Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Michela, Bollati"'
Autor:
Elettra Fasola, Giulia Alboreggia, Stefano Pieraccini, Francesco Oliva, Fatima Ezzahra Agharbaoui, Michela Bollati, Giovanni Bertoni, Sandro Recchia, Marcello Marelli, Umberto Piarulli, Sara Pellegrino, Silvia Gazzola
Publikováno v:
Frontiers in Chemistry, Vol 10 (2022)
Protein-mimetic peptides (PMPs) are shorter sequences of self-assembling proteins, that represent remarkable building blocks for the generation of bioinspired functional supramolecular structures with multiple applications. The identification of nove
Externí odkaz:
https://doaj.org/article/57660a43b92941efa51d02555b2fa7da
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:
Michela Bollati, Kaliroi Peqini, Luigi Barone, Carmina Natale, Marten Beeg, Marco Gobbi, Luisa Diomede, Michelangelo Trucchi, Matteo de Rosa, Sara Pellegrino
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 22, p 13973 (2022)
Gelsolin amyloidosis (AGel) is characterized by multiple systemic and ophthalmic features resulting from pathological tissue deposition of the gelsolin (GSN) protein. To date, no cure is available for the treatment of any form of AGel. More than ten
Externí odkaz:
https://doaj.org/article/7db0697bd1fe4a8d9d78a8fd9c2926f4
Autor:
Maja Potrč, Marija Volk, Matteo de Rosa, Jože Pižem, Nataša Teran, Helena Jaklič, Aleš Maver, Brigita Drnovšek-Olup, Michela Bollati, Katarina Vogelnik, Alojzija Hočevar, Ana Gornik, Vladimir Pfeifer, Borut Peterlin, Marko Hawlina, Ana Fakin
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 3, p 1084 (2021)
Gelsolin amyloidosis typically presents with corneal lattice dystrophy and is most frequently associated with pathogenic GSN variant p.Asp214Asn. Here we report clinical and histopathological features of gelsolin amyloidosis associated with a novel G
Externí odkaz:
https://doaj.org/article/d8d75b2f377c427099932851715d1170
Autor:
Michela, Bollati, Louise J, Gourlay
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2548
The prerequisite for 3D structure determination of macromolecules via X-ray crystallography is well-ordered, diffracting crystals. Here, we report the recombinant production, biophysical/biochemical protein sample characterization, and vapor diffusio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::436e302cbe8a7b0f7f6d027b3a0edf85
https://pubmed.ncbi.nlm.nih.gov/36151502
https://pubmed.ncbi.nlm.nih.gov/36151502
Autor:
Michela Bollati, Louise J. Gourlay
Publikováno v:
Lipopolysaccharide Transport ISBN: 9781071625804
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f23cd9f2acc4b8cd44c9601790b7f67
http://hdl.handle.net/2434/940747
http://hdl.handle.net/2434/940747
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
Autor:
Maja, Potrč, Marija, Volk, Matteo, de Rosa, Jože, Pižem, Nataša, Teran, Helena, Jaklič, Aleš, Maver, Brigita, Drnovšek-Olup, Michela, Bollati, Katarina, Vogelnik, Alojzija, Hočevar, Ana, Gornik, Vladimir, Pfeifer, Borut, Peterlin, Marko, Hawlina, Ana, Fakin
Publikováno v:
International Journal of Molecular Sciences
Simple Summary Gelsolin amyloidosis is a rare autosomal dominant genetic disease, which typically affects the cornea, skin and sometimes other organ systems and is caused by mutations in a gene coding for gelsolin protein (GSN). We describe a novel m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fb428a044bff32f083ec8072769d477e
https://pubmed.ncbi.nlm.nih.gov/33499149
https://pubmed.ncbi.nlm.nih.gov/33499149
The SARS-unique domain (SUD) of SARS coronavirus contains two macrodomains that bind G-quadruplexes.
Autor:
Jinzhi Tan, Clemens Vonrhein, Oliver S Smart, Gerard Bricogne, Michela Bollati, Yuri Kusov, Guido Hansen, Jeroen R Mesters, Christian L Schmidt, Rolf Hilgenfeld
Publikováno v:
PLoS Pathogens, Vol 5, Iss 5, p e1000428 (2009)
Since the outbreak of severe acute respiratory syndrome (SARS) in 2003, the three-dimensional structures of several of the replicase/transcriptase components of SARS coronavirus (SARS-CoV), the non-structural proteins (Nsps), have been determined. Ho
Externí odkaz:
https://doaj.org/article/137c81640abf4e259792909f4b067f85
High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion
Autor:
Mario Milani, Eloise Mastrangelo, Michela Bollati, Francesco Bonì, Toni Giorgino, Emanuele Scalone, Matteo de Rosa
Publikováno v:
Biochemical and biophysical research communications
518 (2019): 94–99. doi:10.1016/j.bbrc.2019.08.013
info:cnr-pdr/source/autori:Bollati M, Scalone E, Bonì F, Mastrangelo E, Giorgino T, Milani M, de Rosa M/titolo:High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion/doi:10.1016%2Fj.bbrc.2019.08.013/rivista:Biochemical and biophysical research communications (Print)/anno:2019/pagina_da:94/pagina_a:99/intervallo_pagine:94–99/volume:518
518 (2019): 94–99. doi:10.1016/j.bbrc.2019.08.013
info:cnr-pdr/source/autori:Bollati M, Scalone E, Bonì F, Mastrangelo E, Giorgino T, Milani M, de Rosa M/titolo:High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion/doi:10.1016%2Fj.bbrc.2019.08.013/rivista:Biochemical and biophysical research communications (Print)/anno:2019/pagina_da:94/pagina_a:99/intervallo_pagine:94–99/volume:518
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:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f539b61e933396a7a3f683fc968c97a5
http://arxiv.org/abs/1911.08188
http://arxiv.org/abs/1911.08188