Characterisation of the willow phenylalanine ammonia-lyase (PAL) gene family reveals expression differences compared with poplar.
Identifieur interne : 001C61 ( Main/Corpus ); précédent : 001C60; suivant : 001C62Characterisation of the willow phenylalanine ammonia-lyase (PAL) gene family reveals expression differences compared with poplar.
Auteurs : Femke De Jong ; Steven J. Hanley ; Michael H. Beale ; Angela KarpSource :
- Phytochemistry [ 1873-3700 ] ; 2015.
English descriptors
- KwdEn :
- Coenzyme A Ligases (metabolism), Flavonoids (biosynthesis), Isoenzymes (MeSH), Lignin (metabolism), Molecular Structure (MeSH), Phenylalanine (metabolism), Phenylalanine Ammonia-Lyase (genetics), Phenylalanine Ammonia-Lyase (metabolism), Populus (enzymology), Populus (genetics), Salicaceae (enzymology), Salicaceae (genetics), Salix (enzymology), Salix (genetics), Trans-Cinnamate 4-Monooxygenase (metabolism).
- MESH :
- chemical , biosynthesis : Flavonoids.
- chemical , genetics : Phenylalanine Ammonia-Lyase.
- chemical , metabolism : Coenzyme A Ligases, Lignin, Phenylalanine, Phenylalanine Ammonia-Lyase, Trans-Cinnamate 4-Monooxygenase.
- chemical : Isoenzymes.
- enzymology : Populus, Salicaceae, Salix.
- genetics : Populus, Salicaceae, Salix.
- Molecular Structure.
Abstract
Willow is an important biomass crop for the bioenergy industry, and therefore optimal growth with minimal effects of biotic and abiotic stress is essential. The phenylpropanoid pathway is responsible for the biosynthesis of not only lignin but also of flavonoids, condensed tannins, benzenoids and phenolic glycosides which all have a role in protecting the plant against biotic and abiotic stress. All products of the phenylpropanoid pathway are important for the healthy growth of short rotation cropping species such as willow. However, the phenylpropanoid pathway in willow remains largely uncharacterised. In the current study we identified and characterised five willow phenylalanine ammonia-lyase (PAL) genes, which encode enzymes that catalyse the deamination of l-phenylalanine to form trans-cinnamic acid, the entry point into the phenylpropanoid pathway. Willow PAL1, PAL2, PAL3 and PAL4 genes were orthologous to the poplar genes. However no orthologue of PAL5 appears to be present in willow. Moreover, two tandemly repeated PAL2 orthologues were identified in a single contig. Willow PALs show similar sub-cellular localisation to the poplar genes. However, the enzyme kinetics and gene expression of the willow PAL genes differed slightly, with willow PAL2 being more widely expressed than its poplar orthologues implying a wider role for PALs in the production of flavonoids, condensed tannins, benzenoids, and phenolic glycosides, in willow.
DOI: 10.1016/j.phytochem.2015.06.005
PubMed: 26070140
PubMed Central: PMC4560161
Links to Exploration step
pubmed:26070140Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Characterisation of the willow phenylalanine ammonia-lyase (PAL) gene family reveals expression differences compared with poplar.</title>
<author><name sortKey="De Jong, Femke" sort="De Jong, Femke" uniqKey="De Jong F" first="Femke" last="De Jong">Femke De Jong</name>
<affiliation><nlm:affiliation>AgroEcology Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: femke.dejong@rothamsted.ac.uk.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Hanley, Steven J" sort="Hanley, Steven J" uniqKey="Hanley S" first="Steven J" last="Hanley">Steven J. Hanley</name>
<affiliation><nlm:affiliation>AgroEcology Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: steve.hanley@rothamsted.ac.uk.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Beale, Michael H" sort="Beale, Michael H" uniqKey="Beale M" first="Michael H" last="Beale">Michael H. Beale</name>
<affiliation><nlm:affiliation>Plant Biology and Crop Sciences Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: mike.beale@rothamsted.ac.uk.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Karp, Angela" sort="Karp, Angela" uniqKey="Karp A" first="Angela" last="Karp">Angela Karp</name>
<affiliation><nlm:affiliation>AgroEcology Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: angela.karp@rothamsted.ac.uk.</nlm:affiliation>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2015">2015</date>
<idno type="RBID">pubmed:26070140</idno>
<idno type="pmid">26070140</idno>
<idno type="doi">10.1016/j.phytochem.2015.06.005</idno>
<idno type="pmc">PMC4560161</idno>
<idno type="wicri:Area/Main/Corpus">001C61</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001C61</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Characterisation of the willow phenylalanine ammonia-lyase (PAL) gene family reveals expression differences compared with poplar.</title>
<author><name sortKey="De Jong, Femke" sort="De Jong, Femke" uniqKey="De Jong F" first="Femke" last="De Jong">Femke De Jong</name>
<affiliation><nlm:affiliation>AgroEcology Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: femke.dejong@rothamsted.ac.uk.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Hanley, Steven J" sort="Hanley, Steven J" uniqKey="Hanley S" first="Steven J" last="Hanley">Steven J. Hanley</name>
<affiliation><nlm:affiliation>AgroEcology Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: steve.hanley@rothamsted.ac.uk.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Beale, Michael H" sort="Beale, Michael H" uniqKey="Beale M" first="Michael H" last="Beale">Michael H. Beale</name>
<affiliation><nlm:affiliation>Plant Biology and Crop Sciences Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: mike.beale@rothamsted.ac.uk.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Karp, Angela" sort="Karp, Angela" uniqKey="Karp A" first="Angela" last="Karp">Angela Karp</name>
<affiliation><nlm:affiliation>AgroEcology Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: angela.karp@rothamsted.ac.uk.</nlm:affiliation>
</affiliation>
</author>
</analytic>
<series><title level="j">Phytochemistry</title>
<idno type="eISSN">1873-3700</idno>
<imprint><date when="2015" type="published">2015</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coenzyme A Ligases (metabolism)</term>
<term>Flavonoids (biosynthesis)</term>
<term>Isoenzymes (MeSH)</term>
<term>Lignin (metabolism)</term>
<term>Molecular Structure (MeSH)</term>
<term>Phenylalanine (metabolism)</term>
<term>Phenylalanine Ammonia-Lyase (genetics)</term>
<term>Phenylalanine Ammonia-Lyase (metabolism)</term>
<term>Populus (enzymology)</term>
<term>Populus (genetics)</term>
<term>Salicaceae (enzymology)</term>
<term>Salicaceae (genetics)</term>
<term>Salix (enzymology)</term>
<term>Salix (genetics)</term>
<term>Trans-Cinnamate 4-Monooxygenase (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Flavonoids</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Phenylalanine Ammonia-Lyase</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Coenzyme A Ligases</term>
<term>Lignin</term>
<term>Phenylalanine</term>
<term>Phenylalanine Ammonia-Lyase</term>
<term>Trans-Cinnamate 4-Monooxygenase</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Isoenzymes</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term>
<term>Salicaceae</term>
<term>Salix</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term>
<term>Salicaceae</term>
<term>Salix</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Molecular Structure</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Willow is an important biomass crop for the bioenergy industry, and therefore optimal growth with minimal effects of biotic and abiotic stress is essential. The phenylpropanoid pathway is responsible for the biosynthesis of not only lignin but also of flavonoids, condensed tannins, benzenoids and phenolic glycosides which all have a role in protecting the plant against biotic and abiotic stress. All products of the phenylpropanoid pathway are important for the healthy growth of short rotation cropping species such as willow. However, the phenylpropanoid pathway in willow remains largely uncharacterised. In the current study we identified and characterised five willow phenylalanine ammonia-lyase (PAL) genes, which encode enzymes that catalyse the deamination of l-phenylalanine to form trans-cinnamic acid, the entry point into the phenylpropanoid pathway. Willow PAL1, PAL2, PAL3 and PAL4 genes were orthologous to the poplar genes. However no orthologue of PAL5 appears to be present in willow. Moreover, two tandemly repeated PAL2 orthologues were identified in a single contig. Willow PALs show similar sub-cellular localisation to the poplar genes. However, the enzyme kinetics and gene expression of the willow PAL genes differed slightly, with willow PAL2 being more widely expressed than its poplar orthologues implying a wider role for PALs in the production of flavonoids, condensed tannins, benzenoids, and phenolic glycosides, in willow. </div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26070140</PMID>
<DateCompleted><Year>2016</Year>
<Month>04</Month>
<Day>13</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>12</Month>
<Day>10</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3700</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>117</Volume>
<PubDate><Year>2015</Year>
<Month>Sep</Month>
</PubDate>
</JournalIssue>
<Title>Phytochemistry</Title>
<ISOAbbreviation>Phytochemistry</ISOAbbreviation>
</Journal>
<ArticleTitle>Characterisation of the willow phenylalanine ammonia-lyase (PAL) gene family reveals expression differences compared with poplar.</ArticleTitle>
<Pagination><MedlinePgn>90-97</MedlinePgn>
</Pagination>
<ELocationID EIdType="pii" ValidYN="Y">S0031-9422(15)30016-9</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.phytochem.2015.06.005</ELocationID>
<Abstract><AbstractText>Willow is an important biomass crop for the bioenergy industry, and therefore optimal growth with minimal effects of biotic and abiotic stress is essential. The phenylpropanoid pathway is responsible for the biosynthesis of not only lignin but also of flavonoids, condensed tannins, benzenoids and phenolic glycosides which all have a role in protecting the plant against biotic and abiotic stress. All products of the phenylpropanoid pathway are important for the healthy growth of short rotation cropping species such as willow. However, the phenylpropanoid pathway in willow remains largely uncharacterised. In the current study we identified and characterised five willow phenylalanine ammonia-lyase (PAL) genes, which encode enzymes that catalyse the deamination of l-phenylalanine to form trans-cinnamic acid, the entry point into the phenylpropanoid pathway. Willow PAL1, PAL2, PAL3 and PAL4 genes were orthologous to the poplar genes. However no orthologue of PAL5 appears to be present in willow. Moreover, two tandemly repeated PAL2 orthologues were identified in a single contig. Willow PALs show similar sub-cellular localisation to the poplar genes. However, the enzyme kinetics and gene expression of the willow PAL genes differed slightly, with willow PAL2 being more widely expressed than its poplar orthologues implying a wider role for PALs in the production of flavonoids, condensed tannins, benzenoids, and phenolic glycosides, in willow. </AbstractText>
<CopyrightInformation>Copyright © 2015 The Authors. Published by Elsevier Ltd.. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>de Jong</LastName>
<ForeName>Femke</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>AgroEcology Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: femke.dejong@rothamsted.ac.uk.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hanley</LastName>
<ForeName>Steven J</ForeName>
<Initials>SJ</Initials>
<AffiliationInfo><Affiliation>AgroEcology Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: steve.hanley@rothamsted.ac.uk.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Beale</LastName>
<ForeName>Michael H</ForeName>
<Initials>MH</Initials>
<AffiliationInfo><Affiliation>Plant Biology and Crop Sciences Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: mike.beale@rothamsted.ac.uk.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Karp</LastName>
<ForeName>Angela</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>AgroEcology Department, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom. Electronic address: angela.karp@rothamsted.ac.uk.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>BB/G016216/1</GrantID>
<Agency>Biotechnology and Biological Sciences Research Council</Agency>
<Country>United Kingdom</Country>
</Grant>
<Grant><GrantID>BB/I014934/1</GrantID>
<Agency>Biotechnology and Biological Sciences Research Council</Agency>
<Country>United Kingdom</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2015</Year>
<Month>06</Month>
<Day>09</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Phytochemistry</MedlineTA>
<NlmUniqueID>0151434</NlmUniqueID>
<ISSNLinking>0031-9422</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D005419">Flavonoids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>47E5O17Y3R</RegistryNumber>
<NameOfSubstance UI="D010649">Phenylalanine</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>9005-53-2</RegistryNumber>
<NameOfSubstance UI="D008031">Lignin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.14.14.91</RegistryNumber>
<NameOfSubstance UI="D050564">Trans-Cinnamate 4-Monooxygenase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 4.3.1.24</RegistryNumber>
<NameOfSubstance UI="D010650">Phenylalanine Ammonia-Lyase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 6.2.1.-</RegistryNumber>
<NameOfSubstance UI="D003066">Coenzyme A Ligases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 6.2.1.12</RegistryNumber>
<NameOfSubstance UI="C019943">4-coumarate-CoA ligase</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D003066" MajorTopicYN="N">Coenzyme A Ligases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005419" MajorTopicYN="N">Flavonoids</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010649" MajorTopicYN="N">Phenylalanine</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010650" MajorTopicYN="Y">Phenylalanine Ammonia-Lyase</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D031308" MajorTopicYN="N">Salicaceae</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D032108" MajorTopicYN="N">Salix</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D050564" MajorTopicYN="N">Trans-Cinnamate 4-Monooxygenase</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Enzyme kinetics</Keyword>
<Keyword MajorTopicYN="N">Gene expression</Keyword>
<Keyword MajorTopicYN="N">Gene family</Keyword>
<Keyword MajorTopicYN="N">Phenylpropanoid metabolism</Keyword>
<Keyword MajorTopicYN="N">Salix viminalis (willow)</Keyword>
<Keyword MajorTopicYN="N">Subcellular localisation</Keyword>
<Keyword MajorTopicYN="N">l-Phenylalanine ammonia-lyase (PAL)</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year>
<Month>02</Month>
<Day>20</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2015</Year>
<Month>06</Month>
<Day>01</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2015</Year>
<Month>06</Month>
<Day>02</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2015</Year>
<Month>6</Month>
<Day>13</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2015</Year>
<Month>6</Month>
<Day>13</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2016</Year>
<Month>4</Month>
<Day>14</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">26070140</ArticleId>
<ArticleId IdType="pii">S0031-9422(15)30016-9</ArticleId>
<ArticleId IdType="doi">10.1016/j.phytochem.2015.06.005</ArticleId>
<ArticleId IdType="pmc">PMC4560161</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>New Phytol. 2006;172(1):47-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16945088</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 2009 Dec 1;424(2):233-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19725811</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell Physiol. 2010 Jan;51(1):144-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19996151</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 1999 Aug 20;457(1):47-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10486561</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 2013 Dec;25(12):4994-5010</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24363316</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Plant. 2010 Jan;3(1):2-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20035037</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>BMC Res Notes. 2012;5:366</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22824181</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Chem Ecol. 2010 Mar;36(3):286-97</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20177744</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 2012 Feb;158(2):1067-78</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22158677</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Protoc. 2006;1(4):2019-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17487191</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Protoc. 2008;3(6):1101-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18546601</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Phytochemistry. 2011 Sep;72(13):1497-509</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21376356</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Plant Physiol. 2008 Sep 29;165(14):1491-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18242769</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Integr Plant Biol. 2011 Feb;53(2):151-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21205181</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 1997 Jan;113(1):175-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9008393</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7608-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8052628</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>New Phytol. 2015 Jun;206(4):1297-313</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25684249</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Planta. 2013 Jul;238(1):35-49</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23546528</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2006 Sep 15;313(5793):1596-604</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16973872</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 1999 Aug;11(8):1537-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10449586</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Sci. 2014 Oct;227:21-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25219302</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Protein Chem. 2001;58:175-214</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11665488</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS J. 2006 Mar;273(5):1004-19</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16478474</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Phytochemistry. 2004 Jun;65(11):1557-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15276452</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 2014 Mar;26(3):894-914</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24619611</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 2002 Oct;130(2):796-807</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12376645</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Biochem. 2002 Jun;269(12):3065-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12071972</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Int J Genomics. 2013;2013:678969</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23671845</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Planta. 2013 Sep;238(3):487-97</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23765265</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 2010 Aug;153(4):1526-38</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20566705</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 2004 Dec;16(12):3426-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15548745</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Plant Biol. 2007 Dec;10(6):564-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17950657</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 2004 Nov;16(11):3098-109</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15472080</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Plant Sci. 2011 Apr;16(4):227-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21227733</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PoplarV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001C61 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 001C61 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Bois |area= PoplarV1 |flux= Main |étape= Corpus |type= RBID |clé= pubmed:26070140 |texte= Characterisation of the willow phenylalanine ammonia-lyase (PAL) gene family reveals expression differences compared with poplar. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Corpus/RBID.i -Sk "pubmed:26070140" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd \ | NlmPubMed2Wicri -a PoplarV1
![]() | This area was generated with Dilib version V0.6.37. | ![]() |