Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Irene Boniardi"'
Autor:
Irene Boniardi, Angela Corona, Jerome Basquin, Claire Basquin, Jessica Milia, István Nagy, Enzo Tramontano, Luca Zinzula
Publikováno v:
Virus Research, Vol 336, Iss , Pp 199221- (2023)
The coronavirus disease 2019 (COVID-19) pandemic is fading, however its etiologic agent severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues posing - despite the availability of licensed vaccines – a global health threat, due to t
Externí odkaz:
https://doaj.org/article/c9f157f1bbc3493584d7abde09ddb9a6
Autor:
Michela Bollati, Luisa Diomede, Toni Giorgino, Carmina Natale, Elisa Fagnani, Irene Boniardi, Alberto Barbiroli, Rebecca Alemani, Marten Beeg, Marco Gobbi, Ana Fakin, Eloise Mastrangelo, Mario Milani, Gianluca Presciuttini, Edi Gabellieri, Patrizia Cioni, Matteo de Rosa
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 6355-6365 (2021)
Gelsolin comprises six homologous domains, named G1 to G6. Single point substitutions in this protein are responsible for AGel amyloidosis, a hereditary disease causing progressive corneal lattice dystrophy, cutis laxa, and polyneuropathy. Although s
Externí odkaz:
https://doaj.org/article/28c0fa7cd36a48168031138ec41efe6d
Autor:
Marco Gobbi, Carmina Natale, Luisa Diomede, Rebecca Alemani, Mario Milani, Alberto Barbiroli, Michela Bollati, Patrizia Cioni, Irene Boniardi, Toni Giorgino, Eloise Mastrangelo, Gianluca Presciuttini, Ana Fakin, Marten Beeg, Matteo de Rosa, Edi Gabellieri, Elisa Fagnani
Publikováno v:
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 6355-6365 (2021)
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 6355-6365 (2021)
Graphical abstract
Highlights • Three novel gelsolin amyloidogenic substitutions cluster at the G4:G5 interface. • Mutations impair stability through strand distortion, charge and steric repulsion. • Mutations do not increase sensitivity t
Highlights • Three novel gelsolin amyloidogenic substitutions cluster at the G4:G5 interface. • Mutations impair stability through strand distortion, charge and steric repulsion. • Mutations do not increase sensitivity t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e76cf088c80ac1558bf8a9d5ff7a2bc
