Results 1 to 10 of about 12,894 (157)

Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors. [PDF]

Commun Chem
Antibiotic resistance is a growing global health threat that risks the lives of millions. Among the resistance mechanisms, that mediated by metallo-β-lactamases is of particular concern as these bacterial enzymes dismantle most β-lactam antibiotics ...
Gulyás KV, Zhou L, Salamonsen D, Prester A, Bartels K, Bosman R, Haffke P, Li J, Tamási V, Deufel F, Thoma J, Andersson Rasmussen A, Csala M, Schroder Leiros HK, Xu Z, Widersten M, Rohde H, Schulz EC, Zhu W, Erdélyi M.   +19 more
europepmc   +7 more sources

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

Frontiers in Microbiology, 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-
Michaela Simon, Michaela Simon, Roman G. Gerlach, Yvonne Pfeifer, Niels Pfennigwerth, Sören G. Gatermann, Agnes Schröder, Agnes Schröder, Andreas Hiergeist, Axel Hamprecht, Axel Hamprecht, Axel Hamprecht, Axel Hamprecht, Tamara Rügamer, André Gessner, Jonathan Jantsch, Jonathan Jantsch   +16 more
doaj   +1 more source

Analysis of the genes encoding the MBL-fold metallohydrolase superfamily proteins of the Pseudomonas putida BS3701 petroleum component-degrading strain [PDF]

Клиническая микробиология и антимикробная химиотерапия, 2022
Objective. To determine whether the genes whose products are annotated as "MBL-fold metallohydrolase superfamily" are related to the proteins of the metallo-β-lactamase group. Materials and Methods.
Pozdnyakova-Filatova I.Yu., Zagoskin A.A., Zakharova M.V., Nagornykh M.O.   +3 more
doaj   +1 more source

Metallo-β Lactamase Producing Non-Fermentative Gram-Negative Bacilli from Various Clinical Isolates in a Tertiary Care Hospital: A Descriptive Cross-sectional Study

Journal of Nepal Medical Association, 2021
Introduction: Non-fermentative gram-negative bacilli are common causes of human infections especially nosocomial infections. These organisms are usually resistant to multiple antimicrobial agents including carbapenems.
Mahendra Shrestha, Ratna Baral, Lok Bahadur Shrestha   +2 more
doaj   +1 more source

Discovery of potential inhibitors against New Delhi metallo-β-lactamase-1 from natural compounds: in silico-based methods

Scientific Reports, 2021
New Delhi metallo-β-lactamase variants and different types of metallo-β-lactamases have attracted enormous consideration for hydrolyzing almost all β-lactam antibiotics, which leads to multi drug resistance bacteria.
Azhar Salari-jazi, Karim Mahnam, Parisa Sadeghi, Mohamad Sadegh Damavandi, Jamshid Faghri   +4 more
doaj   +1 more source

Neutralizing Carbapenem Resistance by Co-Administering Meropenem with Novel β-Lactam-Metallo-β-Lactamase Inhibitors

Antibiotics, 2023
Virulent Enterobacterale strains expressing serine and metallo-β-lactamases (MBL) genes have emerged responsible for conferring resistance to hard-to-treat infectious diseases. One strategy that exists is to develop β-lactamase inhibitors to counter this
Nakita Reddy, Letisha Girdhari, Mbongeni Shungube, Arnoldus C. Gouws, Byron K. Peters, Kamal K. Rajbongshi, Sooraj Baijnath, Sipho Mdanda, Thandokuhle Ntombela, Thilona Arumugam, Linda A. Bester, Sanil D. Singh, Anil Chuturgoon, Per I. Arvidsson, Glenn E. M Maguire, Hendrik G. Kruger, Thavendran Govender, Tricia Naicker   +17 more
doaj   +1 more source

Novel metallo β-lactamase mediated by aShigella flexneriplasmid [PDF]

FEMS Microbiology Letters, 1998
Novel carbapenem-hydrolyzing beta-lactamase (newly named MET-1) encoded on a transferable plasmid pMS390 from Shigella flexneri JS19622 was purified. The molecular weight was 28,000 by SDS-PAGE and the isoelectric point was higher than 9.3. This beta-lactamase favorably hydrolyzed classical cephalosporins and oxyimino-cephalosporins rather than ...
K, O'Hara, S, Haruta, T, Sawai, M, Tsunoda, S, Iyobe   +4 more
openaire   +2 more sources

Taxifolin as a Metallo-β-Lactamase Inhibitor in Combination with Augmentin against Verona Imipenemase 2 Expressing Pseudomonas aeruginosa

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, Trae Hillyer, Aylin S. Crugnale, Andrew Fulk, Caitlyn A. Thomas, Michael W. Crowder, Matthew A. Smith, Woo Shik Shin   +7 more
doaj   +1 more source

Identification, Speciation and Antibiogram along with Detection of Metallo Beta-lactamase Production in Acinetobacter Isolated from Clinical Samples in a Tertiary Care Hospital

Journal of Pure and Applied Microbiology, 2021
Acinetobacter species are gram negative non fermenters, which are important nosocomial pathogens involved in various outbreaks in hospitals due to widespread resistance to majority antibiotics.
N Ashwin Chitrabanu, Shrikara Mallya
doaj   +1 more source

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, Peter A, Lambert, Patrick W J, West   +2 more
openaire   +2 more sources