Results 11 to 20 of about 9,732 (155)
RUHS Journal of Health Sciences, 2023 Introduction: Infections are the major cause of morbidity and mortality in burn patients. The ESBL, MBL and AmpC are the major mediators of antimicrobial resistance in gram negative bacteria. Early detection of ESBL, MBL and AmpC β -lactamases is crucial
Kusum Lata Lodha, Seema Surana
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Microorganisms, 2023 Among the various mechanisms that bacteria use to develop antibiotic resistance, the multiple expression of β-lactamases is particularly problematic, threatening public health and increasing patient mortality rates. Even if a combination therapy—in which
Bogdan M. Benin +7 more
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Multi-Drug-Resistant Gram-Negative Microorganisms: Epidemiology, Treatment and Alternative Approach
Antibiotics, 2022 The presence of enzymes such as Extended-Spectrum β-lactamase (ESBL) and carbapenemases (KPCs, Metallo β-lactamases and OXA) constitutes the principal resistance mechanism to antibiotics [...]
Maria Teresa Mascellino
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The flavonoid galangin inhibits the L1 metallo-β-lactamase fromStenotrophomonas maltophilia [PDF]
FEMS Microbiology Letters, 2002 The flavonoid galangin inhibits the partially purified metallo-beta-lactamase from Stenotrophomonas maltophilia. The effect was not reversed by the addition of ZnCl(2) suggesting that the inhibitory effect is not related to metal chelation. The flavonoid quercetin also has some inhibitory effect against the enzyme.
Brian J, Denny +2 more
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Isolation and partial purification of a carbapenem-hydrolysing metallo-β-lactamase fromPseudomonas cepacia [PDF]
FEMS Microbiology Letters, 1994 A metallo-beta-lactamase has been isolated from a clinical strain of Pseudomonas cepacia and partially purified using Cibacron blue F3GA coupled agarose. The resulting preparation showed a single band of beta-lactamase activity (pI 8.45) after analytical isoelectric focusing.
I A, Baxter, P A, Lambert
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Characterization of the active-site residues asparagine 167 and lysine 161 of the IMP-1 metallo β-lactamase [PDF]
FEMS Microbiology Letters, 2001 The roles of lysine at position 161 and asparagine at position 167 in IMP-1 metallo beta-lactamase were studied by site-directed mutagenesis. These residues are highly conserved in metallo beta-lactamases and are thought to be present in the active-site cavity.
S, Haruta +3 more
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Frontiers in Microbiology, 2022 Metallo β-Lactamases (MBLs) degrade most clinical β-lactam antibiotics, especially Carbapenem, posing a huge threat to global health. Studies on environmental MBLs are important for risk assessment of the MBLs transmission among connected habitats, and ...
Lingxu Fang +5 more
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Inhibition of IMP-1 metallo-β-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives [PDF]
FEMS Microbiology Letters, 1999 IMP-1 metallo-beta-lactamase is a transferable carbapenem-hydrolyzing enzyme found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescens and Klebsiella pneumoniae. Bacteria that express IMP-1 show significantly reduced sensitivity to carbapenems and other beta-lactam antibiotics.
G G, Hammond +11 more
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Indonesia Journal of Biomedical Science, 2019 Background: Escherichia coli belong to the family of Enterobacteriaceae that are responsible as one of the leading cause of nosocomial infections. The emergence of Carbapenem-resistant Enterobacteriaceae presents therapeutic challenges for clinicians on choosing the correct type of antibiotics to prescribe.
Muhammad Ardi Afriansyah +2 more
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Cefiderocol: An Overview of Its in-vitro and in-vivo Activity and Underlying Resistant Mechanisms
Frontiers in Medicine, 2021 Treatment of multidrug-resistant (MDR) Gram-negative bacteria (GNB) infections has led to a global public health challenging due to the bacterial resistance and limited choices of antibiotics.
Jiahui Yao +3 more
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