Results 11 to 20 of about 811,638 (168)

Evolution of metallo-beta-lactamases in focus of the antibiotic resistance problem [PDF]

Вісник Харківського Національного Університету Імені В.Н. Каразіна: Серія Біологія
The article considers the place of metallo-beta-lactamases among the mechanisms of antibiotic resistance. These enzymes have important differences from serine beta-lactamases, which affect the mechanism of their catalytic activity, inhibition, rate of ...
V.B. Moskalov, I.V. Kadenko, A.M. Mukhin
doaj   +2 more sources

INHIBITORS OF METALLO-BETA-LACTAMASES

, 2020
The present invention relates to compounds that function as inhibitors of metallo-beta-lactamases (MBL). The present invention also relates to pharmaceutical compositions comprising such MBL inhibitors, and uses thereof in the treatment of bacterial ...
HERNANDEZ JEAN-FRANÇOIS, GAVARA LAURENT, DOCQUIER JEAN-DENIS, SEVAILLE LAURENT, LEGRU ALICE   +4 more
core   +8 more sources

Antarctic soil microbiomes encode structurally conserved and phylogenetically diverse beta‐lactamases

iMetaOmics
Antimicrobial resistance is a major global health threat shaped not only by clinical settings but also by environmental reservoirs, in line with the One Health framework.
José Coche‐Miranda, Patricio Arros, Nicolás Canales, Camilo Berríos‐Pastén, Gastón Azziz, Rosalba Lagos, Julieta Orlando, Francisco P. Chávez, Andrés E. Marcoleta   +8 more
doaj   +2 more sources

Imipenem-resistant Pseudomonas aeruginosa strains carry vim-type metallo-beta-lactamases isolated from intensive care unit, Shahid Beheshti Hospital, North of Iran

Research in Molecular Medicine, 2015
Background: Pseudomonas aeruginosa is the causing agent of many hospital infections and metallo-beta-lactamases (MBL) are being reported with increasing frequency. The aim of this study was to determine the frequency of metallo-&beta-lactamases (MBL) and
Zahra Moulana, Ramazan Rajabnia, Fariba Asgharpour   +2 more
doaj   +1 more source

Metallo-beta-lactamases: a last frontier for beta-lactams?

, 2011
Metallo-beta-lactamases are resistance determinants of increasing clinical relevance in Gram-negative bacteria. Because of their broad range, potent carbapenemase activity and resistance to inhibitors, these enzymes can confer resistance to almost all beta-lactams.
Cornaglia, Giuseppe, Giamarellou, Helen, Rossolini, Gian Maria   +2 more
openaire   +2 more sources

The Mechanisms of Catalysis by Metallo β-Lactamases [PDF]

, 2008
Class B β-lactamases or metallo-β-lactamases (MBLs) require zinc ions to catalyse the hydrolysis of β-lactam antibiotics such as penicillins, cephalosporins, carbapenems, and cephamycins.
Michael I. Page, Page, Michael I., Badarau, Adriana, Adriana Badarau   +3 more
core   +3 more sources

Rapid Evolution of a Fragment-like Molecule to Pan-Metallo-Beta-Lactamase Inhibitors: Initial Leads toward Clinical Candidates

, 2022
With the emergence and rapid spreading of NDM-1 and existence of clinically relevant VIM-1 and IMP-1, discovery of pan inhibitors targeting metallo-beta-lactamases (MBLs) became critical in our battle against bacterial infection.
Winnie Prosise (14231582), Shu-Wei Yang (2351068), Alex G. Therien (10156446), Weidong Pan (1427614), Giovanna Scapin (1427611), Christine Yang (149071), Li Xiao (307908), Jianping Pan (5473910), Amy Flattery (1349508), Thierry Fischmann (1586191), Alexander Pasternak (161010), Mihirbaran Mandal (2026381), Priya Dayananth (1720108), Todd W. Mayhood (2383978), Alexei V. Buevich (1433287), Katherine Young (526710), Jim Tata (1463734), Carrie Markgraf (14231588), Jacqueline D. Hicks (2335909), Nicholas Murgolo (1349487), Reynalda Keh de Jesus (14231579), Asra Mirza (1427602), Payal Sheth (3875491), Haifeng Tang (488592), Jin Wu (216487), Todd Black (1882981), Jing Su (23377), Yuriko Root (14231576), Rumin Zhang (2729599), Shuzhi Dong (2352922), Emma R. Parmee (298242), Haiqun Tang (2127373), Daniel F. Wyss (2177280), Inhou Chu (2026375), Charles Garlisi (4397194), Hai-Young Kim (156469), Lianzhu Liang (2276707), William K. Hagmann (1370268), Donald Chu (14231585), Artjohn Villafania (6917033), Guoqing Li (23674), Ronald Painter (2646250), Edward DiNunzio (12293994), Ann E. Weber (1416991)   +43 more
core   +2 more sources

Broad antibiotic resistance profile of the subclass B3 metallo-β-lactamase GOB-1, a di-zinc enzyme. [PDF]

, 2011
peer reviewedThe metallo-β-lactamase (MBL) GOB-1 was expressed via a T7 expression system in Escherichia coli BL21(DE3). The MBL was purified to homogeneity and shown to exhibit a broad substrate profile, hydrolyzing all the tested β-lactam compounds ...
Nathalie Selevsek, Carine Bebrone, Louise E. Horsfall, Lassaux, Patricia, Benoit M. R. Liénard, Kurt M. Hoffmann, Hoffmann, Kurt, Poirel, Laurent, Michael B. Kupper, Horsfall, Louise E., Horsfall, Louise E.; id_orcid, Bebrone, Carine, Izougarhane, Youssef, Jean-Marie Frère, Lienard, Benoit M. R., Youssef Izougarhane, Selevsek, Nathalie, Kupper, Michael B., Patricia Lassaux, Kupper, Michaël, Horsfall, Louise, Laurent Poirel, Liénard, Benoit, Galleni, Moreno, Frère, Jean-Marie, Hoffmann, Kurt M., Moreno Galleni   +26 more
core   +1 more source

Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily [PDF]

, 2007
peer reviewedOne strategy employed by bacterial strains to resist beta-lactam antibiotics is the expression of metallo-beta-lactamases requiring Zn+2 for activity.
Bebrone, Carine
core   +1 more source

Metallo-β-lactamases producing Gram negative isolates from VAP patients.

, 2021
Metallo-β-lactamases producing Gram negative isolates from VAP patients.
Suhail Sarwar Siddiqui (11408618), Prashant Gupta (4046920), Piyush Tripathi (5567492), Ved Prakash (4970143), Mithlesh Kumari (11408615), Sheetal Verma (5225192), Avinash Agarwal (6823241), Vimala Venkatesh (41044), Zia Arshad (4969093)   +8 more
core   +1 more source