Zobrazeno 1 - 10
of 257
pro vyhledávání: '"Mastrangelo Eloise"'
Autor:
Erba Fulvio, Di Paola Luisa, Di Venere Almerinda, Mastrangelo Eloise, Cossu Federica, Mei Giampiero, Minicozzi Velia
Publikováno v:
Biomolecular Concepts, Vol 14, Iss 1, Pp 105-53 (2023)
Tumor necrosis factor receptor-associated factor proteins (TRAFs) are trimeric proteins that play a fundamental role in signaling, acting as intermediaries between the tumor necrosis factor (TNF) receptors and the proteins that transmit the downstrea
Externí odkaz:
https://doaj.org/article/404fe9b9284f48bb990a644098ea3431
Autor:
Bollati, Michela, Diomede, Luisa, Giorgino, Toni, Natale, Carmina, Fagnani, Elisa, Boniardi, Irene, Barbiroli, Alberto, Alemani, Rebecca, Beeg, Marten, Gobbi, Marco, Fakin, Ana, Mastrangelo, Eloise, Milani, Mario, Presciuttini, Gianluca, Gabellieri, Edi, Cioni, Patrizia, de Rosa, Matteo
The multidomain protein gelsolin (GSN) is composed of six homologous modules, sequentially named G1 to G6. Single point substitutions in this protein are responsible for AGel amyloidosis, a hereditary disease characterized by progressive corneal latt
Externí odkaz:
http://arxiv.org/abs/2109.07190
Autor:
Fagnani, Elisa, Cocomazzi, Paolo, Pellegrino, Sara, Tedeschi, Gabriella, Scalvini, Francesca Grassi, Cossu, Federica, Da Vela, Stefano, Aliverti, Alessandro, Mastrangelo, Eloise, Milani, Mario
Publikováno v:
In Structure 2 May 2024 32(5):594-602
Autor:
Cossu, Federica, Sorrentino, Luca, Fagnani, Elisa, Zaffaroni, Mattia, Milani, Mario, Giorgino, Toni, Mastrangelo, Eloise
Publikováno v:
J. Chem. Inf. Model. 2020, 60, 10, 5036-5044
Protein-protein interactions are the basis of many important physiological processes and are currently promising, yet difficult, targets for drug discovery. In this context, inhibitor of apoptosis proteins (IAPs)-mediated interactions are pivotal for
Externí odkaz:
http://arxiv.org/abs/2103.10915
Akademický článek
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High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion
Autor:
Bollati, Michela, Scalone, Emanuele, Bonì, Francesco, Mastrangelo, Eloise, Giorgino, Toni, Milani, Mario, de Rosa, Matteo
Publikováno v:
Biochem Biophys Res Commun. 2019 Oct 8;518(1):94-99
The second domain of gelsolin (G2) hosts mutations responsible for a hereditary form of amyloidosis. The active form of gelsolin is Ca2+-bound; it is also a dynamic protein, hence structural biologists often rely on the study of the isolated G2. Howe
Externí odkaz:
http://arxiv.org/abs/1911.08188
Autor:
de Rosa, Matteo, Barbiroli, Alberto, Bonì, Francesco, Scalone, Emanuele, Mattioni, Davide, Vanoni, Maria A., Patrone, Marco, Bollati, Michela, Mastrangelo, Eloise, Giorgino, Toni, Milani, Mario
Publikováno v:
Eur Biophys J. 2019 Nov 13
Mutations in the gelsolin protein are responsible for a rare conformational disease known as AGel amyloidosis. Four of these mutations are hosted by the second domain of the protein (G2): D187N/Y, G167R and N184K. The impact of the latter has been so
Externí odkaz:
http://arxiv.org/abs/1911.08194
Autor:
Giorgino, Toni, Mattioni, Davide, Hassan, Amal, Milani, Mario, Mastrangelo, Eloise, Barbiroli, Alberto, Verhelle, Adriaan, Gettemans, Jan, Barzago, Maria Monica, Diomede, Luisa, de Rosa, Matteo
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. Volume 1865, Issue 3, 1 March 2019, Pages 648-660
AGel amyloidosis, formerly known as familial amyloidosis of the Finnish-type, is caused by pathological aggregation of proteolytic fragments of plasma gelsolin. So far, four mutations in the gelsolin gene have been reported as responsible for the dis
Externí odkaz:
http://arxiv.org/abs/1903.07308
Akademický článek
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Akademický článek
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