PoplarV1, Main, Exploration, bibRecord, 003E63

Ascorbate peroxidase-thioredoxin interaction.

Identifieur interne : 003E63 ( Main/Exploration ); précédent : 003E62; suivant : 003E64

Ascorbate peroxidase-thioredoxin interaction.

Auteurs : Eric Gelhaye [France] ; Nicolas Navrot ; Isabel K. Macdonald ; Nicolas Rouhier ; Emma Lloyd Raven ; Jean-Pierre Jacquot

Source :

Photosynthesis research [ 0166-8595 ] ; 2006.

RBID : pubmed:17031543

Descripteurs français

KwdFr :
- Arabidopsis (enzymologie), Ascorbate peroxidases (MeSH), Consommation d'oxygène (MeSH), Dithiothréitol (métabolisme), Fluorescence (MeSH), Glutathion (métabolisme), Peroxidases (métabolisme), Pois (enzymologie), Thioredoxin-disulfide reductase (génétique), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (métabolisme).
MESH :
- enzymologie : Arabidopsis, Pois.
- génétique : Thioredoxin-disulfide reductase.
- métabolisme : Dithiothréitol, Glutathion, Peroxidases, Thioredoxin-disulfide reductase, Thiorédoxines.
- Ascorbate peroxidases, Consommation d'oxygène, Fluorescence.

English descriptors

KwdEn :
- Arabidopsis (enzymology), Ascorbate Peroxidases (MeSH), Dithiothreitol (metabolism), Fluorescence (MeSH), Glutathione (metabolism), Oxygen Consumption (MeSH), Peas (enzymology), Peroxidases (metabolism), Thioredoxin-Disulfide Reductase (genetics), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (metabolism).
MESH :
- chemical , genetics : Thioredoxin-Disulfide Reductase.
- chemical , metabolism : Dithiothreitol, Glutathione, Peroxidases, Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical : Ascorbate Peroxidases.
- enzymology : Arabidopsis, Peas.
- Fluorescence, Oxygen Consumption.

Abstract

Proteomics data have suggested ascorbate peroxidase (APX) to be a potential thioredoxin-interacting protein. Using recombinant enzymes, we observed that incubation of pea cytosolic APX with reduced poplar thioredoxins h drastically inactivated the peroxidase. A similar inactivation is induced by reduced glutathione and dithiothreitol, whereas diamide and oxidized glutathione have no effect. Oxygen consumption measurements, modifications of the APX visible spectrum and protection by hydrogen peroxide scavenging enzymes suggest that APX oxidizes thiols leading to the generation of thiyl radicals. These radicals can in turn react with thiyl anions to produce the disulfide radical anions, which are responsible for oxygen reduction and subsequent hydrogen peroxide production. The APX inactivation is not due solely to hydrogen peroxide since fluorimetry indicates that the environment of the APX tryptophan residues is dramatically modified only in the presence of thiol groups. The physiological implications of this interaction are discussed.

DOI: 10.1007/s11120-006-9100-x
PubMed: 17031543

Affiliations:

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

to stream Main, to step Corpus: 003D11
to stream Main, to step Curation: 003D11

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Ascorbate peroxidase-thioredoxin interaction.</title>
<author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name>
<affiliation wicri:level="4"><nlm:affiliation>Unité Mixte de Recherches 1136 INRA UHP (Interaction Arbres Microorganismes), IFR 110 Génomique Ecophysiologie et Ecologie Fonctionnelles, Faculté des Sciences, Nancy Université, BP 239, 54506, Vandoeuvre-lès-Nancy Cedex, France. gelhaye@lcb.uhp-nancy.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Unité Mixte de Recherches 1136 INRA UHP (Interaction Arbres Microorganismes), IFR 110 Génomique Ecophysiologie et Ecologie Fonctionnelles, Faculté des Sciences, Nancy Université, BP 239, 54506, Vandoeuvre-lès-Nancy Cedex</wicri:regionArea>
<placeName><region type="region" nuts="2">Grand Est</region>
<region type="old region" nuts="2">Lorraine (région)</region>
<settlement type="city">Vandœuvre-lès-Nancy</settlement>
</placeName>
<orgName type="university">Nancy-Université</orgName>
</affiliation>
</author>
<author><name sortKey="Navrot, Nicolas" sort="Navrot, Nicolas" uniqKey="Navrot N" first="Nicolas" last="Navrot">Nicolas Navrot</name>
</author>
<author><name sortKey="Macdonald, Isabel K" sort="Macdonald, Isabel K" uniqKey="Macdonald I" first="Isabel K" last="Macdonald">Isabel K. Macdonald</name>
</author>
<author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name>
</author>
<author><name sortKey="Raven, Emma Lloyd" sort="Raven, Emma Lloyd" uniqKey="Raven E" first="Emma Lloyd" last="Raven">Emma Lloyd Raven</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="2006">2006</date>
<idno type="RBID">pubmed:17031543</idno>
<idno type="pmid">17031543</idno>
<idno type="doi">10.1007/s11120-006-9100-x</idno>
<idno type="wicri:Area/Main/Corpus">003D11</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003D11</idno>
<idno type="wicri:Area/Main/Curation">003D11</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">003D11</idno>
<idno type="wicri:Area/Main/Exploration">003D11</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Ascorbate peroxidase-thioredoxin interaction.</title>
<author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name>
<affiliation wicri:level="4"><nlm:affiliation>Unité Mixte de Recherches 1136 INRA UHP (Interaction Arbres Microorganismes), IFR 110 Génomique Ecophysiologie et Ecologie Fonctionnelles, Faculté des Sciences, Nancy Université, BP 239, 54506, Vandoeuvre-lès-Nancy Cedex, France. gelhaye@lcb.uhp-nancy.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Unité Mixte de Recherches 1136 INRA UHP (Interaction Arbres Microorganismes), IFR 110 Génomique Ecophysiologie et Ecologie Fonctionnelles, Faculté des Sciences, Nancy Université, BP 239, 54506, Vandoeuvre-lès-Nancy Cedex</wicri:regionArea>
<placeName><region type="region" nuts="2">Grand Est</region>
<region type="old region" nuts="2">Lorraine (région)</region>
<settlement type="city">Vandœuvre-lès-Nancy</settlement>
</placeName>
<orgName type="university">Nancy-Université</orgName>
</affiliation>
</author>
<author><name sortKey="Navrot, Nicolas" sort="Navrot, Nicolas" uniqKey="Navrot N" first="Nicolas" last="Navrot">Nicolas Navrot</name>
</author>
<author><name sortKey="Macdonald, Isabel K" sort="Macdonald, Isabel K" uniqKey="Macdonald I" first="Isabel K" last="Macdonald">Isabel K. Macdonald</name>
</author>
<author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name>
</author>
<author><name sortKey="Raven, Emma Lloyd" sort="Raven, Emma Lloyd" uniqKey="Raven E" first="Emma Lloyd" last="Raven">Emma Lloyd Raven</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">Photosynthesis research</title>
<idno type="ISSN">0166-8595</idno>
<imprint><date when="2006" type="published">2006</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arabidopsis (enzymology)</term>
<term>Ascorbate Peroxidases (MeSH)</term>
<term>Dithiothreitol (metabolism)</term>
<term>Fluorescence (MeSH)</term>
<term>Glutathione (metabolism)</term>
<term>Oxygen Consumption (MeSH)</term>
<term>Peas (enzymology)</term>
<term>Peroxidases (metabolism)</term>
<term>Thioredoxin-Disulfide Reductase (genetics)</term>
<term>Thioredoxin-Disulfide Reductase (metabolism)</term>
<term>Thioredoxins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Arabidopsis (enzymologie)</term>
<term>Ascorbate peroxidases (MeSH)</term>
<term>Consommation d'oxygène (MeSH)</term>
<term>Dithiothréitol (métabolisme)</term>
<term>Fluorescence (MeSH)</term>
<term>Glutathion (métabolisme)</term>
<term>Peroxidases (métabolisme)</term>
<term>Pois (enzymologie)</term>
<term>Thioredoxin-disulfide reductase (génétique)</term>
<term>Thioredoxin-disulfide reductase (métabolisme)</term>
<term>Thiorédoxines (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Thioredoxin-Disulfide Reductase</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Dithiothreitol</term>
<term>Glutathione</term>
<term>Peroxidases</term>
<term>Thioredoxin-Disulfide Reductase</term>
<term>Thioredoxins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Ascorbate Peroxidases</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term>
<term>Pois</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arabidopsis</term>
<term>Peas</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Thioredoxin-disulfide reductase</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Dithiothréitol</term>
<term>Glutathion</term>
<term>Peroxidases</term>
<term>Thioredoxin-disulfide reductase</term>
<term>Thiorédoxines</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Fluorescence</term>
<term>Oxygen Consumption</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Ascorbate peroxidases</term>
<term>Consommation d'oxygène</term>
<term>Fluorescence</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Proteomics data have suggested ascorbate peroxidase (APX) to be a potential thioredoxin-interacting protein. Using recombinant enzymes, we observed that incubation of pea cytosolic APX with reduced poplar thioredoxins h drastically inactivated the peroxidase. A similar inactivation is induced by reduced glutathione and dithiothreitol, whereas diamide and oxidized glutathione have no effect. Oxygen consumption measurements, modifications of the APX visible spectrum and protection by hydrogen peroxide scavenging enzymes suggest that APX oxidizes thiols leading to the generation of thiyl radicals. These radicals can in turn react with thiyl anions to produce the disulfide radical anions, which are responsible for oxygen reduction and subsequent hydrogen peroxide production. The APX inactivation is not due solely to hydrogen peroxide since fluorimetry indicates that the environment of the APX tryptophan residues is dramatically modified only in the presence of thiol groups. The physiological implications of this interaction are discussed.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17031543</PMID>
<DateCompleted><Year>2007</Year>
<Month>03</Month>
<Day>28</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>09</Month>
<Day>30</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0166-8595</ISSN>
<JournalIssue CitedMedium="Print"><Volume>89</Volume>
<Issue>2-3</Issue>
<PubDate><Year>2006</Year>
<Month>Sep</Month>
</PubDate>
</JournalIssue>
<Title>Photosynthesis research</Title>
<ISOAbbreviation>Photosynth Res</ISOAbbreviation>
</Journal>
<ArticleTitle>Ascorbate peroxidase-thioredoxin interaction.</ArticleTitle>
<Pagination><MedlinePgn>193-200</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Proteomics data have suggested ascorbate peroxidase (APX) to be a potential thioredoxin-interacting protein. Using recombinant enzymes, we observed that incubation of pea cytosolic APX with reduced poplar thioredoxins h drastically inactivated the peroxidase. A similar inactivation is induced by reduced glutathione and dithiothreitol, whereas diamide and oxidized glutathione have no effect. Oxygen consumption measurements, modifications of the APX visible spectrum and protection by hydrogen peroxide scavenging enzymes suggest that APX oxidizes thiols leading to the generation of thiyl radicals. These radicals can in turn react with thiyl anions to produce the disulfide radical anions, which are responsible for oxygen reduction and subsequent hydrogen peroxide production. The APX inactivation is not due solely to hydrogen peroxide since fluorimetry indicates that the environment of the APX tryptophan residues is dramatically modified only in the presence of thiol groups. The physiological implications of this interaction are discussed.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gelhaye</LastName>
<ForeName>Eric</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Unité Mixte de Recherches 1136 INRA UHP (Interaction Arbres Microorganismes), IFR 110 Génomique Ecophysiologie et Ecologie Fonctionnelles, Faculté des Sciences, Nancy Université, BP 239, 54506, Vandoeuvre-lès-Nancy Cedex, France. gelhaye@lcb.uhp-nancy.fr</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Navrot</LastName>
<ForeName>Nicolas</ForeName>
<Initials>N</Initials>
</Author>
<Author ValidYN="Y"><LastName>Macdonald</LastName>
<ForeName>Isabel K</ForeName>
<Initials>IK</Initials>
</Author>
<Author ValidYN="Y"><LastName>Rouhier</LastName>
<ForeName>Nicolas</ForeName>
<Initials>N</Initials>
</Author>
<Author ValidYN="Y"><LastName>Raven</LastName>
<ForeName>Emma Lloyd</ForeName>
<Initials>EL</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>B19083</GrantID>
<Agency>Biotechnology and Biological Sciences Research Council</Agency>
<Country>United Kingdom</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2006</Year>
<Month>09</Month>
<Day>22</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Netherlands</Country>
<MedlineTA>Photosynth Res</MedlineTA>
<NlmUniqueID>100954728</NlmUniqueID>
<ISSNLinking>0166-8595</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>52500-60-4</RegistryNumber>
<NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber>
<NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.11.1.11</RegistryNumber>
<NameOfSubstance UI="D060387">Ascorbate Peroxidases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber>
<NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber>
<NameOfSubstance UI="D005978">Glutathione</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>T8ID5YZU6Y</RegistryNumber>
<NameOfSubstance UI="D004229">Dithiothreitol</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D060387" MajorTopicYN="N">Ascorbate Peroxidases</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004229" MajorTopicYN="N">Dithiothreitol</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005453" MajorTopicYN="N">Fluorescence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010101" MajorTopicYN="N">Oxygen Consumption</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018532" MajorTopicYN="N">Peas</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year>
<Month>06</Month>
<Day>12</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2006</Year>
<Month>08</Month>
<Day>21</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2006</Year>
<Month>10</Month>
<Day>13</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2007</Year>
<Month>3</Month>
<Day>29</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2006</Year>
<Month>10</Month>
<Day>13</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">17031543</ArticleId>
<ArticleId IdType="doi">10.1007/s11120-006-9100-x</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Plant Cell Physiol. 2004 Jan;45(1):18-27</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14749482</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Exp Bot. 2002 May;53(372):1351-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11997381</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Arch Biochem Biophys. 1988 Nov 1;266(2):496-507</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3190242</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1995 Apr 11;34(14):4765-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7718583</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 2005 Jan;17(1):268-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15608336</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 2005 Jan 3;168(1):17-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15631987</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2003 Jan 7;100(1):370-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12509500</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 1997 Jul 14;411(2-3):269-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9271219</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Biol. 2003 Apr;10(4):303-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12640445</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Exp Bot. 2002 May;53(372):1305-19</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11997377</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Phytochemistry. 2004 Jun;65(11):1629-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15276458</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proteomics. 2004 Sep;4(9):2696-706</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15352244</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 2003 Dec 18;555(3):443-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14675753</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Feb 24;101(8):2642-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14983062</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 2001 Nov;127(3):1299-309</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11706208</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2004 Jul 13;43(27):8644-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15236572</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Plant Sci. 2003 Jul;8(7):335-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12878018</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Mol Life Sci. 2005 Jan;62(1):24-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15619004</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Oct 5;101(40):14545-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15385674</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Plant Biol. 2005;56:187-220</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15862094</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):14144-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11717467</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1999 Apr 23;284(5414):654-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10213690</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol Biochem. 2004 Apr;42(4):265-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15120110</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Mar 26;279(13):13272-83</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14724284</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1994 Jan 28;235(4):1357-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8308900</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2003 Nov 21;278(47):46869-77</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12954611</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Am Chem Soc. 2004 Dec 15;126(49):16242-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15584761</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Biochem. 2001 May;268(10):3091-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11358529</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2002 Nov 19;41(46):13774-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12427040</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1998 Dec 15;37(50):17610-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9860877</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Physiol Plant. 2002 Feb;114(2):165-171</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11903963</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 2002;347:394-402</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11898430</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 2000 Jun 1;348 Pt 2:321-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10816425</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 2002 Jun;129(2):838-53</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12068123</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2005 Jul-Aug;7(7-8):919-29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15998247</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>France</li>
</country>
<region><li>Grand Est</li>
<li>Lorraine (région)</li>
</region>
<settlement><li>Vandœuvre-lès-Nancy</li>
</settlement>
<orgName><li>Nancy-Université</li>
</orgName>
</list>
<tree><noCountry><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name>
<name sortKey="Macdonald, Isabel K" sort="Macdonald, Isabel K" uniqKey="Macdonald I" first="Isabel K" last="Macdonald">Isabel K. Macdonald</name>
<name sortKey="Navrot, Nicolas" sort="Navrot, Nicolas" uniqKey="Navrot N" first="Nicolas" last="Navrot">Nicolas Navrot</name>
<name sortKey="Raven, Emma Lloyd" sort="Raven, Emma Lloyd" uniqKey="Raven E" first="Emma Lloyd" last="Raven">Emma Lloyd Raven</name>
<name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name>
</noCountry>
<country name="France"><region name="Grand Est"><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name>
</region>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PoplarV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003E63 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 003E63 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    PoplarV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:17031543
   |texte=   Ascorbate peroxidase-thioredoxin interaction.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:17031543" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a PoplarV1

This area was generated with Dilib version V0.6.37.
Data generation: Wed Nov 18 12:07:19 2020. Site generation: Wed Nov 18 12:16:31 2020

	Serveur d'exploration sur le peuplier
	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 le peuplier

Ascorbate peroxidase-thioredoxin interaction.

Ascorbate peroxidase-thioredoxin interaction.

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