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Systemic amyloidoses and proteomics: The state of the art

Systemic amyloidoses are caused by misfolding-prone proteins that polymerize in tissues, causing organ dysfunction. Since proteins are etiological agents of these diseases, proteomics was soon recognized as a privileged instrument for their investigation. Mass spectrometry-based proteomics has acqui...

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Autores principales: Lavatelli, Francesca, di Fonzo, Andrea, Palladini, Giovanni, Merlini, Giampaolo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5988550/
https://www.ncbi.nlm.nih.gov/pubmed/29900105
http://dx.doi.org/10.1016/j.euprot.2016.02.003
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author Lavatelli, Francesca
di Fonzo, Andrea
Palladini, Giovanni
Merlini, Giampaolo
author_facet Lavatelli, Francesca
di Fonzo, Andrea
Palladini, Giovanni
Merlini, Giampaolo
author_sort Lavatelli, Francesca
collection PubMed
description Systemic amyloidoses are caused by misfolding-prone proteins that polymerize in tissues, causing organ dysfunction. Since proteins are etiological agents of these diseases, proteomics was soon recognized as a privileged instrument for their investigation. Mass spectrometry-based proteomics has acquired a fundamental role in management of systemic amyloidoses, being now considered a gold standard approach for amyloid typing. In parallel, approaches for analyzing circulating amyloid precursors have been developed. Moreover, differential and functional proteomics hold promise for identifying novel biomarkers and clarifying disease mechanisms. This review discusses recent proteomics achievements in systemic amyloidoses, providing a perspective on its present and future applications.
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spelling pubmed-59885502018-06-13 Systemic amyloidoses and proteomics: The state of the art Lavatelli, Francesca di Fonzo, Andrea Palladini, Giovanni Merlini, Giampaolo EuPA Open Proteom Special Section: Proceedings of the 9th Annual EuPA Congress “Proteomics - Back to the Future” (June 23 - 28, 2015, Milano, Italy) Systemic amyloidoses are caused by misfolding-prone proteins that polymerize in tissues, causing organ dysfunction. Since proteins are etiological agents of these diseases, proteomics was soon recognized as a privileged instrument for their investigation. Mass spectrometry-based proteomics has acquired a fundamental role in management of systemic amyloidoses, being now considered a gold standard approach for amyloid typing. In parallel, approaches for analyzing circulating amyloid precursors have been developed. Moreover, differential and functional proteomics hold promise for identifying novel biomarkers and clarifying disease mechanisms. This review discusses recent proteomics achievements in systemic amyloidoses, providing a perspective on its present and future applications. Elsevier 2016-02-23 /pmc/articles/PMC5988550/ /pubmed/29900105 http://dx.doi.org/10.1016/j.euprot.2016.02.003 Text en © 2016 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Special Section: Proceedings of the 9th Annual EuPA Congress “Proteomics - Back to the Future” (June 23 - 28, 2015, Milano, Italy)
Lavatelli, Francesca
di Fonzo, Andrea
Palladini, Giovanni
Merlini, Giampaolo
Systemic amyloidoses and proteomics: The state of the art
title Systemic amyloidoses and proteomics: The state of the art
title_full Systemic amyloidoses and proteomics: The state of the art
title_fullStr Systemic amyloidoses and proteomics: The state of the art
title_full_unstemmed Systemic amyloidoses and proteomics: The state of the art
title_short Systemic amyloidoses and proteomics: The state of the art
title_sort systemic amyloidoses and proteomics: the state of the art
topic Special Section: Proceedings of the 9th Annual EuPA Congress “Proteomics - Back to the Future” (June 23 - 28, 2015, Milano, Italy)
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5988550/
https://www.ncbi.nlm.nih.gov/pubmed/29900105
http://dx.doi.org/10.1016/j.euprot.2016.02.003
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