Results 31 to 40 of about 9,673 (155)

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

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   +1 more source

Molecular heterogeneity ofbla_VIM-2-containing integrons fromPseudomonas aeruginosaplasmids encoding the VIM-2 metallo-β-lactamase [PDF]

FEMS Microbiology Letters, 2001
A bla(VIM-2) metallo-beta-lactamase determinant, identical to that previously identified in Pseudomonas aeruginosa COL-1 isolate from a French hospital, was detected on a 28-kb plasmid carried by a nosocomial isolate of P. aeruginosa from Verona, Italy.
PALLECCHI L., RICCIO M. L., DOCQUIER J. D., FONTANA R., ROSSOLINI G. M.   +4 more
openaire   +4 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

Prediction of Phytochemicals for Their Potential to Inhibit New Delhi Metallo β-Lactamase (NDM-1)

Pharmaceuticals, 2023
The effectiveness of all antibiotics in the β-lactam group to cure bacterial infections has been impaired by the introduction of the New Delhi Metallo-β-lactamase (NDM-1) enzyme.
Zainab Bibi, Irfa Asghar, Naeem Mahmood Ashraf, Iftikhar Zeb, Umer Rashid, Arslan Hamid, Maria Kanwal Ali, Ashraf Atef Hatamleh, Munirah Abdullah Al-Dosary, Raza Ahmad, Muhammad Ali   +10 more
doaj   +1 more source

β-lactamase-mediated resistance in MDR-Pseudomonas aeruginosa from Qatar

Antimicrobial Resistance and Infection Control, 2020
Background The distribution of β-lactam resistance genes in P. aeruginosa is often closely related to the distribution of certain high-risk international clones.
Mazen A. Sid Ahmed, Faisal Ahmad Khan, Ali A. Sultan, Bo Söderquist, Emad Bashir Ibrahim, Jana Jass, Ali S. Omrani   +6 more
doaj   +1 more source

Procedure of the overexpression, purification and crystallization of BLEG-1, a bifunctional and evolutionary divergent B3 metallo-β-lactamase, for structure-function studies

MethodsX, 2022
Metallo-β-lactamases (MBLs) are class B β-lactamases from the metallo-hydrolase-like MBL-fold superfamily which act on a broad range of β-lactam antibiotics, thus conferring antibiotics resistance to bacterial pathogens.
Shaw Xian Au, Noor Dina Muhd Noor, Hiroyoshi Matsumura, Raja Noor Zaliha Raja Abdul Rahman, Yahaya M. Normi   +4 more
doaj   +1 more source

ENTEROBACTERIACAE, PRODUCING ESBLS AND METALLO-β-LACTAMASE NDM-1, ISOLATED IN HOSPITALS OF BALTIC REGION COUNTRIES

Инфекция и иммунитет, 2014
. We studied the prevalence of K. pneumoniae and E. coli resistance to extended spectrum cephalosporins and carbapenems, isolated from patients of eight hospitals in St-Petersburg from January to May, 2012.
S. A. Egorova, L. A. Kaftyreva, L. V. Lipskaya, I. B. Konovalenko, M. F. Pyasetskaya, T. S. Kurchikova, N. B. Vedernikova, O. T. Morozova, M. V. Smirnova, L. N. Popenko, M. I. Lubushkina, J. A. Savochkina, M. A. Makarova, L. V. Suzhaeva, J. V. Ostankova, M. N. Ivanova, A. M. Pavelkovich, P. Naaber, E. Sepp, S. Kõljalg, J. Miciuleviciene, A. Balode   +21 more
doaj   +1 more source

Synthesis and enzyme-based evaluation of analogues L-tyrosine thiol carboxylic acid inhibitor of metallo-β-lactamase IMP-1

Journal of Enzyme Inhibition and Medicinal Chemistry, 2019
The emergence of drug-resistant pathogenic bacteria is occurring due to the global overuse and misuse of β-lactam antibiotics. Infections caused by some bacteria which secrete metallo-β-lactamases (enzymes that inactivate β-lactam antibiotics) are ...
Omid Khalili Arjomandi, Mahboubeh Kavoosi, Hadi Adibi   +2 more
doaj   +1 more source

Additional file 2: of Mortality related to Verona Integron-encoded Metallo-β-lactamase-positive Pseudomonas aeruginosa: assessment by a novel clinical tool

, 2019
Updated Charlson index score. (DOCX 14 kb)
Persoon, Marjolein, Voor in ‘t holt, Anne, Meer, Maurits, Bokhoven, Karen, Gommers, Diederik, Vos, Margreet, Severin, JuliĂŤtte   +6 more
openaire   +1 more source

Redirecting pantoprazole as a metallo-beta-lactamase inhibitor in carbapenem-resistant Klebsiella pneumoniae

Frontiers in Pharmacology
The development of resistance to carbapenems in Klebsiella pneumoniae due to the production of metallo-β-lactamases (MBLs) is a critical public health problem because carbapenems are the last-resort drugs used for treating severe infections of extended ...
Wesam H. Abdulaal, Nabil A. Alhakamy, Nabil A. Alhakamy, Nabil A. Alhakamy, Amer H. Asseri, Amer H. Asseri, Mohamed F. Radwan, Tarek S. Ibrahim, Solomon Z. Okbazghi, Hisham A. Abbas, Basem Mansour, Aly A. Shoun, Wael A. H. Hegazy, Wael A. H. Hegazy, Mahmoud Saad Abdel-Halim   +14 more
doaj   +1 more source