Elucidation of new structures in lignins of CAD- and COMT-deficient plants by NMR.
Identifieur interne : 004713 ( Main/Exploration ); précédent : 004712; suivant : 004714Elucidation of new structures in lignins of CAD- and COMT-deficient plants by NMR.
Auteurs : J. Ralph [États-Unis] ; C. Lapierre ; J M Marita ; H. Kim ; F. Lu ; R D Hatfield ; S. Ralph ; C. Chapple ; R. Franke ; M R Hemm ; J. Van Doorsselaere ; R R Sederoff ; D M O'Malley ; J T Scott ; J J Mackay ; N. Yahiaoui ; A. Boudet ; M. Pean ; G. Pilate ; L. Jouanin ; W. BoerjanSource :
- Phytochemistry [ 0031-9422 ] ; 2001.
Descripteurs français
- KwdFr :
- Alcohol oxidoreductases (déficit), Alcohol oxidoreductases (métabolisme), Cycadopsida (enzymologie), Cycadopsida (métabolisme), Lignine (biosynthèse), Lignine (composition chimique), Methyltransferases (déficit), Methyltransferases (métabolisme), Modèles chimiques (MeSH), Résonance magnétique nucléaire biomoléculaire (méthodes), Structure moléculaire (MeSH), Tabac (enzymologie), Tabac (métabolisme), Végétaux toxiques (MeSH).
- MESH :
- biosynthèse : Lignine.
- composition chimique : Lignine.
- déficit : Alcohol oxidoreductases, Methyltransferases.
- enzymologie : Cycadopsida, Tabac.
- métabolisme : Alcohol oxidoreductases, Cycadopsida, Methyltransferases, Tabac.
- méthodes : Résonance magnétique nucléaire biomoléculaire.
- Modèles chimiques, Structure moléculaire, Végétaux toxiques.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (deficiency), Alcohol Oxidoreductases (metabolism), Cycadopsida (enzymology), Cycadopsida (metabolism), Lignin (biosynthesis), Lignin (chemistry), Methyltransferases (deficiency), Methyltransferases (metabolism), Models, Chemical (MeSH), Molecular Structure (MeSH), Nuclear Magnetic Resonance, Biomolecular (methods), Plants, Toxic (MeSH), Tobacco (enzymology), Tobacco (metabolism).
- MESH :
- chemical , biosynthesis : Lignin.
- chemical , chemistry : Lignin.
- chemical , deficiency : Alcohol Oxidoreductases, Methyltransferases.
- chemical , metabolism : Alcohol Oxidoreductases, Methyltransferases.
- enzymology : Cycadopsida, Tobacco.
- metabolism : Cycadopsida, Tobacco.
- methods : Nuclear Magnetic Resonance, Biomolecular.
- Models, Chemical, Molecular Structure, Plants, Toxic.
Abstract
Studying lignin-biosynthetic-pathway mutants and transgenics provides insights into plant responses to perturbations of the lignification system, and enhances our understanding of normal lignification. When enzymes late in the pathway are downregulated, significant changes in the composition and structure of lignin may result. NMR spectroscopy provides powerful diagnostic tools for elucidating structures in the difficult lignin polymer, hinting at the chemical and biochemical changes that have occurred. COMT (caffeic acid O-methyl transferase) downregulation in poplar results in the incorporation of 5-hydroxyconiferyl alcohol into lignins via typical radical coupling reactions, but post-coupling quinone methide internal trapping reactions produce novel benzodioxane units in the lignin. CAD (cinnamyl alcohol dehydrogenase) downregulation results in the incorporation of the hydroxycinnamyl aldehyde monolignol precursors intimately into the polymer. Sinapyl aldehyde cross-couples 8-O-4 with both guaiacyl and syringyl units in the growing polymer, whereas coniferyl aldehyde cross-couples 8-O-4 only with syringyl units, reflecting simple chemical cross-coupling propensities. The incorporation of hydroxycinnamyl aldehyde and 5-hydroxyconiferyl alcohol monomers indicates that these monolignol intermediates are secreted to the cell wall for lignification. The recognition that novel units can incorporate into lignins portends significantly expanded opportunities for engineering the composition and consequent properties of lignin for improved utilization of valuable plant resources.
DOI: 10.1016/s0031-9422(01)00109-1
PubMed: 11423146
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Ralph</name><affiliation wicri:level="2"><nlm:affiliation>US Dairy Forage Research Center, USDA-Agricultural Research Service, 1925 Linden Drive West, Madison, WI 53706, USA. jralph@facstaff.wisc.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>US Dairy Forage Research Center, USDA-Agricultural Research Service, 1925 Linden Drive West, Madison, WI 53706</wicri:regionArea><placeName><region type="state">Wisconsin</region></placeName></affiliation></author><author><name sortKey="Lapierre, C" sort="Lapierre, C" uniqKey="Lapierre C" first="C" last="Lapierre">C. Lapierre</name></author><author><name sortKey="Marita, J M" sort="Marita, J M" uniqKey="Marita J" first="J M" last="Marita">J M Marita</name></author><author><name sortKey="Kim, H" sort="Kim, H" uniqKey="Kim H" first="H" last="Kim">H. Kim</name></author><author><name sortKey="Lu, F" sort="Lu, F" uniqKey="Lu F" first="F" last="Lu">F. Lu</name></author><author><name sortKey="Hatfield, R D" sort="Hatfield, R D" uniqKey="Hatfield R" first="R D" last="Hatfield">R D Hatfield</name></author><author><name sortKey="Ralph, S" sort="Ralph, S" uniqKey="Ralph S" first="S" last="Ralph">S. Ralph</name></author><author><name sortKey="Chapple, C" sort="Chapple, C" uniqKey="Chapple C" first="C" last="Chapple">C. Chapple</name></author><author><name sortKey="Franke, R" sort="Franke, R" uniqKey="Franke R" first="R" last="Franke">R. Franke</name></author><author><name sortKey="Hemm, M R" sort="Hemm, M R" uniqKey="Hemm M" first="M R" last="Hemm">M R Hemm</name></author><author><name sortKey="Van Doorsselaere, J" sort="Van Doorsselaere, J" uniqKey="Van Doorsselaere J" first="J" last="Van Doorsselaere">J. Van Doorsselaere</name></author><author><name sortKey="Sederoff, R R" sort="Sederoff, R R" uniqKey="Sederoff R" first="R R" last="Sederoff">R R Sederoff</name></author><author><name sortKey="O Malley, D M" sort="O Malley, D M" uniqKey="O Malley D" first="D M" last="O'Malley">D M O'Malley</name></author><author><name sortKey="Scott, J T" sort="Scott, J T" uniqKey="Scott J" first="J T" last="Scott">J T Scott</name></author><author><name sortKey="Mackay, J J" sort="Mackay, J J" uniqKey="Mackay J" first="J J" last="Mackay">J J Mackay</name></author><author><name sortKey="Yahiaoui, N" sort="Yahiaoui, N" uniqKey="Yahiaoui N" first="N" last="Yahiaoui">N. Yahiaoui</name></author><author><name sortKey="Boudet, A" sort="Boudet, A" uniqKey="Boudet A" first="A" last="Boudet">A. Boudet</name></author><author><name sortKey="Pean, M" sort="Pean, M" uniqKey="Pean M" first="M" last="Pean">M. Pean</name></author><author><name sortKey="Pilate, G" sort="Pilate, G" uniqKey="Pilate G" first="G" last="Pilate">G. Pilate</name></author><author><name sortKey="Jouanin, L" sort="Jouanin, L" uniqKey="Jouanin L" first="L" last="Jouanin">L. Jouanin</name></author><author><name sortKey="Boerjan, W" sort="Boerjan, W" uniqKey="Boerjan W" first="W" last="Boerjan">W. Boerjan</name></author></analytic><series><title level="j">Phytochemistry</title><idno type="ISSN">0031-9422</idno><imprint><date when="2001" type="published">2001</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (deficiency)</term><term>Alcohol Oxidoreductases (metabolism)</term><term>Cycadopsida (enzymology)</term><term>Cycadopsida (metabolism)</term><term>Lignin (biosynthesis)</term><term>Lignin (chemistry)</term><term>Methyltransferases (deficiency)</term><term>Methyltransferases (metabolism)</term><term>Models, Chemical (MeSH)</term><term>Molecular Structure (MeSH)</term><term>Nuclear Magnetic Resonance, Biomolecular (methods)</term><term>Plants, Toxic (MeSH)</term><term>Tobacco (enzymology)</term><term>Tobacco (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcohol oxidoreductases (déficit)</term><term>Alcohol oxidoreductases (métabolisme)</term><term>Cycadopsida (enzymologie)</term><term>Cycadopsida (métabolisme)</term><term>Lignine (biosynthèse)</term><term>Lignine (composition chimique)</term><term>Methyltransferases (déficit)</term><term>Methyltransferases (métabolisme)</term><term>Modèles chimiques (MeSH)</term><term>Résonance magnétique nucléaire biomoléculaire (méthodes)</term><term>Structure moléculaire (MeSH)</term><term>Tabac (enzymologie)</term><term>Tabac (métabolisme)</term><term>Végétaux toxiques (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Methyltransferases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Methyltransferases</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Lignine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Lignine</term></keywords><keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Methyltransferases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Cycadopsida</term><term>Tabac</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cycadopsida</term><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cycadopsida</term><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Nuclear Magnetic Resonance, Biomolecular</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Cycadopsida</term><term>Methyltransferases</term><term>Tabac</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Résonance magnétique nucléaire biomoléculaire</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Models, Chemical</term><term>Molecular Structure</term><term>Plants, Toxic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Modèles chimiques</term><term>Structure moléculaire</term><term>Végétaux toxiques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Studying lignin-biosynthetic-pathway mutants and transgenics provides insights into plant responses to perturbations of the lignification system, and enhances our understanding of normal lignification. When enzymes late in the pathway are downregulated, significant changes in the composition and structure of lignin may result. NMR spectroscopy provides powerful diagnostic tools for elucidating structures in the difficult lignin polymer, hinting at the chemical and biochemical changes that have occurred. COMT (caffeic acid O-methyl transferase) downregulation in poplar results in the incorporation of 5-hydroxyconiferyl alcohol into lignins via typical radical coupling reactions, but post-coupling quinone methide internal trapping reactions produce novel benzodioxane units in the lignin. CAD (cinnamyl alcohol dehydrogenase) downregulation results in the incorporation of the hydroxycinnamyl aldehyde monolignol precursors intimately into the polymer. Sinapyl aldehyde cross-couples 8-O-4 with both guaiacyl and syringyl units in the growing polymer, whereas coniferyl aldehyde cross-couples 8-O-4 only with syringyl units, reflecting simple chemical cross-coupling propensities. The incorporation of hydroxycinnamyl aldehyde and 5-hydroxyconiferyl alcohol monomers indicates that these monolignol intermediates are secreted to the cell wall for lignification. The recognition that novel units can incorporate into lignins portends significantly expanded opportunities for engineering the composition and consequent properties of lignin for improved utilization of valuable plant resources.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11423146</PMID><DateCompleted><Year>2001</Year><Month>10</Month><Day>04</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0031-9422</ISSN><JournalIssue CitedMedium="Print"><Volume>57</Volume><Issue>6</Issue><PubDate><Year>2001</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Phytochemistry</Title><ISOAbbreviation>Phytochemistry</ISOAbbreviation></Journal><ArticleTitle>Elucidation of new structures in lignins of CAD- and COMT-deficient plants by NMR.</ArticleTitle><Pagination><MedlinePgn>993-1003</MedlinePgn></Pagination><Abstract><AbstractText>Studying lignin-biosynthetic-pathway mutants and transgenics provides insights into plant responses to perturbations of the lignification system, and enhances our understanding of normal lignification. When enzymes late in the pathway are downregulated, significant changes in the composition and structure of lignin may result. NMR spectroscopy provides powerful diagnostic tools for elucidating structures in the difficult lignin polymer, hinting at the chemical and biochemical changes that have occurred. COMT (caffeic acid O-methyl transferase) downregulation in poplar results in the incorporation of 5-hydroxyconiferyl alcohol into lignins via typical radical coupling reactions, but post-coupling quinone methide internal trapping reactions produce novel benzodioxane units in the lignin. CAD (cinnamyl alcohol dehydrogenase) downregulation results in the incorporation of the hydroxycinnamyl aldehyde monolignol precursors intimately into the polymer. Sinapyl aldehyde cross-couples 8-O-4 with both guaiacyl and syringyl units in the growing polymer, whereas coniferyl aldehyde cross-couples 8-O-4 only with syringyl units, reflecting simple chemical cross-coupling propensities. The incorporation of hydroxycinnamyl aldehyde and 5-hydroxyconiferyl alcohol monomers indicates that these monolignol intermediates are secreted to the cell wall for lignification. The recognition that novel units can incorporate into lignins portends significantly expanded opportunities for engineering the composition and consequent properties of lignin for improved utilization of valuable plant resources.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ralph</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>US Dairy Forage Research Center, USDA-Agricultural Research Service, 1925 Linden Drive West, Madison, WI 53706, USA. jralph@facstaff.wisc.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lapierre</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Marita</LastName><ForeName>J M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Hatfield</LastName><ForeName>R D</ForeName><Initials>RD</Initials></Author><Author ValidYN="Y"><LastName>Ralph</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Chapple</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Franke</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Hemm</LastName><ForeName>M R</ForeName><Initials>MR</Initials></Author><Author ValidYN="Y"><LastName>Van Doorsselaere</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Sederoff</LastName><ForeName>R R</ForeName><Initials>RR</Initials></Author><Author ValidYN="Y"><LastName>O'Malley</LastName><ForeName>D M</ForeName><Initials>DM</Initials></Author><Author ValidYN="Y"><LastName>Scott</LastName><ForeName>J T</ForeName><Initials>JT</Initials></Author><Author ValidYN="Y"><LastName>MacKay</LastName><ForeName>J J</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Yahiaoui</LastName><ForeName>N</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Boudet</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Pean</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Pilate</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Jouanin</LastName><ForeName>L</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Boerjan</LastName><ForeName>W</ForeName><Initials>W</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM45344-07</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><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><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Phytochemistry</MedlineTA><NlmUniqueID>0151434</NlmUniqueID><ISSNLinking>0031-9422</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.195</RegistryNumber><NameOfSubstance UI="C018656">cinnamyl alcohol dehydrogenase</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="D000429" MajorTopicYN="N">Alcohol Oxidoreductases</DescriptorName><QualifierName UI="Q000172" MajorTopicYN="N">deficiency</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032462" MajorTopicYN="N">Cycadopsida</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000172" MajorTopicYN="N">deficiency</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="N">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019906" MajorTopicYN="N">Nuclear Magnetic Resonance, Biomolecular</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010947" MajorTopicYN="Y">Plants, Toxic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014026" MajorTopicYN="N">Tobacco</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>6</Month><Day>26</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>10</Month><Day>5</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>6</Month><Day>26</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11423146</ArticleId><ArticleId IdType="pii">S0031942201001091</ArticleId><ArticleId IdType="doi">10.1016/s0031-9422(01)00109-1</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Wisconsin</li></region></list><tree><noCountry><name sortKey="Boerjan, W" sort="Boerjan, W" uniqKey="Boerjan W" first="W" last="Boerjan">W. Boerjan</name><name sortKey="Boudet, A" sort="Boudet, A" uniqKey="Boudet A" first="A" last="Boudet">A. Boudet</name><name sortKey="Chapple, C" sort="Chapple, C" uniqKey="Chapple C" first="C" last="Chapple">C. Chapple</name><name sortKey="Franke, R" sort="Franke, R" uniqKey="Franke R" first="R" last="Franke">R. Franke</name><name sortKey="Hatfield, R D" sort="Hatfield, R D" uniqKey="Hatfield R" first="R D" last="Hatfield">R D Hatfield</name><name sortKey="Hemm, M R" sort="Hemm, M R" uniqKey="Hemm M" first="M R" last="Hemm">M R Hemm</name><name sortKey="Jouanin, L" sort="Jouanin, L" uniqKey="Jouanin L" first="L" last="Jouanin">L. Jouanin</name><name sortKey="Kim, H" sort="Kim, H" uniqKey="Kim H" first="H" last="Kim">H. Kim</name><name sortKey="Lapierre, C" sort="Lapierre, C" uniqKey="Lapierre C" first="C" last="Lapierre">C. Lapierre</name><name sortKey="Lu, F" sort="Lu, F" uniqKey="Lu F" first="F" last="Lu">F. Lu</name><name sortKey="Mackay, J J" sort="Mackay, J J" uniqKey="Mackay J" first="J J" last="Mackay">J J Mackay</name><name sortKey="Marita, J M" sort="Marita, J M" uniqKey="Marita J" first="J M" last="Marita">J M Marita</name><name sortKey="O Malley, D M" sort="O Malley, D M" uniqKey="O Malley D" first="D M" last="O'Malley">D M O'Malley</name><name sortKey="Pean, M" sort="Pean, M" uniqKey="Pean M" first="M" last="Pean">M. Pean</name><name sortKey="Pilate, G" sort="Pilate, G" uniqKey="Pilate G" first="G" last="Pilate">G. Pilate</name><name sortKey="Ralph, S" sort="Ralph, S" uniqKey="Ralph S" first="S" last="Ralph">S. Ralph</name><name sortKey="Scott, J T" sort="Scott, J T" uniqKey="Scott J" first="J T" last="Scott">J T Scott</name><name sortKey="Sederoff, R R" sort="Sederoff, R R" uniqKey="Sederoff R" first="R R" last="Sederoff">R R Sederoff</name><name sortKey="Van Doorsselaere, J" sort="Van Doorsselaere, J" uniqKey="Van Doorsselaere J" first="J" last="Van Doorsselaere">J. Van Doorsselaere</name><name sortKey="Yahiaoui, N" sort="Yahiaoui, N" uniqKey="Yahiaoui N" first="N" last="Yahiaoui">N. Yahiaoui</name></noCountry><country name="États-Unis"><region name="Wisconsin"><name sortKey="Ralph, J" sort="Ralph, J" uniqKey="Ralph J" first="J" last="Ralph">J. Ralph</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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