Characterization of the redox properties of poplar glutaredoxin.
Identifieur interne : 000F48 ( Main/Exploration ); précédent : 000F47; suivant : 000F49Characterization of the redox properties of poplar glutaredoxin.
Auteurs : Nicolas Rouhier [France] ; Alexios Vlamis-Gardikas ; Christopher Horst Lillig ; Carsten Berndt ; Jens-Dirk Schwenn ; Arne Holmgren ; Jean-Pierre JacquotSource :
- Antioxidants & redox signaling [ 1523-0864 ] ; 2003.
Descripteurs français
- KwdFr :
- Cinétique (MeSH), Clonage moléculaire (MeSH), Cytidine diphosphate (métabolisme), Données de séquences moléculaires (MeSH), Escherichia coli (enzymologie), Escherichia coli (métabolisme), Glutarédoxines (MeSH), Modèles biologiques (MeSH), Ménadione (métabolisme), Oryza (métabolisme), Oxidoreductases (MeSH), Oxidoreductases acting on sulfur group donors (métabolisme), Oxydants (métabolisme), Oxydoréduction (MeSH), PAPS (composition chimique), Peroxidases (métabolisme), Peroxirédoxines (MeSH), Peroxyde d'hydrogène (métabolisme), Phylogenèse (MeSH), Populus (métabolisme), Protéines (composition chimique), Protéines (métabolisme), Protéines fongiques (métabolisme), Relation dose-effet des médicaments (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Électrons (MeSH).
- MESH :
- composition chimique : PAPS, Protéines.
- enzymologie : Escherichia coli.
- métabolisme : Cytidine diphosphate, Escherichia coli, Ménadione, Oryza, Oxidoreductases acting on sulfur group donors, Oxydants, Peroxidases, Peroxyde d'hydrogène, Populus, Protéines, Protéines fongiques.
- Cinétique, Clonage moléculaire, Données de séquences moléculaires, Glutarédoxines, Modèles biologiques, Oxidoreductases, Oxydoréduction, Peroxirédoxines, Phylogenèse, Relation dose-effet des médicaments, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Électrons.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Cloning, Molecular (MeSH), Cytidine Diphosphate (metabolism), Dose-Response Relationship, Drug (MeSH), Electrons (MeSH), Escherichia coli (enzymology), Escherichia coli (metabolism), Fungal Proteins (metabolism), Glutaredoxins (MeSH), Hydrogen Peroxide (metabolism), Kinetics (MeSH), Models, Biological (MeSH), Molecular Sequence Data (MeSH), Oryza (metabolism), Oxidants (metabolism), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Oxidoreductases Acting on Sulfur Group Donors (metabolism), Peroxidases (metabolism), Peroxiredoxins (MeSH), Phosphoadenosine Phosphosulfate (chemistry), Phylogeny (MeSH), Populus (metabolism), Proteins (chemistry), Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Vitamin K 3 (metabolism).
- MESH :
- chemical , chemistry : Phosphoadenosine Phosphosulfate, Proteins.
- chemical , metabolism : Cytidine Diphosphate, Fungal Proteins, Hydrogen Peroxide, Oxidants, Oxidoreductases Acting on Sulfur Group Donors, Peroxidases, Proteins, Vitamin K 3.
- enzymology : Escherichia coli.
- metabolism : Escherichia coli, Oryza, Populus.
- Amino Acid Sequence, Cloning, Molecular, Dose-Response Relationship, Drug, Electrons, Glutaredoxins, Kinetics, Models, Biological, Molecular Sequence Data, Oxidation-Reduction, Oxidoreductases, Peroxiredoxins, Phylogeny, Sequence Homology, Amino Acid.
Abstract
The presence of glutaredoxins in plants is now well recognized, but their functions and natural substrates remain largely unknown. Recently, a poplar glutaredoxin has been biochemically characterized and several mutants have been engineered in order to explore its reactivity. This work focuses on some physiological functions of the enzyme. According to our findings, the poplar glutaredoxin can serve as an electron donor to the bacterial 3'-phosphoadenylylsulfate reductase as it supports both the catalysis by the enzyme in vitro and complements a methionine auxotroph strain of Escherichia coli. In addition, poplar glutaredoxin is able to reduce the Escherichia coli ribonucleotide reductase 1a (in vitro reduction of cytidine diphosphate). Although this glutaredoxin is described as an electron donor to a phloem-located peroxiredoxin, whose function is to detoxify hydroperoxides, we found that it does not directly reduce hydrogen peroxide or other alkyl hydroperoxides as described for yeast and rice glutaredoxins. However, the poplar glutaredoxin may be involved in the response to oxidative stress as its overexpression in Escherichia coli resulted in a higher resistance toward hydrogen peroxide, menadione, and tert-butyl hydroperoxide.
DOI: 10.1089/152308603321223504
PubMed: 12626113
Affiliations:
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Université Henri Poincaré, 54506 Vandoeuvre Cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Unité Mixte de Recherche 1136 IaM, INRA-UHP Nancy I. Université Henri Poincaré, 54506 Vandoeuvre Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Vandoeuvre</settlement></placeName><orgName type="university">Université Henri Poincaré</orgName></affiliation></author><author><name sortKey="Vlamis Gardikas, Alexios" sort="Vlamis Gardikas, Alexios" uniqKey="Vlamis Gardikas A" first="Alexios" last="Vlamis-Gardikas">Alexios Vlamis-Gardikas</name></author><author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name></author><author><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name></author><author><name sortKey="Schwenn, Jens Dirk" sort="Schwenn, Jens Dirk" uniqKey="Schwenn J" first="Jens-Dirk" last="Schwenn">Jens-Dirk Schwenn</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</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">Antioxidants & redox signaling</title><idno type="ISSN">1523-0864</idno><imprint><date when="2003" type="published">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Cytidine Diphosphate (metabolism)</term><term>Dose-Response Relationship, Drug (MeSH)</term><term>Electrons (MeSH)</term><term>Escherichia coli (enzymology)</term><term>Escherichia coli (metabolism)</term><term>Fungal Proteins (metabolism)</term><term>Glutaredoxins (MeSH)</term><term>Hydrogen Peroxide (metabolism)</term><term>Kinetics (MeSH)</term><term>Models, Biological (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oryza (metabolism)</term><term>Oxidants (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxidoreductases Acting on Sulfur Group Donors (metabolism)</term><term>Peroxidases (metabolism)</term><term>Peroxiredoxins (MeSH)</term><term>Phosphoadenosine Phosphosulfate (chemistry)</term><term>Phylogeny (MeSH)</term><term>Populus (metabolism)</term><term>Proteins (chemistry)</term><term>Proteins (metabolism)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Vitamin K 3 (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Cytidine diphosphate (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (enzymologie)</term><term>Escherichia coli (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Modèles biologiques (MeSH)</term><term>Ménadione (métabolisme)</term><term>Oryza (métabolisme)</term><term>Oxidoreductases (MeSH)</term><term>Oxidoreductases acting on sulfur group donors (métabolisme)</term><term>Oxydants (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>PAPS (composition chimique)</term><term>Peroxidases (métabolisme)</term><term>Peroxirédoxines (MeSH)</term><term>Peroxyde d'hydrogène (métabolisme)</term><term>Phylogenèse (MeSH)</term><term>Populus (métabolisme)</term><term>Protéines (composition chimique)</term><term>Protéines (métabolisme)</term><term>Protéines fongiques (métabolisme)</term><term>Relation dose-effet des médicaments (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Phosphoadenosine Phosphosulfate</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cytidine Diphosphate</term><term>Fungal Proteins</term><term>Hydrogen Peroxide</term><term>Oxidants</term><term>Oxidoreductases Acting on Sulfur Group Donors</term><term>Peroxidases</term><term>Proteins</term><term>Vitamin K 3</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>PAPS</term><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Oryza</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytidine diphosphate</term><term>Escherichia coli</term><term>Ménadione</term><term>Oryza</term><term>Oxidoreductases acting on sulfur group donors</term><term>Oxydants</term><term>Peroxidases</term><term>Peroxyde d'hydrogène</term><term>Populus</term><term>Protéines</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cloning, Molecular</term><term>Dose-Response Relationship, Drug</term><term>Electrons</term><term>Glutaredoxins</term><term>Kinetics</term><term>Models, Biological</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Oxidoreductases</term><term>Peroxiredoxins</term><term>Phylogeny</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Modèles biologiques</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Peroxirédoxines</term><term>Phylogenèse</term><term>Relation dose-effet des médicaments</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The presence of glutaredoxins in plants is now well recognized, but their functions and natural substrates remain largely unknown. Recently, a poplar glutaredoxin has been biochemically characterized and several mutants have been engineered in order to explore its reactivity. This work focuses on some physiological functions of the enzyme. According to our findings, the poplar glutaredoxin can serve as an electron donor to the bacterial 3'-phosphoadenylylsulfate reductase as it supports both the catalysis by the enzyme in vitro and complements a methionine auxotroph strain of Escherichia coli. In addition, poplar glutaredoxin is able to reduce the Escherichia coli ribonucleotide reductase 1a (in vitro reduction of cytidine diphosphate). Although this glutaredoxin is described as an electron donor to a phloem-located peroxiredoxin, whose function is to detoxify hydroperoxides, we found that it does not directly reduce hydrogen peroxide or other alkyl hydroperoxides as described for yeast and rice glutaredoxins. However, the poplar glutaredoxin may be involved in the response to oxidative stress as its overexpression in Escherichia coli resulted in a higher resistance toward hydrogen peroxide, menadione, and tert-butyl hydroperoxide.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12626113</PMID><DateCompleted><Year>2003</Year><Month>11</Month><Day>28</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1523-0864</ISSN><JournalIssue CitedMedium="Print"><Volume>5</Volume><Issue>1</Issue><PubDate><Year>2003</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Characterization of the redox properties of poplar glutaredoxin.</ArticleTitle><Pagination><MedlinePgn>15-22</MedlinePgn></Pagination><Abstract><AbstractText>The presence of glutaredoxins in plants is now well recognized, but their functions and natural substrates remain largely unknown. Recently, a poplar glutaredoxin has been biochemically characterized and several mutants have been engineered in order to explore its reactivity. This work focuses on some physiological functions of the enzyme. According to our findings, the poplar glutaredoxin can serve as an electron donor to the bacterial 3'-phosphoadenylylsulfate reductase as it supports both the catalysis by the enzyme in vitro and complements a methionine auxotroph strain of Escherichia coli. In addition, poplar glutaredoxin is able to reduce the Escherichia coli ribonucleotide reductase 1a (in vitro reduction of cytidine diphosphate). Although this glutaredoxin is described as an electron donor to a phloem-located peroxiredoxin, whose function is to detoxify hydroperoxides, we found that it does not directly reduce hydrogen peroxide or other alkyl hydroperoxides as described for yeast and rice glutaredoxins. However, the poplar glutaredoxin may be involved in the response to oxidative stress as its overexpression in Escherichia coli resulted in a higher resistance toward hydrogen peroxide, menadione, and tert-butyl hydroperoxide.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Unité Mixte de Recherche 1136 IaM, INRA-UHP Nancy I. Université Henri Poincaré, 54506 Vandoeuvre Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vlamis-Gardikas</LastName><ForeName>Alexios</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials></Author><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>Carsten</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Schwenn</LastName><ForeName>Jens-Dirk</ForeName><Initials>JD</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>Arne</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016877">Oxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>482-67-7</RegistryNumber><NameOfSubstance UI="D010724">Phosphoadenosine Phosphosulfate</NameOfSubstance></Chemical><Chemical><RegistryNumber>63-38-7</RegistryNumber><NameOfSubstance UI="D003565">Cytidine Diphosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>723JX6CXY5</RegistryNumber><NameOfSubstance UI="D024483">Vitamin K 3</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.-</RegistryNumber><NameOfSubstance UI="D050862">Oxidoreductases Acting on Sulfur Group Donors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.99.2</RegistryNumber><NameOfSubstance UI="C019618">adenylylsulfate reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003565" MajorTopicYN="N">Cytidine Diphosphate</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004583" MajorTopicYN="N">Electrons</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012275" MajorTopicYN="N">Oryza</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016877" MajorTopicYN="N">Oxidants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="Y">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050862" MajorTopicYN="N">Oxidoreductases Acting on Sulfur Group Donors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010724" MajorTopicYN="N">Phosphoadenosine Phosphosulfate</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D024483" MajorTopicYN="N">Vitamin K 3</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name><name sortKey="Schwenn, Jens Dirk" sort="Schwenn, Jens Dirk" uniqKey="Schwenn J" first="Jens-Dirk" last="Schwenn">Jens-Dirk Schwenn</name><name sortKey="Vlamis Gardikas, Alexios" sort="Vlamis Gardikas, Alexios" uniqKey="Vlamis Gardikas A" first="Alexios" last="Vlamis-Gardikas">Alexios Vlamis-Gardikas</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:12626113" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |