Fabio Doro
University of Milan
5 Papers
35 Citations
Fabio Doro is an academic researcher from University of Milan. The author has contributed to research in topics: Energy landscape & Langerin. The author has an hindex of 5, co-authored 5 publications.
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Papers
Insights into molecular recognition of Lewis(X) mimics by DC-SIGN using NMR and molecular modelling.
Cinzia Guzzi,Jesús Angulo,Fabio Doro,José J. Reina,Michel Thépaut,Franck Fieschi,Franck Fieschi,Anna Bernardi,Javier Rojo,Pedro M. Nieto +9 more
TL;DR: This work has studied in detail the binding of two α-fucosylamide-based mimics of Lewis(X) to DC-SIGN ECD (ECD = extracellular domain) using STD NMR and docking and concluded that the binding mode occurs mainly through the fucose moiety.
Computational design of novel peptidomimetic inhibitors of cadherin homophilic interactions.
Fabio Doro,Cinzia Colombo,Chiara Alberti,Daniela Arosio,Laura Belvisi,Cesare Casagrande,Roberto Fanelli,Leonardo Manzoni,Emilio Parisini,Umberto Piarulli,Elena Luison,Mariangela Figini,Antonella Tomassetti,Monica Civera +13 more
TL;DR: A first set of peptidomimetic ligands mimicking the adhesive interface identified by recent crystallographic structures of E- and N-cadherin are reported, inhibit adhesion of epithelial ovarian cancer cells with improved efficacy compared to the ADH-1 peptide.
α-N-Linked glycopeptides: conformational analysis and bioactivity as lectin ligands
Filipa Marcelo,Francisco Javier Cañada,Sabine André,Cinzia Colombo,Fabio Doro,Hans-Joachim Gabius,Anna Bernardi,Jesús Jiménez-Barbero +7 more
TL;DR: NMR- and modelling-based data on glycomimetics containing α-glycosidic linkages provide the basis to introduce α-substituted neoglycopeptides to the toolbox of scaffold for the design of potent lectin inhibitors.
New Insights into the Molecular Mechanism of E-Cadherin-Mediated Cell Adhesion by Free Energy Calculations
TL;DR: The conformational changes that lead to activation and dimerization via domain swapping of E-cadherin are studied, finding that the open state population is increased in the presence of calcium ions at the extracellular boundary, suggesting their possible role as allosteric activators of the conformational change.
Second generation of fucose-based DC-SIGN ligands: affinity improvement and specificity versus Langerin.
Manuel Andreini,Daniela Doknic,Ieva Sutkeviciute,José J. Reina,Janxin Duan,Eric Chabrol,Michel Thépaut,Elisabetta Moroni,Fabio Doro,Laura Belvisi,Joerg Weiser,Javier Rojo,Franck Fieschi,Franck Fieschi,Anna Bernardi +14 more
TL;DR: DC-SIGN and Langerin are two C-type lectins involved in the initial steps of HIV infections: the former acts as a viral attachment factor and facilitates viral invasion of the immune system, the latter has a protective effect.