J
Jesús Jiménez-Barbero
Researcher at Ikerbasque
Publications - 701
Citations - 21186
Jesús Jiménez-Barbero is an academic researcher from Ikerbasque. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Molecular recognition. The author has an hindex of 67, co-authored 673 publications receiving 18902 citations. Previous affiliations of Jesús Jiménez-Barbero include SIDI & Hunter College.
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Journal ArticleDOI
New Glucosamine-Based TLR4 Agonists: Design, Synthesis, Mechanism of Action, and In Vivo Activity as Vaccine Adjuvants
Alessio Romerio,Nicole Gotri,Ana Rita Franco,Valentina Artusa,Mohammed Monsoor Shaik,Samuel T Pasco,Unai Atxabal,Alejandra Matamoros-Recio,Marina Mínguez-Toral,Juan Diego Zalamea,Antonio Franconetti,Nicola G. A. Abrescia,Jesús Jiménez-Barbero,Juan Anguita,Sonsoles Martín-Santamaría,Francesco Peri +15 more
TL;DR: In this paper, a panel of small-molecule TLR4 agonists (the FP20 series) whose structure is derived from previously developed TLR 4 ligands (FP18 series) was revealed.
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Syntheses of All the Possible Monomethyl Ethers and Several Deoxyhalo Analogues of Methyl β-Lactoside as Ligands for the Ricinus communis Lectins.
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Conformational analysis of peptides and glycopeptides derived from the consensus sequence for β-O-glucosylation.
Víctor J. Somovilla,Nuria Martinez-Saez,Alberto Fernández-Tejada,Beatriz G. de la Torre,David Andreu,Jesús Jiménez-Barbero,Juan Luis Asensio,Alberto Avenoza,Jesús H. Busto,Francisco Corzana,Jesús M. Peregrina +10 more
TL;DR: These studies, based on the use of NOESY experiments in combination with molecular dynamics simulations, indicate that for this particular fragment, initially characterized by a type I β-turn motif, the glycosylation with β-O-Glc forces the peptide backbone into an extended conformation.
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Hydrogen Bonding and Cooperativity Effects on the Assembly of Carbohydrates.
TL;DR: In this article, the authors studied the role of hydrogen bonding and cation binding in the recognition processes in which carbohydrates are involved, and found that their relative participations are related to the topology of the carbohydrate, to the particular orientation of the residues exposed to the interaction, and to the medium which surrounds the sugar.
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NMR Investigation of Protein‐Carbohydrate Interactions: The Recognition of Glycans by Galectins Engineered with Fluorotryptophan Residues
Marta G. Lete,Antonio Franconetti,Sara Bertuzzi,Sandra Delgado,Mikel Azkargorta,Felix Elortza,Oscar Millet,Gonzalo Jiménez-Osés,Ana Ardá,Jesús Jiménez-Barbero +9 more
TL;DR: In this paper , the presence of fluorine did not significantly modify the affinity for glycan binding, which was in slow exchange on the 19F NMR chemical shift timescale, and allowed binding events taking place at two different binding sites within the same lectin to be individualized.