Activation of CDK-activating kinase is dependent on interaction with H-type cyclins in plants.
Identifieur interne : 004838 ( Main/Exploration ); précédent : 004837; suivant : 004839Activation of CDK-activating kinase is dependent on interaction with H-type cyclins in plants.
Auteurs : M. Yamaguchi [Japon] ; T. Fabian ; M. Sauter ; R P Bhalerao ; J. Schrader ; G. Sandberg ; M. Umeda ; H. UchimiyaSource :
- The Plant journal : for cell and molecular biology [ 0960-7412 ] ; 2000.
Descripteurs français
- KwdFr :
- Activation enzymatique (MeSH), Alignement de séquences (MeSH), Animaux (MeSH), Arbres (cytologie), Arbres (génétique), Arbres (métabolisme), Clonage moléculaire (MeSH), Cycle cellulaire (MeSH), Cyclines (composition chimique), Cyclines (génétique), Cyclines (métabolisme), Données de séquences moléculaires (MeSH), Humains (MeSH), Kinase-2 cycline-dépendante (MeSH), Kinases CDC2-CDC28 (MeSH), Kinases cyclines-dépendantes (génétique), Kinases cyclines-dépendantes (métabolisme), Oryza (cytologie), Oryza (génétique), Oryza (métabolisme), Phylogenèse (MeSH), Protein-Serine-Threonine Kinases (génétique), Protein-Serine-Threonine Kinases (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (métabolisme), Saccharomyces cerevisiae (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Cyclines, Protéines recombinantes.
- cytologie : Arbres, Oryza.
- génétique : Arbres, Cyclines, Kinases cyclines-dépendantes, Oryza, Protein-Serine-Threonine Kinases.
- métabolisme : Arbres, Cyclines, Kinases cyclines-dépendantes, Oryza, Protein-Serine-Threonine Kinases, Protéines recombinantes.
- Activation enzymatique, Alignement de séquences, Animaux, Clonage moléculaire, Cycle cellulaire, Données de séquences moléculaires, Humains, Kinase-2 cycline-dépendante, Kinases CDC2-CDC28, Phylogenèse, Saccharomyces cerevisiae, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), CDC2-CDC28 Kinases (MeSH), Cell Cycle (MeSH), Cloning, Molecular (MeSH), Cyclin-Dependent Kinase 2 (MeSH), Cyclin-Dependent Kinases (genetics), Cyclin-Dependent Kinases (metabolism), Cyclins (chemistry), Cyclins (genetics), Cyclins (metabolism), Enzyme Activation (MeSH), Humans (MeSH), Molecular Sequence Data (MeSH), Oryza (cytology), Oryza (genetics), Oryza (metabolism), Phylogeny (MeSH), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Saccharomyces cerevisiae (MeSH), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Trees (cytology), Trees (genetics), Trees (metabolism).
- MESH :
- chemical , chemistry : Cyclins, Recombinant Proteins.
- chemical , genetics : Cyclin-Dependent Kinases, Cyclins, Protein-Serine-Threonine Kinases.
- chemical , metabolism : Cyclin-Dependent Kinases, Cyclins, Protein-Serine-Threonine Kinases, Recombinant Proteins.
- chemical : CDC2-CDC28 Kinases, Cyclin-Dependent Kinase 2.
- cytology : Oryza, Trees.
- genetics : Oryza, Trees.
- metabolism : Oryza, Trees.
- Amino Acid Sequence, Animals, Cell Cycle, Cloning, Molecular, Enzyme Activation, Humans, Molecular Sequence Data, Phylogeny, Saccharomyces cerevisiae, Sequence Alignment, Sequence Homology, Amino Acid.
Abstract
cDNAs encoding cyclin H homologs were isolated from poplar (Populus tremula X tremuloides) and rice (Oryza sativa) plants, and were designated Pt;cycH;1 and Os;cycH;1, respectively. The deduced amino-acid sequences showed 40-60% similarity to human cyclin H and Schizosaccharomyces pombe Mcs2, with higher similarity in the cyclin box region. While Pt;cycH;1 and Os;cycH;1 were expressed in all tissues examined, the transcripts accumulated abundantly in dividing cells. Expression of Os;cycH;1 was abundant in the S-phase in partially synchronized suspension cells, and was induced by submergence in internodes of deepwater rice. A yeast two-hybrid assay demonstrated that both Pt;CycH;1 and Os;CycH;1 were able to interact with rice R2 kinase, which is structurally and functionally similar to cyclin-dependent kinase (CDK)-activating kinase (CAK) of vertebrates. Moreover, an in vitro pull-down assay showed that Os;CycH;1 specifically bound to R2 but not to other rice CDKs. When R2 was expressed in budding yeast CAK mutant, the suppression activity in terms of temperature-sensitivity was enhanced by co-expression with Os;cycH;1. Furthermore, in vitro kinase assay indicated that the kinase activities of R2 on CDKs and the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II were markedly elevated by binding to Os;CycH;1. Our results suggest that cyclin H is a regulatory subunit of CAK, which positively controls CDK- and CTD-kinase activities in plant cells.
DOI: 10.1046/j.1365-313x.2000.00846.x
PubMed: 11029700
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Animals (MeSH)</term>
<term>CDC2-CDC28 Kinases (MeSH)</term>
<term>Cell Cycle (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Cyclin-Dependent Kinase 2 (MeSH)</term>
<term>Cyclin-Dependent Kinases (genetics)</term>
<term>Cyclin-Dependent Kinases (metabolism)</term>
<term>Cyclins (chemistry)</term>
<term>Cyclins (genetics)</term>
<term>Cyclins (metabolism)</term>
<term>Enzyme Activation (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Oryza (cytology)</term>
<term>Oryza (genetics)</term>
<term>Oryza (metabolism)</term>
<term>Phylogeny (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (genetics)</term>
<term>Protein-Serine-Threonine Kinases (metabolism)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae (MeSH)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Trees (cytology)</term>
<term>Trees (genetics)</term>
<term>Trees (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term>
<term>Alignement de séquences (MeSH)</term>
<term>Animaux (MeSH)</term>
<term>Arbres (cytologie)</term>
<term>Arbres (génétique)</term>
<term>Arbres (métabolisme)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Cycle cellulaire (MeSH)</term>
<term>Cyclines (composition chimique)</term>
<term>Cyclines (génétique)</term>
<term>Cyclines (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Kinase-2 cycline-dépendante (MeSH)</term>
<term>Kinases CDC2-CDC28 (MeSH)</term>
<term>Kinases cyclines-dépendantes (génétique)</term>
<term>Kinases cyclines-dépendantes (métabolisme)</term>
<term>Oryza (cytologie)</term>
<term>Oryza (génétique)</term>
<term>Oryza (métabolisme)</term>
<term>Phylogenèse (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (génétique)</term>
<term>Protein-Serine-Threonine Kinases (métabolisme)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Saccharomyces cerevisiae (MeSH)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cyclins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cyclin-Dependent Kinases</term>
<term>Cyclins</term>
<term>Protein-Serine-Threonine Kinases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cyclin-Dependent Kinases</term>
<term>Cyclins</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>CDC2-CDC28 Kinases</term>
<term>Cyclin-Dependent Kinase 2</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cyclines</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Arbres</term>
<term>Oryza</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Oryza</term>
<term>Trees</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Oryza</term>
<term>Trees</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Arbres</term>
<term>Cyclines</term>
<term>Kinases cyclines-dépendantes</term>
<term>Oryza</term>
<term>Protein-Serine-Threonine Kinases</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Oryza</term>
<term>Trees</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arbres</term>
<term>Cyclines</term>
<term>Kinases cyclines-dépendantes</term>
<term>Oryza</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Cell Cycle</term>
<term>Cloning, Molecular</term>
<term>Enzyme Activation</term>
<term>Humans</term>
<term>Molecular Sequence Data</term>
<term>Phylogeny</term>
<term>Saccharomyces cerevisiae</term>
<term>Sequence Alignment</term>
<term>Sequence Homology, Amino Acid</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term>
<term>Alignement de séquences</term>
<term>Animaux</term>
<term>Clonage moléculaire</term>
<term>Cycle cellulaire</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Kinase-2 cycline-dépendante</term>
<term>Kinases CDC2-CDC28</term>
<term>Phylogenèse</term>
<term>Saccharomyces cerevisiae</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">cDNAs encoding cyclin H homologs were isolated from poplar (Populus tremula X tremuloides) and rice (Oryza sativa) plants, and were designated Pt;cycH;1 and Os;cycH;1, respectively. The deduced amino-acid sequences showed 40-60% similarity to human cyclin H and Schizosaccharomyces pombe Mcs2, with higher similarity in the cyclin box region. While Pt;cycH;1 and Os;cycH;1 were expressed in all tissues examined, the transcripts accumulated abundantly in dividing cells. Expression of Os;cycH;1 was abundant in the S-phase in partially synchronized suspension cells, and was induced by submergence in internodes of deepwater rice. A yeast two-hybrid assay demonstrated that both Pt;CycH;1 and Os;CycH;1 were able to interact with rice R2 kinase, which is structurally and functionally similar to cyclin-dependent kinase (CDK)-activating kinase (CAK) of vertebrates. Moreover, an in vitro pull-down assay showed that Os;CycH;1 specifically bound to R2 but not to other rice CDKs. When R2 was expressed in budding yeast CAK mutant, the suppression activity in terms of temperature-sensitivity was enhanced by co-expression with Os;cycH;1. Furthermore, in vitro kinase assay indicated that the kinase activities of R2 on CDKs and the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II were markedly elevated by binding to Os;CycH;1. Our results suggest that cyclin H is a regulatory subunit of CAK, which positively controls CDK- and CTD-kinase activities in plant cells.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11029700</PMID>
<DateCompleted><Year>2001</Year>
<Month>01</Month>
<Day>11</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>09</Month>
<Day>06</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0960-7412</ISSN>
<JournalIssue CitedMedium="Print"><Volume>24</Volume>
<Issue>1</Issue>
<PubDate><Year>2000</Year>
<Month>Oct</Month>
</PubDate>
</JournalIssue>
<Title>The Plant journal : for cell and molecular biology</Title>
<ISOAbbreviation>Plant J</ISOAbbreviation>
</Journal>
<ArticleTitle>Activation of CDK-activating kinase is dependent on interaction with H-type cyclins in plants.</ArticleTitle>
<Pagination><MedlinePgn>11-20</MedlinePgn>
</Pagination>
<Abstract><AbstractText>cDNAs encoding cyclin H homologs were isolated from poplar (Populus tremula X tremuloides) and rice (Oryza sativa) plants, and were designated Pt;cycH;1 and Os;cycH;1, respectively. The deduced amino-acid sequences showed 40-60% similarity to human cyclin H and Schizosaccharomyces pombe Mcs2, with higher similarity in the cyclin box region. While Pt;cycH;1 and Os;cycH;1 were expressed in all tissues examined, the transcripts accumulated abundantly in dividing cells. Expression of Os;cycH;1 was abundant in the S-phase in partially synchronized suspension cells, and was induced by submergence in internodes of deepwater rice. A yeast two-hybrid assay demonstrated that both Pt;CycH;1 and Os;CycH;1 were able to interact with rice R2 kinase, which is structurally and functionally similar to cyclin-dependent kinase (CDK)-activating kinase (CAK) of vertebrates. Moreover, an in vitro pull-down assay showed that Os;CycH;1 specifically bound to R2 but not to other rice CDKs. When R2 was expressed in budding yeast CAK mutant, the suppression activity in terms of temperature-sensitivity was enhanced by co-expression with Os;cycH;1. Furthermore, in vitro kinase assay indicated that the kinase activities of R2 on CDKs and the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II were markedly elevated by binding to Os;CycH;1. Our results suggest that cyclin H is a regulatory subunit of CAK, which positively controls CDK- and CTD-kinase activities in plant cells.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yamaguchi</LastName>
<ForeName>M</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Institute of Molecular and Cellular Biosciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-0032, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fabian</LastName>
<ForeName>T</ForeName>
<Initials>T</Initials>
</Author>
<Author ValidYN="Y"><LastName>Sauter</LastName>
<ForeName>M</ForeName>
<Initials>M</Initials>
</Author>
<Author ValidYN="Y"><LastName>Bhalerao</LastName>
<ForeName>R P</ForeName>
<Initials>RP</Initials>
</Author>
<Author ValidYN="Y"><LastName>Schrader</LastName>
<ForeName>J</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Sandberg</LastName>
<ForeName>G</ForeName>
<Initials>G</Initials>
</Author>
<Author ValidYN="Y"><LastName>Umeda</LastName>
<ForeName>M</ForeName>
<Initials>M</Initials>
</Author>
<Author ValidYN="Y"><LastName>Uchimiya</LastName>
<ForeName>H</ForeName>
<Initials>H</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Plant J</MedlineTA>
<NlmUniqueID>9207397</NlmUniqueID>
<ISSNLinking>0960-7412</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D016213">Cyclins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.22</RegistryNumber>
<NameOfSubstance UI="D042846">CDC2-CDC28 Kinases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.22</RegistryNumber>
<NameOfSubstance UI="C495894">CDK2 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.22</RegistryNumber>
<NameOfSubstance UI="D051357">Cyclin-Dependent Kinase 2</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.22</RegistryNumber>
<NameOfSubstance UI="D018844">Cyclin-Dependent Kinases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.22</RegistryNumber>
<NameOfSubstance UI="C066067">cyclin-dependent kinase-activating kinase</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>Plant J 2001 Feb;25(4):473</RefSource>
</CommentsCorrections>
</CommentsCorrectionsList>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D042846" MajorTopicYN="Y">CDC2-CDC28 Kinases</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002453" MajorTopicYN="Y">Cell Cycle</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051357" MajorTopicYN="N">Cyclin-Dependent Kinase 2</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018844" MajorTopicYN="N">Cyclin-Dependent Kinases</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016213" MajorTopicYN="N">Cyclins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012275" MajorTopicYN="N">Oryza</DescriptorName>
<QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName>
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<MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName>
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<MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName>
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<MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName>
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<MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName>
<QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName>
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</MedlineCitation>
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<Month>10</Month>
<Day>13</Day>
<Hour>11</Hour>
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<PubMedPubDate PubStatus="medline"><Year>2001</Year>
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<ArticleIdList><ArticleId IdType="pubmed">11029700</ArticleId>
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<ArticleId IdType="doi">10.1046/j.1365-313x.2000.00846.x</ArticleId>
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<affiliations><list><country><li>Japon</li>
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<region><li>Région de Kantō</li>
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<settlement><li>Tokyo</li>
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<orgName><li>Université de Tokyo</li>
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</list>
<tree><noCountry><name sortKey="Bhalerao, R P" sort="Bhalerao, R P" uniqKey="Bhalerao R" first="R P" last="Bhalerao">R P Bhalerao</name>
<name sortKey="Fabian, T" sort="Fabian, T" uniqKey="Fabian T" first="T" last="Fabian">T. Fabian</name>
<name sortKey="Sandberg, G" sort="Sandberg, G" uniqKey="Sandberg G" first="G" last="Sandberg">G. Sandberg</name>
<name sortKey="Sauter, M" sort="Sauter, M" uniqKey="Sauter M" first="M" last="Sauter">M. Sauter</name>
<name sortKey="Schrader, J" sort="Schrader, J" uniqKey="Schrader J" first="J" last="Schrader">J. Schrader</name>
<name sortKey="Uchimiya, H" sort="Uchimiya, H" uniqKey="Uchimiya H" first="H" last="Uchimiya">H. Uchimiya</name>
<name sortKey="Umeda, M" sort="Umeda, M" uniqKey="Umeda M" first="M" last="Umeda">M. Umeda</name>
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<country name="Japon"><region name="Région de Kantō"><name sortKey="Yamaguchi, M" sort="Yamaguchi, M" uniqKey="Yamaguchi M" first="M" last="Yamaguchi">M. Yamaguchi</name>
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