Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Giulia Faravelli"'
Autor:
Sara Raimondi, Giulia Faravelli, Paola Nocerino, Valentina Mondani, Alma Baruffaldi, Loredana Marchese, Maria Chiara Mimmi, Diana Canetti, Guglielmo Verona, Marianna Caterino, Margherita Ruoppolo, P. Patrizia Mangione, Vittorio Bellotti, Francesca Lavatelli, Sofia Giorgetti
Publikováno v:
FASEB BioAdvances, Vol 5, Iss 11, Pp 484-505 (2023)
Abstract β2‐microglobulin (β2‐m) is a plasma protein derived from physiological shedding of the class I major histocompatibility complex (MHCI), causing human systemic amyloidosis either due to persistently high concentrations of the wild‐typ
Externí odkaz:
https://doaj.org/article/5149cb901be64b8ea5200c5f776cb102
Autor:
Giulia Faravelli, Valentina Mondani, P. Patrizia Mangione, Sara Raimondi, Loredana Marchese, Francesca Lavatelli, Monica Stoppini, Alessandra Corazza, Diana Canetti, Guglielmo Verona, Laura Obici, Graham W. Taylor, Julian D. Gillmore, Sofia Giorgetti, Vittorio Bellotti
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
The globular to fibrillar transition of proteins represents a key pathogenic event in the development of amyloid diseases. Although systemic amyloidoses share the common characteristic of amyloid deposition in the extracellular matrix, they are clini
Externí odkaz:
https://doaj.org/article/78918c93ba684ff5a907851006159caf
Autor:
Guglielmo Verona, P. Patrizia Mangione, Sara Raimondi, Sofia Giorgetti, Giulia Faravelli, Riccardo Porcari, Alessandra Corazza, Julian D. Gillmore, Philip N. Hawkins, Mark B. Pepys, Graham W. Taylor, Vittorio Bellotti
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-7 (2017)
Abstract Dissociation of the native transthyretin (TTR) tetramer is widely accepted as the critical step in TTR amyloid fibrillogenesis. It is modelled by exposure of the protein to non-physiological low pH in vitro and is inhibited by small molecule
Externí odkaz:
https://doaj.org/article/f338b2bcadbe45189416b0237ad95585
Autor:
Giulia, Faravelli, Valentina, Mondani, P Patrizia, Mangione, Sara, Raimondi, Loredana, Marchese, Francesca, Lavatelli, Monica, Stoppini, Alessandra, Corazza, Diana, Canetti, Guglielmo, Verona, Laura, Obici, Graham W, Taylor, Julian D, Gillmore, Sofia, Giorgetti, Vittorio, Bellotti
Publikováno v:
Frontiers in molecular biosciences. 9
The globular to fibrillar transition of proteins represents a key pathogenic event in the development of amyloid diseases. Although systemic amyloidoses share the common characteristic of amyloid deposition in the extracellular matrix, they are clini
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c156592fb1fc0f02d9a8e1e785981cf2
https://pubmed.ncbi.nlm.nih.gov/35237660
https://pubmed.ncbi.nlm.nih.gov/35237660
Autor:
Sara, Raimondi, P Patrizia, Mangione, Guglielmo, Verona, Diana, Canetti, Paola, Nocerino, Loredana, Marchese, Rebecca, Piccarducci, Valentina, Mondani, Giulia, Faravelli, Graham W, Taylor, Julian D, Gillmore, Alessandra, Corazza, Mark B, Pepys, Sofia, Giorgetti, Vittorio, Bellotti
Publikováno v:
J Biol Chem
Systemic amyloidosis caused by extracellular deposition of insoluble fibrils derived from the pathological aggregation of circulating proteins, such as transthyretin, is a severe and usually fatal condition. Elucidation of the molecular pathogenic me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::994f9e6186050d9cd7bdaba0d4804705
https://pubmed.ncbi.nlm.nih.gov/32571879
https://pubmed.ncbi.nlm.nih.gov/32571879
Autor:
Vittorio Bellotti, Sofia Giorgetti, Sudhir Kumar Sharma, Ramesh Jagannathan, Yamanappa Hunashal, Valentina Mondani, Cristina Cantarutti, Gennaro Esposito, Thirumurugan Prakasam, Giovanni Palmisano, John Carl Olsen, Ali Trabolsi, Giulia Faravelli, Federico Fogolari
Publikováno v:
Cell Reports Physical Science. 2:100477
Summary Inhibiting amyloid aggregation through high-turnover dynamic interactions could be an efficient strategy that is already used by small heat-shock proteins in different biological contexts. We report the interactions of three topologically non
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9f6765a8bf1be1555b7d7b8728ae14c
https://doi.org/10.1016/j.xcrp.2021.100477
https://doi.org/10.1016/j.xcrp.2021.100477
Autor:
P Patrizia, Mangione, Guglielmo, Verona, Alessandra, Corazza, Julien, Marcoux, Diana, Canetti, Sofia, Giorgetti, Sara, Raimondi, Monica, Stoppini, Marilena, Esposito, Annalisa, Relini, Claudio, Canale, Maurizia, Valli, Loredana, Marchese, Giulia, Faravelli, Laura, Obici, Philip N, Hawkins, Graham W, Taylor, Julian D, Gillmore, Mark B, Pepys, Vittorio, Bellotti
Publikováno v:
The Journal of biological chemistry. 293(37)
Systemic amyloidosis is a usually fatal disease caused by extracellular accumulation of abnormal protein fibers, amyloid fibrils, derived by misfolding and aggregation of soluble globular plasma protein precursors. Both WT and genetic variants of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8fbf03fc6731c2a9cede9b964738b555
https://pubmed.ncbi.nlm.nih.gov/30018138
https://pubmed.ncbi.nlm.nih.gov/30018138
Autor:
Guglielmo Verona, Philip N. Hawkins, Sofia Giorgetti, Vittorio Bellotti, Julian D. Gillmore, Alessandra Corazza, Mark B. Pepys, Palma Mangione, Graham W. Taylor, Sara Raimondi, Giulia Faravelli, Riccardo Porcari
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-7 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-7 (2017)
Dissociation of the native transthyretin (TTR) tetramer is widely accepted as the critical step in TTR amyloid fibrillogenesis. It is modelled by exposure of the protein to non-physiological low pH in vitro and is inhibited by small molecule compound
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a754c02914edd6586213dc72337f2e5e
https://pubmed.ncbi.nlm.nih.gov/28298647
https://pubmed.ncbi.nlm.nih.gov/28298647