Loading…
The eIF4E-binding protein Eap1p functions in Vts1p-mediated transcript decay
Sequence-specific RNA binding proteins can induce the degradation of mRNAs through their ability to recruit proteins that trigger transcript destabilization. For example, Vts1p, the S. cerevisiae member of the Smaug family of RNA binding proteins, is thought to induce transcript decay by recruiting...
Saved in:
Published in: | PloS one 2012-10, Vol.7 (10), p.e47121-e47121 |
---|---|
Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c692t-375f557d3c701aef9cfea2b0bc2f8de58f84f251be1d794b7a44d8ad61023f63 |
---|---|
cites | |
container_end_page | e47121 |
container_issue | 10 |
container_start_page | e47121 |
container_title | PloS one |
container_volume | 7 |
creator | Rendl, Laura M Bieman, Melissa A Vari, Heli K Smibert, Craig A |
description | Sequence-specific RNA binding proteins can induce the degradation of mRNAs through their ability to recruit proteins that trigger transcript destabilization. For example, Vts1p, the S. cerevisiae member of the Smaug family of RNA binding proteins, is thought to induce transcript decay by recruiting the Ccr4p-Pop2p-Not deadenylase complex to target mRNAs. The resulting deadenylation triggers transcript decapping followed by 5'-to-3' exonucleolytic decay. Here we show that the eIF4E-binding protein, Eap1p, is required for efficient degradation of Vts1p target transcripts and that this role involves the ability of Eap1p to interact with eIF4E. Eap1p does not stimulate deadenylation of Vts1p target transcripts but is instead involved in decapping. Eap1p interacts with Vts1p and mediates an indirect interaction between Vts1p and eIF4E. Taken together these data suggest a model whereby the interaction of Vts1p with Eap1p at target mRNAs stimulates decapping. |
doi_str_mv | 10.1371/journal.pone.0047121 |
format | article |
fullrecord | <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_1326559263</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A543329864</galeid><doaj_id>oai_doaj_org_article_d7c3ffe5155142fd848d5f732e19c6e9</doaj_id><sourcerecordid>A543329864</sourcerecordid><originalsourceid>FETCH-LOGICAL-c692t-375f557d3c701aef9cfea2b0bc2f8de58f84f251be1d794b7a44d8ad61023f63</originalsourceid><addsrcrecordid>eNqNkl1r2zAUhs3YWLtu_2BshsHYLpJZ3_bNoJR0CwQKW-itkKWjRMGxPEse67-f0rglHr0YEkgcPeeVztGbZW9RMUdEoC87P_Stauadb2FeFFQgjJ5l56gieMZxQZ6f7M-yVyHsioKRkvOX2RkmhUACl-fZar2FHJbXdDGrXWtcu8m73kdwbb5QHepyO7Q6Ot-GPIVuY0DdbA_GqQgmj71qg-5dF3MDWt29zl5Y1QR4M64X2fp6sb76PlvdfFteXa5mmlc4zohgljFhiBYFUmArbUHhuqg1tqUBVtqSWsxQDciIitZCUWpKZTgqMLGcXGTvj7Jd44Mc-xAkIpgzVmFOErE8Esarnex6t1f9nfTKyfuA7zdS9dHpBqQRmlgLDDGGKLampKVhVhAMqNIcqqT1dbxtqFPlGtpUdjMRnZ60bis3_rcklJdpJoFPo0Dvfw0Qoty7oKFpVAt-SO9GCHNRCnFAP_yDPl3dSG1UKsC11qd79UFUXjJKCK5KThM1f4JKw8De6WQa61J8kvB5kpCYCH_iRg0hyOXPH__P3txO2Y8n7BZUE7fBN8O9q6YgPYK69yH0YB-bjAp58PxDN-TB83L0fEp7d_pBj0kPJid_Ae1n-wQ</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1326559263</pqid></control><display><type>article</type><title>The eIF4E-binding protein Eap1p functions in Vts1p-mediated transcript decay</title><source>Publicly Available Content (ProQuest)</source><source>PubMed Central</source><creator>Rendl, Laura M ; Bieman, Melissa A ; Vari, Heli K ; Smibert, Craig A</creator><contributor>Mata, Juan</contributor><creatorcontrib>Rendl, Laura M ; Bieman, Melissa A ; Vari, Heli K ; Smibert, Craig A ; Mata, Juan</creatorcontrib><description>Sequence-specific RNA binding proteins can induce the degradation of mRNAs through their ability to recruit proteins that trigger transcript destabilization. For example, Vts1p, the S. cerevisiae member of the Smaug family of RNA binding proteins, is thought to induce transcript decay by recruiting the Ccr4p-Pop2p-Not deadenylase complex to target mRNAs. The resulting deadenylation triggers transcript decapping followed by 5'-to-3' exonucleolytic decay. Here we show that the eIF4E-binding protein, Eap1p, is required for efficient degradation of Vts1p target transcripts and that this role involves the ability of Eap1p to interact with eIF4E. Eap1p does not stimulate deadenylation of Vts1p target transcripts but is instead involved in decapping. Eap1p interacts with Vts1p and mediates an indirect interaction between Vts1p and eIF4E. Taken together these data suggest a model whereby the interaction of Vts1p with Eap1p at target mRNAs stimulates decapping.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0047121</identifier><identifier>PMID: 23071728</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Binding proteins ; Biochemistry ; Biology ; Decay ; Degradation ; Destabilization ; Eukaryotic Initiation Factor-4E - metabolism ; Gene expression ; Initiation factor eIF-4E ; Messenger RNA ; Nucleotide sequence ; Protein Binding ; Proteins ; Ribonucleic acid ; RNA ; RNA Caps - metabolism ; RNA Stability ; RNA, Messenger - metabolism ; RNA-binding protein ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Transcription ; Transcription Factors - genetics ; Transcription Factors - metabolism ; Yeast</subject><ispartof>PloS one, 2012-10, Vol.7 (10), p.e47121-e47121</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>Rendl et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2012 Rendl et al 2012 Rendl et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-375f557d3c701aef9cfea2b0bc2f8de58f84f251be1d794b7a44d8ad61023f63</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1326559263/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1326559263?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,882,25734,27905,27906,36993,36994,44571,53772,53774,74875</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23071728$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Mata, Juan</contributor><creatorcontrib>Rendl, Laura M</creatorcontrib><creatorcontrib>Bieman, Melissa A</creatorcontrib><creatorcontrib>Vari, Heli K</creatorcontrib><creatorcontrib>Smibert, Craig A</creatorcontrib><title>The eIF4E-binding protein Eap1p functions in Vts1p-mediated transcript decay</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Sequence-specific RNA binding proteins can induce the degradation of mRNAs through their ability to recruit proteins that trigger transcript destabilization. For example, Vts1p, the S. cerevisiae member of the Smaug family of RNA binding proteins, is thought to induce transcript decay by recruiting the Ccr4p-Pop2p-Not deadenylase complex to target mRNAs. The resulting deadenylation triggers transcript decapping followed by 5'-to-3' exonucleolytic decay. Here we show that the eIF4E-binding protein, Eap1p, is required for efficient degradation of Vts1p target transcripts and that this role involves the ability of Eap1p to interact with eIF4E. Eap1p does not stimulate deadenylation of Vts1p target transcripts but is instead involved in decapping. Eap1p interacts with Vts1p and mediates an indirect interaction between Vts1p and eIF4E. Taken together these data suggest a model whereby the interaction of Vts1p with Eap1p at target mRNAs stimulates decapping.</description><subject>Binding proteins</subject><subject>Biochemistry</subject><subject>Biology</subject><subject>Decay</subject><subject>Degradation</subject><subject>Destabilization</subject><subject>Eukaryotic Initiation Factor-4E - metabolism</subject><subject>Gene expression</subject><subject>Initiation factor eIF-4E</subject><subject>Messenger RNA</subject><subject>Nucleotide sequence</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA Caps - metabolism</subject><subject>RNA Stability</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA-binding protein</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Transcription</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><subject>Yeast</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNqNkl1r2zAUhs3YWLtu_2BshsHYLpJZ3_bNoJR0CwQKW-itkKWjRMGxPEse67-f0rglHr0YEkgcPeeVztGbZW9RMUdEoC87P_Stauadb2FeFFQgjJ5l56gieMZxQZ6f7M-yVyHsioKRkvOX2RkmhUACl-fZar2FHJbXdDGrXWtcu8m73kdwbb5QHepyO7Q6Ot-GPIVuY0DdbA_GqQgmj71qg-5dF3MDWt29zl5Y1QR4M64X2fp6sb76PlvdfFteXa5mmlc4zohgljFhiBYFUmArbUHhuqg1tqUBVtqSWsxQDciIitZCUWpKZTgqMLGcXGTvj7Jd44Mc-xAkIpgzVmFOErE8Esarnex6t1f9nfTKyfuA7zdS9dHpBqQRmlgLDDGGKLampKVhVhAMqNIcqqT1dbxtqFPlGtpUdjMRnZ60bis3_rcklJdpJoFPo0Dvfw0Qoty7oKFpVAt-SO9GCHNRCnFAP_yDPl3dSG1UKsC11qd79UFUXjJKCK5KThM1f4JKw8De6WQa61J8kvB5kpCYCH_iRg0hyOXPH__P3txO2Y8n7BZUE7fBN8O9q6YgPYK69yH0YB-bjAp58PxDN-TB83L0fEp7d_pBj0kPJid_Ae1n-wQ</recordid><startdate>20121010</startdate><enddate>20121010</enddate><creator>Rendl, Laura M</creator><creator>Bieman, Melissa A</creator><creator>Vari, Heli K</creator><creator>Smibert, Craig A</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20121010</creationdate><title>The eIF4E-binding protein Eap1p functions in Vts1p-mediated transcript decay</title><author>Rendl, Laura M ; Bieman, Melissa A ; Vari, Heli K ; Smibert, Craig A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-375f557d3c701aef9cfea2b0bc2f8de58f84f251be1d794b7a44d8ad61023f63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Binding proteins</topic><topic>Biochemistry</topic><topic>Biology</topic><topic>Decay</topic><topic>Degradation</topic><topic>Destabilization</topic><topic>Eukaryotic Initiation Factor-4E - metabolism</topic><topic>Gene expression</topic><topic>Initiation factor eIF-4E</topic><topic>Messenger RNA</topic><topic>Nucleotide sequence</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>RNA Caps - metabolism</topic><topic>RNA Stability</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA-binding protein</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Transcription</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rendl, Laura M</creatorcontrib><creatorcontrib>Bieman, Melissa A</creatorcontrib><creatorcontrib>Vari, Heli K</creatorcontrib><creatorcontrib>Smibert, Craig A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Opposing Viewpoints Resource Center</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>https://resources.nclive.org/materials</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agriculture Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest advanced technologies & aerospace journals</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials science collection</collection><collection>Publicly Available Content (ProQuest)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Directory of Open Access Journals(OpenAccess)</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rendl, Laura M</au><au>Bieman, Melissa A</au><au>Vari, Heli K</au><au>Smibert, Craig A</au><au>Mata, Juan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The eIF4E-binding protein Eap1p functions in Vts1p-mediated transcript decay</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2012-10-10</date><risdate>2012</risdate><volume>7</volume><issue>10</issue><spage>e47121</spage><epage>e47121</epage><pages>e47121-e47121</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Sequence-specific RNA binding proteins can induce the degradation of mRNAs through their ability to recruit proteins that trigger transcript destabilization. For example, Vts1p, the S. cerevisiae member of the Smaug family of RNA binding proteins, is thought to induce transcript decay by recruiting the Ccr4p-Pop2p-Not deadenylase complex to target mRNAs. The resulting deadenylation triggers transcript decapping followed by 5'-to-3' exonucleolytic decay. Here we show that the eIF4E-binding protein, Eap1p, is required for efficient degradation of Vts1p target transcripts and that this role involves the ability of Eap1p to interact with eIF4E. Eap1p does not stimulate deadenylation of Vts1p target transcripts but is instead involved in decapping. Eap1p interacts with Vts1p and mediates an indirect interaction between Vts1p and eIF4E. Taken together these data suggest a model whereby the interaction of Vts1p with Eap1p at target mRNAs stimulates decapping.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23071728</pmid><doi>10.1371/journal.pone.0047121</doi><tpages>e47121</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1932-6203 |
ispartof | PloS one, 2012-10, Vol.7 (10), p.e47121-e47121 |
issn | 1932-6203 1932-6203 |
language | eng |
recordid | cdi_plos_journals_1326559263 |
source | Publicly Available Content (ProQuest); PubMed Central |
subjects | Binding proteins Biochemistry Biology Decay Degradation Destabilization Eukaryotic Initiation Factor-4E - metabolism Gene expression Initiation factor eIF-4E Messenger RNA Nucleotide sequence Protein Binding Proteins Ribonucleic acid RNA RNA Caps - metabolism RNA Stability RNA, Messenger - metabolism RNA-binding protein RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Transcription Transcription Factors - genetics Transcription Factors - metabolism Yeast |
title | The eIF4E-binding protein Eap1p functions in Vts1p-mediated transcript decay |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T22%3A38%3A43IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20eIF4E-binding%20protein%20Eap1p%20functions%20in%20Vts1p-mediated%20transcript%20decay&rft.jtitle=PloS%20one&rft.au=Rendl,%20Laura%20M&rft.date=2012-10-10&rft.volume=7&rft.issue=10&rft.spage=e47121&rft.epage=e47121&rft.pages=e47121-e47121&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0047121&rft_dat=%3Cgale_plos_%3EA543329864%3C/gale_plos_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c692t-375f557d3c701aef9cfea2b0bc2f8de58f84f251be1d794b7a44d8ad61023f63%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1326559263&rft_id=info:pmid/23071728&rft_galeid=A543329864&rfr_iscdi=true |