Zobrazeno 1 - 10
of 63
pro vyhledávání: '"Mariano M. González"'
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
Autor:
Lisandro J. González, Guillermo Bahr, Mariano M. González, Robert A. Bonomo, Alejandro J. Vila
Publikováno v:
Nature Chemical Biology.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7971ad6b69615f6ec40ded045b705ecb
https://doi.org/10.1038/s41589-023-01319-0
https://doi.org/10.1038/s41589-023-01319-0
Autor:
Alejandro J. Vila, Lorena Martínez, Mariano M. González, Graciela Mahler, Cecilia Saiz, Leopoldo Suescun, Valentina Villamil, Ma. Agustina Rossi
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
The synthesis of new oxazolidinylthiazolidines bicycles, oxygen analogues of bisthiazolidines, also known as metallo-β-lactamase inhibitors is described. The reaction of β-aminoalcohols and 2,5-dihydroxy-1,4-dithiane led to oxazolidinylthiazolidine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df08682e7b31c19b9357b095e8447d5b
https://doi.org/10.1016/j.tetasy.2016.11.002
https://doi.org/10.1016/j.tetasy.2016.11.002
Autor:
Mariano M. González, Antonela Rocio Palacios, Leticia I. Llarrull, Diego M. Moreno, James Spencer, Michael W. Crowder, Mahesh Aitha, Robert A. Bonomo, David L. Tierney, Alejandro J. Vila, María-Natalia Lisa
Publikováno v:
Nature Communications
RepHipUNR (UNR)
Universidad Nacional de Rosario
instacron:UNR
Lisa, M N, Palacios, A R, Aitha, M, González, M M, Moreno, DI M, Crowder, M W, Bonomo, R A, Spencer, J, Tierney, D L, Llarrull, L I & Vila, A J 2017, ' A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases ', Nature Communications, vol. 8, 538 . https://doi.org/10.1038/s41467-017-00601-9
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
RepHipUNR (UNR)
Universidad Nacional de Rosario
instacron:UNR
Lisa, M N, Palacios, A R, Aitha, M, González, M M, Moreno, DI M, Crowder, M W, Bonomo, R A, Spencer, J, Tierney, D L, Llarrull, L I & Vila, A J 2017, ' A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases ', Nature Communications, vol. 8, 538 . https://doi.org/10.1038/s41467-017-00601-9
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Carbapenem-resistant Enterobacteriaceae threaten human health, since carbapenems are last resort drugs for infections by such organisms. Metallo-β-lactamases (MβLs) are the main mechanism of resistance against carbapenems. Clinically approved inhib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4031d3f015cc4ce5eb16ce40db85d578
https://www.nature.com/articles/s41467-017-00601-9
https://www.nature.com/articles/s41467-017-00601-9
Autor:
Valerie Castillo, Jürgen Brem, Maria F. Mojica, Alejandro J. Vila, Robert A. Bonomo, Leticia I. Llarrull, James Spencer, Magda Kosmopoulou, Ilaria Pettinati, Graciela Mahler, Philip Hinchliffe, Christopher J. Schofield, Mariano M. González
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Pathogenic Gram-negative bacteria resistant to almost all β-lactam antibiotics are a major public health threat. Zn(II)-dependent or metallo-β-lactamases (MBLs) produced by these bacteria inactivate most β-lactam antibiotics, including the carbape
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::903a1f448d1ec5683530479343fb7c8a
https://doi.org/10.1021/acsinfecdis.5b00046
https://doi.org/10.1021/acsinfecdis.5b00046
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
The understanding of protein evolution depends on the ability to relate the impact of mutations on molecular traits to organismal fitness. Biological activity and robustness have been regarded as important features in shaping protein evolutionary lan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92933ce73ac9004b15ce019fe2ab7345
https://academic.oup.com/mbe/article/33/7/1768/2578968
https://academic.oup.com/mbe/article/33/7/1768/2578968
Autor:
Valerie Castillo, Alejandro J. Vila, Graciela Mahler, Javier M. González, Maria F. Mojica, Cecilia Saiz, Magda Kosmopoulou, Mariano M. González, James Spencer, Catherine L. Tooke, Philip Hinchliffe, Robert A. Bonomo, Leticia I. Llarrull
Publikováno v:
Hinchliffe, P, Gonzalez, M M, Mojica, M F, Gonzalez, J M, Castillo, V, Saiz, C, Kosmopoulou, M, Tooke, C, Llarrull, L, Mahler, G, Bonomo, R A, Villa, A J & Spencer, J 2016, ' Cross-class metallo-β-lactamase inhibition by bisthiazolidines reveals multiple binding modes ', Proceedings of the National Academy of Sciences of the United States of America, vol. 113, no. 26, pp. E3745-E3754 . https://doi.org/10.1073/pnas.1601368113
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Metallo-β-lactamases (MBLs) hydrolyze almost all β-lactam antibiotics and are unaffected by clinically available β-lactamase inhibitors (βLIs). Active-site architecture divides MBLs into three classes (B1, B2, and B3), complicating development of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68799a23a5f1b0de2ff1b3625c35706a
https://research-information.bris.ac.uk/en/publications/e66e5c86-fd98-4326-9bee-15426e11504f
https://research-information.bris.ac.uk/en/publications/e66e5c86-fd98-4326-9bee-15426e11504f
Autor:
Alejandro J. Vila, Mariano M. González
Publikováno v:
Topics in Medicinal Chemistry ISBN: 9783319461113
Multidrug-resistant bacterial infections have become in recent years an increasingly worrisome problem in the medical community. The β-lactams are the most used antibiotics consisting in more than 60% of the prescribed antibacterials. Indeed, carbap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fc0cd69d5741f97c4f7869b327e57a6f
https://doi.org/10.1007/7355_2016_6
https://doi.org/10.1007/7355_2016_6
Autor:
Barrio AR; Applied Vision Research Group, Faculty of Optics and Optometry, Complutense University of Madrid, 28037 Madrid, Spain. Electronic address: arbarrio@ucm.es., González-Pérez M; Faculty of Optics and Optometry, Complutense University of Madrid, 28037 Madrid, Spain., Arriola-Villalobos P; Servicio de Oftalmología, Hospital Clínico San Carlos; Departamento de Inmunología, Oftalmología y ORL, Facultad de Medicina, Universidad Complutense de Madrid (UCM); IdISSC, Madrid, Spain., Antona B; Applied Vision Research Group, Faculty of Optics and Optometry, Complutense University of Madrid, 28037 Madrid, Spain.
Publikováno v:
Contact lens & anterior eye : the journal of the British Contact Lens Association [Cont Lens Anterior Eye] 2024 Nov 13, pp. 102333. Date of Electronic Publication: 2024 Nov 13.
Autor:
Agudo Castillo B; Gastroenterology, Hospital Universitario Puerta de Hierro Majadahonda, Spain., Mascarenhas M; Gastroenterology, Centro Hospitalar Universitário de São João, Portugal., Martins M; Gastroenterology, Centro Hospitalar Universitário de São João., Mendes F; Gastroenterology, Centro Hospitalar Universitário de São João, Portugal., de la Iglesia D; Gastroenterology, Hospital Universitario Puerta de Hierro Majadahonda, Spain., Costa AMMPD; Gastroenterology, Hospital Universitario Puerta de Hierro Majadahonda., Esteban Fernández-Zarza C; Gastroenterology, Hospital Universitario Puerta de Hierro Majadahonda, Spain., González-Haba Ruiz M; Department of Gastroenterology, Hospital Universitario Puerta de Hierro Majadahonda, Spain.
Publikováno v:
Revista espanola de enfermedades digestivas [Rev Esp Enferm Dig] 2024 Nov; Vol. 116 (11), pp. 613-622.