个人简介

Francesco Luigi Gervasio is Professor of Chemistry and Structural and Molecular Biology. Prof. Gervasio’s research focuses on the development of computational methods to study molecular recognition and large-scale conformational changes in bio-molecules. His multidisciplinary research group consists in 1 PDRA and 4 PhD students and it is supported by EPSRC (EP/M013898/1), BBSRC, Wellcome, A*STAR and EU FP7 (IMI, MC). He has an H-index of 34, a total of 3483 citations and more than 80 publications in high-impact journals, including Cancer Cell, PNAS, JACS, Angew. Chem. Acc. Chem. Res., PRL. He has worked at UCL since 2013. Before this he was assistant PDRA and assistant professor at ETH Zurich (2002-2009), Leader of the computational biophysics group at the Spanish National Cancer Research Centre in Madrid (2009-2013).

研究领域

Physical Chemistry

Biomolecular Simulations Development of enhanced-sampling algorithms Drug discovery Structural Biology NMR

近期论文

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Saleh, N., Saladino, G., Gervasio, F. L., Haensele, E., Banting, L., Whitley, D. C., . . . Clark, T. (2016). A Three-Site Mechanism for Agonist/Antagonist Selective Binding to Vasopressin Receptors. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 55 (28), 8008-8012. doi:10.1002/anie.201602729 Ruiz-Pérez, L., Messager, L., Gaitzsch, J., Joseph, A., Sutto, L., Gervasio, F. L., & Battaglia, G. (2016). Molecular engineering of polymersome surface topology. Science advances, 2 (4), e1500948. doi:10.1126/sciadv.1500948 Papaleo, E., Saladino, G., Lambrughi, M., Lindorff-Larsen, K., Gervasio, F. L., & Nussinov, R. (2016). The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery. CHEMICAL REVIEWS, 116 (11), 6391-6423. doi:10.1021/acs.chemrev.5b00623 Oleinikovas, V., Saladino, G., Cossins, B. P., & Gervasio, F. L. (2016). Understanding Cryptic Pocket Formation in Protein Targets by Enhanced Sampling Simulations. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 138 (43), 14257-14263. doi:10.1021/jacs.6b05425 Sutto, L., Marsili, S., Valencia, A., & Gervasio, F. L. (2015). From residue coevolution to protein conformational ensembles and functional dynamics. Proceedings of the National Academy of Sciences, 112 (44), 13567-13572. doi:10.1073/pnas.1508584112 Cavalli, A., Spitaleri, A., Saladino, G., & Gervasio, F. L. (2015). Investigating Drug–Target Association and Dissociation Mechanisms Using Metadynamics-Based Algorithms. Accounts of Chemical Research, 48 (2), 277-285. doi:10.1021/ar500356n Marino, K. A., Sutto, L., & Gervasio, F. L. (2015). The Effect of a Widespread Cancer-Causing Mutation on the Inactive to Active Dynamics of the B-Raf Kinase. Journal of the American Chemical Society, 137, 5280-5283. doi:10.1021/jacs.5b01421 Sutto, L., & Gervasio, F. L. (2013). Effects of oncogenic mutations on the conformational free-energy landscape of EGFR kinase. Proceedings of the National Academy of Sciences, 110 (26), 10616-10621. doi:10.1073/pnas.1221953110 Juraszek, J., Saladino, G., van Erp, T. S., & Gervasio, F. L. (2013). Efficient Numerical Reconstruction of Protein Folding Kinetics with Partial Path Sampling and Pathlike Variables. Phys. Rev. Lett., 110, 108106. doi:10.1103/PhysRevLett.110.108106 Herbert, C., Schieborr, U., Saxena, K., Juraszek, J., De Smet, F., Alcouffe, C., . . . Bono, F. C. C. (2013). Molecular Mechanism of SSR128129E, an Extracellularly Acting, Small-Molecule, Allosteric Inhibitor of FGF Receptor Signaling. Cancer cell, 23, 489-501. Sahún-Roncero, M., Rubio-Ruiz, B., Saladino, G., Conejo-García, A., Espinosa, A., Velázquez-Campoy, A., . . . Hurtado-Guerrero, R. (2013). The mechanism of allosteric coupling in choline kinase α1 revealed by the action of a rationally designed inhibitor. Angew Chem Int Ed Engl, 52 (17), 4582-4586. doi:10.1002/anie.201209660 D'Abramo, M., Rabal, O., Oyarzabal, J., & Gervasio, F. L. (2012). Conformational Selection versus Induced Fit in Kinases: The Case of PI3K-gamma. Angewandte Chemie-International Edition, 51 (3), 642-646. doi:10.1002/anie.201103264 Lovera, S., Sutto, L., Boubeva, R., Scapozza, L., Doelker, N., & Gervasio, F. L. (2012). The Different Flexibility of c-Src and c-Abl Kinases Regulates the Accessibility of a Druggable Inactive Conformation. Journal of the American Chemical Society, 134 (5), 2496-2499. doi:10.1021/ja210751t Limongelli, V., Bonomi, M., Marinelli, L., Luigi Gervasio, F., Cavalli, A., Novellino, E., & Parrinello, M. (2010). Molecular basis of cyclooxygenase enzymes (COXs) selective inhibition. Proceedings of the National Academy of Sciences of the United States of America, 107 (12), 5411-5416. doi:10.1073/pnas.0913377107 Perdios, P., Lowe, A. R., Saladino, G., Bunney, D. T., Thiyagarajan, N., Alexandrov, Y., . . . Katan, M. (2017). Conformational transition of FGFR kinase activation revealed by site-­specific unnatural amino acid reporter and single molecule FRET. Scientific Reports. Pucheta-Martinez, E., Saladino, G., Morando, M. A., Martinez-Torrecuadrada, J., Lelli, M., Sutto, L., . . . Gervasio, F. L. (2016). An Allosteric Cross-Talk Between the Activation Loop and the ATP Binding Site Regulates the Activation of Src Kinase. SCIENTIFIC REPORTS, 6, ARTN 24235. doi:10.1038/srep24235 Schulze, J. O., Saladino, G., Busschots, K., Neimanis, S., Süß, E., Odadzic, D., . . . Biondi, R. M. (2016). Bidirectional Allosteric Communication between the ATP-Binding Site and the Regulatory PIF Pocket in PDK1 Protein Kinase. Cell Chem Biol. doi:10.1016/j.chembiol.2016.06.017 Agnese Morando, M., Saladino, G., D'Amelio, N., Pucheta-Martinez, E., Lovera, S., Lelli, M., . . . Gervasio, F. L. (2016). Conformational Selection and Induced Fit Mechanisms in the Binding of an Anticancer Drug to the c-Src Kinase. SCIENTIFIC REPORTS, 6, ARTN 24439. doi:10.1038/srep24439 Lambrughi, M., De Gioia, L., Gervasio, F. L., Lindorff-Larsen, K., Nussinov, R., Urani, C., . . . Papaleo, E. (2016). DNA-binding protects p53 from interactions with cofactors involved in transcription-independent functions. Nucleic Acids Research, gkw770. doi:10.1093/nar/gkw770 Saladino, G., & Gervasio, F. L. (2016). Modeling the effect of pathogenic mutations on the conformational landscape of protein kinases. CURRENT OPINION IN STRUCTURAL BIOLOGY, 37, 108-114. doi:10.1016/j.sbi.2016.01.005 Doro, F., Saladino, G., Belvisi, L., Civera, M., & Gervasio, F. L. (2015). New Insights into the Molecular Mechanism of E-Cadherin-Mediated Cell Adhesion by Free Energy Calculations. Journal of Chemical Theory and Computation, 11, 1354-1359. doi:10.1021/ct5010164 Bunney, T. D., Wan, S., Thiyagarajan, N., Sutto, L., Williams, S. V., Ashford, P., . . . Katan, M. (2015). The Effect of Mutations on Drug Sensitivity and Kinase Activity of Fibroblast Growth Factor Receptors: A Combined Experimental and Theoretical Study. EBioMedicine, 2 (3), 194-204. Papaleo, E., Sutto, L., Gervasio, F. L., & Lindorff-Larsen, K. (2014). Conformational Changes and Free Energies in a Proline Isomerase. Journal of Chemical Theory and Computation, 10, 4169-4174. doi:10.1021/ct500536r Wolkenhauer, O., Auffray, C., Brass, O., Clairambault, J., Deutsch, A., Drasdo, D., . . . Byrne, H. (2014). Enabling multiscale modeling in systems medicine. Genome medicine, 6, 1-3. Goñi, G. M., Epifano, C., Boskovic, J., Camacho-Artacho, M., Zhou, J., Bronowska, A., . . . Lietha, D. (2014). Phosphatidylinositol 4,5-bisphosphate triggers activation of focal adhesion kinase by inducing clustering and conformational changes. Proceedings of the National Academy of Sciences, 111, E3177-E3186. doi:10.1073/pnas.1317022111