5-hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation, a new view of monolignol biosynthesis in angiosperms.
Identifieur interne : 004841 ( Main/Exploration ); précédent : 004840; suivant : 0048425-hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation, a new view of monolignol biosynthesis in angiosperms.
Auteurs : L. Li [États-Unis] ; J L Popko ; T. Umezawa ; V L ChiangSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2000.
Descripteurs français
- KwdFr :
- Acides coumariques (métabolisme), Acroléine (analogues et dérivés), Acroléine (métabolisme), Acroléine (pharmacologie), Aldéhydes (pharmacologie), Antienzymes (pharmacologie), Catéchols (métabolisme), Catéchols (pharmacologie), Cinétique (MeSH), Cytochrome P-450 enzyme system (métabolisme), Escherichia coli (MeSH), Hydroxylation (MeSH), Lignine (biosynthèse), Magnoliopsida (enzymologie), Magnoliopsida (métabolisme), Methyltransferases (métabolisme), Microsomes (enzymologie), Mixed function oxygenases (métabolisme), Méthylation (MeSH), Protéines recombinantes (métabolisme), Protéines végétales (MeSH), Spécificité du substrat (MeSH), Structure moléculaire (MeSH).
- MESH :
- analogues et dérivés : Acroléine.
- biosynthèse : Lignine.
- enzymologie : Magnoliopsida, Microsomes.
- métabolisme : Acides coumariques, Acroléine, Catéchols, Cytochrome P-450 enzyme system, Magnoliopsida, Methyltransferases, Mixed function oxygenases, Protéines recombinantes.
- pharmacologie : Acroléine, Aldéhydes, Antienzymes, Catéchols.
- Cinétique, Escherichia coli, Hydroxylation, Méthylation, Protéines végétales, Spécificité du substrat, Structure moléculaire.
English descriptors
- KwdEn :
- Acrolein (analogs & derivatives), Acrolein (metabolism), Acrolein (pharmacology), Aldehydes (pharmacology), Catechols (metabolism), Catechols (pharmacology), Coumaric Acids (metabolism), Cytochrome P-450 Enzyme System (metabolism), Enzyme Inhibitors (pharmacology), Escherichia coli (MeSH), Hydroxylation (MeSH), Kinetics (MeSH), Lignin (biosynthesis), Magnoliopsida (enzymology), Magnoliopsida (metabolism), Methylation (MeSH), Methyltransferases (metabolism), Microsomes (enzymology), Mixed Function Oxygenases (metabolism), Molecular Structure (MeSH), Plant Proteins (MeSH), Recombinant Proteins (metabolism), Substrate Specificity (MeSH).
- MESH :
- chemical , analogs & derivatives : Acrolein.
- chemical , biosynthesis : Lignin.
- chemical , metabolism : Acrolein, Catechols, Coumaric Acids, Cytochrome P-450 Enzyme System, Methyltransferases, Mixed Function Oxygenases, Recombinant Proteins.
- chemical , pharmacology : Acrolein, Aldehydes, Catechols, Enzyme Inhibitors.
- enzymology : Magnoliopsida, Microsomes.
- metabolism : Magnoliopsida.
- Escherichia coli, Hydroxylation, Kinetics, Methylation, Molecular Structure, Plant Proteins, Substrate Specificity.
Abstract
S-Adenosyl-L-methionine-dependent caffeate O-methyltransferase (COMT, EC 2.1.1.6) has traditionally been thought to catalyze the methylation of caffeate and 5- hydroxyferulate for the biosynthesis of syringyl monolignol, a lignin constituent of angiosperm wood that enables efficient lignin degradation for cellulose production. However, recent recognition that coniferyl aldehyde prevents 5-hydroxyferulate biosynthesis in lignifying tissue, and that the hydroxylated form of coniferyl aldehyde, 5-hydroxyconiferyl aldehyde, is an alternative COMT substrate, demands a re-evaluation of the role of COMT during monolignol biosynthesis. Based on recombinant aspen (Populus tremuloides) COMT enzyme kinetics coupled with mass spectrometry analysis, this study establishes for the first time that COMT is in fact a 5-hydroxyconiferyl aldehyde O-methyltransferase (AldOMT), and that 5-hydroxyconiferyl aldehyde is both the preferred AldOMT substrate and an inhibitor of caffeate and 5-hydroxyferulate methylation, as measured by K(m) and K(i) values. 5-Hydroxyconiferyl aldehyde also inhibited the caffeate and 5-hydroxyferulate methylation activities of xylem proteins from various angiosperm tree species. The evidence that syringyl monolignol biosynthesis is independent of caffeate and 5-hydroxyferulate methylation supports our previous discovery that coniferyl aldehyde prevents ferulate 5-hydroxylation and at the same time ensures a coniferyl aldehyde 5-hydroxylase (CAld5H)-mediated biosynthesis of 5-hydroxyconiferyl aldehyde. Together, our results provide conclusive evidence for the presence of a CAld5H/AldOMT-catalyzed coniferyl aldehyde 5-hydroxylation/methylation pathway that directs syringyl monolignol biosynthesis in angiosperms.
DOI: 10.1074/jbc.275.9.6537
PubMed: 10692459
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Li</name><affiliation wicri:level="1"><nlm:affiliation>Plant Biotechnology Research Center, School of Forestry and Wood Products, Michigan Technological University, Houghton, Michigan 49931, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Plant Biotechnology Research Center, School of Forestry and Wood Products, Michigan Technological University, Houghton, Michigan 49931</wicri:regionArea><wicri:noRegion>Michigan 49931</wicri:noRegion></affiliation></author><author><name sortKey="Popko, J L" sort="Popko, J L" uniqKey="Popko J" first="J L" last="Popko">J L Popko</name></author><author><name sortKey="Umezawa, T" sort="Umezawa, T" uniqKey="Umezawa T" first="T" last="Umezawa">T. 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Li</name><affiliation wicri:level="1"><nlm:affiliation>Plant Biotechnology Research Center, School of Forestry and Wood Products, Michigan Technological University, Houghton, Michigan 49931, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Plant Biotechnology Research Center, School of Forestry and Wood Products, Michigan Technological University, Houghton, Michigan 49931</wicri:regionArea><wicri:noRegion>Michigan 49931</wicri:noRegion></affiliation></author><author><name sortKey="Popko, J L" sort="Popko, J L" uniqKey="Popko J" first="J L" last="Popko">J L Popko</name></author><author><name sortKey="Umezawa, T" sort="Umezawa, T" uniqKey="Umezawa T" first="T" last="Umezawa">T. Umezawa</name></author><author><name sortKey="Chiang, V L" sort="Chiang, V L" uniqKey="Chiang V" first="V L" last="Chiang">V L Chiang</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acrolein (analogs & derivatives)</term><term>Acrolein (metabolism)</term><term>Acrolein (pharmacology)</term><term>Aldehydes (pharmacology)</term><term>Catechols (metabolism)</term><term>Catechols (pharmacology)</term><term>Coumaric Acids (metabolism)</term><term>Cytochrome P-450 Enzyme System (metabolism)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Escherichia coli (MeSH)</term><term>Hydroxylation (MeSH)</term><term>Kinetics (MeSH)</term><term>Lignin (biosynthesis)</term><term>Magnoliopsida (enzymology)</term><term>Magnoliopsida (metabolism)</term><term>Methylation (MeSH)</term><term>Methyltransferases (metabolism)</term><term>Microsomes (enzymology)</term><term>Mixed Function Oxygenases (metabolism)</term><term>Molecular Structure (MeSH)</term><term>Plant Proteins (MeSH)</term><term>Recombinant Proteins (metabolism)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides coumariques (métabolisme)</term><term>Acroléine (analogues et dérivés)</term><term>Acroléine (métabolisme)</term><term>Acroléine (pharmacologie)</term><term>Aldéhydes (pharmacologie)</term><term>Antienzymes (pharmacologie)</term><term>Catéchols (métabolisme)</term><term>Catéchols (pharmacologie)</term><term>Cinétique (MeSH)</term><term>Cytochrome P-450 enzyme system (métabolisme)</term><term>Escherichia coli (MeSH)</term><term>Hydroxylation (MeSH)</term><term>Lignine (biosynthèse)</term><term>Magnoliopsida (enzymologie)</term><term>Magnoliopsida (métabolisme)</term><term>Methyltransferases (métabolisme)</term><term>Microsomes (enzymologie)</term><term>Mixed function oxygenases (métabolisme)</term><term>Méthylation (MeSH)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines végétales (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Structure moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Acrolein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acrolein</term><term>Catechols</term><term>Coumaric Acids</term><term>Cytochrome P-450 Enzyme System</term><term>Methyltransferases</term><term>Mixed Function Oxygenases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Acrolein</term><term>Aldehydes</term><term>Catechols</term><term>Enzyme Inhibitors</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Acroléine</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Lignine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Magnoliopsida</term><term>Microsomes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Magnoliopsida</term><term>Microsomes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Magnoliopsida</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides coumariques</term><term>Acroléine</term><term>Catéchols</term><term>Cytochrome P-450 enzyme system</term><term>Magnoliopsida</term><term>Methyltransferases</term><term>Mixed function oxygenases</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acroléine</term><term>Aldéhydes</term><term>Antienzymes</term><term>Catéchols</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Escherichia coli</term><term>Hydroxylation</term><term>Kinetics</term><term>Methylation</term><term>Molecular Structure</term><term>Plant Proteins</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Escherichia coli</term><term>Hydroxylation</term><term>Méthylation</term><term>Protéines végétales</term><term>Spécificité du substrat</term><term>Structure moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">S-Adenosyl-L-methionine-dependent caffeate O-methyltransferase (COMT, EC 2.1.1.6) has traditionally been thought to catalyze the methylation of caffeate and 5- hydroxyferulate for the biosynthesis of syringyl monolignol, a lignin constituent of angiosperm wood that enables efficient lignin degradation for cellulose production. However, recent recognition that coniferyl aldehyde prevents 5-hydroxyferulate biosynthesis in lignifying tissue, and that the hydroxylated form of coniferyl aldehyde, 5-hydroxyconiferyl aldehyde, is an alternative COMT substrate, demands a re-evaluation of the role of COMT during monolignol biosynthesis. Based on recombinant aspen (Populus tremuloides) COMT enzyme kinetics coupled with mass spectrometry analysis, this study establishes for the first time that COMT is in fact a 5-hydroxyconiferyl aldehyde O-methyltransferase (AldOMT), and that 5-hydroxyconiferyl aldehyde is both the preferred AldOMT substrate and an inhibitor of caffeate and 5-hydroxyferulate methylation, as measured by K(m) and K(i) values. 5-Hydroxyconiferyl aldehyde also inhibited the caffeate and 5-hydroxyferulate methylation activities of xylem proteins from various angiosperm tree species. The evidence that syringyl monolignol biosynthesis is independent of caffeate and 5-hydroxyferulate methylation supports our previous discovery that coniferyl aldehyde prevents ferulate 5-hydroxylation and at the same time ensures a coniferyl aldehyde 5-hydroxylase (CAld5H)-mediated biosynthesis of 5-hydroxyconiferyl aldehyde. Together, our results provide conclusive evidence for the presence of a CAld5H/AldOMT-catalyzed coniferyl aldehyde 5-hydroxylation/methylation pathway that directs syringyl monolignol biosynthesis in angiosperms.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10692459</PMID><DateCompleted><Year>2000</Year><Month>04</Month><Day>03</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>275</Volume><Issue>9</Issue><PubDate><Year>2000</Year><Month>Mar</Month><Day>03</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>5-hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation, a new view of monolignol biosynthesis in angiosperms.</ArticleTitle><Pagination><MedlinePgn>6537-45</MedlinePgn></Pagination><Abstract><AbstractText>S-Adenosyl-L-methionine-dependent caffeate O-methyltransferase (COMT, EC 2.1.1.6) has traditionally been thought to catalyze the methylation of caffeate and 5- hydroxyferulate for the biosynthesis of syringyl monolignol, a lignin constituent of angiosperm wood that enables efficient lignin degradation for cellulose production. However, recent recognition that coniferyl aldehyde prevents 5-hydroxyferulate biosynthesis in lignifying tissue, and that the hydroxylated form of coniferyl aldehyde, 5-hydroxyconiferyl aldehyde, is an alternative COMT substrate, demands a re-evaluation of the role of COMT during monolignol biosynthesis. Based on recombinant aspen (Populus tremuloides) COMT enzyme kinetics coupled with mass spectrometry analysis, this study establishes for the first time that COMT is in fact a 5-hydroxyconiferyl aldehyde O-methyltransferase (AldOMT), and that 5-hydroxyconiferyl aldehyde is both the preferred AldOMT substrate and an inhibitor of caffeate and 5-hydroxyferulate methylation, as measured by K(m) and K(i) values. 5-Hydroxyconiferyl aldehyde also inhibited the caffeate and 5-hydroxyferulate methylation activities of xylem proteins from various angiosperm tree species. The evidence that syringyl monolignol biosynthesis is independent of caffeate and 5-hydroxyferulate methylation supports our previous discovery that coniferyl aldehyde prevents ferulate 5-hydroxylation and at the same time ensures a coniferyl aldehyde 5-hydroxylase (CAld5H)-mediated biosynthesis of 5-hydroxyconiferyl aldehyde. Together, our results provide conclusive evidence for the presence of a CAld5H/AldOMT-catalyzed coniferyl aldehyde 5-hydroxylation/methylation pathway that directs syringyl monolignol biosynthesis in angiosperms.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>L</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Plant Biotechnology Research Center, School of Forestry and Wood Products, Michigan Technological University, Houghton, Michigan 49931, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Popko</LastName><ForeName>J L</ForeName><Initials>JL</Initials></Author><Author ValidYN="Y"><LastName>Umezawa</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Chiang</LastName><ForeName>V L</ForeName><Initials>VL</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C405696">5-hydroxyconiferyl aldehyde</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000447">Aldehydes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002396">Catechols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003373">Coumaric Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>1782-55-4</RegistryNumber><NameOfSubstance UI="C071744">5-hydroxyferulic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>7864XYD3JJ</RegistryNumber><NameOfSubstance UI="D000171">Acrolein</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>9035-51-2</RegistryNumber><NameOfSubstance UI="D003577">Cytochrome P-450 Enzyme System</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D006899">Mixed Function Oxygenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.13.-</RegistryNumber><NameOfSubstance UI="C120927">Ald5H protein, Liquidambar styraciflua</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.68</RegistryNumber><NameOfSubstance UI="C019608">caffeate O-methyltransferase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000171" MajorTopicYN="N">Acrolein</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000447" MajorTopicYN="N">Aldehydes</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002396" MajorTopicYN="N">Catechols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003373" MajorTopicYN="N">Coumaric Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003577" MajorTopicYN="N">Cytochrome P-450 Enzyme System</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006900" MajorTopicYN="N">Hydroxylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019684" MajorTopicYN="N">Magnoliopsida</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008745" MajorTopicYN="N">Methylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008861" MajorTopicYN="N">Microsomes</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006899" MajorTopicYN="N">Mixed Function Oxygenases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="Y">Plant Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>2</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2000</Year><Month>2</Month><Day>29</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>2</Month><Day>29</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10692459</ArticleId><ArticleId IdType="doi">10.1074/jbc.275.9.6537</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Chiang, V L" sort="Chiang, V L" uniqKey="Chiang V" first="V L" last="Chiang">V L Chiang</name><name sortKey="Popko, J L" sort="Popko, J L" uniqKey="Popko J" first="J L" last="Popko">J L Popko</name><name sortKey="Umezawa, T" sort="Umezawa, T" uniqKey="Umezawa T" first="T" last="Umezawa">T. Umezawa</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Li, L" sort="Li, L" uniqKey="Li L" first="L" last="Li">L. Li</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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