Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver.
Identifieur interne : 000518 ( Main/Exploration ); précédent : 000517; suivant : 000519Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver.
Auteurs : David J. Mcgarry [Royaume-Uni] ; Wenzhang Chen [Royaume-Uni] ; Probir Chakravarty [Royaume-Uni] ; Douglas L. Lamont [Royaume-Uni] ; C Roland Wolf [Royaume-Uni] ; Colin J. Henderson [Royaume-Uni]Source :
- The Biochemical journal [ 1470-8728 ] ; 2015.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Foie (métabolisme), Glutathion (génétique), Glutathion (métabolisme), Glutathione transferase (génétique), Glutathione transferase (métabolisme), Maturation post-traductionnelle des protéines (MeSH), Protéines mitochondriales (génétique), Protéines mitochondriales (métabolisme), Protéome (génétique), Protéome (métabolisme), Souris (MeSH), Souris knockout (MeSH).
- MESH :
English descriptors
- KwdEn :
- Animals (MeSH), Glutathione (genetics), Glutathione (metabolism), Glutathione Transferase (genetics), Glutathione Transferase (metabolism), Liver (metabolism), Mice (MeSH), Mice, Knockout (MeSH), Mitochondrial Proteins (genetics), Mitochondrial Proteins (metabolism), Protein Processing, Post-Translational (MeSH), Proteome (genetics), Proteome (metabolism).
- MESH :
- chemical , genetics : Glutathione, Glutathione Transferase, Mitochondrial Proteins, Proteome.
- chemical , metabolism : Glutathione, Glutathione Transferase, Mitochondrial Proteins, Proteome.
- metabolism : Liver.
- Animals, Mice, Mice, Knockout, Protein Processing, Post-Translational.
Abstract
Protein S-glutathionylation is a reversible post-translational modification regulating sulfhydryl homeostasis. However, little is known about the proteins and pathways regulated by S-glutathionylation in whole organisms and current approaches lack the sensitivity to examine this modification under basal conditions. We now report the quantification and identification of S-glutathionylated proteins from animal tissue, using a highly sensitive methodology combining high-accuracy proteomics with tandem mass tagging to provide precise, extensive coverage of S-glutathionylated targets in mouse liver. Critically, we show significant enrichment of S-glutathionylated mitochondrial and Krebs cycle proteins, identifying that S-glutathionylation is heavily involved in energy metabolism processes in vivo. Furthermore, using mice nulled for GST Pi (GSTP) we address the potential for S-glutathionylation to be mediated enzymatically. The data demonstrate the impact of S-glutathionylation in cellular homeostasis, particularly in relation to energy regulation and is of significant interest for those wishing to examine S-glutathionylation in an animal model.
DOI: 10.1042/BJ20141256
PubMed: 25891661
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver.</title><author><name sortKey="Mcgarry, David J" sort="Mcgarry, David J" uniqKey="Mcgarry D" first="David J" last="Mcgarry">David J. Mcgarry</name><affiliation wicri:level="1"><nlm:affiliation>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY, U.K. d.mcgarry@dundee.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY</wicri:regionArea><wicri:noRegion>Dundee DD1 9SY</wicri:noRegion></affiliation></author><author><name sortKey="Chen, Wenzhang" sort="Chen, Wenzhang" uniqKey="Chen W" first="Wenzhang" last="Chen">Wenzhang Chen</name><affiliation wicri:level="1"><nlm:affiliation>FingerPrints Proteomics Facility, MSI/WTB/JBC Complex, College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>FingerPrints Proteomics Facility, MSI/WTB/JBC Complex, College of Life Sciences, University of Dundee, Dundee DD1 5EH</wicri:regionArea><wicri:noRegion>Dundee DD1 5EH</wicri:noRegion></affiliation></author><author><name sortKey="Chakravarty, Probir" sort="Chakravarty, Probir" uniqKey="Chakravarty P" first="Probir" last="Chakravarty">Probir Chakravarty</name><affiliation wicri:level="1"><nlm:affiliation>Bioinformatics & Biostatistics Group, Cancer Research UK London Research Institute, 44, Lincoln's Inn Fields, London WC2A 3PX, U.K.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Bioinformatics & Biostatistics Group, Cancer Research UK London Research Institute, 44, Lincoln's Inn Fields, London WC2A 3PX</wicri:regionArea><wicri:noRegion>London WC2A 3PX</wicri:noRegion></affiliation></author><author><name sortKey="Lamont, Douglas L" sort="Lamont, Douglas L" uniqKey="Lamont D" first="Douglas L" last="Lamont">Douglas L. Lamont</name><affiliation wicri:level="1"><nlm:affiliation>FingerPrints Proteomics Facility, MSI/WTB/JBC Complex, College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>FingerPrints Proteomics Facility, MSI/WTB/JBC Complex, College of Life Sciences, University of Dundee, Dundee DD1 5EH</wicri:regionArea><wicri:noRegion>Dundee DD1 5EH</wicri:noRegion></affiliation></author><author><name sortKey="Wolf, C Roland" sort="Wolf, C Roland" uniqKey="Wolf C" first="C Roland" last="Wolf">C Roland Wolf</name><affiliation wicri:level="1"><nlm:affiliation>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY, U.K.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY</wicri:regionArea><wicri:noRegion>Dundee DD1 9SY</wicri:noRegion></affiliation></author><author><name sortKey="Henderson, Colin J" sort="Henderson, Colin J" uniqKey="Henderson C" first="Colin J" last="Henderson">Colin J. Henderson</name><affiliation wicri:level="1"><nlm:affiliation>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY, U.K.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY</wicri:regionArea><wicri:noRegion>Dundee DD1 9SY</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:25891661</idno><idno type="pmid">25891661</idno><idno type="doi">10.1042/BJ20141256</idno><idno type="wicri:Area/Main/Corpus">000534</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000534</idno><idno type="wicri:Area/Main/Curation">000534</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000534</idno><idno type="wicri:Area/Main/Exploration">000534</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver.</title><author><name sortKey="Mcgarry, David J" sort="Mcgarry, David J" uniqKey="Mcgarry D" first="David J" last="Mcgarry">David J. Mcgarry</name><affiliation wicri:level="1"><nlm:affiliation>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY, U.K. d.mcgarry@dundee.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY</wicri:regionArea><wicri:noRegion>Dundee DD1 9SY</wicri:noRegion></affiliation></author><author><name sortKey="Chen, Wenzhang" sort="Chen, Wenzhang" uniqKey="Chen W" first="Wenzhang" last="Chen">Wenzhang Chen</name><affiliation wicri:level="1"><nlm:affiliation>FingerPrints Proteomics Facility, MSI/WTB/JBC Complex, College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>FingerPrints Proteomics Facility, MSI/WTB/JBC Complex, College of Life Sciences, University of Dundee, Dundee DD1 5EH</wicri:regionArea><wicri:noRegion>Dundee DD1 5EH</wicri:noRegion></affiliation></author><author><name sortKey="Chakravarty, Probir" sort="Chakravarty, Probir" uniqKey="Chakravarty P" first="Probir" last="Chakravarty">Probir Chakravarty</name><affiliation wicri:level="1"><nlm:affiliation>Bioinformatics & Biostatistics Group, Cancer Research UK London Research Institute, 44, Lincoln's Inn Fields, London WC2A 3PX, U.K.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Bioinformatics & Biostatistics Group, Cancer Research UK London Research Institute, 44, Lincoln's Inn Fields, London WC2A 3PX</wicri:regionArea><wicri:noRegion>London WC2A 3PX</wicri:noRegion></affiliation></author><author><name sortKey="Lamont, Douglas L" sort="Lamont, Douglas L" uniqKey="Lamont D" first="Douglas L" last="Lamont">Douglas L. Lamont</name><affiliation wicri:level="1"><nlm:affiliation>FingerPrints Proteomics Facility, MSI/WTB/JBC Complex, College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>FingerPrints Proteomics Facility, MSI/WTB/JBC Complex, College of Life Sciences, University of Dundee, Dundee DD1 5EH</wicri:regionArea><wicri:noRegion>Dundee DD1 5EH</wicri:noRegion></affiliation></author><author><name sortKey="Wolf, C Roland" sort="Wolf, C Roland" uniqKey="Wolf C" first="C Roland" last="Wolf">C Roland Wolf</name><affiliation wicri:level="1"><nlm:affiliation>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY, U.K.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY</wicri:regionArea><wicri:noRegion>Dundee DD1 9SY</wicri:noRegion></affiliation></author><author><name sortKey="Henderson, Colin J" sort="Henderson, Colin J" uniqKey="Henderson C" first="Colin J" last="Henderson">Colin J. Henderson</name><affiliation wicri:level="1"><nlm:affiliation>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY, U.K.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY</wicri:regionArea><wicri:noRegion>Dundee DD1 9SY</wicri:noRegion></affiliation></author></analytic><series><title level="j">The Biochemical journal</title><idno type="eISSN">1470-8728</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Glutathione (genetics)</term><term>Glutathione (metabolism)</term><term>Glutathione Transferase (genetics)</term><term>Glutathione Transferase (metabolism)</term><term>Liver (metabolism)</term><term>Mice (MeSH)</term><term>Mice, Knockout (MeSH)</term><term>Mitochondrial Proteins (genetics)</term><term>Mitochondrial Proteins (metabolism)</term><term>Protein Processing, Post-Translational (MeSH)</term><term>Proteome (genetics)</term><term>Proteome (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Foie (métabolisme)</term><term>Glutathion (génétique)</term><term>Glutathion (métabolisme)</term><term>Glutathione transferase (génétique)</term><term>Glutathione transferase (métabolisme)</term><term>Maturation post-traductionnelle des protéines (MeSH)</term><term>Protéines mitochondriales (génétique)</term><term>Protéines mitochondriales (métabolisme)</term><term>Protéome (génétique)</term><term>Protéome (métabolisme)</term><term>Souris (MeSH)</term><term>Souris knockout (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutathione</term><term>Glutathione Transferase</term><term>Mitochondrial Proteins</term><term>Proteome</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Glutathione Transferase</term><term>Mitochondrial Proteins</term><term>Proteome</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutathion</term><term>Glutathione transferase</term><term>Protéines mitochondriales</term><term>Protéome</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Liver</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Foie</term><term>Glutathion</term><term>Glutathione transferase</term><term>Protéines mitochondriales</term><term>Protéome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Mice</term><term>Mice, Knockout</term><term>Protein Processing, Post-Translational</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Maturation post-traductionnelle des protéines</term><term>Souris</term><term>Souris knockout</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Protein S-glutathionylation is a reversible post-translational modification regulating sulfhydryl homeostasis. However, little is known about the proteins and pathways regulated by S-glutathionylation in whole organisms and current approaches lack the sensitivity to examine this modification under basal conditions. We now report the quantification and identification of S-glutathionylated proteins from animal tissue, using a highly sensitive methodology combining high-accuracy proteomics with tandem mass tagging to provide precise, extensive coverage of S-glutathionylated targets in mouse liver. Critically, we show significant enrichment of S-glutathionylated mitochondrial and Krebs cycle proteins, identifying that S-glutathionylation is heavily involved in energy metabolism processes in vivo. Furthermore, using mice nulled for GST Pi (GSTP) we address the potential for S-glutathionylation to be mediated enzymatically. The data demonstrate the impact of S-glutathionylation in cellular homeostasis, particularly in relation to energy regulation and is of significant interest for those wishing to examine S-glutathionylation in an animal model. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25891661</PMID><DateCompleted><Year>2015</Year><Month>09</Month><Day>25</Day></DateCompleted><DateRevised><Year>2018</Year><Month>04</Month><Day>29</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1470-8728</ISSN><JournalIssue CitedMedium="Internet"><Volume>469</Volume><Issue>1</Issue><PubDate><Year>2015</Year><Month>Jul</Month><Day>01</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver.</ArticleTitle><Pagination><MedlinePgn>25-32</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1042/BJ20141256</ELocationID><Abstract><AbstractText>Protein S-glutathionylation is a reversible post-translational modification regulating sulfhydryl homeostasis. However, little is known about the proteins and pathways regulated by S-glutathionylation in whole organisms and current approaches lack the sensitivity to examine this modification under basal conditions. We now report the quantification and identification of S-glutathionylated proteins from animal tissue, using a highly sensitive methodology combining high-accuracy proteomics with tandem mass tagging to provide precise, extensive coverage of S-glutathionylated targets in mouse liver. Critically, we show significant enrichment of S-glutathionylated mitochondrial and Krebs cycle proteins, identifying that S-glutathionylation is heavily involved in energy metabolism processes in vivo. Furthermore, using mice nulled for GST Pi (GSTP) we address the potential for S-glutathionylation to be mediated enzymatically. The data demonstrate the impact of S-glutathionylation in cellular homeostasis, particularly in relation to energy regulation and is of significant interest for those wishing to examine S-glutathionylation in an animal model. </AbstractText><CopyrightInformation>© 2015 Authors; published by Portland Press Limited.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>McGarry</LastName><ForeName>David J</ForeName><Initials>DJ</Initials><AffiliationInfo><Affiliation>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY, U.K. d.mcgarry@dundee.ac.uk.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Wenzhang</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>FingerPrints Proteomics Facility, MSI/WTB/JBC Complex, College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chakravarty</LastName><ForeName>Probir</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Bioinformatics & Biostatistics Group, Cancer Research UK London Research Institute, 44, Lincoln's Inn Fields, London WC2A 3PX, U.K.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lamont</LastName><ForeName>Douglas L</ForeName><Initials>DL</Initials><AffiliationInfo><Affiliation>FingerPrints Proteomics Facility, MSI/WTB/JBC Complex, College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wolf</LastName><ForeName>C Roland</ForeName><Initials>CR</Initials><AffiliationInfo><Affiliation>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY, U.K.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Henderson</LastName><ForeName>Colin J</ForeName><Initials>CJ</Initials><AffiliationInfo><Affiliation>Molecular Pharmacology Group, Medical Research Institute, Level 9, Jacqui Wood Cancer Centre, Dundee DD1 9SY, U.K.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>097945</GrantID><Agency>Wellcome Trust</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>C4639/A10822</GrantID><Agency>Cancer Research UK</Agency><Country>United Kingdom</Country></Grant><Grant><Agency>Medical Research Council</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>04</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024101">Mitochondrial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020543">Proteome</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018345" MajorTopicYN="N">Mice, Knockout</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D024101" MajorTopicYN="N">Mitochondrial Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="Y">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020543" MajorTopicYN="N">Proteome</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">S-glutathionylation</Keyword><Keyword MajorTopicYN="N">energy metabolism</Keyword><Keyword MajorTopicYN="N">glutaredoxin</Keyword><Keyword MajorTopicYN="N">glutathione S-transferase (Pi)</Keyword><Keyword MajorTopicYN="N">liver</Keyword><Keyword MajorTopicYN="N">tandem mass tagging</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>10</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>04</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>4</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>4</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>9</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25891661</ArticleId><ArticleId IdType="pii">BJ20141256</ArticleId><ArticleId IdType="doi">10.1042/BJ20141256</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Mcgarry, David J" sort="Mcgarry, David J" uniqKey="Mcgarry D" first="David J" last="Mcgarry">David J. Mcgarry</name></noRegion><name sortKey="Chakravarty, Probir" sort="Chakravarty, Probir" uniqKey="Chakravarty P" first="Probir" last="Chakravarty">Probir Chakravarty</name><name sortKey="Chen, Wenzhang" sort="Chen, Wenzhang" uniqKey="Chen W" first="Wenzhang" last="Chen">Wenzhang Chen</name><name sortKey="Henderson, Colin J" sort="Henderson, Colin J" uniqKey="Henderson C" first="Colin J" last="Henderson">Colin J. Henderson</name><name sortKey="Lamont, Douglas L" sort="Lamont, Douglas L" uniqKey="Lamont D" first="Douglas L" last="Lamont">Douglas L. Lamont</name><name sortKey="Wolf, C Roland" sort="Wolf, C Roland" uniqKey="Wolf C" first="C Roland" last="Wolf">C Roland Wolf</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000518 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000518 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:25891661
|texte= Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:25891661" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |