GlutaredoxinV1, Main, Exploration, bibRecord, 000A23

Glutaredoxins: roles in iron homeostasis.

Identifieur interne : 000A23 ( Main/Exploration ); précédent : 000A22; suivant : 000A24

Glutaredoxins: roles in iron homeostasis.

Auteurs : Nicolas Rouhier [France] ; Jérémy Couturier ; Michael K. Johnson ; Jean-Pierre Jacquot

Source :

Trends in biochemical sciences [ 0968-0004 ] ; 2010.

RBID : pubmed:19811920

Descripteurs français

KwdFr :
- Animaux (MeSH), Fer (métabolisme), Ferrosulfoprotéines (métabolisme), Glutarédoxines (métabolisme), Humains (MeSH), Hème (métabolisme), Plantes (métabolisme).
MESH :
- métabolisme : Fer, Ferrosulfoprotéines, Glutarédoxines, Hème, Plantes.
- Animaux, Humains.

English descriptors

KwdEn :
- Animals (MeSH), Glutaredoxins (metabolism), Heme (metabolism), Humans (MeSH), Iron (metabolism), Iron-Sulfur Proteins (metabolism), Plants (metabolism).
MESH :
- chemical , metabolism : Glutaredoxins, Heme, Iron, Iron-Sulfur Proteins.
- metabolism : Plants.
- Animals, Humans.

Abstract

Glutaredoxins, proteins traditionally involved in redox reactions, are also required for iron-sulfur cluster assembly and haem biosynthesis. These new roles are probably related to the ability of some glutaredoxins to bind labile [2Fe-2S] clusters and to transfer them rapidly and efficiently to acceptor proteins. Recent results point to putative roles for glutaredoxins in the sensing of cellular iron and in iron-sulfur cluster biogenesis, either as scaffold proteins for the de novo synthesis of iron-sulfur clusters or as carrier proteins for the transfer of preformed iron-sulfur clusters. Based on prokaryote genome analysis and in vivo studies of iron regulation in yeast, we propose putative new roles and binding partners for glutaredoxins in the assembly of metalloproteins.

DOI: 10.1016/j.tibs.2009.08.005
PubMed: 19811920
PubMed Central: PMC2818164

Affiliations:

France

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

to stream Main, to step Corpus: 000A71
to stream Main, to step Curation: 000A71

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Glutaredoxins: roles in iron homeostasis.</title>
<author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name>
<affiliation wicri:level="1"><nlm:affiliation>Unité Mixte de Recherches 1136 INRA Nancy University, Interactions Arbres Microorganismes, IFR 110 EFABA, Faculté des Sciences, Vandoeuvre Cedex, France. nrouhier@scbiol.uhp-nancy.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Unité Mixte de Recherches 1136 INRA Nancy University, Interactions Arbres Microorganismes, IFR 110 EFABA, Faculté des Sciences, Vandoeuvre Cedex</wicri:regionArea>
<wicri:noRegion>Vandoeuvre Cedex</wicri:noRegion>
<wicri:noRegion>Vandoeuvre Cedex</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name>
</author>
<author><name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name>
</author>
<author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2010">2010</date>
<idno type="RBID">pubmed:19811920</idno>
<idno type="pmid">19811920</idno>
<idno type="doi">10.1016/j.tibs.2009.08.005</idno>
<idno type="pmc">PMC2818164</idno>
<idno type="wicri:Area/Main/Corpus">000A71</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000A71</idno>
<idno type="wicri:Area/Main/Curation">000A71</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000A71</idno>
<idno type="wicri:Area/Main/Exploration">000A71</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Glutaredoxins: roles in iron homeostasis.</title>
<author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name>
<affiliation wicri:level="1"><nlm:affiliation>Unité Mixte de Recherches 1136 INRA Nancy University, Interactions Arbres Microorganismes, IFR 110 EFABA, Faculté des Sciences, Vandoeuvre Cedex, France. nrouhier@scbiol.uhp-nancy.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Unité Mixte de Recherches 1136 INRA Nancy University, Interactions Arbres Microorganismes, IFR 110 EFABA, Faculté des Sciences, Vandoeuvre Cedex</wicri:regionArea>
<wicri:noRegion>Vandoeuvre Cedex</wicri:noRegion>
<wicri:noRegion>Vandoeuvre Cedex</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name>
</author>
<author><name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name>
</author>
<author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name>
</author>
</analytic>
<series><title level="j">Trends in biochemical sciences</title>
<idno type="ISSN">0968-0004</idno>
<imprint><date when="2010" type="published">2010</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Heme (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Iron (metabolism)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Plants (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Fer (métabolisme)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Hème (métabolisme)</term>
<term>Plantes (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Heme</term>
<term>Iron</term>
<term>Iron-Sulfur Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Plants</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fer</term>
<term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Hème</term>
<term>Plantes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Humans</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Humains</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Glutaredoxins, proteins traditionally involved in redox reactions, are also required for iron-sulfur cluster assembly and haem biosynthesis. These new roles are probably related to the ability of some glutaredoxins to bind labile [2Fe-2S] clusters and to transfer them rapidly and efficiently to acceptor proteins. Recent results point to putative roles for glutaredoxins in the sensing of cellular iron and in iron-sulfur cluster biogenesis, either as scaffold proteins for the de novo synthesis of iron-sulfur clusters or as carrier proteins for the transfer of preformed iron-sulfur clusters. Based on prokaryote genome analysis and in vivo studies of iron regulation in yeast, we propose putative new roles and binding partners for glutaredoxins in the assembly of metalloproteins.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19811920</PMID>
<DateCompleted><Year>2010</Year>
<Month>02</Month>
<Day>17</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0968-0004</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>35</Volume>
<Issue>1</Issue>
<PubDate><Year>2010</Year>
<Month>Jan</Month>
</PubDate>
</JournalIssue>
<Title>Trends in biochemical sciences</Title>
<ISOAbbreviation>Trends Biochem Sci</ISOAbbreviation>
</Journal>
<ArticleTitle>Glutaredoxins: roles in iron homeostasis.</ArticleTitle>
<Pagination><MedlinePgn>43-52</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.tibs.2009.08.005</ELocationID>
<Abstract><AbstractText>Glutaredoxins, proteins traditionally involved in redox reactions, are also required for iron-sulfur cluster assembly and haem biosynthesis. These new roles are probably related to the ability of some glutaredoxins to bind labile [2Fe-2S] clusters and to transfer them rapidly and efficiently to acceptor proteins. Recent results point to putative roles for glutaredoxins in the sensing of cellular iron and in iron-sulfur cluster biogenesis, either as scaffold proteins for the de novo synthesis of iron-sulfur clusters or as carrier proteins for the transfer of preformed iron-sulfur clusters. Based on prokaryote genome analysis and in vivo studies of iron regulation in yeast, we propose putative new roles and binding partners for glutaredoxins in the assembly of metalloproteins.</AbstractText>
<CopyrightInformation>Copyright 2009 Elsevier Ltd. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rouhier</LastName>
<ForeName>Nicolas</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Unité Mixte de Recherches 1136 INRA Nancy University, Interactions Arbres Microorganismes, IFR 110 EFABA, Faculté des Sciences, Vandoeuvre Cedex, France. nrouhier@scbiol.uhp-nancy.fr</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Couturier</LastName>
<ForeName>Jérémy</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Johnson</LastName>
<ForeName>Michael K</ForeName>
<Initials>MK</Initials>
</Author>
<Author ValidYN="Y"><LastName>Jacquot</LastName>
<ForeName>Jean-Pierre</ForeName>
<Initials>JP</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01 GM062524</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 GM062524-09</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R37 GM062524</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>GM62524</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>
<PublicationType UI="D016454">Review</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2009</Year>
<Month>10</Month>
<Day>05</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Trends Biochem Sci</MedlineTA>
<NlmUniqueID>7610674</NlmUniqueID>
<ISSNLinking>0968-0004</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber>
<NameOfSubstance UI="D006418">Heme</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>E1UOL152H7</RegistryNumber>
<NameOfSubstance UI="D007501">Iron</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<NumberOfReferences>64</NumberOfReferences>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year>
<Month>06</Month>
<Day>10</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2009</Year>
<Month>08</Month>
<Day>04</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2009</Year>
<Month>08</Month>
<Day>10</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2009</Year>
<Month>10</Month>
<Day>9</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2009</Year>
<Month>10</Month>
<Day>9</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2010</Year>
<Month>2</Month>
<Day>18</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">19811920</ArticleId>
<ArticleId IdType="pii">S0968-0004(09)00174-1</ArticleId>
<ArticleId IdType="doi">10.1016/j.tibs.2009.08.005</ArticleId>
<ArticleId IdType="pmc">PMC2818164</ArticleId>
<ArticleId IdType="mid">NIHMS146800</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Trends Biochem Sci. 1998 Sep;23(9):324-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9787636</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 2005 Jan 31;579(3):591-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15670813</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2009 Sep;11(9):2083-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19290777</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Plant Sci. 2009 Jun;14(6):336-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19446492</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Plant Sci. 2005 Jul;10(7):324-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15951221</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 2008;77:669-700</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18366324</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4569-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11283351</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2005 Feb 11;280(6):4713-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15545265</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Blood. 2007 Aug 15;110(4):1353-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17485548</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Plant Biol. 2008;59:143-66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18444899</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2009 Jan;37(Database issue):D412-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18940858</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2008 Oct 10;283(41):27785-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18669638</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2005 Jun 7;102(23):8168-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15917333</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Genet. 2008 Aug;24(8):398-407</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18606475</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2008 Mar;10(3):547-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18092940</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 2005;74:247-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15952888</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2005 Aug 18;436(7053):1035-39</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16110529</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1999 Jul 30;285(5428):751-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10427000</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biochem. 2008 Oct;317(1-2):61-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18548201</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1976 Jul;73(7):2275-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7783</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Microbiol. 2001;55:333-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11544359</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1997 Aug 1;277(5326):653-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9235882</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2008 Apr 9;27(7):1122-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18354500</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2007 May 4;282(18):13342-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17350958</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12870-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15317939</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2007 Nov 9;282(45):32640-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17848555</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2007 Oct 5;131(1):121-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17923092</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2002 Jan 10;415(6868):180-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11805837</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1999 Nov 4;402(6757):86-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10573422</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Plant Biol. 2006;57:623-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16669776</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Plant Sci. 2009 May;14(5):280-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19375375</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>New Phytol. 2008;180(2):391-407</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18513221</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Biol Cell. 2002 Apr;13(4):1109-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11950925</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Sci. 2006 Nov 1;119(Pt 21):4554-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17074835</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2007 Dec 25;46(51):15018-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18044966</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2000 Feb 10;403(6770):623-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10688190</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2007 May 1;104(18):7379-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17460036</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Microbiol. 2008;62:93-111</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18429691</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proteins. 2004 Nov 15;57(3):481-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15382238</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Mol Life Sci. 2007 Jun;64(12):1518-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17415523</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 2006 Apr 17;580(9):2273-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16566929</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2006 Feb 22;25(4):900-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16437155</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2008 Feb 5;47(5):1452-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18171082</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Soc Trans. 2008 Dec;36(Pt 6):1112-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19021507</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Exp Bot. 2006;57(8):1685-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16720602</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2006 Jul 4;45(26):7998-8008</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16800625</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Mol Life Sci. 2009 Aug;66(15):2539-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19506802</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>New Phytol. 2006;171(2):285-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16866936</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2009 Jul 7;48(26):6041-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19505088</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1999 Dec;19(12):8180-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10567543</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>BMC Evol Biol. 2009;9:66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19321008</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 2007 Jul 31;581(19):3598-607</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17659286</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2003 Sep 15;22(18):4815-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12970193</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2008 Apr 18;283(16):10276-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18281282</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2006 Jun 30;281(26):17661-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16648636</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Comp Funct Genomics. 2004;5(4):328-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18629168</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2007 Feb 2;282(5):3077-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17121859</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Inorg Chem. 2005 Nov;10(7):713-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16211402</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Plant Biol. 2009 Jun;12(3):347-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19481497</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2006 Jul;1763(7):723-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16839620</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2008 Apr 4;283(14):8868-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18216016</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2006 Sep 19;45(37):11087-95</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16964969</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2004 Feb;6(1):63-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14713336</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>France</li>
</country>
</list>
<tree><noCountry><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name>
<name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name>
<name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name>
</noCountry>
<country name="France"><noRegion><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name>
</noRegion>
</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 000A23 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000A23 | 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:19811920
   |texte=   Glutaredoxins: roles in iron homeostasis.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:19811920" \
       | 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

Glutaredoxins: roles in iron homeostasis.

Glutaredoxins: roles in iron homeostasis.

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