Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Edoardo Salladini"'
Autor:
Lasse Staby, Katrine Bugge, Rasmus Greve Falbe-Hansen, Edoardo Salladini, Karen Skriver, Birthe B. Kragelund
Publikováno v:
Cell Communication and Signaling, Vol 19, Iss 1, Pp 1-5 (2021)
Abstract Background Signal fidelity depends on protein–protein interaction–‘hubs’ integrating cues from large interactomes. Recently, and based on a common secondary structure motif, the αα-hubs were defined, which are small α-helical doma
Externí odkaz:
https://doaj.org/article/0f3a368892d14c3984eea45a6dc59c50
Autor:
Edoardo Salladini, Frank Gondelaud, Juliet F. Nilsson, Giulia Pesce, Christophe Bignon, Maria Grazia Murrali, Roxane Fabre, Roberta Pierattelli, Andrey V. Kajava, Branka Horvat, Denis Gerlier, Cyrille Mathieu, Sonia Longhi
Publikováno v:
Biomolecules, Vol 11, Iss 9, p 1324 (2021)
Henipaviruses are BSL-4 zoonotic pathogens responsible in humans for severe encephalitis. Their V protein is a key player in the evasion of the host innate immune response. We previously showed that the Henipavirus V proteins consist of a long intrin
Externí odkaz:
https://doaj.org/article/234e3d406813456f85406aebe2351b06
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 24, p 9755 (2020)
Eukaryotic cells are complex biological systems that depend on highly connected molecular interaction networks with intrinsically disordered proteins as essential components. Through specific examples, we relate the conformational ensemble nature of
Externí odkaz:
https://doaj.org/article/535f5cdd28c649c7bca507242bdbdf28
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
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:
Mihaly Varadi, Sreenath Nair, Ian Sillitoe, Gerardo Tauriello, Stephen Anyango, Stefan Bienert, Clemente Borges, Mandar Deshpande, Tim Green, Demis Hassabis, Andras Hatos, Tamas Hegedus, Maarten L Hekkelman, Robbie Joosten, John Jumper, Agata Laydon, Dmitry Molodenskiy, Damiano Piovesan, Edoardo Salladini, Steven L Salzberg, Markus J Sommer, Martin Steinegger, Erzsebet Suhajda, Dmitri Svergun, Luiggi Tenorio-Ku, Silvio Tosatto, Kathryn Tunyasuvunakool, Andrew Mark Waterhouse, Augustin Žídek, Torsten Schwede, Christine Orengo, Sameer Velankar
While scientists can often infer the biological function of proteins from their 3-dimensional quaternary structures, the gap between the number of known protein sequences and their experimentally determined structures keeps increasing. A potential so
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7247b88a364bf7470938c0d77e6c583
https://edoc.unibas.ch/93047/
https://edoc.unibas.ch/93047/
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
Autor:
Juliet F Nilsson, Branka Horvat, Christophe Bignon, Roxane Fabre, Andrey V. Kajava, Sonia Longhi, Edoardo Salladini, Roberta Pierattelli, Frank Gondelaud, Cyrille Mathieu, Giulia Pesce, Denis Gerlier, Maria Grazia Murrali
Publikováno v:
Biomolecules
Biomolecules, 2021, 11 (9), pp.1324. ⟨10.3390/biom11091324⟩
Volume 11
Issue 9
Biomolecules, MDPI, 2021, 11 (9), pp.1324. ⟨10.3390/biom11091324⟩
Biomolecules, Vol 11, Iss 1324, p 1324 (2021)
'Biomolecules ', vol: 11, pages: 1324-1-1324-33 (2021)
Biomolecules, 2021, 11 (9), pp.1324. ⟨10.3390/biom11091324⟩
Volume 11
Issue 9
Biomolecules, MDPI, 2021, 11 (9), pp.1324. ⟨10.3390/biom11091324⟩
Biomolecules, Vol 11, Iss 1324, p 1324 (2021)
'Biomolecules ', vol: 11, pages: 1324-1-1324-33 (2021)
International audience; Henipaviruses are BSL-4 zoonotic pathogens responsible in humans for severe encephalitis. Their V protein is a key player in the evasion of the host innate immune response. We previously showed that the Henipavirus V proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bc0e607cc60e7271ee017074dc1c1db
https://hal.science/hal-03346263
https://hal.science/hal-03346263
Autor:
Frederik Friis Theisen, Edoardo Salladini, Rikke Davidsen, Christina Jo Rasmussen, Lasse Staby, Birthe B. Kragelund, Karen Skriver
Publikováno v:
Theisen, F F, Salladini, E, Davidsen, R, Rasmussen, C J, Staby, L, Kragelund, B B & Skriver, K 2022, ' αα-hub coregulator structure and flexibility determine transcription factor binding and selection in regulatory interactomes ', Journal of Biological Chemistry, vol. 298, no. 6, 101963 . https://doi.org/10.1016/j.jbc.2022.101963
Formation of transcription factor (TF)–coregulator complexes is a key step in transcriptional regulation, with coregulators having essential functions as hub nodes in molecular networks. How specificity and selectivity are maintained in these nodes
Autor:
Kiersten M. Ruff, Tamas Lazar, Claudiu C. Gradinaru, María Silvina Fornasari, Silvio C. E. Tosatto, Javier Iserte, Marie Skepö, Julia Marchetti, Sonia Longhi, Teresa Head-Gordon, Toby J. Gibson, Nicolás A. Méndez, Gregory-Neal W. Gomes, Malene Ringkjøbing Jensen, Nicolás A. Garrone, Pau Bernadó, Martin Blackledge, Alexander Miguel Monzon, Dmitri I. Svergun, András Hatos, Julie D. Forman-Kay, Cristina Marino-Buslje, Edward A. Lemke, Eric Fagerberg, Ana Julia Velez Rueda, Sylvain D. Vallet, Elizabeth Martínez-Pérez, Sylvie Ricard-Blum, Tiago N. Cordeiro, Federica Quaglia, Tadeo E. Saldaño, Damiano Piovesan, Peter Tompa, Tanja Mittag, Gustavo Parisi, Mihaly Varadi, Rohit V. Pappu, Lucía B. Chemes, Giovanni Minervini, Edoardo Salladini
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2021, 49 (D1), pp.D404-D411. ⟨10.1093/nar/gkaa1021⟩
Nucleic acids research, vol 49, iss D1
Nucleic Acids Research, 2021, 49 (D1), pp.D404-D411. ⟨10.1093/nar/gkaa1021⟩
Nucleic Acids Research, Oxford University Press, In press, ⟨10.1093/nar/gkaa1021⟩
Nucleic Acids Research, In press, ⟨10.1093/nar/gkaa1021⟩
Nucleic Acids Research, Oxford University Press, 2021, 49 (D1), pp.D404-D411. ⟨10.1093/nar/gkaa1021⟩
Nucleic acids research, vol 49, iss D1
Nucleic Acids Research, 2021, 49 (D1), pp.D404-D411. ⟨10.1093/nar/gkaa1021⟩
Nucleic Acids Research, Oxford University Press, In press, ⟨10.1093/nar/gkaa1021⟩
Nucleic Acids Research, In press, ⟨10.1093/nar/gkaa1021⟩
The Protein Ensemble Database (PED) (https://proteinensemble.org), which holds structural ensembles of intrinsically disordered proteins (IDPs), has been significantly updated and upgraded since its last release in 2016. The new version, PED 4.0, has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d62579a66daeda9d1cb3ef52f41885bf
https://hal.univ-grenoble-alpes.fr/hal-03433964/document
https://hal.univ-grenoble-alpes.fr/hal-03433964/document