Essential 110Cys in active site of membrane-associated prostaglandin E synthase-2.
Identifieur interne : 000F40 ( Main/Exploration ); précédent : 000F39; suivant : 000F41Essential 110Cys in active site of membrane-associated prostaglandin E synthase-2.
Auteurs : Kikuko Watanabe [Japon] ; Hiroaki Ohkubo ; Haruki Niwa ; Naomi Tanikawa ; Noriko Koda ; Seiji Ito ; Yoshihiro OhmiyaSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2003.
Descripteurs français
- KwdFr :
- Acide lipoïque (analogues et dérivés), Acide lipoïque (composition chimique), Cinétique (MeSH), Cystéine (composition chimique), Dithiothréitol (pharmacologie), Domaine catalytique (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Humains (MeSH), Intramolecular oxidoreductases (composition chimique), Leucine (composition chimique), Liaison aux protéines (MeSH), Mutagenèse dirigée (MeSH), Mutation (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Prostaglandin-E synthases (MeSH), Protéines (composition chimique), Relation dose-effet des médicaments (MeSH), Sites de fixation (MeSH), Stress oxydatif (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Sérine (composition chimique), Thiorédoxines (composition chimique).
- MESH :
- analogues et dérivés : Acide lipoïque.
- composition chimique : Acide lipoïque, Cystéine, Intramolecular oxidoreductases, Leucine, Protéines, Sérine, Thiorédoxines.
- pharmacologie : Dithiothréitol.
- Cinétique, Domaine catalytique, Données de séquences moléculaires, Glutarédoxines, Humains, Liaison aux protéines, Mutagenèse dirigée, Mutation, Oxidoreductases, Oxydoréduction, Prostaglandin-E synthases, Relation dose-effet des médicaments, Sites de fixation, Stress oxydatif, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Catalytic Domain (MeSH), Cysteine (chemistry), Dithiothreitol (pharmacology), Dose-Response Relationship, Drug (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Intramolecular Oxidoreductases (chemistry), Kinetics (MeSH), Leucine (chemistry), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Mutation (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Oxidoreductases (MeSH), Prostaglandin-E Synthases (MeSH), Protein Binding (MeSH), Protein Structure, Tertiary (MeSH), Proteins (chemistry), Serine (chemistry), Thioctic Acid (analogs & derivatives), Thioctic Acid (chemistry), Thioredoxins (chemistry).
- MESH :
- chemical , analogs & derivatives : Thioctic Acid.
- chemical , chemistry : Cysteine, Intramolecular Oxidoreductases, Leucine, Proteins, Serine, Thioctic Acid, Thioredoxins.
- chemical , pharmacology : Dithiothreitol.
- Amino Acid Sequence, Binding Sites, Catalytic Domain, Dose-Response Relationship, Drug, Glutaredoxins, Humans, Kinetics, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Oxidation-Reduction, Oxidative Stress, Oxidoreductases, Prostaglandin-E Synthases, Protein Binding, Protein Structure, Tertiary.
Abstract
The amino acid sequence of membrane-associated prostaglandin (PG) E synthase-2 (mPGE synthase-2), which has a broad specificity in its thiol requirement for a catalytic activity, has the consensus region from 104Leu to 120Leu found in glutaredoxin and of thioredoxin. The sequence of Cys-x-x-Cys in the consensus region is the active site for thioredoxin and mPGE synthase-2 also has this amino acid sequence (110Cys-x-x-113Cys). The mutation from 110Cys to Ser or the double mutation from 110Cys and 113Cys to Ser caused loss of PGE synthase activity, whereas the single mutation from 113Cys to Ser did not affect the enzyme activity. These results indicate that 110Cys, but not 113Cys, is the essential amino acid in the active site of mPGE synthase-2. 110Cys is an important amino acid in PGE synthase activity and plays the critical role as Cys at the same position in redoxin. Moreover, we found that the reduced form of lipoic acid (dihydrolipoic acid) serves as one of the natural activators of mPGE synthase-2 in the cells.
DOI: 10.1016/s0006-291x(03)01025-8
PubMed: 12804604
Affiliations:
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Ohkubo</name></author><author><name sortKey="Niwa, Haruki" sort="Niwa, Haruki" uniqKey="Niwa H" first="Haruki" last="Niwa">Haruki Niwa</name></author><author><name sortKey="Tanikawa, Naomi" sort="Tanikawa, Naomi" uniqKey="Tanikawa N" first="Naomi" last="Tanikawa">Naomi Tanikawa</name></author><author><name sortKey="Koda, Noriko" sort="Koda, Noriko" uniqKey="Koda N" first="Noriko" last="Koda">Noriko Koda</name></author><author><name sortKey="Ito, Seiji" sort="Ito, Seiji" uniqKey="Ito S" first="Seiji" last="Ito">Seiji Ito</name></author><author><name sortKey="Ohmiya, Yoshihiro" sort="Ohmiya, Yoshihiro" uniqKey="Ohmiya Y" first="Yoshihiro" last="Ohmiya">Yoshihiro Ohmiya</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2003">2003</date><idno type="RBID">pubmed:12804604</idno><idno type="pmid">12804604</idno><idno type="doi">10.1016/s0006-291x(03)01025-8</idno><idno type="wicri:Area/Main/Corpus">000F28</idno><idno type="wicri:explorRef" 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Shimonoseki, Yamaguchi 751-8503</wicri:regionArea><wicri:noRegion>Yamaguchi 751-8503</wicri:noRegion></affiliation></author><author><name sortKey="Ohkubo, Hiroaki" sort="Ohkubo, Hiroaki" uniqKey="Ohkubo H" first="Hiroaki" last="Ohkubo">Hiroaki Ohkubo</name></author><author><name sortKey="Niwa, Haruki" sort="Niwa, Haruki" uniqKey="Niwa H" first="Haruki" last="Niwa">Haruki Niwa</name></author><author><name sortKey="Tanikawa, Naomi" sort="Tanikawa, Naomi" uniqKey="Tanikawa N" first="Naomi" last="Tanikawa">Naomi Tanikawa</name></author><author><name sortKey="Koda, Noriko" sort="Koda, Noriko" uniqKey="Koda N" first="Noriko" last="Koda">Noriko Koda</name></author><author><name sortKey="Ito, Seiji" sort="Ito, Seiji" uniqKey="Ito S" first="Seiji" last="Ito">Seiji Ito</name></author><author><name sortKey="Ohmiya, Yoshihiro" sort="Ohmiya, Yoshihiro" uniqKey="Ohmiya Y" first="Yoshihiro" last="Ohmiya">Yoshihiro Ohmiya</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</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>Binding Sites (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Cysteine (chemistry)</term><term>Dithiothreitol (pharmacology)</term><term>Dose-Response Relationship, Drug (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Humans (MeSH)</term><term>Intramolecular Oxidoreductases (chemistry)</term><term>Kinetics (MeSH)</term><term>Leucine (chemistry)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Mutation (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Prostaglandin-E Synthases (MeSH)</term><term>Protein Binding (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Proteins (chemistry)</term><term>Serine (chemistry)</term><term>Thioctic Acid (analogs & derivatives)</term><term>Thioctic Acid (chemistry)</term><term>Thioredoxins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide lipoïque (analogues et dérivés)</term><term>Acide lipoïque (composition chimique)</term><term>Cinétique (MeSH)</term><term>Cystéine (composition chimique)</term><term>Dithiothréitol (pharmacologie)</term><term>Domaine catalytique (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Intramolecular oxidoreductases (composition chimique)</term><term>Leucine (composition chimique)</term><term>Liaison aux protéines (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Mutation (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Prostaglandin-E synthases (MeSH)</term><term>Protéines (composition chimique)</term><term>Relation dose-effet des médicaments (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Sérine (composition chimique)</term><term>Thiorédoxines (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Thioctic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Intramolecular Oxidoreductases</term><term>Leucine</term><term>Proteins</term><term>Serine</term><term>Thioctic Acid</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Dithiothreitol</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Acide lipoïque</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acide lipoïque</term><term>Cystéine</term><term>Intramolecular oxidoreductases</term><term>Leucine</term><term>Protéines</term><term>Sérine</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Dithiothréitol</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Catalytic Domain</term><term>Dose-Response Relationship, Drug</term><term>Glutaredoxins</term><term>Humans</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Mutation</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term><term>Oxidoreductases</term><term>Prostaglandin-E Synthases</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Humains</term><term>Liaison aux protéines</term><term>Mutagenèse dirigée</term><term>Mutation</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Prostaglandin-E synthases</term><term>Relation dose-effet des médicaments</term><term>Sites de fixation</term><term>Stress oxydatif</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The amino acid sequence of membrane-associated prostaglandin (PG) E synthase-2 (mPGE synthase-2), which has a broad specificity in its thiol requirement for a catalytic activity, has the consensus region from 104Leu to 120Leu found in glutaredoxin and of thioredoxin. The sequence of Cys-x-x-Cys in the consensus region is the active site for thioredoxin and mPGE synthase-2 also has this amino acid sequence (110Cys-x-x-113Cys). The mutation from 110Cys to Ser or the double mutation from 110Cys and 113Cys to Ser caused loss of PGE synthase activity, whereas the single mutation from 113Cys to Ser did not affect the enzyme activity. These results indicate that 110Cys, but not 113Cys, is the essential amino acid in the active site of mPGE synthase-2. 110Cys is an important amino acid in PGE synthase activity and plays the critical role as Cys at the same position in redoxin. Moreover, we found that the reduced form of lipoic acid (dihydrolipoic acid) serves as one of the natural activators of mPGE synthase-2 in the cells.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12804604</PMID><DateCompleted><Year>2003</Year><Month>07</Month><Day>25</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>306</Volume><Issue>2</Issue><PubDate><Year>2003</Year><Month>Jun</Month><Day>27</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Essential 110Cys in active site of membrane-associated prostaglandin E synthase-2.</ArticleTitle><Pagination><MedlinePgn>577-81</MedlinePgn></Pagination><Abstract><AbstractText>The amino acid sequence of membrane-associated prostaglandin (PG) E synthase-2 (mPGE synthase-2), which has a broad specificity in its thiol requirement for a catalytic activity, has the consensus region from 104Leu to 120Leu found in glutaredoxin and of thioredoxin. The sequence of Cys-x-x-Cys in the consensus region is the active site for thioredoxin and mPGE synthase-2 also has this amino acid sequence (110Cys-x-x-113Cys). The mutation from 110Cys to Ser or the double mutation from 110Cys and 113Cys to Ser caused loss of PGE synthase activity, whereas the single mutation from 113Cys to Ser did not affect the enzyme activity. These results indicate that 110Cys, but not 113Cys, is the essential amino acid in the active site of mPGE synthase-2. 110Cys is an important amino acid in PGE synthase activity and plays the critical role as Cys at the same position in redoxin. Moreover, we found that the reduced form of lipoic acid (dihydrolipoic acid) serves as one of the natural activators of mPGE synthase-2 in the cells.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Watanabe</LastName><ForeName>Kikuko</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Division of Life Science, Graduate School of Integrated Science and Art, University of East Asia, 2-1 Ichinomiya-gakuencho, Shimonoseki, Yamaguchi 751-8503, Japan. watanabe@po.cc.toia-u.ac.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ohkubo</LastName><ForeName>Hiroaki</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Niwa</LastName><ForeName>Haruki</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Tanikawa</LastName><ForeName>Naomi</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Koda</LastName><ForeName>Noriko</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Ito</LastName><ForeName>Seiji</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Ohmiya</LastName><ForeName>Yoshihiro</ForeName><Initials>Y</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>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>452VLY9402</RegistryNumber><NameOfSubstance UI="D012694">Serine</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>73Y7P0K73Y</RegistryNumber><NameOfSubstance UI="D008063">Thioctic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>7NV2KHU5JA</RegistryNumber><NameOfSubstance UI="C015144">dihydrolipoic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.3.-</RegistryNumber><NameOfSubstance UI="D019746">Intramolecular Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.3.99.3</RegistryNumber><NameOfSubstance UI="D000071876">Prostaglandin-E Synthases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GMW67QNF9C</RegistryNumber><NameOfSubstance UI="D007930">Leucine</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>T8ID5YZU6Y</RegistryNumber><NameOfSubstance UI="D004229">Dithiothreitol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004229" MajorTopicYN="N">Dithiothreitol</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019746" MajorTopicYN="N">Intramolecular Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007930" MajorTopicYN="N">Leucine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000071876" MajorTopicYN="N">Prostaglandin-E Synthases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012694" MajorTopicYN="N">Serine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008063" MajorTopicYN="N">Thioctic Acid</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>6</Month><Day>14</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>7</Month><Day>26</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>6</Month><Day>14</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12804604</ArticleId><ArticleId IdType="pii">S0006291X03010258</ArticleId><ArticleId IdType="doi">10.1016/s0006-291x(03)01025-8</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Ito, Seiji" sort="Ito, Seiji" uniqKey="Ito S" first="Seiji" last="Ito">Seiji Ito</name><name sortKey="Koda, Noriko" sort="Koda, Noriko" uniqKey="Koda N" first="Noriko" last="Koda">Noriko Koda</name><name sortKey="Niwa, Haruki" sort="Niwa, Haruki" uniqKey="Niwa H" first="Haruki" last="Niwa">Haruki Niwa</name><name sortKey="Ohkubo, Hiroaki" sort="Ohkubo, Hiroaki" uniqKey="Ohkubo H" first="Hiroaki" last="Ohkubo">Hiroaki Ohkubo</name><name sortKey="Ohmiya, Yoshihiro" sort="Ohmiya, Yoshihiro" uniqKey="Ohmiya Y" first="Yoshihiro" last="Ohmiya">Yoshihiro Ohmiya</name><name sortKey="Tanikawa, Naomi" sort="Tanikawa, Naomi" uniqKey="Tanikawa N" first="Naomi" last="Tanikawa">Naomi Tanikawa</name></noCountry><country name="Japon"><noRegion><name sortKey="Watanabe, Kikuko" sort="Watanabe, Kikuko" uniqKey="Watanabe K" first="Kikuko" last="Watanabe">Kikuko Watanabe</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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