1,3,4-oxadiazoles as inhibitors of the atypical member of the BET family bromodomain factor 3 from Trypanosoma cruzi (TcBDF3)

Autor: Victoria L. Alonso, Andrea M. Escalante, Elvio Rodríguez Araya, Gianfranco Frattini, Luis E. Tavernelli, Diego M. Moreno, Ricardo L. E. Furlan, Esteban Serra

Publikováno v: Frontiers in Microbiology, Vol 15 (2024)

Chagas disease, caused by the protozoan parasite Trypanosoma cruzi, affects millions globally, with increasing urban cases outside of Latin America. Treatment is based on two compounds, namely, benznidazole (BZ) and nifurtimox, but chronic cases pose

Externí odkaz: https://doaj.org/article/625fa16de8e24adda2e8694cf21c87f1

Longitudinal Evolution of the Pseudomonas-Derived Cephalosporinase (PDC) Structure and Activity in a Cystic Fibrosis Patient Treated with β-Lactams

Autor: Claudia A. Colque, Andrea G. albarracín Orio, Pablo E. Tomatis, Gina Dotta, Diego M. Moreno, Laura G. Hedemann, Rachel A. Hickman, Lea M. Sommer, Sofía Feliziani, Alejandro J. Moyano, Robert A. Bonomo, Helle K. Johansen, Søren Molin, Alejandro J. Vila, Andrea M. Smania

Publikováno v: mBio, Vol 13, Iss 5 (2022)

ABSTRACT Traditional studies on the evolution of antibiotic resistance development use approaches that can range from laboratory-based experimental studies, to epidemiological surveillance, to sequencing of clinical isolates. However, evolutionary tr

Externí odkaz: https://doaj.org/article/70924af419ec406b88dabded5e47d448

A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases

Autor: María-Natalia Lisa, Antonela R. Palacios, Mahesh Aitha, Mariano M. González, Diego M. Moreno, Michael W. Crowder, Robert A. Bonomo, James Spencer, David L. Tierney, Leticia I. Llarrull, Alejandro J. Vila

Publikováno v: Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)

Carbapenem-resistant bacteria pose a major health threat by expressing metallo-β-lactamases (MβLs), enzymes able to hydrolyse these life-saving drugs. Here the authors use biophysical and computational methods and show that different MβLs share th

Externí odkaz: https://doaj.org/article/211e1f98c03048a78682481a30189109

2-Mercaptomethyl Thiazolidines (MMTZs) Inhibit All Metallo-β-Lactamase Classes by Maintaining a Conserved Binding Mode

Autor: Valentina Villamil, Maria F. Mojica, Brad Spellberg, Diego M. Moreno, James Spencer, Claudia Banchio, Alejandro J. Vila, Robert A. Bonomo, Verónica Martínez, Graciela Mahler, Philip Hinchliffe, George L. Drusano, Maria-Agustina Rossi

Publikováno v: Repositorio U. El Bosque
Universidad El Bosque
instacron:Universidad El Bosque
Hinchliffe, P, Moreno, D M, Rossi, M-A, Mojica, M F, Martinez, V, Villamil, V, Spellberg, B, Drusano, G L, Banchio, C, Mahler, G, Bonomo, R A & Spencer, J 2021, ' 2-Mercaptomethyl Thiazolidines (MMTZs) Inhibit All Metallo-β-Lactamase Classes by Maintaining a Conserved Binding Mode ', ACS Infectious Diseases, vol. 7, no. 9, pp. 2697-2706 . https://doi.org/10.1021/acsinfecdis.1c00194, https://doi.org/10.1021/acsinfecdis.1c00194
ACS Infect Dis

Metallo-β-lactamase (MBL) production in Gram-negative bacteria is an important contributor to β-lactam antibiotic resistance. Combining β-lactams with β-lactamase inhibitors (BLIs) is a validated route to overcoming resistance, but MBL inhibitors

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca170f33eb191f60adbd8e767b6d3429
https://doi.org/10.1021/acsinfecdis.1c00194

Versatile Activity of a Copper(II) Complex Bearing a N 4 ‐Tetradentate Schiff Base Ligand with Reduced Oxygen Species

Autor: Micaela Richezzi, Joaquín Ferreyra, Juan Puzzolo, Lisandro Milesi, Claudia M. Palopoli, Diego M. Moreno, Christelle Hureau, Sandra R. Signorella

Publikováno v: European Journal of Inorganic Chemistry
European Journal of Inorganic Chemistry, 2022, 2022 (8), pp.e202101042. ⟨10.1002/ejic.202101042⟩

International audience; The reactivity of the Cu(II) complex of N,N’-bis(pyridin-2-ylmethylene)propane-1,3-diamine (py2pn), [Cu(py2pn)(ClO4)2], toward O2.− and H2O2 has been examined. The complex reacts with O2.− with fast second order kinetics

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::257e805a64eb8ab7f685af569bc970e7
https://doi.org/10.1002/ejic.202101042