GlutaredoxinV1, Main, Exploration, bibRecord, 000B14

In vivo fluorescent detection of Fe-S clusters coordinated by human GRX2.

Identifieur interne : 000B14 ( Main/Exploration ); précédent : 000B13; suivant : 000B15

In vivo fluorescent detection of Fe-S clusters coordinated by human GRX2.

Auteurs : Kevin G. Hoff [États-Unis] ; Stephanie J. Culler ; Peter Q. Nguyen ; Ryan M. Mcguire ; Jonathan J. Silberg ; Christina D. Smolke

Source :

Chemistry & biology [ 1879-1301 ] ; 2009.

RBID : pubmed:20064440

Descripteurs français

KwdFr :
- Dichroïsme circulaire (MeSH), Dimérisation (MeSH), Fer (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Humains (MeSH), Interférence par ARN (MeSH), Lignée cellulaire (MeSH), Microscopie de fluorescence (MeSH), Mutation (MeSH), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines luminescentes (génétique), Protéines luminescentes (métabolisme), Sites de fixation (MeSH), Soufre (composition chimique).
MESH :
- composition chimique : Fer, Soufre.
- génétique : Glutarédoxines, Protéines de fusion recombinantes, Protéines luminescentes.
- métabolisme : Glutarédoxines, Protéines de fusion recombinantes, Protéines luminescentes.
- Dichroïsme circulaire, Dimérisation, Humains, Interférence par ARN, Lignée cellulaire, Microscopie de fluorescence, Mutation, Sites de fixation.

English descriptors

KwdEn :
- Binding Sites (MeSH), Cell Line (MeSH), Circular Dichroism (MeSH), Dimerization (MeSH), Glutaredoxins (genetics), Glutaredoxins (metabolism), Humans (MeSH), Iron (chemistry), Luminescent Proteins (genetics), Luminescent Proteins (metabolism), Microscopy, Fluorescence (MeSH), Mutation (MeSH), RNA Interference (MeSH), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Sulfur (chemistry).
MESH :
- chemical , chemistry : Iron, Sulfur.
- chemical , genetics : Glutaredoxins, Luminescent Proteins, Recombinant Fusion Proteins.
- chemical , metabolism : Glutaredoxins, Luminescent Proteins, Recombinant Fusion Proteins.
- Binding Sites, Cell Line, Circular Dichroism, Dimerization, Humans, Microscopy, Fluorescence, Mutation, RNA Interference.

Abstract

A major challenge to studying Fe-S cluster biosynthesis in higher eukaryotes is the lack of simple tools for imaging metallocluster binding to proteins. We describe the first fluorescent approach for in vivo detection of 2Fe2S clusters that is based upon the complementation of Venus fluorescent protein fragments via human glutaredoxin 2 (GRX2) coordination of a 2Fe2S cluster. We show that Escherichia coli and mammalian cells expressing Venus fragments fused to GRX2 exhibit greater fluorescence than cells expressing fragments fused to a C37A mutant that cannot coordinate a metallocluster. In addition, we find that maximal fluorescence in the cytosol of mammalian cells requires the iron-sulfur cluster assembly proteins ISCU and NFS1. These findings provide evidence that glutaredoxins can dimerize within mammalian cells through coordination of a 2Fe2S cluster as observed with purified recombinant proteins.

DOI: 10.1016/j.chembiol.2009.11.011
PubMed: 20064440

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000A40
to stream Main, to step Curation: 000A40

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">In vivo fluorescent detection of Fe-S clusters coordinated by human GRX2.</title>
<author><name sortKey="Hoff, Kevin G" sort="Hoff, Kevin G" uniqKey="Hoff K" first="Kevin G" last="Hoff">Kevin G. Hoff</name>
<affiliation wicri:level="2"><nlm:affiliation>Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E California Boulevard, Mail Code 210-41, Pasadena, CA 91125, USA. khoff@caltech.edu</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E California Boulevard, Mail Code 210-41, Pasadena, CA 91125</wicri:regionArea>
<placeName><region type="state">Californie</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Culler, Stephanie J" sort="Culler, Stephanie J" uniqKey="Culler S" first="Stephanie J" last="Culler">Stephanie J. Culler</name>
</author>
<author><name sortKey="Nguyen, Peter Q" sort="Nguyen, Peter Q" uniqKey="Nguyen P" first="Peter Q" last="Nguyen">Peter Q. Nguyen</name>
</author>
<author><name sortKey="Mcguire, Ryan M" sort="Mcguire, Ryan M" uniqKey="Mcguire R" first="Ryan M" last="Mcguire">Ryan M. Mcguire</name>
</author>
<author><name sortKey="Silberg, Jonathan J" sort="Silberg, Jonathan J" uniqKey="Silberg J" first="Jonathan J" last="Silberg">Jonathan J. Silberg</name>
</author>
<author><name sortKey="Smolke, Christina D" sort="Smolke, Christina D" uniqKey="Smolke C" first="Christina D" last="Smolke">Christina D. Smolke</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2009">2009</date>
<idno type="RBID">pubmed:20064440</idno>
<idno type="pmid">20064440</idno>
<idno type="doi">10.1016/j.chembiol.2009.11.011</idno>
<idno type="wicri:Area/Main/Corpus">000A40</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000A40</idno>
<idno type="wicri:Area/Main/Curation">000A40</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000A40</idno>
<idno type="wicri:Area/Main/Exploration">000A40</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">In vivo fluorescent detection of Fe-S clusters coordinated by human GRX2.</title>
<author><name sortKey="Hoff, Kevin G" sort="Hoff, Kevin G" uniqKey="Hoff K" first="Kevin G" last="Hoff">Kevin G. Hoff</name>
<affiliation wicri:level="2"><nlm:affiliation>Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E California Boulevard, Mail Code 210-41, Pasadena, CA 91125, USA. khoff@caltech.edu</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E California Boulevard, Mail Code 210-41, Pasadena, CA 91125</wicri:regionArea>
<placeName><region type="state">Californie</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Culler, Stephanie J" sort="Culler, Stephanie J" uniqKey="Culler S" first="Stephanie J" last="Culler">Stephanie J. Culler</name>
</author>
<author><name sortKey="Nguyen, Peter Q" sort="Nguyen, Peter Q" uniqKey="Nguyen P" first="Peter Q" last="Nguyen">Peter Q. Nguyen</name>
</author>
<author><name sortKey="Mcguire, Ryan M" sort="Mcguire, Ryan M" uniqKey="Mcguire R" first="Ryan M" last="Mcguire">Ryan M. Mcguire</name>
</author>
<author><name sortKey="Silberg, Jonathan J" sort="Silberg, Jonathan J" uniqKey="Silberg J" first="Jonathan J" last="Silberg">Jonathan J. Silberg</name>
</author>
<author><name sortKey="Smolke, Christina D" sort="Smolke, Christina D" uniqKey="Smolke C" first="Christina D" last="Smolke">Christina D. Smolke</name>
</author>
</analytic>
<series><title level="j">Chemistry & biology</title>
<idno type="eISSN">1879-1301</idno>
<imprint><date when="2009" type="published">2009</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term>
<term>Cell Line (MeSH)</term>
<term>Circular Dichroism (MeSH)</term>
<term>Dimerization (MeSH)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Iron (chemistry)</term>
<term>Luminescent Proteins (genetics)</term>
<term>Luminescent Proteins (metabolism)</term>
<term>Microscopy, Fluorescence (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>RNA Interference (MeSH)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Sulfur (chemistry)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Dichroïsme circulaire (MeSH)</term>
<term>Dimérisation (MeSH)</term>
<term>Fer (composition chimique)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Interférence par ARN (MeSH)</term>
<term>Lignée cellulaire (MeSH)</term>
<term>Microscopie de fluorescence (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines luminescentes (génétique)</term>
<term>Protéines luminescentes (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
<term>Soufre (composition chimique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Iron</term>
<term>Sulfur</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term>
<term>Luminescent Proteins</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Luminescent Proteins</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Fer</term>
<term>Soufre</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines luminescentes</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines luminescentes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>Cell Line</term>
<term>Circular Dichroism</term>
<term>Dimerization</term>
<term>Humans</term>
<term>Microscopy, Fluorescence</term>
<term>Mutation</term>
<term>RNA Interference</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Dichroïsme circulaire</term>
<term>Dimérisation</term>
<term>Humains</term>
<term>Interférence par ARN</term>
<term>Lignée cellulaire</term>
<term>Microscopie de fluorescence</term>
<term>Mutation</term>
<term>Sites de fixation</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">A major challenge to studying Fe-S cluster biosynthesis in higher eukaryotes is the lack of simple tools for imaging metallocluster binding to proteins. We describe the first fluorescent approach for in vivo detection of 2Fe2S clusters that is based upon the complementation of Venus fluorescent protein fragments via human glutaredoxin 2 (GRX2) coordination of a 2Fe2S cluster. We show that Escherichia coli and mammalian cells expressing Venus fragments fused to GRX2 exhibit greater fluorescence than cells expressing fragments fused to a C37A mutant that cannot coordinate a metallocluster. In addition, we find that maximal fluorescence in the cytosol of mammalian cells requires the iron-sulfur cluster assembly proteins ISCU and NFS1. These findings provide evidence that glutaredoxins can dimerize within mammalian cells through coordination of a 2Fe2S cluster as observed with purified recombinant proteins.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20064440</PMID>
<DateCompleted><Year>2010</Year>
<Month>03</Month>
<Day>11</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>02</Month>
<Day>26</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1879-1301</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>16</Volume>
<Issue>12</Issue>
<PubDate><Year>2009</Year>
<Month>Dec</Month>
<Day>24</Day>
</PubDate>
</JournalIssue>
<Title>Chemistry & biology</Title>
<ISOAbbreviation>Chem Biol</ISOAbbreviation>
</Journal>
<ArticleTitle>In vivo fluorescent detection of Fe-S clusters coordinated by human GRX2.</ArticleTitle>
<Pagination><MedlinePgn>1299-308</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.chembiol.2009.11.011</ELocationID>
<Abstract><AbstractText>A major challenge to studying Fe-S cluster biosynthesis in higher eukaryotes is the lack of simple tools for imaging metallocluster binding to proteins. We describe the first fluorescent approach for in vivo detection of 2Fe2S clusters that is based upon the complementation of Venus fluorescent protein fragments via human glutaredoxin 2 (GRX2) coordination of a 2Fe2S cluster. We show that Escherichia coli and mammalian cells expressing Venus fragments fused to GRX2 exhibit greater fluorescence than cells expressing fragments fused to a C37A mutant that cannot coordinate a metallocluster. In addition, we find that maximal fluorescence in the cytosol of mammalian cells requires the iron-sulfur cluster assembly proteins ISCU and NFS1. These findings provide evidence that glutaredoxins can dimerize within mammalian cells through coordination of a 2Fe2S cluster as observed with purified recombinant proteins.</AbstractText>
<CopyrightInformation>Copyright 2009 Elsevier Ltd. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hoff</LastName>
<ForeName>Kevin G</ForeName>
<Initials>KG</Initials>
<AffiliationInfo><Affiliation>Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E California Boulevard, Mail Code 210-41, Pasadena, CA 91125, USA. khoff@caltech.edu</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Culler</LastName>
<ForeName>Stephanie J</ForeName>
<Initials>SJ</Initials>
</Author>
<Author ValidYN="Y"><LastName>Nguyen</LastName>
<ForeName>Peter Q</ForeName>
<Initials>PQ</Initials>
</Author>
<Author ValidYN="Y"><LastName>McGuire</LastName>
<ForeName>Ryan M</ForeName>
<Initials>RM</Initials>
</Author>
<Author ValidYN="Y"><LastName>Silberg</LastName>
<ForeName>Jonathan J</ForeName>
<Initials>JJ</Initials>
</Author>
<Author ValidYN="Y"><LastName>Smolke</LastName>
<ForeName>Christina D</ForeName>
<Initials>CD</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>F32 GM078901</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>T32 GM008362</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>2T32-GM008362</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>5F32GM078901</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Chem Biol</MedlineTA>
<NlmUniqueID>9500160</NlmUniqueID>
<ISSNLinking>1074-5521</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C516008">GLRX2 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008164">Luminescent Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>70FD1KFU70</RegistryNumber>
<NameOfSubstance UI="D013455">Sulfur</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>E1UOL152H7</RegistryNumber>
<NameOfSubstance UI="D007501">Iron</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Chem Biol. 2009 Dec 24;16(12):1213-4</RefSource>
<PMID Version="1">20064428</PMID>
</CommentsCorrections>
</CommentsCorrectionsList>
<MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008164" MajorTopicYN="N">Luminescent Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008856" MajorTopicYN="N">Microscopy, Fluorescence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D034622" MajorTopicYN="N">RNA Interference</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013455" MajorTopicYN="N">Sulfur</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year>
<Month>09</Month>
<Day>09</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2009</Year>
<Month>10</Month>
<Day>28</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2009</Year>
<Month>11</Month>
<Day>02</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2010</Year>
<Month>1</Month>
<Day>13</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2010</Year>
<Month>1</Month>
<Day>13</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2010</Year>
<Month>3</Month>
<Day>12</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">20064440</ArticleId>
<ArticleId IdType="pii">S1074-5521(09)00402-5</ArticleId>
<ArticleId IdType="doi">10.1016/j.chembiol.2009.11.011</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Californie</li>
</region>
</list>
<tree><noCountry><name sortKey="Culler, Stephanie J" sort="Culler, Stephanie J" uniqKey="Culler S" first="Stephanie J" last="Culler">Stephanie J. Culler</name>
<name sortKey="Mcguire, Ryan M" sort="Mcguire, Ryan M" uniqKey="Mcguire R" first="Ryan M" last="Mcguire">Ryan M. Mcguire</name>
<name sortKey="Nguyen, Peter Q" sort="Nguyen, Peter Q" uniqKey="Nguyen P" first="Peter Q" last="Nguyen">Peter Q. Nguyen</name>
<name sortKey="Silberg, Jonathan J" sort="Silberg, Jonathan J" uniqKey="Silberg J" first="Jonathan J" last="Silberg">Jonathan J. Silberg</name>
<name sortKey="Smolke, Christina D" sort="Smolke, Christina D" uniqKey="Smolke C" first="Christina D" last="Smolke">Christina D. Smolke</name>
</noCountry>
<country name="États-Unis"><region name="Californie"><name sortKey="Hoff, Kevin G" sort="Hoff, Kevin G" uniqKey="Hoff K" first="Kevin G" last="Hoff">Kevin G. Hoff</name>
</region>
</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 000B14 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000B14 | 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:20064440
   |texte=   In vivo fluorescent detection of Fe-S clusters coordinated by human GRX2.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:20064440" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a GlutaredoxinV1

This area was generated with Dilib version V0.6.37.
Data generation: Wed Nov 18 15:13:42 2020. Site generation: Wed Nov 18 15:16:12 2020

	Serveur d'exploration sur la glutarédoxine
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur la glutarédoxine

In vivo fluorescent detection of Fe-S clusters coordinated by human GRX2.

In vivo fluorescent detection of Fe-S clusters coordinated by human GRX2.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki