Current insights into the role of citrullination in thrombosis
Protein citrullination is a post-translational modification of arginine that controls a diverse array of cellular processes, including gene regulation, protein stability, and neutrophil extracellular trap (NET) formation. Histone citrullination promotes chromatin decondensation and NET formation, a...
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Veröffentlicht in: | Current opinion in chemical biology 2023-08, Vol.75, p.102313-102313, Article 102313 |
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description | Protein citrullination is a post-translational modification of arginine that controls a diverse array of cellular processes, including gene regulation, protein stability, and neutrophil extracellular trap (NET) formation. Histone citrullination promotes chromatin decondensation and NET formation, a pro-inflammatory form of cell death that is aberrantly increased in numerous immune disorders. This review will provide insights into NETosis and how this novel form of cell death contributes to inflammatory diseases, with a particular emphasis on its role in thrombosis. We will also discuss recent efforts to develop PAD-specific inhibitors. |
doi_str_mv | 10.1016/j.cbpa.2023.102313 |
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Madison</creatorcontrib><creatorcontrib>Thompson, Paul R.</creatorcontrib><title>Current insights into the role of citrullination in thrombosis</title><title>Current opinion in chemical biology</title><addtitle>Curr Opin Chem Biol</addtitle><description>Protein citrullination is a post-translational modification of arginine that controls a diverse array of cellular processes, including gene regulation, protein stability, and neutrophil extracellular trap (NET) formation. Histone citrullination promotes chromatin decondensation and NET formation, a pro-inflammatory form of cell death that is aberrantly increased in numerous immune disorders. This review will provide insights into NETosis and how this novel form of cell death contributes to inflammatory diseases, with a particular emphasis on its role in thrombosis. We will also discuss recent efforts to develop PAD-specific inhibitors.</description><subject>Chromatin - metabolism</subject><subject>Citrullination</subject><subject>Extracellular Traps - metabolism</subject><subject>Humans</subject><subject>Protein Processing, Post-Translational</subject><subject>Thrombosis - metabolism</subject><issn>1367-5931</issn><issn>1879-0402</issn><issn>1879-0402</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kN1LwzAUxYMobk7_AR-kj7505qNNGxBFhl8w8EWfQ5rebhldM5N04H9vRufQF59yyDn33MsPoUuCpwQTfrOa6mqjphRTFj8oI-wIjUlZiBRnmB5HzXiR5oKRETrzfoUx5rTMT9GIFSQrecbG6G7WOwddSEznzWIZfBTBJmEJibMtJLZJtAmub1vTqWBsF_3oOruurDf-HJ00qvVwsX8n6OPp8X32ks7fnl9nD_NUZzkPqaqbimYVjqcoqEUVJWdMFZorwgXXRDEKRUGrXIlaMICcY0pZllelLkRUE3Q_9G76ag21jhc71cqNM2vlvqRVRv51OrOUC7uVBOeUibKMDdf7Bmc_e_BBro3X0LaqA9t7SUuCBcUlxTFKh6h21nsHzWEPwXJHXq7kjrzckZcD-Th09fvCw8gP6hi4HQIQOW0NOOm1gU5DbRzoIGtr_uv_BuStlSw</recordid><startdate>20230801</startdate><enddate>20230801</enddate><creator>Green, R. 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Madison ; Thompson, Paul R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-adfb24b0931aed9b4b0633a7c6a1696c1a32e772b5a9d93ee56022345b8c79223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Chromatin - metabolism</topic><topic>Citrullination</topic><topic>Extracellular Traps - metabolism</topic><topic>Humans</topic><topic>Protein Processing, Post-Translational</topic><topic>Thrombosis - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Green, R. Madison</creatorcontrib><creatorcontrib>Thompson, Paul R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Current opinion in chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Green, R. Madison</au><au>Thompson, Paul R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Current insights into the role of citrullination in thrombosis</atitle><jtitle>Current opinion in chemical biology</jtitle><addtitle>Curr Opin Chem Biol</addtitle><date>2023-08-01</date><risdate>2023</risdate><volume>75</volume><spage>102313</spage><epage>102313</epage><pages>102313-102313</pages><artnum>102313</artnum><issn>1367-5931</issn><issn>1879-0402</issn><eissn>1879-0402</eissn><abstract>Protein citrullination is a post-translational modification of arginine that controls a diverse array of cellular processes, including gene regulation, protein stability, and neutrophil extracellular trap (NET) formation. Histone citrullination promotes chromatin decondensation and NET formation, a pro-inflammatory form of cell death that is aberrantly increased in numerous immune disorders. 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subjects | Chromatin - metabolism Citrullination Extracellular Traps - metabolism Humans Protein Processing, Post-Translational Thrombosis - metabolism |
title | Current insights into the role of citrullination in thrombosis |
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