L
Laura Ceballos-Laita
Researcher at University of Zaragoza
Publications - 21
Citations - 506
Laura Ceballos-Laita is an academic researcher from University of Zaragoza. The author has contributed to research in topics: Xylem & Proteome. The author has an hindex of 8, co-authored 19 publications receiving 256 citations. Previous affiliations of Laura Ceballos-Laita include Spanish National Research Council.
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Journal ArticleDOI
Structural stability of SARS-CoV-2 3CLpro and identification of quercetin as an inhibitor by experimental screening.
Olga Abian,David Ortega-Alarcon,Ana Jiménez-Alesanco,Laura Ceballos-Laita,Sonia Vega,Hugh T. Reyburn,Bruno Rizzuti,Adrián Velázquez-Campoy +7 more
TL;DR: Quercetin, with well-known pharmacokinetic and ADMET properties, can be considered as a good candidate for further optimization and development, or repositioned for COVID-19 therapeutic treatment.
Journal ArticleDOI
Plant fluid proteomics: Delving into the xylem sap, phloem sap and apoplastic fluid proteomes.
Jorge Rodríguez-Celma,Laura Ceballos-Laita,Michael A. Grusak,Javier Abadía,Ana-Flor López-Millán,Ana-Flor López-Millán +5 more
TL;DR: Comparisons of the proteomes of the three plant fluids indicates that although functional categories are somewhat similar, proteins involved are likely to be fluid-specific, except for a small group of proteins present in the three fluids, which may have a universal role, especially in cell wall maintenance and defense.
Journal ArticleDOI
Rutin Is a Low Micromolar Inhibitor of SARS-CoV-2 Main Protease 3CLpro: Implications for Drug Design of Quercetin Analogs
Bruno Rizzuti,Fedora Grande,Filomena Conforti,Ana Jiménez-Alesanco,Laura Ceballos-Laita,David Ortega-Alarcon,Sonia Vega,Hugh T. Reyburn,Olga Abian,Adrián Velázquez-Campoy +9 more
TL;DR: In this article, the authors used rutin, a natural flavonoid that is the most common glycosylated conjugate of quercetin, as a model combining experimental (spectroscopy and calorimetry) and simulation techniques (docking and molecular dynamics simulations).
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Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3.
M. de las Rivas,E.J. Paul Daniel,Yoshiki Narimatsu,Ismael Compañón,Kentaro Kato,Kentaro Kato,Pablo Hermosilla,A. Thureau,Laura Ceballos-Laita,Helena Coelho,Pau Bernadó,Filipa Marcelo,Lars Hansen,R. Maeda,Anabel Lostao,Anabel Lostao,Francisco Corzana,Henrik Clausen,Thomas A. Gerken,Ramon Hurtado-Guerrero +19 more
TL;DR: Polypeptide GalNAc-T3 catalyzes the specific glycosylation of threonine-178 of fibroblast growth factor 23, and structural insights reveal a unique lectin-based mechanism of substrate recognition.
Journal ArticleDOI
Structural basis for substrate specificity and catalysis of α1,6-fucosyltransferase.
Ana García-García,Laura Ceballos-Laita,Sonia Serna,Raik Artschwager,Niels C. Reichardt,Francisco Corzana,Ramon Hurtado-Guerrero +6 more
TL;DR: Crystal structure of FUT8 complexed with GDP and a biantennary complex N -glycan provides insight into both substrate recognition and catalysis, and serves as a framework for inhibitor design, and helps to assess its potential as a therapeutic target.