Results 1 to 10 of about 27,066 (205)

Novel monoclonal antibodies for immunodetection of AmpC β-lactamases [PDF]

open access: yesPeerJ
Background Accurate and easy-to-perform assays for the detection of antibiotic-resistant bacterial isolates producing AmpC β-lactamases are epidemiologically relevant, leading to more effective use of antibiotics and a comprehensive understanding of β ...
Karolina Bielskė   +6 more
doaj   +3 more sources

Cooperative resistance varies among β-lactamases in E. coli, with some enabling cross-protection and sustained extracellular activity [PDF]

open access: yesCommunications Biology
β-lactamases confer bacteria resistance to β-lactam antibiotics, and interestingly, this protective effect can extend to neighboring susceptible cells. However, knowledge of this cooperative resistance remains limited.
Qinqin Wang   +2 more
doaj   +2 more sources

Characterization of acquired β-lactamases in Pseudomonas aeruginosa and quantification of their contributions to resistance [PDF]

open access: yesMicrobiology Spectrum
Pseudomonas aeruginosa is a highly problematic opportunistic pathogen that causes a range of different infections. Infections are commonly treated with β-lactam antibiotics, including cephalosporins, monobactams, penicillins, and carbapenems, with ...
Karl A. Glen, Iain L. Lamont
doaj   +2 more sources

Enzyme graphene oxide interaction: the case system of β-lactamases. [PDF]

open access: yesRSC Adv
This paper proves that graphene oxide is a potent non-competitive inhibitor for both serine- and metallo-β-lactamases. Its inhibitory effect is significantly diminished when preincubated with a substrate, indicating an oxidation-mediated mechanism.
Piccirilli A   +7 more
europepmc   +3 more sources

Antifungal agent tavaborole as a potential broad-spectrum serine and metallo-β-lactamases inhibitorResearch in context [PDF]

open access: yesEBioMedicine
Summary: Background: The global emergence and spread of carbapenem-resistant Enterobacteriaceae in clinical settings have driven the search for inhibitors that can counteract carbapenemases.
Yan Zhang   +15 more
doaj   +2 more sources

OXA β-lactamases from Acinetobacter spp. are membrane bound and secreted into outer membrane vesicles [PDF]

open access: yesmBio
β-lactamases from Gram-negative bacteria are generally regarded as soluble, periplasmic enzymes. NDMs have been exceptionally characterized as lipoproteins anchored to the outer membrane. A bioinformatics study on all sequenced β-lactamases was performed
Lucia Capodimonte   +6 more
doaj   +2 more sources

Prevalence of Extended Spectrum β-Lactamase, Metallo β-Lactamase, and AmpC β-Lactamase among Gram Negative Bacilli Recovered from Burn Wound Infection

open access: yesRUHS 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
doaj   +1 more source

Drug development concerning metallo-β-lactamases in gram-negative bacteria

open access: yesFrontiers in Microbiology, 2022
β-Lactams have been a clinical focus since their emergence and indeed act as a powerful tool to combat severe bacterial infections, but their effectiveness is threatened by drug resistance in bacteria, primarily by the production of serine- and metallo-β-
Xiuyun Li   +7 more
doaj   +1 more source

TEM-E1: a novel β-lactamase conferring resistance to ceftazidime [PDF]

open access: yesFEMS Microbiology Letters, 1989
A novel β-lactamase, conferring resistance to ceftazidime, has been identified to be encoded by a 31 kb plasmid (pUK720) in a clinical E. coli strain isolated in Belgium. The β-lactamase, new designated TEM-E1, has a pI of approximately 5.4 and lies in between the iso-electric focused bands of the β-lactamases TEM-1 and TEM-7.
D.J. Payne, M.S. Marriott, S.G.B. Amyes
openaire   +1 more source

A β-lactamase produced by a thermophilicBacillus [PDF]

open access: yesFEMS Microbiology Letters, 1996
A β-lactamase was purified from a thermophilic Bacillus strain, that had been isolated from a traditional hot bath in the Meknes area (Morocco). The properties of the enzyme were very similar to those of the β-lactamase produced by Bacillus licheniformis 749C but it exhibited a somewhat increased thermostability and a higher activation energy with ...
Fouzia Rhazi-Filali   +5 more
openaire   +1 more source

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