Insights into ascorbate regeneration in plants: investigating the redox and structural properties of dehydroascorbate reductases from Populus trichocarpa.
Identifieur interne : 001985 ( Main/Corpus ); précédent : 001984; suivant : 001986Insights into ascorbate regeneration in plants: investigating the redox and structural properties of dehydroascorbate reductases from Populus trichocarpa.
Auteurs : Pierre-Alexandre Lallement ; Thomas Roret ; Pascale Tsan ; José M. Gualberto ; Jean-Michel Girardet ; Claude Didierjean ; Nicolas Rouhier ; Arnaud HeckerSource :
- The Biochemical journal [ 1470-8728 ] ; 2016.
English descriptors
- KwdEn :
- Ascorbic Acid (metabolism), Binding Sites (MeSH), Gene Expression Regulation, Enzymologic (physiology), Gene Expression Regulation, Plant (physiology), Magnetic Resonance Spectroscopy (MeSH), Models, Molecular (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (chemistry), Oxidoreductases (genetics), Oxidoreductases (metabolism), Plant Proteins (genetics), Plant Proteins (metabolism), Populus (metabolism), Protein Conformation (MeSH), Tobacco (MeSH).
- MESH :
- chemical , chemistry : Oxidoreductases.
- chemical , genetics : Oxidoreductases, Plant Proteins.
- chemical , metabolism : Ascorbic Acid, Oxidoreductases, Plant Proteins.
- metabolism : Populus.
- physiology : Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant.
- Binding Sites, Magnetic Resonance Spectroscopy, Models, Molecular, Oxidation-Reduction, Protein Conformation, Tobacco.
Abstract
Dehydroascorbate reductases (DHARs), enzymes belonging to the GST superfamily, catalyse the GSH-dependent reduction of dehydroascorbate into ascorbate in plants. By maintaining a reduced ascorbate pool, they notably participate to H2O2 detoxification catalysed by ascorbate peroxidases (APXs). Despite this central role, the catalytic mechanism used by DHARs is still not well understood and there is no supportive 3D structure. In this context, we have performed a thorough biochemical and structural analysis of the three poplar DHARs and coupled this to the analysis of their transcript expression patterns and subcellular localizations. The transcripts for these genes are mainly detected in reproductive and green organs and the corresponding proteins are expressed in plastids, in the cytosol and in the nucleus, but not in mitochondria and peroxisomes where ascorbate regeneration is obviously necessary. Comparing the kinetic properties and the sensitivity to GSSG-mediated oxidation of DHAR2 and DHAR3A, exhibiting 1 or 3 cysteinyl residues respectively, we observed that the presence of additional cysteines in DHAR3A modifies the regeneration mechanism of the catalytic cysteine by forming different redox states. Finally, from the 3D structure of DHAR3A solved by NMR, we were able to map the residues important for the binding of both substrates (GSH and DHA), showing that DHAR active site is very selective for DHA recognition and providing further insights into the catalytic mechanism and the roles of the additional cysteines found in some DHARs.
DOI: 10.1042/BJ20151147
PubMed: 26699905
Links to Exploration step
pubmed:26699905Le document en format XML
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Gualberto</name><affiliation><nlm:affiliation>Institut de Biologie Moléculaire des Plantes, CNRS-UPR 2357, 67084 Strasbourg, France.</nlm:affiliation></affiliation></author><author><name sortKey="Girardet, Jean Michel" sort="Girardet, Jean Michel" uniqKey="Girardet J" first="Jean-Michel" last="Girardet">Jean-Michel Girardet</name><affiliation><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France.</nlm:affiliation></affiliation></author><author><name sortKey="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</name><affiliation><nlm:affiliation>Université de Lorraine, CRM2, UMR 7036, 54506 Vandœuvre-lès-Nancy, France CNRS, CRM2, UMR 7036, 54506 Vandœuvre-lès-Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France.</nlm:affiliation></affiliation></author><author><name sortKey="Hecker, Arnaud" sort="Hecker, Arnaud" uniqKey="Hecker A" first="Arnaud" last="Hecker">Arnaud Hecker</name><affiliation><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France arnaud.hecker@univ-lorraine.fr.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:26699905</idno><idno type="pmid">26699905</idno><idno type="doi">10.1042/BJ20151147</idno><idno type="wicri:Area/Main/Corpus">001985</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001985</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Insights into ascorbate regeneration in plants: investigating the redox and structural properties of dehydroascorbate reductases from Populus trichocarpa.</title><author><name sortKey="Lallement, Pierre Alexandre" sort="Lallement, Pierre Alexandre" uniqKey="Lallement P" first="Pierre-Alexandre" last="Lallement">Pierre-Alexandre Lallement</name><affiliation><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France.</nlm:affiliation></affiliation></author><author><name sortKey="Roret, Thomas" sort="Roret, Thomas" uniqKey="Roret T" first="Thomas" last="Roret">Thomas Roret</name><affiliation><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France.</nlm:affiliation></affiliation></author><author><name sortKey="Tsan, Pascale" sort="Tsan, Pascale" uniqKey="Tsan P" first="Pascale" last="Tsan">Pascale Tsan</name><affiliation><nlm:affiliation>Université de Lorraine, CRM2, UMR 7036, 54506 Vandœuvre-lès-Nancy, France CNRS, CRM2, UMR 7036, 54506 Vandœuvre-lès-Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Gualberto, Jose M" sort="Gualberto, Jose M" uniqKey="Gualberto J" first="José M" last="Gualberto">José M. Gualberto</name><affiliation><nlm:affiliation>Institut de Biologie Moléculaire des Plantes, CNRS-UPR 2357, 67084 Strasbourg, France.</nlm:affiliation></affiliation></author><author><name sortKey="Girardet, Jean Michel" sort="Girardet, Jean Michel" uniqKey="Girardet J" first="Jean-Michel" last="Girardet">Jean-Michel Girardet</name><affiliation><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France.</nlm:affiliation></affiliation></author><author><name sortKey="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</name><affiliation><nlm:affiliation>Université de Lorraine, CRM2, UMR 7036, 54506 Vandœuvre-lès-Nancy, France CNRS, CRM2, UMR 7036, 54506 Vandœuvre-lès-Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France.</nlm:affiliation></affiliation></author><author><name sortKey="Hecker, Arnaud" sort="Hecker, Arnaud" uniqKey="Hecker A" first="Arnaud" last="Hecker">Arnaud Hecker</name><affiliation><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France arnaud.hecker@univ-lorraine.fr.</nlm:affiliation></affiliation></author></analytic><series><title level="j">The Biochemical journal</title><idno type="eISSN">1470-8728</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Ascorbic Acid (metabolism)</term><term>Binding Sites (MeSH)</term><term>Gene Expression Regulation, Enzymologic (physiology)</term><term>Gene Expression Regulation, Plant (physiology)</term><term>Magnetic Resonance Spectroscopy (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (chemistry)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (metabolism)</term><term>Populus (metabolism)</term><term>Protein Conformation (MeSH)</term><term>Tobacco (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Oxidoreductases</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Ascorbic Acid</term><term>Oxidoreductases</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Gene Expression Regulation, Enzymologic</term><term>Gene Expression Regulation, Plant</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Magnetic Resonance Spectroscopy</term><term>Models, Molecular</term><term>Oxidation-Reduction</term><term>Protein Conformation</term><term>Tobacco</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Dehydroascorbate reductases (DHARs), enzymes belonging to the GST superfamily, catalyse the GSH-dependent reduction of dehydroascorbate into ascorbate in plants. By maintaining a reduced ascorbate pool, they notably participate to H2O2 detoxification catalysed by ascorbate peroxidases (APXs). Despite this central role, the catalytic mechanism used by DHARs is still not well understood and there is no supportive 3D structure. In this context, we have performed a thorough biochemical and structural analysis of the three poplar DHARs and coupled this to the analysis of their transcript expression patterns and subcellular localizations. The transcripts for these genes are mainly detected in reproductive and green organs and the corresponding proteins are expressed in plastids, in the cytosol and in the nucleus, but not in mitochondria and peroxisomes where ascorbate regeneration is obviously necessary. Comparing the kinetic properties and the sensitivity to GSSG-mediated oxidation of DHAR2 and DHAR3A, exhibiting 1 or 3 cysteinyl residues respectively, we observed that the presence of additional cysteines in DHAR3A modifies the regeneration mechanism of the catalytic cysteine by forming different redox states. Finally, from the 3D structure of DHAR3A solved by NMR, we were able to map the residues important for the binding of both substrates (GSH and DHA), showing that DHAR active site is very selective for DHA recognition and providing further insights into the catalytic mechanism and the roles of the additional cysteines found in some DHARs. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26699905</PMID><DateCompleted><Year>2016</Year><Month>08</Month><Day>08</Day></DateCompleted><DateRevised><Year>2016</Year><Month>03</Month><Day>11</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1470-8728</ISSN><JournalIssue CitedMedium="Internet"><Volume>473</Volume><Issue>6</Issue><PubDate><Year>2016</Year><Month>Mar</Month><Day>15</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Insights into ascorbate regeneration in plants: investigating the redox and structural properties of dehydroascorbate reductases from Populus trichocarpa.</ArticleTitle><Pagination><MedlinePgn>717-31</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1042/BJ20151147</ELocationID><Abstract><AbstractText>Dehydroascorbate reductases (DHARs), enzymes belonging to the GST superfamily, catalyse the GSH-dependent reduction of dehydroascorbate into ascorbate in plants. By maintaining a reduced ascorbate pool, they notably participate to H2O2 detoxification catalysed by ascorbate peroxidases (APXs). Despite this central role, the catalytic mechanism used by DHARs is still not well understood and there is no supportive 3D structure. In this context, we have performed a thorough biochemical and structural analysis of the three poplar DHARs and coupled this to the analysis of their transcript expression patterns and subcellular localizations. The transcripts for these genes are mainly detected in reproductive and green organs and the corresponding proteins are expressed in plastids, in the cytosol and in the nucleus, but not in mitochondria and peroxisomes where ascorbate regeneration is obviously necessary. Comparing the kinetic properties and the sensitivity to GSSG-mediated oxidation of DHAR2 and DHAR3A, exhibiting 1 or 3 cysteinyl residues respectively, we observed that the presence of additional cysteines in DHAR3A modifies the regeneration mechanism of the catalytic cysteine by forming different redox states. Finally, from the 3D structure of DHAR3A solved by NMR, we were able to map the residues important for the binding of both substrates (GSH and DHA), showing that DHAR active site is very selective for DHA recognition and providing further insights into the catalytic mechanism and the roles of the additional cysteines found in some DHARs. </AbstractText><CopyrightInformation>© 2016 Authors; published by Portland Press Limited.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lallement</LastName><ForeName>Pierre-Alexandre</ForeName><Initials>PA</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Roret</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tsan</LastName><ForeName>Pascale</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Université de Lorraine, CRM2, UMR 7036, 54506 Vandœuvre-lès-Nancy, France CNRS, CRM2, UMR 7036, 54506 Vandœuvre-lès-Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gualberto</LastName><ForeName>José M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Institut de Biologie Moléculaire des Plantes, CNRS-UPR 2357, 67084 Strasbourg, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Girardet</LastName><ForeName>Jean-Michel</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Didierjean</LastName><ForeName>Claude</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Université de Lorraine, CRM2, UMR 7036, 54506 Vandœuvre-lès-Nancy, France CNRS, CRM2, UMR 7036, 54506 Vandœuvre-lès-Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hecker</LastName><ForeName>Arnaud</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506 Vandœuvre-lès-Nancy, France INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280 Champenoux, France arnaud.hecker@univ-lorraine.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>12</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.5.1</RegistryNumber><NameOfSubstance UI="C020666">glutathione dehydrogenase (ascorbate)</NameOfSubstance></Chemical><Chemical><RegistryNumber>PQ6CK8PD0R</RegistryNumber><NameOfSubstance UI="D001205">Ascorbic Acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001205" MajorTopicYN="N">Ascorbic Acid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015971" MajorTopicYN="N">Gene Expression Regulation, Enzymologic</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></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="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014026" MajorTopicYN="N">Tobacco</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Populus trichocarpa</Keyword><Keyword MajorTopicYN="N">ascorbate recycling</Keyword><Keyword MajorTopicYN="N">catalytic cysteine residue</Keyword><Keyword MajorTopicYN="N">dehydroascorbate reductases</Keyword><Keyword MajorTopicYN="N">glutathione</Keyword><Keyword MajorTopicYN="N">nuclear magnetic resonance</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>11</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>12</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>12</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>12</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>8</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26699905</ArticleId><ArticleId IdType="pii">BJ20151147</ArticleId><ArticleId 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