Results 11 to 20 of about 893,574 (181)

Metallo-β-Lactamases and Aptamer-Based Inhibition

Pharmaceuticals, 2011
An evolution of antibiotic-resistant bacteria has resulted in the need for new antibiotics. β-Lactam based drugs are the most predominantly prescribed antibiotics to combat bacterial infections; however, production of β-lactamases, which catalyze the ...
Sung-Kun Kim, Taylor O. Foster, Mieke J. Lahousse, Sara R. Schlesinger   +3 more
doaj   +2 more sources

A DNA aptamer reveals an allosteric site for inhibition in metallo-β-lactamases.

PLoS ONE, 2019
The hydrolysis of β-lactam antibiotics by β-lactamase enzymes is the most prominent antibiotic resistance mechanism for many pathogenic bacteria. Out of this broad class of enzymes, metallo-β-lactamases are of special clinical interest because of their ...
Nazmul H Khan, Anthony A Bui, Yang Xiao, R Bryan Sutton, Robert W Shaw, Benjamin J Wylie, Michael P Latham   +6 more
doaj   +2 more sources

Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases. [PDF]

J Enzyme Inhib Med Chem
The urgent demand for effective countermeasures against metallo-β-lactamases (MBLs) necessitates development of novel metallo-β-lactamase inhibitors (MBLIs).
Lee JH, Kim SG, Jang KM, Shin K, Jin H, Kim DW, Jeong BC, Lee SH.   +7 more
europepmc   +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

OXA β-lactamases

, 2014
The OXA β-lactamases were among the earliest β-lactamases detected; however, these molecular class D β-lactamases were originally relatively rare and always plasmid mediated.
Benjamin A. Evans (3115968), Sebastian G. B. Amyes (16653285)   +1 more
core   +7 more sources

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
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

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
openaire   +2 more sources

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, J L, Huber, M L, Greenlee, J B, Laub, K, Young, L L, Silver, J M, Balkovec, K D, Pryor, J K, Wu, B, Leiting, D L, Pompliano, J H, Toney   +11 more
openaire   +2 more sources

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, E T, Yamamoto, Y, Eriguchi, T, Sawai   +3 more
openaire   +2 more sources