SnapShot: Lysine Methylation beyond Histones
Lysine methylation is a prevalent post-translational modification (PTM) used by the cell to reversibly regulate protein function. Although it has been extensively studied in the context of histones and the associated chromatin, the remaining methyllysine proteome remains largely unexplored. This Sna...
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| Veröffentlicht in: | Molecular cell 2017-12, Vol.68 (5), p.1016-1016.e1 |
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| container_end_page | 1016.e1 |
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| container_title | Molecular cell |
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| creator | Biggar, Kyle K. Wang, Zhentian Li, Shawn S.-C. |
| description | Lysine methylation is a prevalent post-translational modification (PTM) used by the cell to reversibly regulate protein function. Although it has been extensively studied in the context of histones and the associated chromatin, the remaining methyllysine proteome remains largely unexplored. This SnapShot provides an overview of the current state of lysine methylation research and its emergence as a dynamic PTM occurring on histone and non-histone proteins.
Lysine methylation is a prevalent post-translational modification (PTM) used by the cell to reversibly regulate protein function. Although it has been extensively studied in the context of histones and the associated chromatin, the remaining methyllysine proteome remains largely unexplored. This SnapShot provides an overview of the current state of lysine methylation research and its emergence as a dynamic PTM occurring on histone and non-histone proteins. |
| doi_str_mv | 10.1016/j.molcel.2017.11.018 |
| format | Article |
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Lysine methylation is a prevalent post-translational modification (PTM) used by the cell to reversibly regulate protein function. Although it has been extensively studied in the context of histones and the associated chromatin, the remaining methyllysine proteome remains largely unexplored. This SnapShot provides an overview of the current state of lysine methylation research and its emergence as a dynamic PTM occurring on histone and non-histone proteins.</description><identifier>ISSN: 1097-2765</identifier><identifier>EISSN: 1097-4164</identifier><identifier>DOI: 10.1016/j.molcel.2017.11.018</identifier><identifier>PMID: 29220647</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Histones - metabolism ; Humans ; Lysine ; Methylation ; Protein Processing, Post-Translational ; Signal Transduction</subject><ispartof>Molecular cell, 2017-12, Vol.68 (5), p.1016-1016.e1</ispartof><rights>2017</rights><rights>Copyright © 2017. Published by Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c408t-a812a8b770436bba0c0b80f94ceb146c97f3b6723cee3ee7daf8c155e771a4693</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.molcel.2017.11.018$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29220647$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Biggar, Kyle K.</creatorcontrib><creatorcontrib>Wang, Zhentian</creatorcontrib><creatorcontrib>Li, Shawn S.-C.</creatorcontrib><title>SnapShot: Lysine Methylation beyond Histones</title><title>Molecular cell</title><addtitle>Mol Cell</addtitle><description>Lysine methylation is a prevalent post-translational modification (PTM) used by the cell to reversibly regulate protein function. Although it has been extensively studied in the context of histones and the associated chromatin, the remaining methyllysine proteome remains largely unexplored. This SnapShot provides an overview of the current state of lysine methylation research and its emergence as a dynamic PTM occurring on histone and non-histone proteins.
Lysine methylation is a prevalent post-translational modification (PTM) used by the cell to reversibly regulate protein function. Although it has been extensively studied in the context of histones and the associated chromatin, the remaining methyllysine proteome remains largely unexplored. This SnapShot provides an overview of the current state of lysine methylation research and its emergence as a dynamic PTM occurring on histone and non-histone proteins.</description><subject>Animals</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Lysine</subject><subject>Methylation</subject><subject>Protein Processing, Post-Translational</subject><subject>Signal Transduction</subject><issn>1097-2765</issn><issn>1097-4164</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kLFOwzAQhi0EolB4A4Q6MpDgcxw7YUBCFVCkIobCbNnORXWVxCVOkfL2pEphZLobvv9-3UfIFdAYKIi7TVz7ymIVMwoyBogpZEfkDGguIw6CHx92JkU6IechbCgFnmb5KZmwnDEquDwjt6tGb1dr393Pln1wDc7esFv3le6cb2YGe98Us4ULnW8wXJCTUlcBLw9zSj6fnz7mi2j5_vI6f1xGltOsi3QGTGdGSsoTYYymlpqMljm3aIALm8syMUKyxCImiLLQZWYhTVFK0FzkyZTcjHe3rf_aYehU7cLwaqUb9LugIJcpTbhgdED5iNrWh9Biqbatq3XbK6Bq70lt1OhJ7T0pADV4GmLXh4adqbH4C_2KGYCHEcDhz2-HrQrWYWOxcC3aThXe_d_wA2X-ejA</recordid><startdate>20171207</startdate><enddate>20171207</enddate><creator>Biggar, Kyle K.</creator><creator>Wang, Zhentian</creator><creator>Li, Shawn S.-C.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20171207</creationdate><title>SnapShot: Lysine Methylation beyond Histones</title><author>Biggar, Kyle K. ; Wang, Zhentian ; Li, Shawn S.-C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c408t-a812a8b770436bba0c0b80f94ceb146c97f3b6723cee3ee7daf8c155e771a4693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Animals</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Lysine</topic><topic>Methylation</topic><topic>Protein Processing, Post-Translational</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Biggar, Kyle K.</creatorcontrib><creatorcontrib>Wang, Zhentian</creatorcontrib><creatorcontrib>Li, Shawn S.-C.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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><jtitle>Molecular cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Biggar, Kyle K.</au><au>Wang, Zhentian</au><au>Li, Shawn S.-C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SnapShot: Lysine Methylation beyond Histones</atitle><jtitle>Molecular cell</jtitle><addtitle>Mol Cell</addtitle><date>2017-12-07</date><risdate>2017</risdate><volume>68</volume><issue>5</issue><spage>1016</spage><epage>1016.e1</epage><pages>1016-1016.e1</pages><issn>1097-2765</issn><eissn>1097-4164</eissn><abstract>Lysine methylation is a prevalent post-translational modification (PTM) used by the cell to reversibly regulate protein function. Although it has been extensively studied in the context of histones and the associated chromatin, the remaining methyllysine proteome remains largely unexplored. This SnapShot provides an overview of the current state of lysine methylation research and its emergence as a dynamic PTM occurring on histone and non-histone proteins.
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Animals Histones - metabolism Humans Lysine Methylation Protein Processing, Post-Translational Signal Transduction |
| title | SnapShot: Lysine Methylation beyond Histones |
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