Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins: Miniperspective
Post-translational modifications (PTMs) allot versatility to the biological functions of highly conserved proteins. Recently, modifications to non-histone proteins such as methylation, acetylation, phosphorylation, glycosylation, ubiquitination, and many more have been linked to the regulation of pi...
Gespeichert in:
Veröffentlicht in: | Journal of medicinal chemistry 2018-04, Vol.61 (8), p.3239-3252 |
---|---|
Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 3252 |
---|---|
container_issue | 8 |
container_start_page | 3239 |
container_title | Journal of medicinal chemistry |
container_volume | 61 |
creator | Buuh, Zakey Yusuf Lyu, Zhigang Wang, Rongsheng E |
description | Post-translational modifications (PTMs) allot versatility to the biological functions of highly conserved proteins. Recently, modifications to non-histone proteins such as methylation, acetylation, phosphorylation, glycosylation, ubiquitination, and many more have been linked to the regulation of pivotal pathways related to cellular response and stability. Due to the roles these dynamic modifications assume, their dysregulation has been associated with cancer and many other important diseases such as inflammatory disorders and neurodegenerative diseases. For this reason, we present a review and perspective on important post-translational modifications on non-histone proteins, with emphasis on their roles in diseases and small molecule inhibitors developed to target PTM writers. Certain PTMs’ contribution to epigenetics has been extensively expounded; yet more efforts will be needed to systematically dissect their roles on non-histone proteins, especially for their relationships with nononcological diseases. Finally, current research approaches for PTM study will be discussed and compared, including limitations and possible improvements. |
doi_str_mv | 10.1021/acs.jmedchem.6b01817 |
format | Article |
fullrecord | <record><control><sourceid>acs_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1021_acs_jmedchem_6b01817</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>a933642408</sourcerecordid><originalsourceid>FETCH-LOGICAL-a867-8bda47d5e21eb00e8b44561caa0c46e343e373b6fd417dc06ba7c854d3fd24c63</originalsourceid><addsrcrecordid>eNp9kMtOwzAQRS0EEqHwByzyAw7jR5xsUQW0UoEKso8ce9KmSmxkhwV_T0jbLavR6N4z0hxC7hlkDDh70CZmhwGt2eOQqQZYyYoLkrCcA5UlyEuSAHBOueLimtzEeAAAwbhIyOfajRiC3-mxc7t03GP64XuMqW_TrY8jrYJ2sZ9S73SfvnrbtZ2Z17nz5h1ddXH0DtNt8CN2Lt6Sq1b3Ee9Oc0Gq56dquaKb95f18nFDdakKWjZWy8LmyBk2AFg2UuaKGa3BSIVCChSFaFRrJSusAdXowpS5tKK1XBolFkQez5rgYwzY1l-hG3T4qRnUf17qyUt99lKfvEwYHLE59d9h-iv-j_wCybZruQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins: Miniperspective</title><source>American Chemical Society Journals</source><creator>Buuh, Zakey Yusuf ; Lyu, Zhigang ; Wang, Rongsheng E</creator><creatorcontrib>Buuh, Zakey Yusuf ; Lyu, Zhigang ; Wang, Rongsheng E</creatorcontrib><description>Post-translational modifications (PTMs) allot versatility to the biological functions of highly conserved proteins. Recently, modifications to non-histone proteins such as methylation, acetylation, phosphorylation, glycosylation, ubiquitination, and many more have been linked to the regulation of pivotal pathways related to cellular response and stability. Due to the roles these dynamic modifications assume, their dysregulation has been associated with cancer and many other important diseases such as inflammatory disorders and neurodegenerative diseases. For this reason, we present a review and perspective on important post-translational modifications on non-histone proteins, with emphasis on their roles in diseases and small molecule inhibitors developed to target PTM writers. Certain PTMs’ contribution to epigenetics has been extensively expounded; yet more efforts will be needed to systematically dissect their roles on non-histone proteins, especially for their relationships with nononcological diseases. Finally, current research approaches for PTM study will be discussed and compared, including limitations and possible improvements.</description><identifier>ISSN: 0022-2623</identifier><identifier>EISSN: 1520-4804</identifier><identifier>DOI: 10.1021/acs.jmedchem.6b01817</identifier><language>eng</language><publisher>American Chemical Society</publisher><ispartof>Journal of medicinal chemistry, 2018-04, Vol.61 (8), p.3239-3252</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-a867-8bda47d5e21eb00e8b44561caa0c46e343e373b6fd417dc06ba7c854d3fd24c63</cites><orcidid>0000-0002-5749-7447</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.6b01817$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.jmedchem.6b01817$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids></links><search><creatorcontrib>Buuh, Zakey Yusuf</creatorcontrib><creatorcontrib>Lyu, Zhigang</creatorcontrib><creatorcontrib>Wang, Rongsheng E</creatorcontrib><title>Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins: Miniperspective</title><title>Journal of medicinal chemistry</title><addtitle>J. Med. Chem</addtitle><description>Post-translational modifications (PTMs) allot versatility to the biological functions of highly conserved proteins. Recently, modifications to non-histone proteins such as methylation, acetylation, phosphorylation, glycosylation, ubiquitination, and many more have been linked to the regulation of pivotal pathways related to cellular response and stability. Due to the roles these dynamic modifications assume, their dysregulation has been associated with cancer and many other important diseases such as inflammatory disorders and neurodegenerative diseases. For this reason, we present a review and perspective on important post-translational modifications on non-histone proteins, with emphasis on their roles in diseases and small molecule inhibitors developed to target PTM writers. Certain PTMs’ contribution to epigenetics has been extensively expounded; yet more efforts will be needed to systematically dissect their roles on non-histone proteins, especially for their relationships with nononcological diseases. Finally, current research approaches for PTM study will be discussed and compared, including limitations and possible improvements.</description><issn>0022-2623</issn><issn>1520-4804</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNp9kMtOwzAQRS0EEqHwByzyAw7jR5xsUQW0UoEKso8ce9KmSmxkhwV_T0jbLavR6N4z0hxC7hlkDDh70CZmhwGt2eOQqQZYyYoLkrCcA5UlyEuSAHBOueLimtzEeAAAwbhIyOfajRiC3-mxc7t03GP64XuMqW_TrY8jrYJ2sZ9S73SfvnrbtZ2Z17nz5h1ddXH0DtNt8CN2Lt6Sq1b3Ee9Oc0Gq56dquaKb95f18nFDdakKWjZWy8LmyBk2AFg2UuaKGa3BSIVCChSFaFRrJSusAdXowpS5tKK1XBolFkQez5rgYwzY1l-hG3T4qRnUf17qyUt99lKfvEwYHLE59d9h-iv-j_wCybZruQ</recordid><startdate>20180426</startdate><enddate>20180426</enddate><creator>Buuh, Zakey Yusuf</creator><creator>Lyu, Zhigang</creator><creator>Wang, Rongsheng E</creator><general>American Chemical Society</general><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0002-5749-7447</orcidid></search><sort><creationdate>20180426</creationdate><title>Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins</title><author>Buuh, Zakey Yusuf ; Lyu, Zhigang ; Wang, Rongsheng E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a867-8bda47d5e21eb00e8b44561caa0c46e343e373b6fd417dc06ba7c854d3fd24c63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Buuh, Zakey Yusuf</creatorcontrib><creatorcontrib>Lyu, Zhigang</creatorcontrib><creatorcontrib>Wang, Rongsheng E</creatorcontrib><collection>CrossRef</collection><jtitle>Journal of medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Buuh, Zakey Yusuf</au><au>Lyu, Zhigang</au><au>Wang, Rongsheng E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins: Miniperspective</atitle><jtitle>Journal of medicinal chemistry</jtitle><addtitle>J. Med. Chem</addtitle><date>2018-04-26</date><risdate>2018</risdate><volume>61</volume><issue>8</issue><spage>3239</spage><epage>3252</epage><pages>3239-3252</pages><issn>0022-2623</issn><eissn>1520-4804</eissn><abstract>Post-translational modifications (PTMs) allot versatility to the biological functions of highly conserved proteins. Recently, modifications to non-histone proteins such as methylation, acetylation, phosphorylation, glycosylation, ubiquitination, and many more have been linked to the regulation of pivotal pathways related to cellular response and stability. Due to the roles these dynamic modifications assume, their dysregulation has been associated with cancer and many other important diseases such as inflammatory disorders and neurodegenerative diseases. For this reason, we present a review and perspective on important post-translational modifications on non-histone proteins, with emphasis on their roles in diseases and small molecule inhibitors developed to target PTM writers. Certain PTMs’ contribution to epigenetics has been extensively expounded; yet more efforts will be needed to systematically dissect their roles on non-histone proteins, especially for their relationships with nononcological diseases. Finally, current research approaches for PTM study will be discussed and compared, including limitations and possible improvements.</abstract><pub>American Chemical Society</pub><doi>10.1021/acs.jmedchem.6b01817</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0002-5749-7447</orcidid></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0022-2623 |
ispartof | Journal of medicinal chemistry, 2018-04, Vol.61 (8), p.3239-3252 |
issn | 0022-2623 1520-4804 |
language | eng |
recordid | cdi_crossref_primary_10_1021_acs_jmedchem_6b01817 |
source | American Chemical Society Journals |
title | Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins: Miniperspective |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-07T22%3A16%3A18IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-acs_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Interrogating%20the%20Roles%20of%20Post-Translational%20Modifications%20of%20Non-Histone%20Proteins:%20Miniperspective&rft.jtitle=Journal%20of%20medicinal%20chemistry&rft.au=Buuh,%20Zakey%20Yusuf&rft.date=2018-04-26&rft.volume=61&rft.issue=8&rft.spage=3239&rft.epage=3252&rft.pages=3239-3252&rft.issn=0022-2623&rft.eissn=1520-4804&rft_id=info:doi/10.1021/acs.jmedchem.6b01817&rft_dat=%3Cacs_cross%3Ea933642408%3C/acs_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |