Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Amanda Penco"'
Autor:
Antonino Natalello, Annalisa Relini, Amanda Penco, Levon Halabelian, Martino Bolognesi, Silvia Maria Doglia, Stefano Ricagno
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0122449 (2015)
Beta-2 microglobulin (β2m) is the protein responsible for a pathologic condition known as dialysis related amyloidosis. In recent years an important role has been assigned to the peptide loop linking strands D and E (DE loop) in determining β2m sta
Externí odkaz:
https://doaj.org/article/8bca8326294c46ff85a53d754d00d813
Autor:
Claudia Capitini, Simona Conti, Michele Perni, Francesca Guidi, Roberta Cascella, Angela De Poli, Amanda Penco, Annalisa Relini, Cristina Cecchi, Fabrizio Chiti
Publikováno v:
PLoS ONE, Vol 9, Iss 1, p e86720 (2014)
Accumulation of ubiquitin-positive, tau- and α-synuclein-negative intracellular inclusions of TDP-43 in the central nervous system represents the major hallmark correlated to amyotrophic lateral sclerosis and frontotemporal lobar degeneration with u
Externí odkaz:
https://doaj.org/article/41f0b7cc58b04fa68bb214d0accd8853
Autor:
Gaetano Invernizzi, Francesco A Aprile, Antonino Natalello, Andrea Ghisleni, Amanda Penco, Annalisa Relini, Silvia M Doglia, Paolo Tortora, Maria E Regonesi
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e51890 (2012)
Several neurodegenerative diseases are triggered by proteins containing a polyglutamine (polyQ) stretch expanded beyond a critical threshold. Among these, ataxin-3 (AT3) is the causative agent of spinocerebellar ataxia type-3. We expressed three auth
Externí odkaz:
https://doaj.org/article/51f96e25ab6c46fa83b96860acab1cb9
Autor:
Claudia, Capitini, Giulia, Fani, Mirella, Vivoli Vega, Amanda, Penco, Claudio, Canale, Lisa D, Cabrita, Martino, Calamai, John, Christodoulou, Annalisa, Relini, Fabrizio, Chiti
Publikováno v:
Amyloid
Accumulation of ubiquitin-positive, tau- and a-synuclein-negative intracellular inclusions of TDP-43 in the central nervous system represents the major hallmark correlated to amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration w
Autor:
Claudio Canale, Lisa D. Cabrita, Fabrizio Chiti, Mirella Vivoli Vega, Martino Calamai, Amanda Penco, John Christodoulou, Annalisa Relini, Giulia Fani, Claudia Capitini
Publikováno v:
Amyloid (Carnforth) 28 (2021): 56–65. doi:10.1080/13506129.2020.1826425
info:cnr-pdr/source/autori:Capitini, Claudia; Fani, Giulia; Vega, Mirella Vivoli; Penco, Amanda; Canale, Claudio; Cabrita, Lisa D.; Calamai, Martino; Christodoulou, John; Relini, Annalisa; Chiti, Fabrizio/titolo:Full-length TDP-43 and its C-terminal domain form filamentsin vitrohaving non-amyloid properties/doi:10.1080%2F13506129.2020.1826425/rivista:Amyloid (Carnforth)/anno:2021/pagina_da:56/pagina_a:65/intervallo_pagine:56–65/volume:28
info:cnr-pdr/source/autori:Capitini, Claudia; Fani, Giulia; Vega, Mirella Vivoli; Penco, Amanda; Canale, Claudio; Cabrita, Lisa D.; Calamai, Martino; Christodoulou, John; Relini, Annalisa; Chiti, Fabrizio/titolo:Full-length TDP-43 and its C-terminal domain form filamentsin vitrohaving non-amyloid properties/doi:10.1080%2F13506129.2020.1826425/rivista:Amyloid (Carnforth)/anno:2021/pagina_da:56/pagina_a:65/intervallo_pagine:56–65/volume:28
Accumulation of ubiquitin-positive, tau- and alpha-synuclein-negative intracellular inclusions of TDP-43 in the central nervous system represents the major hallmark correlated to amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degenerati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::252b9d144b7fef794c6579c0547dec07
http://hdl.handle.net/11567/1028771
http://hdl.handle.net/11567/1028771
Autor:
Annalisa Relini, Amanda Penco, Elena Gatta, Jacopo Vertemara, Antonino Natalello, Paolo Tortora, Cristina Airoldi, Marcella Bonanomi, Cristina Visentin, Luca De Gioia, Maria Elena Regonesi, Francesca Pellistri
The protein ataxin-3 (ATX3) triggers an amyloid-related neurodegenerative disease when its polyglutamine stretch is expanded beyond a critical threshold. We formerly demonstrated that the polyphenol epigallocatechin-3-gallate (EGCG) could redirect am
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d884547fdb92b4b51b69af70f85d1e66
http://hdl.handle.net/11567/884537
http://hdl.handle.net/11567/884537
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
Autor:
Annalisa Relini, Monica Bucciantini, Guido Mannaioni, Vittorio Bellotti, Elisabetta Cerbai, Laura Sartiani, Daniele Nosi, Valentina Spinelli, Elisabetta Gerace, Massimo Stefani, Sofia Giorgetti, Amanda Penco, Silvia Maria Doglia, Manuela Leri, Stefania Rigacci, Antonino Natalello
Transthyretin (TTR) amyloidoses are familial or sporadic degenerative conditions that often feature heavy cardiac involvement. Presently, no effective pharmacological therapy for TTR amyloidoses is available, mostly due to a substantial lack of knowl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd9e0f04f28f3ef6af079673b732c4c7
http://hdl.handle.net/11567/861039
http://hdl.handle.net/11567/861039
Autor:
Simona Maria Monti, Renata Piccoli, Francesco Itri, Annalisa Relini, Amanda Penco, Maria Chiara Monti, Ganna Petruk, Antonello Merlino, Angela Arciello, Rita Del Giudice, Piero Pucci, Martina Buonanno, Diana Canetti, Daria Maria Monti
Amyloidoses are devastating diseases characterized by accumulation of misfolded proteins which aggregate in fibrils. Specific gene mutations in Apolipoprotein A I (ApoAI) are associated with systemic amyloidoses. Little is known on the effect of muta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6040a6d74e0f2f17640ff2de54a5ece8
http://hdl.handle.net/11588/612579
http://hdl.handle.net/11588/612579
Autor:
Amanda Penco, Cristina Cecchi, Roberta Cascella, Fabrizio Chiti, Benedetta Mannini, Mariagioia Zampagni, Sarah Meehan, Matilde Boninsegna, Mark R. Wilson, Harm H. Kampinga, Christopher M. Dobson, Maria A.W.H. van Waarde-Verhagen, Annalisa Relini, Silvia Campioni, Cintia Roodveldt
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Proceedings of the National Academy of Sciences of the United States of America, 109(31), 12479-12484. NATL ACAD SCIENCES
instname
Proceedings of the National Academy of Sciences of the United States of America, 109(31), 12479-12484. NATL ACAD SCIENCES
Mannini, Benedetta et al.
Chaperones are the primary regulators of the proteostasis network and are known to facilitate protein folding, inhibit protein aggregation, and promote disaggregation and clearance of misfolded aggregates inside cells.
Chaperones are the primary regulators of the proteostasis network and are known to facilitate protein folding, inhibit protein aggregation, and promote disaggregation and clearance of misfolded aggregates inside cells.