Results 61 to 70 of about 52,332 (219)

Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase [PDF]

, 2015
Carbapenems, 'last-resort' β-lactam antibiotics, are inactivated by zinc-dependent metallo-β-lactamases (MBLs). The host innate immune response withholds nutrient metal ions from microbial pathogens by releasing metal-chelating proteins such as ...
A Kovacs-Simon, A Rokney, Alejandro J Vila, B Johne, BD Corbin, C Rumbo, C Schwechheimer, C Zhang, CA Schneider, D King, Elizabeth M Nolan, G Fiorilli, G Patel, G Periyannan, Guillermo Bahr, HJ Bootsma, J Morán-Barrio, JE Irazoqui, JM Bomberger, JM González, JM González, K Hede, KH Choi, KP Haley, L Dortet, L Poirel, LB Randall, Lisandro J González, LJ González, M Cerasi, M Hernandez Valladares, M Hussain, M Park, MB Brophy, ME Kovach, MF Haurat, MI Hood, MR Meini, MS Aschtgen, MW Crowder, N Selevsek, NC Kesty, P Marchiaro, P Ravasi, PD Veith, PS Borra, R Gläser, R Kitagawa, Robert A Bonomo, S Devos, S Santos, S Tottey, S Wommer, TA Murphy, Toshiki G Nakashige, TR Walsh, TR Walsh, V Schaar, V Schaar, VG Pederick, X Chen, Y Kim, Y Luo, Z Hu   +63 more
core   +3 more sources

Imipenem resistance in clinical Escherichia coli from Qom, Iran [PDF]

, 2018
OBJECTIVE: The emergence of metallo-\u3b2-lactamase-producing Enterobacteriaceae is a worldwide health concern. In this study, the first evaluation of MBL genes, bla IMP and bla VIM , in Escherichia coli resistant to imipenem isolated from urine and ...
Esmkhani, M., Hashemi, A., Kermani, S., Piccirillo, A., Shams, E., Shams, S.   +5 more
core   +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

Extended-spectrum ß-lactamase and carbapenemaseproducing Aeromonas species in wild animals from Portugal [PDF]

, 2014
Aeromonas are Gram-negative, facultative-anaerobic, non-spore-forming, glucose-fermenting, oxidase- and catalase-positive rods (Martin-Carnahan and Joseph 2005).
Avison, Bauer, Ceylan, CLSI, Evangelista-barreto, Fontes, Hayes, Henriques, Janda, Janda, Libisch, Martin-carnahan, Martínez-murcia, Martínez-murcia, Neuwirth, Parker, Pearson, Reith, Saavedra, Saavedra, Saavedra, Seshadri, Soler, Turutoglu, Walsh, Yáñez   +25 more
core   +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

Effect of β-lactamase inhibitors on in vitro activity of β-lactam antibiotics against Burkholderia cepacia complex species [PDF]

, 2016
Background: Bacteria belonging to the Burkholderia cepacia complex (Bcc) are an important cause of chronic respiratory tract infections in cystic fibrosis patients. Intrinsic resistance to a wide range of antimicrobial agents, including a variety of beta-
Coenye, Tom, Everaert, Annelien
core   +2 more sources

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

Broad-spectrum β-lactamases among Enterobacteriaceae of animal origin: molecular aspects, mobility and impact on public health [PDF]

, 2010
Broad-spectrum β-lactamase genes (coding for extended-spectrum β-lactamases (ESBLs) and AmpC β-lactamases) have been frequently demonstrated in the microbiota of food-producing animals. This may pose a human health hazard since these genes may be present
Butaye, Patrick, Dewulf, Jeroen, Haesebrouck, Freddy, Herman, Lieve, Heyndrickx, Marc, Martel, An, Persoons, Davy, Smet, Annemieke   +7 more
core   +1 more source

Antimicrobial resistance pattern and molecular genetic distribution of metallo-β-lactamases producing Pseudomonas aeruginosa isolated from hospitals in Minia, Egypt

Infection and Drug Resistance, 2019
Background: Pseudomonas aeruginosa (P. aeruginosa) represents a great threat to public health worldwide, due to its high ability to acquire resistance to different antibiotic classes.
S. M. Farhan, R. Ibrahim, Khaled M. Mahran, H. Hetta, R. A. Abd El-Baky   +4 more
semanticscholar   +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