Identification of plant glutaredoxin targets.
Identifieur interne : 003F00 ( Main/Exploration ); précédent : 003E99; suivant : 003F01Identification of plant glutaredoxin targets.
Auteurs : Nicolas Rouhier [France] ; Arsenio Villarejo ; Manoj Srivastava ; Eric Gelhaye ; Olivier Keech ; Michel Droux ; Iris Finkemeier ; Göran Samuelsson ; Karl Josef Dietz ; Jean-Pierre Jacquot ; Gunnar WingsleSource :
- Antioxidants & redox signaling [ 1523-0864 ]
Descripteurs français
- KwdFr :
- Acide citrique (métabolisme), Adénosine triphosphate (métabolisme), Arabidopsis (enzymologie), Arabidopsis (métabolisme), Biosynthèse des protéines (MeSH), Chaperons moléculaires (métabolisme), Dioxyde de carbone (métabolisme), Glutarédoxines (MeSH), Oxidoreductases (métabolisme), Oxygène (métabolisme), Peroxidases (métabolisme), Peroxirédoxines (MeSH), Photochimie (MeSH), Polyosides (biosynthèse), Polyosides (métabolisme), Respiration cellulaire (effets des radiations), Soufre (métabolisme), Stress oxydatif (MeSH), Transport d'électrons (MeSH).
- MESH :
- biosynthèse : Polyosides.
- effets des radiations : Respiration cellulaire.
- enzymologie : Arabidopsis.
- métabolisme : Acide citrique, Adénosine triphosphate, Arabidopsis, Chaperons moléculaires, Dioxyde de carbone, Oxidoreductases, Oxygène, Peroxidases, Polyosides, Soufre.
- Biosynthèse des protéines, Glutarédoxines, Peroxirédoxines, Photochimie, Stress oxydatif, Transport d'électrons.
English descriptors
- KwdEn :
- Adenosine Triphosphate (metabolism), Arabidopsis (enzymology), Arabidopsis (metabolism), Carbon Dioxide (metabolism), Cell Respiration (radiation effects), Citric Acid (metabolism), Electron Transport (MeSH), Glutaredoxins (MeSH), Molecular Chaperones (metabolism), Oxidative Stress (MeSH), Oxidoreductases (metabolism), Oxygen (metabolism), Peroxidases (metabolism), Peroxiredoxins (MeSH), Photochemistry (MeSH), Polysaccharides (biosynthesis), Polysaccharides (metabolism), Protein Biosynthesis (MeSH), Sulfur (metabolism).
- MESH :
- chemical , biosynthesis : Polysaccharides.
- chemical , metabolism : Adenosine Triphosphate, Carbon Dioxide, Citric Acid, Molecular Chaperones, Oxidoreductases, Oxygen, Peroxidases, Polysaccharides, Sulfur.
- enzymology : Arabidopsis.
- metabolism : Arabidopsis.
- radiation effects : Cell Respiration.
- Electron Transport, Glutaredoxins, Oxidative Stress, Peroxiredoxins, Photochemistry, Protein Biosynthesis.
Abstract
Glutaredoxins (Grxs) are small ubiquitous proteins of the thioredoxin (Trx) family, which catalyze dithiol-disulfide exchange reactions or reduce protein-mixed glutathione disulfides. In plants, several Trx-interacting proteins have been isolated from different compartments, whereas very few Grx-interacting proteins are known. We describe here the determination of Grx target proteins using a mutated poplar Grx, various tissular and subcellular plant extracts, and liquid chromatography coupled to tandem mass spectrometry detection. We have identified 94 putative targets, involved in many processes, including oxidative stress response [peroxiredoxins (Prxs), ascorbate peroxidase, catalase], nitrogen, sulfur, and carbon metabolisms (methionine synthase, alanine aminotransferase, phosphoglycerate kinase), translation (elongation factors E and Tu), or protein folding (heat shock protein 70). Some of these proteins were previously found to interact with Trx or to be glutathiolated in other organisms, but others could be more specific partners of Grx. To substantiate further these data, Grx was shown to support catalysis of the stroma beta-type carbonic anhydrase and Prx IIF of Arabidopsis thaliana, but not of poplar 2-Cys Prx. Overall, these data suggest that the interaction could occur randomly either with exposed cysteinyl disulfide bonds formed within or between target proteins or with mixed disulfides between a protein thiol and glutathione.
DOI: 10.1089/ars.2005.7.919
PubMed: 15998247
Affiliations:
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Vandoeuvre</wicri:regionArea><wicri:noRegion>Vandoeuvre</wicri:noRegion><orgName type="university">Université Henri Poincaré</orgName><placeName><settlement type="city">Nancy</settlement><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region></placeName></affiliation></author><author><name sortKey="Villarejo, Arsenio" sort="Villarejo, Arsenio" uniqKey="Villarejo A" first="Arsenio" last="Villarejo">Arsenio Villarejo</name></author><author><name sortKey="Srivastava, Manoj" sort="Srivastava, Manoj" uniqKey="Srivastava M" first="Manoj" last="Srivastava">Manoj Srivastava</name></author><author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name></author><author><name sortKey="Keech, Olivier" sort="Keech, Olivier" uniqKey="Keech O" first="Olivier" last="Keech">Olivier Keech</name></author><author><name sortKey="Droux, Michel" sort="Droux, Michel" uniqKey="Droux M" first="Michel" last="Droux">Michel Droux</name></author><author><name sortKey="Finkemeier, Iris" sort="Finkemeier, Iris" uniqKey="Finkemeier I" first="Iris" last="Finkemeier">Iris Finkemeier</name></author><author><name sortKey="Samuelsson, Goran" sort="Samuelsson, Goran" uniqKey="Samuelsson G" first="Göran" last="Samuelsson">Göran Samuelsson</name></author><author><name sortKey="Dietz, Karl Josef" sort="Dietz, Karl Josef" uniqKey="Dietz K" first="Karl Josef" last="Dietz">Karl Josef Dietz</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><author><name sortKey="Wingsle, Gunnar" sort="Wingsle, Gunnar" uniqKey="Wingsle G" first="Gunnar" last="Wingsle">Gunnar Wingsle</name></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="ISSN">1523-0864</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphate (metabolism)</term><term>Arabidopsis (enzymology)</term><term>Arabidopsis (metabolism)</term><term>Carbon Dioxide (metabolism)</term><term>Cell Respiration (radiation effects)</term><term>Citric Acid (metabolism)</term><term>Electron Transport (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Molecular Chaperones (metabolism)</term><term>Oxidative Stress (MeSH)</term><term>Oxidoreductases (metabolism)</term><term>Oxygen (metabolism)</term><term>Peroxidases (metabolism)</term><term>Peroxiredoxins (MeSH)</term><term>Photochemistry (MeSH)</term><term>Polysaccharides (biosynthesis)</term><term>Polysaccharides (metabolism)</term><term>Protein Biosynthesis (MeSH)</term><term>Sulfur (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide citrique (métabolisme)</term><term>Adénosine triphosphate (métabolisme)</term><term>Arabidopsis (enzymologie)</term><term>Arabidopsis (métabolisme)</term><term>Biosynthèse des protéines (MeSH)</term><term>Chaperons moléculaires (métabolisme)</term><term>Dioxyde de carbone (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Oxidoreductases (métabolisme)</term><term>Oxygène (métabolisme)</term><term>Peroxidases (métabolisme)</term><term>Peroxirédoxines (MeSH)</term><term>Photochimie (MeSH)</term><term>Polyosides (biosynthèse)</term><term>Polyosides (métabolisme)</term><term>Respiration cellulaire (effets des radiations)</term><term>Soufre (métabolisme)</term><term>Stress oxydatif (MeSH)</term><term>Transport d'électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Polysaccharides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphate</term><term>Carbon Dioxide</term><term>Citric Acid</term><term>Molecular Chaperones</term><term>Oxidoreductases</term><term>Oxygen</term><term>Peroxidases</term><term>Polysaccharides</term><term>Sulfur</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Polyosides</term></keywords><keywords scheme="MESH" qualifier="effets des radiations" xml:lang="fr"><term>Respiration cellulaire</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide citrique</term><term>Adénosine triphosphate</term><term>Arabidopsis</term><term>Chaperons moléculaires</term><term>Dioxyde de carbone</term><term>Oxidoreductases</term><term>Oxygène</term><term>Peroxidases</term><term>Polyosides</term><term>Soufre</term></keywords><keywords scheme="MESH" qualifier="radiation effects" xml:lang="en"><term>Cell Respiration</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Transport</term><term>Glutaredoxins</term><term>Oxidative Stress</term><term>Peroxiredoxins</term><term>Photochemistry</term><term>Protein Biosynthesis</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biosynthèse des protéines</term><term>Glutarédoxines</term><term>Peroxirédoxines</term><term>Photochimie</term><term>Stress oxydatif</term><term>Transport d'électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) are small ubiquitous proteins of the thioredoxin (Trx) family, which catalyze dithiol-disulfide exchange reactions or reduce protein-mixed glutathione disulfides. In plants, several Trx-interacting proteins have been isolated from different compartments, whereas very few Grx-interacting proteins are known. We describe here the determination of Grx target proteins using a mutated poplar Grx, various tissular and subcellular plant extracts, and liquid chromatography coupled to tandem mass spectrometry detection. We have identified 94 putative targets, involved in many processes, including oxidative stress response [peroxiredoxins (Prxs), ascorbate peroxidase, catalase], nitrogen, sulfur, and carbon metabolisms (methionine synthase, alanine aminotransferase, phosphoglycerate kinase), translation (elongation factors E and Tu), or protein folding (heat shock protein 70). Some of these proteins were previously found to interact with Trx or to be glutathiolated in other organisms, but others could be more specific partners of Grx. To substantiate further these data, Grx was shown to support catalysis of the stroma beta-type carbonic anhydrase and Prx IIF of Arabidopsis thaliana, but not of poplar 2-Cys Prx. Overall, these data suggest that the interaction could occur randomly either with exposed cysteinyl disulfide bonds formed within or between target proteins or with mixed disulfides between a protein thiol and glutathione.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15998247</PMID><DateCompleted><Year>2005</Year><Month>09</Month><Day>23</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1523-0864</ISSN><JournalIssue CitedMedium="Print"><Volume>7</Volume><Issue>7-8</Issue><PubDate><MedlineDate>2005 Jul-Aug</MedlineDate></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Identification of plant glutaredoxin targets.</ArticleTitle><Pagination><MedlinePgn>919-29</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxins (Grxs) are small ubiquitous proteins of the thioredoxin (Trx) family, which catalyze dithiol-disulfide exchange reactions or reduce protein-mixed glutathione disulfides. In plants, several Trx-interacting proteins have been isolated from different compartments, whereas very few Grx-interacting proteins are known. We describe here the determination of Grx target proteins using a mutated poplar Grx, various tissular and subcellular plant extracts, and liquid chromatography coupled to tandem mass spectrometry detection. We have identified 94 putative targets, involved in many processes, including oxidative stress response [peroxiredoxins (Prxs), ascorbate peroxidase, catalase], nitrogen, sulfur, and carbon metabolisms (methionine synthase, alanine aminotransferase, phosphoglycerate kinase), translation (elongation factors E and Tu), or protein folding (heat shock protein 70). Some of these proteins were previously found to interact with Trx or to be glutathiolated in other organisms, but others could be more specific partners of Grx. To substantiate further these data, Grx was shown to support catalysis of the stroma beta-type carbonic anhydrase and Prx IIF of Arabidopsis thaliana, but not of poplar 2-Cys Prx. Overall, these data suggest that the interaction could occur randomly either with exposed cysteinyl disulfide bonds formed within or between target proteins or with mixed disulfides between a protein thiol and glutathione.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Unité Mixte de Recherches 1136 INRA UHP (Interaction Arbres Microorganismes), IFR 110 Génomique Ecophysiologie et Ecologie Fonctionnelles, Université Henri Poincaré, Vandoeuvre, France. nrouhier@scbiol.uhp-nancy.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Villarejo</LastName><ForeName>Arsenio</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Srivastava</LastName><ForeName>Manoj</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Keech</LastName><ForeName>Olivier</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Droux</LastName><ForeName>Michel</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Finkemeier</LastName><ForeName>Iris</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Samuelsson</LastName><ForeName>Göran</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Dietz</LastName><ForeName>Karl Josef</ForeName><Initials>KJ</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Wingsle</LastName><ForeName>Gunnar</ForeName><Initials>G</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="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018832">Molecular Chaperones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011134">Polysaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>142M471B3J</RegistryNumber><NameOfSubstance UI="D002245">Carbon Dioxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>2968PHW8QP</RegistryNumber><NameOfSubstance UI="D019343">Citric Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>70FD1KFU70</RegistryNumber><NameOfSubstance UI="D013455">Sulfur</NameOfSubstance></Chemical><Chemical><RegistryNumber>8L70Q75FXE</RegistryNumber><NameOfSubstance UI="D000255">Adenosine Triphosphate</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>S88TT14065</RegistryNumber><NameOfSubstance UI="D010100">Oxygen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000255" MajorTopicYN="N">Adenosine Triphosphate</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002245" MajorTopicYN="N">Carbon Dioxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019069" MajorTopicYN="N">Cell Respiration</DescriptorName><QualifierName UI="Q000528" MajorTopicYN="N">radiation effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019343" MajorTopicYN="N">Citric Acid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018832" MajorTopicYN="N">Molecular Chaperones</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</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="D010777" MajorTopicYN="N">Photochemistry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014176" MajorTopicYN="N">Protein Biosynthesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013455" MajorTopicYN="N">Sulfur</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>7</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>9</Month><Day>24</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>7</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15998247</ArticleId><ArticleId IdType="doi">10.1089/ars.2005.7.919</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Nancy</li></settlement><orgName><li>Université Henri Poincaré</li></orgName></list><tree><noCountry><name sortKey="Dietz, Karl Josef" sort="Dietz, Karl Josef" uniqKey="Dietz K" first="Karl Josef" last="Dietz">Karl Josef Dietz</name><name sortKey="Droux, Michel" sort="Droux, Michel" uniqKey="Droux M" first="Michel" last="Droux">Michel Droux</name><name sortKey="Finkemeier, Iris" sort="Finkemeier, Iris" uniqKey="Finkemeier I" first="Iris" last="Finkemeier">Iris Finkemeier</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Keech, Olivier" sort="Keech, Olivier" uniqKey="Keech O" first="Olivier" last="Keech">Olivier Keech</name><name sortKey="Samuelsson, Goran" sort="Samuelsson, Goran" uniqKey="Samuelsson G" first="Göran" last="Samuelsson">Göran Samuelsson</name><name sortKey="Srivastava, Manoj" sort="Srivastava, Manoj" uniqKey="Srivastava M" first="Manoj" last="Srivastava">Manoj Srivastava</name><name sortKey="Villarejo, Arsenio" sort="Villarejo, Arsenio" uniqKey="Villarejo A" first="Arsenio" last="Villarejo">Arsenio Villarejo</name><name sortKey="Wingsle, Gunnar" sort="Wingsle, Gunnar" uniqKey="Wingsle G" first="Gunnar" last="Wingsle">Gunnar Wingsle</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:15998247" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PoplarV1
| This area was generated with Dilib version V0.6.37. |  |