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

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

Analytical characterization of biosimilar antibodies and Fc-fusion proteins

Autor: Alain Beck, Hélène Diemer, Christine Carapito, François Debaene, Daniel Ayoub, Elsa Wagner-Rousset, Alain Van Dorsselaer, Sarah Sanglier-Cianférani

Publikováno v: TrAC Trends in Analytical Chemistry. 48:81-95

Mass spectrometry (MS) is one of the key analytical techniques to detect and to identify primary sequence differences, to assess similarity and to evaluate batch variability of reference monoclonal antibodies (mAbs). The next generation of high-resol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b8654c8988bf9b525250982407e34a13
https://doi.org/10.1016/j.trac.2013.02.014

Crystal packing modifies ligand binding affinity: The case of aldose reductase

Autor: Eduardo Howard, Alexandra Cousido-Siah, Alain Van Dorsselaer, Alberto Podjarny, Isabelle Hazemann, Andrzej Joachimiak, Andre Mitschler, F.X. Ruiz, Cédric Atmanene, Sarah Sanglier-Cianférani, Stephan L. Ginell, Tatiana Petrova

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 80:2552-2561

The relationship between the structures of protein–ligand complexes existing in the crystal and in solution, essential in the case of fragment-based screening by X-ray crystallography (FBS-X), has been often an object of controversy. To address thi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::86c933c85da514b69ee1133d1618b20a
https://doi.org/10.1002/prot.24136

Poly(ADP-ribose) polymerase 3 (PARP3), a newcomer in cellular response to DNA damage and mitotic progression

Autor: Valérie Schreiber, Susan Smith, Laurent Gauthier, Anne Bresson, Denis Biard, François D. Boussin, Christian Boehler, Jean-Michel Saliou, Françoise Dantzer, Sarah Sanglier-Cianférani, Oliver Mortusewicz

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2011, 108 (7), pp.2783-8. ⟨10.1073/pnas.1016574108⟩

The ADP ribosyl transferase [poly(ADP-ribose) polymerase] ARTD3(PARP3) is a newly characterized member of the ARTD(PARP) family that catalyzes the reaction of ADP ribosylation, a key posttranslational modification of proteins involved in different si

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::610836a812f4a34c09ee3ea97ab0add3
https://doi.org/10.1073/pnas.1016574108