Amyloid Formation by Globular Proteins: The Need to Narrow the Gap Between in Vitro and in Vivo Mechanisms

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

A novel mechano‐enzymatic cleavage mechanism underlies transthyretin amyloidogenesis

Autor: Julien Marcoux, P Patrizia Mangione, Riccardo Porcari, Matteo T Degiacomi, Guglielmo Verona, Graham W Taylor, Sofia Giorgetti, Sara Raimondi, Sarah Sanglier‐Cianférani, Justin LP Benesch, Ciro Cecconi, Mohsin M Naqvi, Julian D Gillmore, Philip N Hawkins, Monica Stoppini, Carol V Robinson, Mark B Pepys, Vittorio Bellotti

Publikováno v: EMBO Molecular Medicine, Vol 7, Iss 10, Pp 1337-1349 (2015)

Abstract The mechanisms underlying transthyretin‐related amyloidosis in vivo remain unclear. The abundance of the 49–127 transthyretin fragment in ex vivo deposits suggests that a proteolytic cleavage has a crucial role in destabilizing the tetra

Externí odkaz: https://doaj.org/article/73bd04162dae41c1a8592516fd43e2e6

C. elegans expressing human β2-microglobulin: a novel model for studying the relationship between the molecular assembly and the toxic phenotype.

Autor: Luisa Diomede, Cristina Soria, Margherita Romeo, Sofia Giorgetti, Loredana Marchese, Patrizia Palma Mangione, Riccardo Porcari, Irene Zorzoli, Mario Salmona, Vittorio Bellotti, Monica Stoppini

Publikováno v: PLoS ONE, Vol 7, Iss 12, p e52314 (2012)

Availability of living organisms to mimic key step of amyloidogenesis of human protein has become an indispensable tool for our translation approach aiming at filling the deep gap existing between the biophysical and biochemical data obtained in vitr

Externí odkaz: https://doaj.org/article/92eb5bedcc3d488182f60b30e7517ace

A novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis

Autor: Sofia Giorgetti, Julien Marcoux, Palma Mangione, Ciro Cecconi, Graham W. Taylor, Monica Stoppini, Justin L. P. Benesch, Riccardo Porcari, Mohsin M. Naqvi, Guglielmo Verona, Philip N. Hawkins, Carol V. Robinson, Sarah Sanglier-Cianférani, Mark B. Pepys, Matteo T. Degiacomi, Sara Raimondi, Vittorio Bellotti, Julian D. Gillmore

Publikováno v: EMBO Molecular Medicine
EMBO molecular medicine, 2015, Vol.7(10), pp.1337-1349 [Peer Reviewed Journal]
EMBO Molecular Medicine, Wiley Open Access, 2015, 7 (10), pp.1337-1349. ⟨10.15252/emmm.201505357⟩
EMBO molecular medicine (Online) 7 (2015): 1337–1349. doi:10.15252/emmm.201505357
info:cnr-pdr/source/autori:Marcoux, Julien[ 1,2 ] ; Mangione, P. Patrizia[ 3,4 ] ; Porcari, Riccardo[ 3 ] ; Degiacomi, Matteo T.[ 1 ] ; Verona, Guglielmo)ù[ 3,4 ] ; Taylor, Graham W.[ 3 ] ; Giorgetti, Sofia[ 4 ] ; Raimondi, Sara[ 4 ] ; Sanglier-Cianferani, Sarah[ 2 ] ; Benesch, Justin L. P.[ 1 ] ; Cecconi, Ciro[ 5,6 ] ; Naqvi, Mohsin M.[ 6 ] ; Gillmore, Julian D.[ 3 ] ; Hawkins, Philip N.[ 3 ] ; Stoppini, Monica[ 4 ] ; Robinson, Carol V.[ 1 ] ; Pepys, Mark B.[ 3 ] ; Bellotti, Vittorio[ 3,4 ]/titolo:A novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis/doi:10.15252%2Femmm.201505357/rivista:EMBO molecular medicine (Online)/anno:2015/pagina_da:1337/pagina_a:1349/intervallo_pagine:1337–1349/volume:7

International audience; The mechanisms underlying transthyretin-related amyloidosis in vivo remain unclear. The abundance of the 49-127 transthyretin fragment in ex vivo deposits suggests that a proteolytic cleavage has a crucial role in destabilizin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5dda55b6a8c3e36783aa9813490d1102
http://europepmc.org/articles/PMC4604687

Structure, Folding Dynamics, and Amyloidogenesis of D76N β2-Microglobulin

Autor: Mark B. Pepys, Young-Ho Lee, Sofia Giorgetti, Palma Mangione, Alessandra Corazza, Ranieri Rolandi, Vittorio Bellotti, Graham W. Taylor, Julian D. Gillmore, Monica Stoppini, Fabrizio Chiti, Philip N. Hawkins, Riccardo Porcari, Annalisa Relini, Sara Raimondi, Hisashi Yagi, Amanda Penco, Gennaro Esposito, Federico Fogolari, Yuji Goto, Mohsin M. Naqvi, Ciro Cecconi

Publikováno v: Journal of Biological Chemistry. 288:30917-30930

Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins, which then aggregate extracellularly as insoluble fibrils, damaging the structure and function of affected organs. The formation of amyloid fibrils in vivo is p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cd53e9658d081993d4745611e3bcb5de
https://doi.org/10.1074/jbc.m113.498857