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Deimination, Intermediate Filaments and Associated Proteins
Deimination (or citrullination) is a post-translational modification catalyzed by a calcium-dependent enzyme family of five peptidylarginine deiminases (PADs). Deimination is involved in physiological processes (cell differentiation, embryogenesis, innate and adaptive immunity, etc.) and in autoimmu...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7699402/ https://www.ncbi.nlm.nih.gov/pubmed/33228136 http://dx.doi.org/10.3390/ijms21228746 |
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author | Briot, Julie Simon, Michel Méchin, Marie-Claire |
author_facet | Briot, Julie Simon, Michel Méchin, Marie-Claire |
author_sort | Briot, Julie |
collection | PubMed |
description | Deimination (or citrullination) is a post-translational modification catalyzed by a calcium-dependent enzyme family of five peptidylarginine deiminases (PADs). Deimination is involved in physiological processes (cell differentiation, embryogenesis, innate and adaptive immunity, etc.) and in autoimmune diseases (rheumatoid arthritis, multiple sclerosis and lupus), cancers and neurodegenerative diseases. Intermediate filaments (IF) and associated proteins (IFAP) are major substrates of PADs. Here, we focus on the effects of deimination on the polymerization and solubility properties of IF proteins and on the proteolysis and cross-linking of IFAP, to finally expose some features of interest and some limitations of citrullinomes. |
format | Online Article Text |
id | pubmed-7699402 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76994022020-11-29 Deimination, Intermediate Filaments and Associated Proteins Briot, Julie Simon, Michel Méchin, Marie-Claire Int J Mol Sci Review Deimination (or citrullination) is a post-translational modification catalyzed by a calcium-dependent enzyme family of five peptidylarginine deiminases (PADs). Deimination is involved in physiological processes (cell differentiation, embryogenesis, innate and adaptive immunity, etc.) and in autoimmune diseases (rheumatoid arthritis, multiple sclerosis and lupus), cancers and neurodegenerative diseases. Intermediate filaments (IF) and associated proteins (IFAP) are major substrates of PADs. Here, we focus on the effects of deimination on the polymerization and solubility properties of IF proteins and on the proteolysis and cross-linking of IFAP, to finally expose some features of interest and some limitations of citrullinomes. MDPI 2020-11-19 /pmc/articles/PMC7699402/ /pubmed/33228136 http://dx.doi.org/10.3390/ijms21228746 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Briot, Julie Simon, Michel Méchin, Marie-Claire Deimination, Intermediate Filaments and Associated Proteins |
title | Deimination, Intermediate Filaments and Associated Proteins |
title_full | Deimination, Intermediate Filaments and Associated Proteins |
title_fullStr | Deimination, Intermediate Filaments and Associated Proteins |
title_full_unstemmed | Deimination, Intermediate Filaments and Associated Proteins |
title_short | Deimination, Intermediate Filaments and Associated Proteins |
title_sort | deimination, intermediate filaments and associated proteins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7699402/ https://www.ncbi.nlm.nih.gov/pubmed/33228136 http://dx.doi.org/10.3390/ijms21228746 |
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