Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant.
Identifieur interne : 000856 ( Main/Curation ); précédent : 000855; suivant : 000857Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant.
Auteurs : C. Merle [France] ; S. Perret ; T. Lacour ; V. Jonval ; S. Hudaverdian ; R. Garrone ; F. Ruggiero ; M. TheisenSource :
- FEBS letters [ 0014-5793 ] ; 2002.
Descripteurs français
- KwdFr :
- Acides aminés (analyse), Agrobacterium tumefaciens (métabolisme), Chromatographie en phase liquide à haute performance (MeSH), Collagène de type I (génétique), Collagène de type I (isolement et purification), Collagène de type I (métabolisme), Conformation des protéines (MeSH), Dichroïsme circulaire (MeSH), Dosage biologique (MeSH), Expression des gènes (MeSH), Humains (MeSH), Hydroxylation (MeSH), Pepsine A (composition chimique), Procollagen-Proline Dioxygenase (génétique), Procollagen-Proline Dioxygenase (métabolisme), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), RT-PCR (MeSH), Tabac (composition chimique), Tabac (génétique), Tabac (métabolisme), Température (MeSH), Transformation génétique (MeSH), Végétaux génétiquement modifiés (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- analyse : Acides aminés.
- composition chimique : Pepsine A, Tabac.
- génétique : Collagène de type I, Procollagen-Proline Dioxygenase, Protéines de fusion recombinantes, Protéines recombinantes, Tabac.
- isolement et purification : Collagène de type I.
- métabolisme : Agrobacterium tumefaciens, Collagène de type I, Procollagen-Proline Dioxygenase, Protéines de fusion recombinantes, Protéines recombinantes, Tabac.
- Chromatographie en phase liquide à haute performance, Conformation des protéines, Dichroïsme circulaire, Dosage biologique, Expression des gènes, Humains, Hydroxylation, RT-PCR, Température, Transformation génétique, Végétaux génétiquement modifiés, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Agrobacterium tumefaciens (metabolism), Amino Acids (analysis), Biological Assay (MeSH), Chromatography, High Pressure Liquid (MeSH), Circular Dichroism (MeSH), Collagen Type I (genetics), Collagen Type I (isolation & purification), Collagen Type I (metabolism), Electrophoresis, Polyacrylamide Gel (MeSH), Gene Expression (MeSH), Humans (MeSH), Hydroxylation (MeSH), Pepsin A (chemistry), Plants, Genetically Modified (MeSH), Procollagen-Proline Dioxygenase (genetics), Procollagen-Proline Dioxygenase (metabolism), Protein Conformation (MeSH), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Temperature (MeSH), Tobacco (chemistry), Tobacco (genetics), Tobacco (metabolism), Transformation, Genetic (MeSH).
- MESH :
- chemical , analysis : Amino Acids.
- chemical , chemistry : Pepsin A.
- chemical , genetics : Collagen Type I, Procollagen-Proline Dioxygenase, Recombinant Fusion Proteins, Recombinant Proteins.
- chemical , isolation & purification : Collagen Type I.
- chemistry : Tobacco.
- genetics : Tobacco.
- metabolism : Agrobacterium tumefaciens, Collagen Type I, Procollagen-Proline Dioxygenase, Recombinant Fusion Proteins, Recombinant Proteins, Tobacco.
- Biological Assay, Chromatography, High Pressure Liquid, Circular Dichroism, Electrophoresis, Polyacrylamide Gel, Gene Expression, Humans, Hydroxylation, Plants, Genetically Modified, Protein Conformation, Reverse Transcriptase Polymerase Chain Reaction, Temperature, Transformation, Genetic.
Abstract
Potential contamination of animal-derived collagen with pathogens has led to the demand for safe recombinant sources of this complex molecule. In continuation of our previous work [Ruggiero et al. (2000) FEBS Lett. 469, 132-136], here we show that it is possible to produce recombinant hydroxylated homotrimeric collagen in tobacco plants that are co-transformed with a human type I collagen and a chimeric proline-4-hydroxylase (P4H). This is to our knowledge the first time that transient expression in tobacco was used to improve the quality of a recombinant protein produced in plants through co-expression with an animal cell-derived modifying enzyme. We demonstrated the functionality of the new chimeric P4H and thus improved the thermal stability of recombinant collagen I from plants to 37 degrees C.
DOI: 10.1016/s0014-5793(02)02452-3
PubMed: 11943205
Links toward previous steps (curation, corpus...)
- to stream Main, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000856
Links to Exploration step
pubmed:11943205Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant.</title><author><name sortKey="Merle, C" sort="Merle, C" uniqKey="Merle C" first="C" last="Merle">C. Merle</name><affiliation wicri:level="1"><nlm:affiliation>Meristem Therapeutics, 8 rue des Frères Lumière, 63100, Clermont-Ferrand, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Meristem Therapeutics, 8 rue des Frères Lumière, 63100, Clermont-Ferrand</wicri:regionArea></affiliation></author><author><name sortKey="Perret, S" sort="Perret, S" uniqKey="Perret S" first="S" last="Perret">S. Perret</name></author><author><name sortKey="Lacour, T" sort="Lacour, T" uniqKey="Lacour T" first="T" last="Lacour">T. Lacour</name></author><author><name sortKey="Jonval, V" sort="Jonval, V" uniqKey="Jonval V" first="V" last="Jonval">V. Jonval</name></author><author><name sortKey="Hudaverdian, S" sort="Hudaverdian, S" uniqKey="Hudaverdian S" first="S" last="Hudaverdian">S. Hudaverdian</name></author><author><name sortKey="Garrone, R" sort="Garrone, R" uniqKey="Garrone R" first="R" last="Garrone">R. Garrone</name></author><author><name sortKey="Ruggiero, F" sort="Ruggiero, F" uniqKey="Ruggiero F" first="F" last="Ruggiero">F. Ruggiero</name></author><author><name sortKey="Theisen, M" sort="Theisen, M" uniqKey="Theisen M" first="M" last="Theisen">M. Theisen</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:11943205</idno><idno type="pmid">11943205</idno><idno type="doi">10.1016/s0014-5793(02)02452-3</idno><idno type="wicri:Area/Main/Corpus">000856</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000856</idno><idno type="wicri:Area/Main/Curation">000856</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000856</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant.</title><author><name sortKey="Merle, C" sort="Merle, C" uniqKey="Merle C" first="C" last="Merle">C. Merle</name><affiliation wicri:level="1"><nlm:affiliation>Meristem Therapeutics, 8 rue des Frères Lumière, 63100, Clermont-Ferrand, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Meristem Therapeutics, 8 rue des Frères Lumière, 63100, Clermont-Ferrand</wicri:regionArea></affiliation></author><author><name sortKey="Perret, S" sort="Perret, S" uniqKey="Perret S" first="S" last="Perret">S. Perret</name></author><author><name sortKey="Lacour, T" sort="Lacour, T" uniqKey="Lacour T" first="T" last="Lacour">T. Lacour</name></author><author><name sortKey="Jonval, V" sort="Jonval, V" uniqKey="Jonval V" first="V" last="Jonval">V. Jonval</name></author><author><name sortKey="Hudaverdian, S" sort="Hudaverdian, S" uniqKey="Hudaverdian S" first="S" last="Hudaverdian">S. Hudaverdian</name></author><author><name sortKey="Garrone, R" sort="Garrone, R" uniqKey="Garrone R" first="R" last="Garrone">R. Garrone</name></author><author><name sortKey="Ruggiero, F" sort="Ruggiero, F" uniqKey="Ruggiero F" first="F" last="Ruggiero">F. Ruggiero</name></author><author><name sortKey="Theisen, M" sort="Theisen, M" uniqKey="Theisen M" first="M" last="Theisen">M. Theisen</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Agrobacterium tumefaciens (metabolism)</term><term>Amino Acids (analysis)</term><term>Biological Assay (MeSH)</term><term>Chromatography, High Pressure Liquid (MeSH)</term><term>Circular Dichroism (MeSH)</term><term>Collagen Type I (genetics)</term><term>Collagen Type I (isolation & purification)</term><term>Collagen Type I (metabolism)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Gene Expression (MeSH)</term><term>Humans (MeSH)</term><term>Hydroxylation (MeSH)</term><term>Pepsin A (chemistry)</term><term>Plants, Genetically Modified (MeSH)</term><term>Procollagen-Proline Dioxygenase (genetics)</term><term>Procollagen-Proline Dioxygenase (metabolism)</term><term>Protein Conformation (MeSH)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Reverse Transcriptase Polymerase Chain Reaction (MeSH)</term><term>Temperature (MeSH)</term><term>Tobacco (chemistry)</term><term>Tobacco (genetics)</term><term>Tobacco (metabolism)</term><term>Transformation, Genetic (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (analyse)</term><term>Agrobacterium tumefaciens (métabolisme)</term><term>Chromatographie en phase liquide à haute performance (MeSH)</term><term>Collagène de type I (génétique)</term><term>Collagène de type I (isolement et purification)</term><term>Collagène de type I (métabolisme)</term><term>Conformation des protéines (MeSH)</term><term>Dichroïsme circulaire (MeSH)</term><term>Dosage biologique (MeSH)</term><term>Expression des gènes (MeSH)</term><term>Humains (MeSH)</term><term>Hydroxylation (MeSH)</term><term>Pepsine A (composition chimique)</term><term>Procollagen-Proline Dioxygenase (génétique)</term><term>Procollagen-Proline Dioxygenase (métabolisme)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>RT-PCR (MeSH)</term><term>Tabac (composition chimique)</term><term>Tabac (génétique)</term><term>Tabac (métabolisme)</term><term>Température (MeSH)</term><term>Transformation génétique (MeSH)</term><term>Végétaux génétiquement modifiés (MeSH)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Amino Acids</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Pepsin A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Collagen Type I</term><term>Procollagen-Proline Dioxygenase</term><term>Recombinant Fusion Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Collagen Type I</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Acides aminés</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Pepsine A</term><term>Tabac</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Collagène de type I</term><term>Procollagen-Proline Dioxygenase</term><term>Protéines de fusion recombinantes</term><term>Protéines recombinantes</term><term>Tabac</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Collagène de type I</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Agrobacterium tumefaciens</term><term>Collagen Type I</term><term>Procollagen-Proline Dioxygenase</term><term>Recombinant Fusion Proteins</term><term>Recombinant Proteins</term><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Agrobacterium tumefaciens</term><term>Collagène de type I</term><term>Procollagen-Proline Dioxygenase</term><term>Protéines de fusion recombinantes</term><term>Protéines recombinantes</term><term>Tabac</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biological Assay</term><term>Chromatography, High Pressure Liquid</term><term>Circular Dichroism</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Gene Expression</term><term>Humans</term><term>Hydroxylation</term><term>Plants, Genetically Modified</term><term>Protein Conformation</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>Temperature</term><term>Transformation, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie en phase liquide à haute performance</term><term>Conformation des protéines</term><term>Dichroïsme circulaire</term><term>Dosage biologique</term><term>Expression des gènes</term><term>Humains</term><term>Hydroxylation</term><term>RT-PCR</term><term>Température</term><term>Transformation génétique</term><term>Végétaux génétiquement modifiés</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Potential contamination of animal-derived collagen with pathogens has led to the demand for safe recombinant sources of this complex molecule. In continuation of our previous work [Ruggiero et al. (2000) FEBS Lett. 469, 132-136], here we show that it is possible to produce recombinant hydroxylated homotrimeric collagen in tobacco plants that are co-transformed with a human type I collagen and a chimeric proline-4-hydroxylase (P4H). This is to our knowledge the first time that transient expression in tobacco was used to improve the quality of a recombinant protein produced in plants through co-expression with an animal cell-derived modifying enzyme. We demonstrated the functionality of the new chimeric P4H and thus improved the thermal stability of recombinant collagen I from plants to 37 degrees C.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11943205</PMID><DateCompleted><Year>2002</Year><Month>05</Month><Day>10</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>515</Volume><Issue>1-3</Issue><PubDate><Year>2002</Year><Month>Mar</Month><Day>27</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant.</ArticleTitle><Pagination><MedlinePgn>114-8</MedlinePgn></Pagination><Abstract><AbstractText>Potential contamination of animal-derived collagen with pathogens has led to the demand for safe recombinant sources of this complex molecule. In continuation of our previous work [Ruggiero et al. (2000) FEBS Lett. 469, 132-136], here we show that it is possible to produce recombinant hydroxylated homotrimeric collagen in tobacco plants that are co-transformed with a human type I collagen and a chimeric proline-4-hydroxylase (P4H). This is to our knowledge the first time that transient expression in tobacco was used to improve the quality of a recombinant protein produced in plants through co-expression with an animal cell-derived modifying enzyme. We demonstrated the functionality of the new chimeric P4H and thus improved the thermal stability of recombinant collagen I from plants to 37 degrees C.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Merle</LastName><ForeName>C</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Meristem Therapeutics, 8 rue des Frères Lumière, 63100, Clermont-Ferrand, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Perret</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Lacour</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Jonval</LastName><ForeName>V</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Hudaverdian</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Garrone</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Ruggiero</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Theisen</LastName><ForeName>M</ForeName><Initials>M</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>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024042">Collagen Type I</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.11.2</RegistryNumber><NameOfSubstance UI="D011393">Procollagen-Proline Dioxygenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.23.1</RegistryNumber><NameOfSubstance UI="D010434">Pepsin A</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D016960" MajorTopicYN="N">Agrobacterium tumefaciens</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001681" MajorTopicYN="N">Biological Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D024042" MajorTopicYN="N">Collagen Type I</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006900" MajorTopicYN="N">Hydroxylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010434" MajorTopicYN="N">Pepsin A</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D030821" MajorTopicYN="N">Plants, Genetically Modified</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011393" MajorTopicYN="N">Procollagen-Proline Dioxygenase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020133" MajorTopicYN="N">Reverse Transcriptase Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014026" MajorTopicYN="N">Tobacco</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="D014170" MajorTopicYN="N">Transformation, Genetic</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>4</Month><Day>12</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>5</Month><Day>11</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>4</Month><Day>12</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11943205</ArticleId><ArticleId IdType="pii">S0014579302024523</ArticleId><ArticleId IdType="doi">10.1016/s0014-5793(02)02452-3</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/AgrobacTransV1/Data/Main/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000856 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Curation/biblio.hfd -nk 000856 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= AgrobacTransV1
|flux= Main
|étape= Curation
|type= RBID
|clé= pubmed:11943205
|texte= Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Curation/RBID.i -Sk "pubmed:11943205" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Curation/biblio.hfd \
| NlmPubMed2Wicri -a AgrobacTransV1
| This area was generated with Dilib version V0.6.38. |  |