Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Federica, Quaglia"'
Autor:
Damiano Piovesan, Andras Hatos, Giovanni Minervini, Federica Quaglia, Alexander Miguel Monzon, Silvio C E Tosatto
Publikováno v:
PLoS Computational Biology, Vol 16, Iss 6, p e1007967 (2020)
Post-translational modification (PTM) sites have become popular for predictor development. However, with the exception of phosphorylation and a handful of other examples, PTMs suffer from a limited number of available training examples and sparsity i
Externí odkaz:
https://doaj.org/article/622e220bd713406783649d3739009b3a
Publikováno v:
Italian Journal of Medicine, Vol 11, Iss 1, Pp 41-47 (2017)
Leukocytosis is regarded as a reliable marker of a serious disorder requiring hospitalization. However, leukocytosis often disappears once the patient is admitted to a medical ward; differential diagnosis of leukocytosis is often overlooked in the bu
Externí odkaz:
https://doaj.org/article/97ecfdc69b2b4adcbfefb2a81a67af6f
Publikováno v:
PLoS Computational Biology, Vol 15, Iss 4, p e1006478 (2019)
Familiar cancers represent a privileged point of view for studying the complex cellular events inducing tumor transformation. Von Hippel-Lindau syndrome, a familiar predisposition to develop cancer is a clear example. Here, we present our efforts to
Externí odkaz:
https://doaj.org/article/9fcacfd197c44bd9829457b25ca7e04b
Autor:
Federica Quaglia, Edoardo Salladini, Marco Carraro, Giovanni Minervini, Silvio C.E. Tosatto, Philippe Le Mercier
Publikováno v:
The FEBS Journal. 289:4240-4250
The SARS-CoV-2 pandemic is maintained by the emergence of successive variants, highlighting the flexibility of the protein sequences of the virus. We show that experimentally determined intrinsically disordered regions (IDRs) are abundant in the SARS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bcc08fd340dd77f634bdd7cdcd9eebd
https://doi.org/10.1111/febs.16379
https://doi.org/10.1111/febs.16379
Autor:
Eric W. Deutsch, Juan Antonio Vizcaíno, Andrew R. Jones, Pierre-Alain Binz, Henry Lam, Joshua Klein, Wout Bittremieux, Yasset Perez-Riverol, David L. Tabb, Mathias Walzer, Sylvie Ricard-Blum, Henning Hermjakob, Steffen Neumann, Tytus D. Mak, Shin Kawano, Luis Mendoza, Tim Van Den Bossche, Ralf Gabriels, Nuno Bandeira, Jeremy Carver, Benjamin Pullman, Zhi Sun, Nils Hoffmann, Jim Shofstahl, Yunping Zhu, Luana Licata, Federica Quaglia, Silvio C. E. Tosatto, Sandra E. Orchard
Publikováno v:
Journal of proteome research
JOURNAL OF PROTEOME RESEARCH
JOURNAL OF PROTEOME RESEARCH
The Human Proteome Organization (HUPO) Proteomics Standards Initiative (PSI) has been successfully developing guidelines, data formats, and controlled vocabularies (CVs) for the proteomics community and other fields supported by mass spectrometry sin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c134d30524765e956ad3db0844e8b11
https://hdl.handle.net/10067/1935320151162165141
https://hdl.handle.net/10067/1935320151162165141
Autor:
Alexander Miguel Monzon, Marco Necci, Federica Quaglia, Ian Walsh, Giuseppe Zanotti, Damiano Piovesan, Silvio C. E. Tosatto
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 12, p 4496 (2020)
Intrinsically disordered protein regions are commonly defined from missing electron density in X-ray structures. Experimental evidence for long disorder regions (LDRs) of at least 30 residues was so far limited to manually curated proteins. Here, we
Externí odkaz:
https://doaj.org/article/e1acc286f2a44e91b0b34aad82e9a160
Autor:
Eric W Deutsch, Juan Antonio Vizcaíno, Andrew R Jones, Pierre-Alain Binz, Henry Lam, Joshua Klein, Wout Bittremieux, Yasset Perez-Riverol, David L Tabb, Mathias Walzer, Sylvie Ricard-Blum, Henning Hermjakob, Steffen Neumann, Tytus D Mak, Shin Kawano, Luis Mendoza, Tim Van Den Bossche, Ralf Gabriels, Nuno Bandeira, Jeremy Carver, Benjamin Pullman, Zhi Sun, Nils Hoffmann, Jim Shofstahl, Yunping Zhu, Luana Licata, Federica Quaglia, Silvio CE Tosatto, Sandra E Orchard
The Human Proteome Organization (HUPO) Proteomics Standards Initiative (PSI) has been successfully developing guidelines, data formats, and controlled vocabularies (CVs) for the proteomics community and other fields supported by mass spectrometry sin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ba7caa58ce0d862afd310bf15929bc27
https://doi.org/10.26434/chemrxiv-2022-ksqg1
https://doi.org/10.26434/chemrxiv-2022-ksqg1
Autor:
Bálint Mészáros, András Hatos, Nicolas Palopoli, Federica Quaglia, Edoardo Salladini, Kim Van Roey, Haribabu Arthanari, Zsuzsanna Dosztányi, Isabella C. Felli, Patrick D Fischer, Jeffrey C. Hoch, Cy M Jeffries, Sonia Longhi, Emiliano Maiani, Sandra Orchard, Rita Pancsa, Elena Papaleo, Roberta Pierattelli, Damiano Piovesan, Iva Pritisanac, Thibault Viennet, Peter Tompa, Wim Vranken, Silvio CE Tosatto, Norman E Davey
An unambiguous description of an experimental setup and analysis, and the subsequent biological observation is vital for accurate data interpretation and reproducible results. Consequently, experimental analyses should be described in a concise, uneq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::21f49f4a10a13805abedf2e351f974a8
https://doi.org/10.1101/2022.07.12.495092
https://doi.org/10.1101/2022.07.12.495092
Autor:
Suvarna Nadendla, Rebecca Jackson, James Munro, Federica Quaglia, Bálint Mészáros, Dustin Olley, Elizabeth T Hobbs, Stephen M Goralski, Marcus Chibucos, Christopher John Mungall, Silvio C E Tosatto, Ivan Erill, Michelle G Giglio
Publikováno v:
Nucleic Acids Research
Nucleic Acids Res.
Nucleic Acids Res.
The Evidence and Conclusion Ontology (ECO) is a community resource that provides an ontology of terms used to capture the type of evidence that supports biomedical annotations and assertions. Consistent capture of evidence information with ECO allows
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3807b9c89c6de356e9661dca9e387843
http://hdl.handle.net/11577/3412567
http://hdl.handle.net/11577/3412567
DisProt is the major repository of manually curated data for intrinsically disordered proteins collected from the literature. Although lacking a stable three-dimensional structure under physiological conditions, intrinsically disordered proteins carr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3f5de0de811a5a15f5be36f68b81ef7
https://hdl.handle.net/11577/3469413
https://hdl.handle.net/11577/3469413