Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductase.
Identifieur interne : 000D94 ( Main/Exploration ); précédent : 000D93; suivant : 000D95Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductase.
Auteurs : Qi-An Sun [États-Unis] ; Dan Su ; Sergey V. Novoselov ; Bradley A. Carlson ; Dolph L. Hatfield ; Vadim N. GladyshevSource :
- Biochemistry [ 0006-2960 ] ; 2005.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Complexes multienzymatiques (composition chimique), Complexes multienzymatiques (génétique), Complexes multienzymatiques (métabolisme), Conformation des protéines (MeSH), Distribution tissulaire (MeSH), Glutarédoxines (MeSH), Humains (MeSH), Modèles moléculaires (MeSH), NADH, NADPH oxidoreductases (composition chimique), NADH, NADPH oxidoreductases (génétique), NADH, NADPH oxidoreductases (métabolisme), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Rats (MeSH), Souris (MeSH), Sélénium (métabolisme), Thiorédoxines (composition chimique), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Complexes multienzymatiques, NADH, NADPH oxidoreductases, Oxidoreductases, Protéines recombinantes, Thiorédoxines.
- génétique : Complexes multienzymatiques, NADH, NADPH oxidoreductases, Protéines recombinantes.
- métabolisme : Complexes multienzymatiques, NADH, NADPH oxidoreductases, Oxidoreductases, Protéines recombinantes, Sélénium, Thiorédoxines.
- Animaux, Conformation des protéines, Distribution tissulaire, Glutarédoxines, Humains, Modèles moléculaires, Oxydoréduction, Rats, Souris.
English descriptors
- KwdEn :
- Animals (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Mice (MeSH), Models, Molecular (MeSH), Multienzyme Complexes (chemistry), Multienzyme Complexes (genetics), Multienzyme Complexes (metabolism), NADH, NADPH Oxidoreductases (chemistry), NADH, NADPH Oxidoreductases (genetics), NADH, NADPH Oxidoreductases (metabolism), Oxidation-Reduction (MeSH), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Protein Conformation (MeSH), Rats (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Selenium (metabolism), Thioredoxins (chemistry), Thioredoxins (metabolism), Tissue Distribution (MeSH).
- MESH :
- chemical , chemistry : Multienzyme Complexes, NADH, NADPH Oxidoreductases, Oxidoreductases, Recombinant Proteins, Thioredoxins.
- chemical , genetics : Multienzyme Complexes, NADH, NADPH Oxidoreductases, Recombinant Proteins.
- chemical , metabolism : Multienzyme Complexes, NADH, NADPH Oxidoreductases, Oxidoreductases, Recombinant Proteins, Selenium, Thioredoxins.
- chemical : Glutaredoxins.
- Animals, Humans, Mice, Models, Molecular, Oxidation-Reduction, Protein Conformation, Rats, Tissue Distribution.
Abstract
Thioredoxin/glutathione reductase (TGR) is a recently discovered member of the selenoprotein thioredoxin reductase family in mammals. In contrast to two other mammalian thioredoxin reductases, it contains an N-terminal glutaredoxin domain and exhibits a wide spectrum of enzyme activities. To elucidate the reaction mechanism and regulation of TGR, we prepared a recombinant mouse TGR in the selenoprotein form as well as various mutants and individual domains of this enzyme. Using these proteins, we showed that the glutaredoxin and thioredoxin reductase domains of TGR could independently catalyze reactions normally associated with each domain. The glutaredoxin domain is a monothiol glutaredoxin containing a CxxS motif at the active site, which could receive electrons from either the thioredoxin reductase domain of TGR or thioredoxin reductase 1. We also found that the C-terminal penultimate selenocysteine was required for transfer of reducing equivalents from the thiol/disulfide active site of TGR to the glutaredoxin domain. Thus, the physiologically relevant NADPH-dependent activities of TGR were dependent on this residue. In addition, we examined the effects of selenium levels in the diet and perturbations in selenocysteine tRNA function on TGR biosynthesis and found that expression of this protein was regulated by both selenium and tRNA status in liver, but was more resistant to this regulation in testes.
DOI: 10.1021/bi051321w
PubMed: 16262253
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductase.</title><author><name sortKey="Sun, Qi An" sort="Sun, Qi An" uniqKey="Sun Q" first="Qi-An" last="Sun">Qi-An Sun</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588-0664, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588-0664</wicri:regionArea><wicri:noRegion>Nebraska 68588-0664</wicri:noRegion></affiliation></author><author><name sortKey="Su, Dan" sort="Su, Dan" uniqKey="Su D" first="Dan" last="Su">Dan Su</name></author><author><name sortKey="Novoselov, Sergey V" sort="Novoselov, Sergey V" uniqKey="Novoselov S" first="Sergey V" last="Novoselov">Sergey V. Novoselov</name></author><author><name sortKey="Carlson, Bradley A" sort="Carlson, Bradley A" uniqKey="Carlson B" first="Bradley A" last="Carlson">Bradley A. Carlson</name></author><author><name sortKey="Hatfield, Dolph L" sort="Hatfield, Dolph L" uniqKey="Hatfield D" first="Dolph L" last="Hatfield">Dolph L. Hatfield</name></author><author><name sortKey="Gladyshev, Vadim N" sort="Gladyshev, Vadim N" uniqKey="Gladyshev V" first="Vadim N" last="Gladyshev">Vadim N. Gladyshev</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:16262253</idno><idno type="pmid">16262253</idno><idno type="doi">10.1021/bi051321w</idno><idno type="wicri:Area/Main/Corpus">000D77</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D77</idno><idno type="wicri:Area/Main/Curation">000D77</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D77</idno><idno type="wicri:Area/Main/Exploration">000D77</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductase.</title><author><name sortKey="Sun, Qi An" sort="Sun, Qi An" uniqKey="Sun Q" first="Qi-An" last="Sun">Qi-An Sun</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588-0664, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588-0664</wicri:regionArea><wicri:noRegion>Nebraska 68588-0664</wicri:noRegion></affiliation></author><author><name sortKey="Su, Dan" sort="Su, Dan" uniqKey="Su D" first="Dan" last="Su">Dan Su</name></author><author><name sortKey="Novoselov, Sergey V" sort="Novoselov, Sergey V" uniqKey="Novoselov S" first="Sergey V" last="Novoselov">Sergey V. Novoselov</name></author><author><name sortKey="Carlson, Bradley A" sort="Carlson, Bradley A" uniqKey="Carlson B" first="Bradley A" last="Carlson">Bradley A. Carlson</name></author><author><name sortKey="Hatfield, Dolph L" sort="Hatfield, Dolph L" uniqKey="Hatfield D" first="Dolph L" last="Hatfield">Dolph L. Hatfield</name></author><author><name sortKey="Gladyshev, Vadim N" sort="Gladyshev, Vadim N" uniqKey="Gladyshev V" first="Vadim N" last="Gladyshev">Vadim N. Gladyshev</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Humans (MeSH)</term><term>Mice (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Multienzyme Complexes (chemistry)</term><term>Multienzyme Complexes (genetics)</term><term>Multienzyme Complexes (metabolism)</term><term>NADH, NADPH Oxidoreductases (chemistry)</term><term>NADH, NADPH Oxidoreductases (genetics)</term><term>NADH, NADPH Oxidoreductases (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (chemistry)</term><term>Oxidoreductases (metabolism)</term><term>Protein Conformation (MeSH)</term><term>Rats (MeSH)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Selenium (metabolism)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (metabolism)</term><term>Tissue Distribution (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Complexes multienzymatiques (composition chimique)</term><term>Complexes multienzymatiques (génétique)</term><term>Complexes multienzymatiques (métabolisme)</term><term>Conformation des protéines (MeSH)</term><term>Distribution tissulaire (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>NADH, NADPH oxidoreductases (composition chimique)</term><term>NADH, NADPH oxidoreductases (génétique)</term><term>NADH, NADPH oxidoreductases (métabolisme)</term><term>Oxidoreductases (composition chimique)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Rats (MeSH)</term><term>Souris (MeSH)</term><term>Sélénium (métabolisme)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term><term>Oxidoreductases</term><term>Recombinant Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term><term>Oxidoreductases</term><term>Recombinant Proteins</term><term>Selenium</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Complexes multienzymatiques</term><term>NADH, NADPH oxidoreductases</term><term>Oxidoreductases</term><term>Protéines recombinantes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Complexes multienzymatiques</term><term>NADH, NADPH oxidoreductases</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexes multienzymatiques</term><term>NADH, NADPH oxidoreductases</term><term>Oxidoreductases</term><term>Protéines recombinantes</term><term>Sélénium</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Mice</term><term>Models, Molecular</term><term>Oxidation-Reduction</term><term>Protein Conformation</term><term>Rats</term><term>Tissue Distribution</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Conformation des protéines</term><term>Distribution tissulaire</term><term>Glutarédoxines</term><term>Humains</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Rats</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thioredoxin/glutathione reductase (TGR) is a recently discovered member of the selenoprotein thioredoxin reductase family in mammals. In contrast to two other mammalian thioredoxin reductases, it contains an N-terminal glutaredoxin domain and exhibits a wide spectrum of enzyme activities. To elucidate the reaction mechanism and regulation of TGR, we prepared a recombinant mouse TGR in the selenoprotein form as well as various mutants and individual domains of this enzyme. Using these proteins, we showed that the glutaredoxin and thioredoxin reductase domains of TGR could independently catalyze reactions normally associated with each domain. The glutaredoxin domain is a monothiol glutaredoxin containing a CxxS motif at the active site, which could receive electrons from either the thioredoxin reductase domain of TGR or thioredoxin reductase 1. We also found that the C-terminal penultimate selenocysteine was required for transfer of reducing equivalents from the thiol/disulfide active site of TGR to the glutaredoxin domain. Thus, the physiologically relevant NADPH-dependent activities of TGR were dependent on this residue. In addition, we examined the effects of selenium levels in the diet and perturbations in selenocysteine tRNA function on TGR biosynthesis and found that expression of this protein was regulated by both selenium and tRNA status in liver, but was more resistant to this regulation in testes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16262253</PMID><DateCompleted><Year>2006</Year><Month>02</Month><Day>13</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>44</Volume><Issue>44</Issue><PubDate><Year>2005</Year><Month>Nov</Month><Day>08</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductase.</ArticleTitle><Pagination><MedlinePgn>14528-37</MedlinePgn></Pagination><Abstract><AbstractText>Thioredoxin/glutathione reductase (TGR) is a recently discovered member of the selenoprotein thioredoxin reductase family in mammals. In contrast to two other mammalian thioredoxin reductases, it contains an N-terminal glutaredoxin domain and exhibits a wide spectrum of enzyme activities. To elucidate the reaction mechanism and regulation of TGR, we prepared a recombinant mouse TGR in the selenoprotein form as well as various mutants and individual domains of this enzyme. Using these proteins, we showed that the glutaredoxin and thioredoxin reductase domains of TGR could independently catalyze reactions normally associated with each domain. The glutaredoxin domain is a monothiol glutaredoxin containing a CxxS motif at the active site, which could receive electrons from either the thioredoxin reductase domain of TGR or thioredoxin reductase 1. We also found that the C-terminal penultimate selenocysteine was required for transfer of reducing equivalents from the thiol/disulfide active site of TGR to the glutaredoxin domain. Thus, the physiologically relevant NADPH-dependent activities of TGR were dependent on this residue. In addition, we examined the effects of selenium levels in the diet and perturbations in selenocysteine tRNA function on TGR biosynthesis and found that expression of this protein was regulated by both selenium and tRNA status in liver, but was more resistant to this regulation in testes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Qi-An</ForeName><Initials>QA</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588-0664, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Su</LastName><ForeName>Dan</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Novoselov</LastName><ForeName>Sergey V</ForeName><Initials>SV</Initials></Author><Author ValidYN="Y"><LastName>Carlson</LastName><ForeName>Bradley A</ForeName><Initials>BA</Initials></Author><Author ValidYN="Y"><LastName>Hatfield</LastName><ForeName>Dolph L</ForeName><Initials>DL</Initials></Author><Author ValidYN="Y"><LastName>Gladyshev</LastName><ForeName>Vadim N</ForeName><Initials>VN</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM065204</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></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009097">Multienzyme Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.-</RegistryNumber><NameOfSubstance UI="D009247">NADH, NADPH Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.4.-</RegistryNumber><NameOfSubstance UI="C466433">thioredoxin glutathione reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>H6241UJ22B</RegistryNumber><NameOfSubstance UI="D012643">Selenium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009097" MajorTopicYN="N">Multienzyme Complexes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009247" MajorTopicYN="N">NADH, NADPH Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012643" MajorTopicYN="N">Selenium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014018" MajorTopicYN="N">Tissue Distribution</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>11</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>2</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>11</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16262253</ArticleId><ArticleId IdType="doi">10.1021/bi051321w</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Carlson, Bradley A" sort="Carlson, Bradley A" uniqKey="Carlson B" first="Bradley A" last="Carlson">Bradley A. Carlson</name><name sortKey="Gladyshev, Vadim N" sort="Gladyshev, Vadim N" uniqKey="Gladyshev V" first="Vadim N" last="Gladyshev">Vadim N. Gladyshev</name><name sortKey="Hatfield, Dolph L" sort="Hatfield, Dolph L" uniqKey="Hatfield D" first="Dolph L" last="Hatfield">Dolph L. Hatfield</name><name sortKey="Novoselov, Sergey V" sort="Novoselov, Sergey V" uniqKey="Novoselov S" first="Sergey V" last="Novoselov">Sergey V. Novoselov</name><name sortKey="Su, Dan" sort="Su, Dan" uniqKey="Su D" first="Dan" last="Su">Dan Su</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Sun, Qi An" sort="Sun, Qi An" uniqKey="Sun Q" first="Qi-An" last="Sun">Qi-An Sun</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 000D94 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000D94 | 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:16262253
|texte= Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductase.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:16262253" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |