M
Matilde Yáñez
Researcher at University of Santiago de Compostela
Publications - 90
Citations - 3270
Matilde Yáñez is an academic researcher from University of Santiago de Compostela. The author has contributed to research in topics: Monoamine oxidase & Platelet aggregation inhibitor. The author has an hindex of 31, co-authored 88 publications receiving 2994 citations. Previous affiliations of Matilde Yáñez include Sapienza University of Rome & Autonomous University of Madrid.
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Journal ArticleDOI
Inhibitory effects of cis- and trans-resveratrol on noradrenaline and 5-hydroxytryptamine uptake and on monoamine oxidase activity.
TL;DR: These natural polyphenols may be of value as structural templates for the design and development of new antidepressant drugs with two important biochemical activities combined in the same chemical structure: NA/5-HT uptake and MAO inhibitory activity.
Journal ArticleDOI
Chalcones: a valid scaffold for monoamine oxidases inhibitors.
Franco Chimenti,Rossella Fioravanti,Adriana Bolasco,Paola Chimenti,Daniela Secci,Francesca Rossi,Matilde Yáñez,Francisco Orallo,Francesco Ortuso,Stefano Alcaro +9 more
TL;DR: The docking technique provided new insight on the inhibition mechanism and the rational drug design of more potent/selective hMAO inhibitors based on the chalcone scaffold.
Journal ArticleDOI
Expression profiles of genes involved in the mouse nuclear factor-kappa B signal transduction pathway are modulated by mangiferin.
TL;DR: Results indicate that MA modulates the expression of a large number of genes that are critical for the regulation of apoptosis, viral replication, tumorogenesis, inflammation and various autoimmune diseases, and raise the possibility that it may be of value in the treatment of inflammatory diseases and/or cancer.
Book ChapterDOI
Calcium binding proteins.
TL;DR: This chapter reviews the main Ca(2+)-modulated CBP, starting with those intracellular CBP that contain the structural EF-hand domain and addressing their structure, location and function and additionally their potential as pharmacological targets in several human diseases.
Journal ArticleDOI
Chromone, a privileged scaffold for the development of monoamine oxidase inhibitors.
Alexandra Gaspar,Tiago H. Silva,Matilde Yáñez,Dolores Viña,Franscisco Orallo,Francesco Ortuso,Eugenio Uriarte,Stefano Alcaro,Fernanda Borges +8 more
TL;DR: The differential analysis of the solvation effects among the chromone isomers gave additional insight about the superior outline of the 3-substituted chromone derivatives, which act preferably as MAO-B inhibitors.