Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Giorgio Saladino"'
Autor:
Antonija Kuzmanic, Ludovico Sutto, Giorgio Saladino, Angel R Nebreda, Francesco L Gervasio, Modesto Orozco
Publikováno v:
eLife, Vol 6 (2017)
p38α is a Ser/Thr protein kinase involved in a variety of cellular processes and pathological conditions, which makes it a promising pharmacological target. Although the activity of the enzyme is highly regulated, its molecular mechanism of activati
Externí odkaz:
https://doaj.org/article/c79167d437ac42e5abc1ec4d6f61c530
Autor:
Silvia Lovera, Maria Morando, Encarna Pucheta-Martinez, Jorge L Martinez-Torrecuadrada, Giorgio Saladino, Francesco L Gervasio
Publikováno v:
PLoS Computational Biology, Vol 11, Iss 11, p e1004578 (2015)
Due to its inhibition of the Abl kinase domain in the BCR-ABL fusion protein, imatinib is strikingly effective in the initial stage of chronic myeloid leukemia with more than 90% of the patients showing complete remission. However, as in the case of
Externí odkaz:
https://doaj.org/article/2ecc17297dab46118e8fb7153abf9af8
Publikováno v:
Chemical Science
We propose an experimentally testable extended ternary complex model, where direction of the cooperative effect between ligand and intracellular binding partner (positive or negative) and its magnitude are predicted to be a characteristic of the liga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13c01531d2c93923709cf6488713cc1b
https://doi.org/10.1039/c6sc04647a
https://doi.org/10.1039/c6sc04647a
Autor:
Lorella Franzoni, F. Javier Luque, Francesco Luigi Gervasio, Carolina Estarellas, Salvatore Scaffidi, Carles Galdeano, Axel Bidon-Chanal, Giorgio Saladino, Francesca Spyrakis
Publikováno v:
Dipòsit Digital de la UB
Universidad de Barcelona
The Journal of Physical Chemistry Letters
Universidad de Barcelona
The Journal of Physical Chemistry Letters
Due to the poor aqueous solubility of retinoids, evolution has tuned their binding to cellular proteins to address specialized physiological roles by modulating uptake, storage, and delivery to specific targets. With the aim to disentangle the struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6001d4fdf4e93a8516512060fb92dbf
http://hdl.handle.net/2445/169992
http://hdl.handle.net/2445/169992
Autor:
Ricardo M. Biondi, Sonja Neimanis, Katrien Busschots, Pedro M. Alzari, Jörg O. Schulze, Evelyn Süß, Giorgio Saladino, Dalibor Odadzic, María-Natalia Lisa, Francesco Luigi Gervasio, Stefan Zeuzem, V. Hindie, Amanda K. Herbrand
Publikováno v:
Cell Chemical Biology
Cell Chemical Biology, 2016, 23 (10), pp.1193-1205. ⟨10.1016/j.chembiol.2016.06.017⟩
Cell Chemical Biology, Cell Press, 2016, 23 (10), pp.1193-1205. ⟨10.1016/j.chembiol.2016.06.017⟩
Cell Chemical Biology, 2016, 23 (10), pp.1193-1205. ⟨10.1016/j.chembiol.2016.06.017⟩
Cell Chemical Biology, Cell Press, 2016, 23 (10), pp.1193-1205. ⟨10.1016/j.chembiol.2016.06.017⟩
Allostery is a phenomenon observed in many proteins where binding of a macromolecular partner or a small-molecule ligand at one location leads to specific perturbations at a site not in direct contact with the region where the binding occurs. The lis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d867b386e72af28a9d576ede95d57628
https://doi.org/10.1016/j.chembiol.2016.06.017
https://doi.org/10.1016/j.chembiol.2016.06.017
Publikováno v:
Current Opinion in Structural Biology. 37:108-114
Most proteins assume different conformations to perform their cellular functions. This conformational dynamics is physiologically regulated by binding events and post-translational modifications, but can also be affected by pathogenic mutations. Atom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c58b09d529af341d0d2f4deedbf02a7
https://doi.org/10.1016/j.sbi.2016.01.005
https://doi.org/10.1016/j.sbi.2016.01.005
Autor:
Elena Papaleo, Francesco Luigi Gervasio, Kresten Lindorff-Larsen, Ruth Nussinov, Matteo Lambrughi, Giorgio Saladino
Publikováno v:
Chemical Reviews. 116:6391-6423
Proteins are dynamic entities that undergo a plethora of conformational changes that may take place on a wide range of time scales. These changes can be as small as the rotation of one or a few side-chain dihedral angles or involve concerted motions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e157c6398f4ba9068dcda65efa2c7ee
https://doi.org/10.1021/acs.chemrev.5b00623
https://doi.org/10.1021/acs.chemrev.5b00623
Autor:
Christopher J. Woods, Federico Comitani, Giorgio Saladino, Marc W. van der Kamp, Francesco Luigi Gervasio, Susanta Haldar, Adrian J. Mulholland
Publikováno v:
Haldar, S, Comitani, F, Saladino, G, Woods, C, Van der Kamp, M, Mulholland, A & Gervasio, F L 2018, ' A multiscale simulation approach to modelling drug-protein binding kinetics ', Journal of Chemical Theory and Computation . https://doi.org/10.1021/acs.jctc.8b00687
Drug–target binding kinetics has recently emerged as a sometimes critical determinant of in vivo efficacy and toxicity. Its rational optimization to improve potency or reduce side effects of drugs is, however, extremely difficult. Molecular simulat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0aac9b0c67247961843338bd5c04c1e4
https://pubmed.ncbi.nlm.nih.gov/30208708
https://pubmed.ncbi.nlm.nih.gov/30208708
Autor:
Christian Lange, Johan Hofkens, Sandra Liekens, Hongling Huang, Xu Wu, Joris Souffreau, Giorgio Saladino, Guy Eelen, Jaap D. van Buul, Saar Vandekeere, Wouter H. Lamers, Xuri Li, Gopala K. Jarugumilli, Federico Comitani, Annalisa Zecchin, Jermaine Goveia, Bert Cruys, Katleen Brepoels, Joanna Kalucka, Bart Ghesquière, Leanne M. Ramer, Ulrike Bruning, Michael DeRan, Charlotte Dubois, Francesco Luigi Gervasio, Jos van Rijssel, Stefan Vinckier, Sabine Wyns, Yi I. Wu, Mieke Dewerchin, Francisco Morales-Rodriguez, Susana Rocha, Rongyuan Chen, Richard M Cubbon, Luc Schoonjans, Lucas Treps, Peter Carmeliet, Anna Rita Cantelmo, Jurgen Haustraete
Publikováno v:
Nature, 561(7721), 63-69. Nature Publishing Group
Nature
Nature
Glutamine synthetase, encoded by the gene GLUL, is an enzyme that converts glutamate and ammonia to glutamine. It is expressed by endothelial cells, but surprisingly shows negligible glutamine-synthesizing activity in these cells at physiological glu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12d200895d1b6e0032d3de22a7951093
Small compounds modulating bi‐directional allostery in protein kinases: a new grip with an old trick
Autor:
Francesco Luigi Gervasio, Jörg O. Schulze, Klaus Strebhardt, Monika Raab, Evelyn Süß, Mourad Sanhaji, Ricardo M. Biondi, Larissa Pietsch, Giorgio Saladino, Katrien Busschots
Publikováno v:
The FASEB Journal. 32
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6bf3f6e684d6dceb7a077a5ec98f7227
https://doi.org/10.1096/fasebj.2018.32.1_supplement.797.2
https://doi.org/10.1096/fasebj.2018.32.1_supplement.797.2