The enigmatic role of Sir2 in aging.
Identifieur interne : 001810 ( Main/Exploration ); précédent : 001809; suivant : 001811The enigmatic role of Sir2 in aging.
Auteurs : Brian K. Kennedy [États-Unis] ; Erica D. Smith ; Matt KaeberleinSource :
- Cell [ 0092-8674 ] ; 2005.
Descripteurs français
- KwdFr :
- Alcohol dehydrogenase (métabolisme), Cyclic AMP-Dependent Protein Kinases (génétique), Cyclic AMP-Dependent Protein Kinases (physiologie), Facteurs temps (MeSH), Histone deacetylases (génétique), Histone deacetylases (physiologie), Modèles biologiques (MeSH), Mutation (génétique), Protein kinases (génétique), Protein kinases (physiologie), Protein-Serine-Threonine Kinases (MeSH), Protéines SIR de Saccharomyces cerevisiae (génétique), Protéines SIR de Saccharomyces cerevisiae (physiologie), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (physiologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (physiologie), Sirtuine-1 (MeSH), Sirtuine-2 (MeSH), Sirtuines (génétique), Sirtuines (physiologie), Stress oxydatif (MeSH), Température élevée (MeSH), Éthanol (métabolisme).
- MESH :
- génétique : Cyclic AMP-Dependent Protein Kinases, Histone deacetylases, Mutation, Protein kinases, Protéines SIR de Saccharomyces cerevisiae, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Sirtuines.
- métabolisme : Alcohol dehydrogenase, Éthanol.
- physiologie : Cyclic AMP-Dependent Protein Kinases, Histone deacetylases, Protein kinases, Protéines SIR de Saccharomyces cerevisiae, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Sirtuines.
- Facteurs temps, Modèles biologiques, Protein-Serine-Threonine Kinases, Sirtuine-1, Sirtuine-2, Stress oxydatif, Température élevée.
English descriptors
- KwdEn :
- Alcohol Dehydrogenase (metabolism), Cyclic AMP-Dependent Protein Kinases (genetics), Cyclic AMP-Dependent Protein Kinases (physiology), Ethanol (metabolism), Histone Deacetylases (genetics), Histone Deacetylases (physiology), Hot Temperature (MeSH), Models, Biological (MeSH), Mutation (genetics), Oxidative Stress (MeSH), Protein Kinases (genetics), Protein Kinases (physiology), Protein-Serine-Threonine Kinases (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (physiology), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (physiology), Silent Information Regulator Proteins, Saccharomyces cerevisiae (genetics), Silent Information Regulator Proteins, Saccharomyces cerevisiae (physiology), Sirtuin 1 (MeSH), Sirtuin 2 (MeSH), Sirtuins (genetics), Sirtuins (physiology), Time Factors (MeSH).
- MESH :
- chemical , genetics : Cyclic AMP-Dependent Protein Kinases, Histone Deacetylases, Protein Kinases, Saccharomyces cerevisiae Proteins, Silent Information Regulator Proteins, Saccharomyces cerevisiae, Sirtuins.
- chemical , metabolism : Alcohol Dehydrogenase, Ethanol.
- chemical , physiology : Cyclic AMP-Dependent Protein Kinases, Histone Deacetylases, Protein Kinases, Saccharomyces cerevisiae Proteins, Silent Information Regulator Proteins, Saccharomyces cerevisiae, Sirtuins.
- genetics : Mutation, Saccharomyces cerevisiae.
- physiology : Saccharomyces cerevisiae.
- Hot Temperature, Models, Biological, Oxidative Stress, Protein-Serine-Threonine Kinases, Sirtuin 1, Sirtuin 2, Time Factors.
Abstract
In this issue of Cell, Longo and colleagues (Fabrizio et al., 2005) examine the role of Sir2, a histone deacetylase, in chronological aging in yeast by measuring the long-term survival of nondividing cells. In contrast to measurements of aging for mitotic cells, cell survival in the nonmitotic state is decreased by Sir2 activity under conditions that mimic calorie restriction.
DOI: 10.1016/j.cell.2005.11.002
PubMed: 16286003
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The enigmatic role of Sir2 in aging.</title><author><name sortKey="Kennedy, Brian K" sort="Kennedy, Brian K" uniqKey="Kennedy B" first="Brian K" last="Kennedy">Brian K. Kennedy</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Washington, Seattle, Washington 98195</wicri:regionArea><orgName type="university">Université de Washington</orgName><placeName><settlement type="city">Seattle</settlement><region type="state">Washington (État)</region></placeName></affiliation></author><author><name sortKey="Smith, Erica D" sort="Smith, Erica D" uniqKey="Smith E" first="Erica D" last="Smith">Erica D. Smith</name></author><author><name sortKey="Kaeberlein, Matt" sort="Kaeberlein, Matt" uniqKey="Kaeberlein M" first="Matt" last="Kaeberlein">Matt Kaeberlein</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:16286003</idno><idno type="pmid">16286003</idno><idno type="doi">10.1016/j.cell.2005.11.002</idno><idno type="wicri:Area/Main/Corpus">001811</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001811</idno><idno type="wicri:Area/Main/Curation">001811</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001811</idno><idno type="wicri:Area/Main/Exploration">001811</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The enigmatic role of Sir2 in aging.</title><author><name sortKey="Kennedy, Brian K" sort="Kennedy, Brian K" uniqKey="Kennedy B" first="Brian K" last="Kennedy">Brian K. Kennedy</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Washington, Seattle, Washington 98195</wicri:regionArea><orgName type="university">Université de Washington</orgName><placeName><settlement type="city">Seattle</settlement><region type="state">Washington (État)</region></placeName></affiliation></author><author><name sortKey="Smith, Erica D" sort="Smith, Erica D" uniqKey="Smith E" first="Erica D" last="Smith">Erica D. Smith</name></author><author><name sortKey="Kaeberlein, Matt" sort="Kaeberlein, Matt" uniqKey="Kaeberlein M" first="Matt" last="Kaeberlein">Matt Kaeberlein</name></author></analytic><series><title level="j">Cell</title><idno type="ISSN">0092-8674</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Dehydrogenase (metabolism)</term><term>Cyclic AMP-Dependent Protein Kinases (genetics)</term><term>Cyclic AMP-Dependent Protein Kinases (physiology)</term><term>Ethanol (metabolism)</term><term>Histone Deacetylases (genetics)</term><term>Histone Deacetylases (physiology)</term><term>Hot Temperature (MeSH)</term><term>Models, Biological (MeSH)</term><term>Mutation (genetics)</term><term>Oxidative Stress (MeSH)</term><term>Protein Kinases (genetics)</term><term>Protein Kinases (physiology)</term><term>Protein-Serine-Threonine Kinases (MeSH)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (physiology)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (physiology)</term><term>Silent Information Regulator Proteins, Saccharomyces cerevisiae (genetics)</term><term>Silent Information Regulator Proteins, Saccharomyces cerevisiae (physiology)</term><term>Sirtuin 1 (MeSH)</term><term>Sirtuin 2 (MeSH)</term><term>Sirtuins (genetics)</term><term>Sirtuins (physiology)</term><term>Time Factors (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcohol dehydrogenase (métabolisme)</term><term>Cyclic AMP-Dependent Protein Kinases (génétique)</term><term>Cyclic AMP-Dependent Protein Kinases (physiologie)</term><term>Facteurs temps (MeSH)</term><term>Histone deacetylases (génétique)</term><term>Histone deacetylases (physiologie)</term><term>Modèles biologiques (MeSH)</term><term>Mutation (génétique)</term><term>Protein kinases (génétique)</term><term>Protein kinases (physiologie)</term><term>Protein-Serine-Threonine Kinases (MeSH)</term><term>Protéines SIR de Saccharomyces cerevisiae (génétique)</term><term>Protéines SIR de Saccharomyces cerevisiae (physiologie)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (physiologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (physiologie)</term><term>Sirtuine-1 (MeSH)</term><term>Sirtuine-2 (MeSH)</term><term>Sirtuines (génétique)</term><term>Sirtuines (physiologie)</term><term>Stress oxydatif (MeSH)</term><term>Température élevée (MeSH)</term><term>Éthanol (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cyclic AMP-Dependent Protein Kinases</term><term>Histone Deacetylases</term><term>Protein Kinases</term><term>Saccharomyces cerevisiae Proteins</term><term>Silent Information Regulator Proteins, Saccharomyces cerevisiae</term><term>Sirtuins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Dehydrogenase</term><term>Ethanol</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Cyclic AMP-Dependent Protein Kinases</term><term>Histone Deacetylases</term><term>Protein Kinases</term><term>Saccharomyces cerevisiae Proteins</term><term>Silent Information Regulator Proteins, Saccharomyces cerevisiae</term><term>Sirtuins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cyclic AMP-Dependent Protein Kinases</term><term>Histone deacetylases</term><term>Mutation</term><term>Protein kinases</term><term>Protéines SIR de Saccharomyces cerevisiae</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term><term>Sirtuines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcohol dehydrogenase</term><term>Éthanol</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cyclic AMP-Dependent Protein Kinases</term><term>Histone deacetylases</term><term>Protein kinases</term><term>Protéines SIR de Saccharomyces cerevisiae</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term><term>Sirtuines</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hot Temperature</term><term>Models, Biological</term><term>Oxidative Stress</term><term>Protein-Serine-Threonine Kinases</term><term>Sirtuin 1</term><term>Sirtuin 2</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Facteurs temps</term><term>Modèles biologiques</term><term>Protein-Serine-Threonine Kinases</term><term>Sirtuine-1</term><term>Sirtuine-2</term><term>Stress oxydatif</term><term>Température élevée</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In this issue of Cell, Longo and colleagues (Fabrizio et al., 2005) examine the role of Sir2, a histone deacetylase, in chronological aging in yeast by measuring the long-term survival of nondividing cells. In contrast to measurements of aging for mitotic cells, cell survival in the nonmitotic state is decreased by Sir2 activity under conditions that mimic calorie restriction.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16286003</PMID><DateCompleted><Year>2006</Year><Month>01</Month><Day>19</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0092-8674</ISSN><JournalIssue CitedMedium="Print"><Volume>123</Volume><Issue>4</Issue><PubDate><Year>2005</Year><Month>Nov</Month><Day>18</Day></PubDate></JournalIssue><Title>Cell</Title><ISOAbbreviation>Cell</ISOAbbreviation></Journal><ArticleTitle>The enigmatic role of Sir2 in aging.</ArticleTitle><Pagination><MedlinePgn>548-50</MedlinePgn></Pagination><Abstract><AbstractText>In this issue of Cell, Longo and colleagues (Fabrizio et al., 2005) examine the role of Sir2, a histone deacetylase, in chronological aging in yeast by measuring the long-term survival of nondividing cells. In contrast to measurements of aging for mitotic cells, cell survival in the nonmitotic state is decreased by Sir2 activity under conditions that mimic calorie restriction.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kennedy</LastName><ForeName>Brian K</ForeName><Initials>BK</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Smith</LastName><ForeName>Erica D</ForeName><Initials>ED</Initials></Author><Author ValidYN="Y"><LastName>Kaeberlein</LastName><ForeName>Matt</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016420">Comment</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Cell</MedlineTA><NlmUniqueID>0413066</NlmUniqueID><ISSNLinking>0092-8674</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D038281">Silent Information Regulator Proteins, Saccharomyces cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>3K9958V90M</RegistryNumber><NameOfSubstance UI="D000431">Ethanol</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.1</RegistryNumber><NameOfSubstance UI="D000426">Alcohol Dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="C071569">SCH9 protein kinase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C500749">target of rapamycin protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.11</RegistryNumber><NameOfSubstance UI="D017868">Cyclic AMP-Dependent Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.5.1.-</RegistryNumber><NameOfSubstance UI="C087778">SIR2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.5.1.-</RegistryNumber><NameOfSubstance UI="C470545">Sirt1 protein, mouse</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.5.1.-</RegistryNumber><NameOfSubstance UI="D056564">Sirtuin 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.5.1.-</RegistryNumber><NameOfSubstance UI="D056565">Sirtuin 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.5.1.-</RegistryNumber><NameOfSubstance UI="D037761">Sirtuins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.5.1.98</RegistryNumber><NameOfSubstance UI="D006655">Histone Deacetylases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="CommentOn"><RefSource>Cell. 2005 Nov 18;123(4):655-67</RefSource><PMID Version="1">16286010</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000426" MajorTopicYN="N">Alcohol Dehydrogenase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017868" MajorTopicYN="N">Cyclic AMP-Dependent Protein Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000431" MajorTopicYN="N">Ethanol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006655" MajorTopicYN="N">Histone Deacetylases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="N">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D038281" MajorTopicYN="N">Silent Information Regulator Proteins, Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D056564" MajorTopicYN="N">Sirtuin 1</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D056565" MajorTopicYN="N">Sirtuin 2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D037761" MajorTopicYN="N">Sirtuins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>11</Month><Day>16</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>1</Month><Day>20</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>11</Month><Day>16</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16286003</ArticleId><ArticleId IdType="pii">S0092-8674(05)01160-8</ArticleId><ArticleId IdType="doi">10.1016/j.cell.2005.11.002</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Washington (État)</li></region><settlement><li>Seattle</li></settlement><orgName><li>Université de Washington</li></orgName></list><tree><noCountry><name sortKey="Kaeberlein, Matt" sort="Kaeberlein, Matt" uniqKey="Kaeberlein M" first="Matt" last="Kaeberlein">Matt Kaeberlein</name><name sortKey="Smith, Erica D" sort="Smith, Erica D" uniqKey="Smith E" first="Erica D" last="Smith">Erica D. Smith</name></noCountry><country name="États-Unis"><region name="Washington (État)"><name sortKey="Kennedy, Brian K" sort="Kennedy, Brian K" uniqKey="Kennedy B" first="Brian K" last="Kennedy">Brian K. Kennedy</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/RapamycinFungusV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001810 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001810 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= RapamycinFungusV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:16286003
|texte= The enigmatic role of Sir2 in aging.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:16286003" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a RapamycinFungusV1
| This area was generated with Dilib version V0.6.38. |  |