ed.20240702c2.

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Escudero, Daniela Vieira da Silva, Diogo Boldim Ferreira, Thaysa Sobral Antonelli, et al. "141094 - EMERGÊNCIA DE NEW DELHI METALLO-BETA-LACTAMASE-1 (NDM-1) EM HOSPITAL UNIVERSITÁRIO: UM NOVO PROBLEMA DE SAÚDE PÚBLICA?" In Revista Mineira de Epidemiologia, Prevenção e Controle de Infecções, 2nd ed. AMECI & SMI & ABIH, 2025. https://doi.org/10.29327/5477619.2-239.

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Qureshi, Mohammed Ansar. "Detection and Prevalence of Metallo-Beta- Lactamase (MBL) Enzymes Producing Pseudomonas aeruginosa Isolated from Various Clinical Samples: A Microbiological Assessment." In Microbiology and Biotechnology Research: An Overview Vol. 1. BP International, 2025. https://doi.org/10.9734/bpi/mbrao/v1/4751.

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Conference papers on the topic "METALLO-beta-LACTAMASE"

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Mengual Barroso, MR, AB Pousada Fonseca, N. Garrido Peño, et al. "2SPD-006 Budgetary impact of aztreonam shortage in the treatment of metallo-beta-lactamase-producing gram-negative bacteria." In 29th EAHP Congress, Copenhagen, Denmark, 12-13-14 March 2025, Person centred pharmacy — Navigating digital health. British Medical Journal Publishing Group, 2025. https://doi.org/10.1136/ejhpharm-2025-eahp.22.

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Almayali, Enas Jalil Baqer, and Abbas Shaker AL-Muhana. "Prevalence and detection of New Delhi-metallo beta lactamase gene among beta lactam drug resistance Stenotrophomonas maltophilia and Pseudomonas aeruginosa isolated from burns patients in Al-Najaf Province." In 4TH INTERNATIONAL SCIENTIFIC CONFERENCE OF ALKAFEEL UNIVERSITY (ISCKU 2022). AIP Publishing, 2023. http://dx.doi.org/10.1063/5.0182159.

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Abed, Dina, Ammar Jusmani, and Sinan Alrifai. "Detection of Potential ESBL, Ampc, and Metallo-Beta-Lactamase Producers (MDR-GNB) Through In-vitro Susceptibility Testing of Genitourinary Specimens in a Community-based Pilot Study." In 1st International Ninevah Conference on Medical Sciences (INCMS 2021). Atlantis Press, 2021. http://dx.doi.org/10.2991/ahsr.k.211012.010.

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