Results 11 to 20 of about 905,435 (191)

New Delhi Metallo-β-Lactamase–producing Enterobacteriaceae, United States

Emerging Infectious Diseases, 2013
We characterized 9 New Delhi metallo-β-lactamase–producing Enterobacteriaceae (5 Klebsiella pneumoniae, 2 Escherichia coli, 1 Enterobacter cloacae, 1 Salmonella enterica serovar Senftenberg) isolates identified in the United States and cultured from 8 ...
J. Kamile Rasheed, Brandon Kitchel, Wenming Zhu, Karen F. Anderson, Nancye C. Clark, Mary Jane Ferraro, Patrice Savard, Romney M. Humphries, Alexander J. Kallen, Brandi M. Limbago   +9 more
doaj   +2 more sources

Production of metallo-β-lactamase among Pseudomonas aeruginosa strains isolated in the State of Sergipe, Brazil [PDF]

Revista da Sociedade Brasileira de Medicina Tropical, 2015
INTRODUCTION: Acquired production of metallo-β-lactamases is an important mechanism of resistance in Pseudomonas aeruginosa. The objective of this study was to investigate the production of metallo-β-lactamase and the genetic diversity among ceftazidime ...
Lívia Maria do Amorim Costa, Maria Emília de Castro Kling Fleming, Geraldo Renato de Paula, Lenise Arneiro Teixeira, Pedro Juan José Mondino, Sílvia Susana Bona de Mondino, Cláudia Rezende de Vieira Mendonça-Souza   +6 more
doaj   +2 more sources

Metallo-β-Lactamase Inhibitor Phosphonamidate Monoesters [PDF]

, 2022
Being the second leading cause of death and the leading cause of disability-adjusted life years worldwide, infectious diseases remaincontrary to earlier predictionsa major consideration for the public health of the 21st century. Resistance development of
Hanna Andersson (1408987), Linus Sandegren (12066), Manuela Vorácová (11998639), Anna Andersson Rasmussen (11998645), Lisa Allander (11998648), Susann Skagseth (11998642), Katarzyna Palica (11998636), Madlen Hubert (1963375), Hanna-Kirstirep Schrøder Leiros (11998651), Máté Erdélyi (1364241)   +9 more
core   +2 more sources

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

Affimer Inhibition of Verona Integron-encoded Metallo-β-Lactamase 1 [PDF]

, 2022
Metallo-β-lactamases (MBLs) are a class of enzyme that hydrolyse the β-lactam ring in β-lactam antibiotics through their active site Zn2+ rendering them inactive. Verona Integron-encoded metallo-β-lactamase 1 (VIM-1) is a class B1, group 3, carbapenemase
McLean-Ash, Trent Leigh
core   +5 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

A rapid method for detecting and distinguishing metallo-β-lactamase-and serine carbapenemase-producing Enterobacteriales using MALDI-TOF MS

Frontiers in Microbiology, 2023
IntroductionCarbapenemase-producing Enterobacteriales (CPE) are a major health threat worldwide, and therefore the development of rapid detection methods is needed.
Xiaopeng Jing, Yanyan Hu, Tingting Wu, Xing Zhang, Shaofeng Luo, Wei Wang, Xiaochun Min, Ruiling Sun, Ji Zeng   +8 more
doaj   +1 more source

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

Occurrences of Metalo-β-lactamase Producing Pseudomonas aeruginosa among Clinical Samples in Kwara state, Nigeria

Journal of Applied Sciences and Environmental Management, 2022
Pseudomonas aeruginosa is a frequent nosocomial pathogen that causes severe disease in many clinical and community settings. The objective of this paper was to isolate Pseudomonas aeruginosa from clinical samples and to investigate the occurrence of ...
O.C. Adekunle, A. Mustapha, G. Odewale , R.O. Ojedele   +3 more
doaj   +1 more source