Person:
Andreu Rodríguez, José Manuel

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First Name
José Manuel
Last Name
Andreu Rodríguez
Affiliation
Universidad Complutense de Madrid
Faculty / Institute
Psicología
Department
Personalidad, Evaluación y Psicología Clínica
Area
Personalidad, Evaluación y Tratamiento Psicológico
Identifiers
UCM identifierORCIDScopus Author IDDialnet IDGoogle Scholar ID

Search Results

Now showing 1 - 3 of 3
  • Publication
    Elaboración de un sistema de evaluación digital de la calidad docente e inserción laboral del Master Habilitante en Psicología General Sanitaria
    (2021-06) Peña Fernández, María Elena; Andreu Rodríguez, José Manuel; Peces-Barba Recio, Vanesa; Gómez Gutierrez, María del Mar
    Diseño y desarrollo de un sistema de evaluación digital que permita la valoración y análisis de la calidad docente del profesorado que imparte docencia en el mismo, así mismo como la evaluación de la calidad de la supervisión y tutorización de los TFM realizada por los profesores y por último evaluar y analizar no sólo la calidad docente de los tutores de prácticas externos, sino también la calidad de los centros de prácticas de los que dispone actualmente el Master. De forma complementaria, se diseñará y desarrollará un sistema de evaluación digital que permita la valoración y análisis de la inserción laboral de nuestros egresados.
  • Publication
    The Search for Antibacterial Inhibitors Targeting Cell Division Protein FtsZ at Its Nucleotide and Allosteric Binding Sites.
    (MDPI, 2022-07-28) Andreu Rodríguez, José Manuel; Huecas Gayo, Sonia; Araujo Bazán, Lidia; Vázquez Villa, Henar; Martín-Fontecha Corrales, María del Mar
    The global spread of bacterial antimicrobial resistance is associated to millions of deaths from bacterial infections per year, many of which were previously treatable. This, combined with slow antibiotic deployment, has created an urgent need for developing new antibiotics. A still clinically unexploited mode of action consists in suppressing bacterial cell division. FtsZ, an assembling GTPase, is the key protein organizing division in most bacteria and an attractive target for antibiotic discovery. Nevertheless, developing effective antibacterial inhibitors targeting FtsZ has proven challenging. Here we review our decade-long multidisciplinary research on small molecule inhibitors of bacterial division, in the context of global efforts to discover FtsZ-targeting antibiotics. We focus on methods to characterize synthetic inhibitors that either replace bound GTP from the FtsZ nucleotide binding pocket conserved across diverse bacteria or selectively bind into the allosteric site at the interdomain cleft of FtsZ from Bacillus subtilis and the pathogen Staphylococcus aureus. These approaches include phenotype screening combined with fluorescence polarization screens for ligands binding into each site, followed by detailed cytological profiling, and biochemical and structural studies. The results are analyzed to design an optimized workflow to identify effective FtsZ inhibitors, and new approaches for the discovery of FtsZ-targeting antibiotics are discussed.
  • Publication
    Targeting the FtsZ Allosteric Binding Site with a Novel Fluorescence Polarization Screen, Cytological and Structural Approaches for Antibacterial Discovery
    (ACS Publications, 2021-04-28) Huecas , Sonia; Araújo Bazán , Lidia; Rúiz, Federico M.; Ruiz Ávila, , Laura B.; Martínez, R.Fernando; Escobar Peña, Ana Andrea; Artola, Marta; Vázquez Villa, María Del Henar; Martín-Fontecha Corrales, María Del Mar; Fernández Tornero, Carlos; López Rodríguez, María L.; Andreu Rodríguez, José Manuel
    Bacterial resistance to antibiotics makes previously manageable infections again disabling and lethal, highlighting the need for new antibacterial strategies. In this regard, inhibition of the bacterial division process by targeting key protein FtsZ has been recognized as an attractive approach for discovering new antibiotics. Binding of small molecules to the cleft between the N-terminal guanosine triphosphate (GTP)-binding and the C-terminal subdomains allosterically impairs the FtsZ function, eventually inhibiting bacterial division. Nonetheless, the lack of appropriate chemical tools to develop a binding screen against this site has hampered the discovery of FtsZ antibacterial inhibitors. Herein, we describe the first competitive binding assay to identify FtsZ allosteric ligands interacting with the interdomain cleft, based on the use of specific high-affinity fluorescent probes. This novel assay, together with phenotypic profiling and X-ray crystallographic insights, enables the identification and characterization of FtsZ inhibitors of bacterial division aiming at the discovery of more effective antibacterials.