Identification of actin as a direct proteomic target of berberine using an affinity-based chemical probe and elucidation of its modulatory role in actin assemblyElectronic supplementary information (ESI) available: Experimental procedures and characterization data. See DOI: 10.1039/c7cc02789c

Despite the diverse pharmacological activities of berberine, including anti-cancer and anti-inflammatory effects, the direct proteomic targets of berberine have remained largely unknown. Here, we have identified actin as a direct proteomic target of berberine using an affinity-based chemical probe....

Full description

Saved in:
Bibliographic Details
Main Authors: Yi, Chae-Min, Yu, Jihyun, Kim, Hyunbin, Lee, Na-Rae, Kim, Sang Won, Lee, Noh-Jin, Lee, Jun, Seong, Jihye, Kim, Nam-Jung, Inn, Kyung-Soo
Format: Article
Language:English
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page 747
container_issue 52
container_start_page 745
container_title
container_volume 53
creator Yi, Chae-Min
Yu, Jihyun
Kim, Hyunbin
Lee, Na-Rae
Kim, Sang Won
Lee, Noh-Jin
Lee, Jun
Seong, Jihye
Kim, Nam-Jung
Inn, Kyung-Soo
description Despite the diverse pharmacological activities of berberine, including anti-cancer and anti-inflammatory effects, the direct proteomic targets of berberine have remained largely unknown. Here, we have identified actin as a direct proteomic target of berberine using an affinity-based chemical probe. In addition, we found that actin assembly was significantly modulated by berberine in vitro at the biochemical level and cellular level. Actin was identified as a direct target of berberine via a chemoproteomic approach and its assembly was modulated by berberine.
doi_str_mv 10.1039/c7cc02789c
format article
fullrecord <record><control><sourceid>rsc</sourceid><recordid>TN_cdi_rsc_primary_c7cc02789c</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>c7cc02789c</sourcerecordid><originalsourceid>FETCH-rsc_primary_c7cc02789c3</originalsourceid><addsrcrecordid>eNqFkL1PwzAQxQMCifKxsCMdAxIMKQlp6McKQXRiKANbdbEvrZFjR7aDWv56Lm0FAxJYJ9nSe8_vp4ui8zTpp0k2vhVDIZK74Wgs9qNemt0P4nwwejvo3vk4HmaD_Cg69v494ZPmo97e1VSSCapSAoOyBmwFKIIygB4QpHIkAjTOBrK1EhDQLSh0rpIcjzIErVdmAciRqlJGhXVcoicJYkkcQd3FS2KDBNKtUPK7SQUPtZWtxmDdGpzVBF31DsBTXep1oRnBWcPtvm0aTTUDI9uVqayrt59dF7PpDeAHKo2lpgkUq4bpNtYNgCDZOvIbCrFExx2sf27TTIR9mBHB48t0Ar-XeRodVqg9ne3uk-jiqXh9eI6dF_OGe5hn_mPP_tcv_9LnjayyL7TXmIw</addsrcrecordid><sourcetype>Enrichment Source</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Identification of actin as a direct proteomic target of berberine using an affinity-based chemical probe and elucidation of its modulatory role in actin assemblyElectronic supplementary information (ESI) available: Experimental procedures and characterization data. See DOI: 10.1039/c7cc02789c</title><source>Royal Society of Chemistry Journals</source><creator>Yi, Chae-Min ; Yu, Jihyun ; Kim, Hyunbin ; Lee, Na-Rae ; Kim, Sang Won ; Lee, Noh-Jin ; Lee, Jun ; Seong, Jihye ; Kim, Nam-Jung ; Inn, Kyung-Soo</creator><creatorcontrib>Yi, Chae-Min ; Yu, Jihyun ; Kim, Hyunbin ; Lee, Na-Rae ; Kim, Sang Won ; Lee, Noh-Jin ; Lee, Jun ; Seong, Jihye ; Kim, Nam-Jung ; Inn, Kyung-Soo</creatorcontrib><description>Despite the diverse pharmacological activities of berberine, including anti-cancer and anti-inflammatory effects, the direct proteomic targets of berberine have remained largely unknown. Here, we have identified actin as a direct proteomic target of berberine using an affinity-based chemical probe. In addition, we found that actin assembly was significantly modulated by berberine in vitro at the biochemical level and cellular level. Actin was identified as a direct target of berberine via a chemoproteomic approach and its assembly was modulated by berberine.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/c7cc02789c</identifier><language>eng</language><creationdate>2017-06</creationdate><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids></links><search><creatorcontrib>Yi, Chae-Min</creatorcontrib><creatorcontrib>Yu, Jihyun</creatorcontrib><creatorcontrib>Kim, Hyunbin</creatorcontrib><creatorcontrib>Lee, Na-Rae</creatorcontrib><creatorcontrib>Kim, Sang Won</creatorcontrib><creatorcontrib>Lee, Noh-Jin</creatorcontrib><creatorcontrib>Lee, Jun</creatorcontrib><creatorcontrib>Seong, Jihye</creatorcontrib><creatorcontrib>Kim, Nam-Jung</creatorcontrib><creatorcontrib>Inn, Kyung-Soo</creatorcontrib><title>Identification of actin as a direct proteomic target of berberine using an affinity-based chemical probe and elucidation of its modulatory role in actin assemblyElectronic supplementary information (ESI) available: Experimental procedures and characterization data. See DOI: 10.1039/c7cc02789c</title><description>Despite the diverse pharmacological activities of berberine, including anti-cancer and anti-inflammatory effects, the direct proteomic targets of berberine have remained largely unknown. Here, we have identified actin as a direct proteomic target of berberine using an affinity-based chemical probe. In addition, we found that actin assembly was significantly modulated by berberine in vitro at the biochemical level and cellular level. Actin was identified as a direct target of berberine via a chemoproteomic approach and its assembly was modulated by berberine.</description><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNqFkL1PwzAQxQMCifKxsCMdAxIMKQlp6McKQXRiKANbdbEvrZFjR7aDWv56Lm0FAxJYJ9nSe8_vp4ui8zTpp0k2vhVDIZK74Wgs9qNemt0P4nwwejvo3vk4HmaD_Cg69v494ZPmo97e1VSSCapSAoOyBmwFKIIygB4QpHIkAjTOBrK1EhDQLSh0rpIcjzIErVdmAciRqlJGhXVcoicJYkkcQd3FS2KDBNKtUPK7SQUPtZWtxmDdGpzVBF31DsBTXep1oRnBWcPtvm0aTTUDI9uVqayrt59dF7PpDeAHKo2lpgkUq4bpNtYNgCDZOvIbCrFExx2sf27TTIR9mBHB48t0Ar-XeRodVqg9ne3uk-jiqXh9eI6dF_OGe5hn_mPP_tcv_9LnjayyL7TXmIw</recordid><startdate>20170627</startdate><enddate>20170627</enddate><creator>Yi, Chae-Min</creator><creator>Yu, Jihyun</creator><creator>Kim, Hyunbin</creator><creator>Lee, Na-Rae</creator><creator>Kim, Sang Won</creator><creator>Lee, Noh-Jin</creator><creator>Lee, Jun</creator><creator>Seong, Jihye</creator><creator>Kim, Nam-Jung</creator><creator>Inn, Kyung-Soo</creator><scope/></search><sort><creationdate>20170627</creationdate><title>Identification of actin as a direct proteomic target of berberine using an affinity-based chemical probe and elucidation of its modulatory role in actin assemblyElectronic supplementary information (ESI) available: Experimental procedures and characterization data. See DOI: 10.1039/c7cc02789c</title><author>Yi, Chae-Min ; Yu, Jihyun ; Kim, Hyunbin ; Lee, Na-Rae ; Kim, Sang Won ; Lee, Noh-Jin ; Lee, Jun ; Seong, Jihye ; Kim, Nam-Jung ; Inn, Kyung-Soo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-rsc_primary_c7cc02789c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yi, Chae-Min</creatorcontrib><creatorcontrib>Yu, Jihyun</creatorcontrib><creatorcontrib>Kim, Hyunbin</creatorcontrib><creatorcontrib>Lee, Na-Rae</creatorcontrib><creatorcontrib>Kim, Sang Won</creatorcontrib><creatorcontrib>Lee, Noh-Jin</creatorcontrib><creatorcontrib>Lee, Jun</creatorcontrib><creatorcontrib>Seong, Jihye</creatorcontrib><creatorcontrib>Kim, Nam-Jung</creatorcontrib><creatorcontrib>Inn, Kyung-Soo</creatorcontrib></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yi, Chae-Min</au><au>Yu, Jihyun</au><au>Kim, Hyunbin</au><au>Lee, Na-Rae</au><au>Kim, Sang Won</au><au>Lee, Noh-Jin</au><au>Lee, Jun</au><au>Seong, Jihye</au><au>Kim, Nam-Jung</au><au>Inn, Kyung-Soo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of actin as a direct proteomic target of berberine using an affinity-based chemical probe and elucidation of its modulatory role in actin assemblyElectronic supplementary information (ESI) available: Experimental procedures and characterization data. See DOI: 10.1039/c7cc02789c</atitle><date>2017-06-27</date><risdate>2017</risdate><volume>53</volume><issue>52</issue><spage>745</spage><epage>747</epage><pages>745-747</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>Despite the diverse pharmacological activities of berberine, including anti-cancer and anti-inflammatory effects, the direct proteomic targets of berberine have remained largely unknown. Here, we have identified actin as a direct proteomic target of berberine using an affinity-based chemical probe. In addition, we found that actin assembly was significantly modulated by berberine in vitro at the biochemical level and cellular level. Actin was identified as a direct target of berberine via a chemoproteomic approach and its assembly was modulated by berberine.</abstract><doi>10.1039/c7cc02789c</doi><tpages>3</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1359-7345
ispartof
issn 1359-7345
1364-548X
language eng
recordid cdi_rsc_primary_c7cc02789c
source Royal Society of Chemistry Journals
title Identification of actin as a direct proteomic target of berberine using an affinity-based chemical probe and elucidation of its modulatory role in actin assemblyElectronic supplementary information (ESI) available: Experimental procedures and characterization data. See DOI: 10.1039/c7cc02789c
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T14%3A06%3A19IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-rsc&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20of%20actin%20as%20a%20direct%20proteomic%20target%20of%20berberine%20using%20an%20affinity-based%20chemical%20probe%20and%20elucidation%20of%20its%20modulatory%20role%20in%20actin%20assemblyElectronic%20supplementary%20information%20(ESI)%20available:%20Experimental%20procedures%20and%20characterization%20data.%20See%20DOI:%2010.1039/c7cc02789c&rft.au=Yi,%20Chae-Min&rft.date=2017-06-27&rft.volume=53&rft.issue=52&rft.spage=745&rft.epage=747&rft.pages=745-747&rft.issn=1359-7345&rft.eissn=1364-548X&rft_id=info:doi/10.1039/c7cc02789c&rft_dat=%3Crsc%3Ec7cc02789c%3C/rsc%3E%3Cgrp_id%3Ecdi_FETCH-rsc_primary_c7cc02789c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true