Arginine transcriptional response does not require inositol phosphate synthesis.
Identifieur interne : 001222 ( Main/Exploration ); précédent : 001221; suivant : 001223Arginine transcriptional response does not require inositol phosphate synthesis.
Auteurs : Daniel Bosch [Royaume-Uni] ; Adolfo SaiardiSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2012.
Descripteurs français
- KwdFr :
- Aldehyde oxidoreductases (génétique), Aldehyde oxidoreductases (métabolisme), Arginine (métabolisme), Arginine (pharmacologie), Biocatalyse (MeSH), Complexes multienzymatiques (génétique), Complexes multienzymatiques (métabolisme), Composés d'ammonium quaternaire (métabolisme), Composés d'ammonium quaternaire (pharmacologie), Facteurs temps (MeSH), Humains (MeSH), Inositol 1,4,5-trisphosphate (métabolisme), Inositol phosphates (biosynthèse), Mutation (MeSH), Ornithine (métabolisme), Ornithine (pharmacologie), Ornithine carbamoyltransferase (génétique), Ornithine carbamoyltransferase (métabolisme), Phosphotransferases (Alcohol Group Acceptor) (génétique), Phosphotransferases (Alcohol Group Acceptor) (métabolisme), Phosphotransferases (Carboxyl Group Acceptor) (génétique), Phosphotransferases (Carboxyl Group Acceptor) (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Régions promotrices (génétique) (génétique), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Techniques de knock-out de gènes (MeSH), Test de complémentation (MeSH), Transcription génétique (génétique).
- MESH :
- biosynthèse : Inositol phosphates.
- croissance et développement : Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Régulation de l'expression des gènes fongiques.
- génétique : Aldehyde oxidoreductases, Complexes multienzymatiques, Ornithine carbamoyltransferase, Phosphotransferases (Alcohol Group Acceptor), Phosphotransferases (Carboxyl Group Acceptor), Protéines de Saccharomyces cerevisiae, Régions promotrices (génétique), Saccharomyces cerevisiae, Transcription génétique.
- métabolisme : Aldehyde oxidoreductases, Arginine, Complexes multienzymatiques, Composés d'ammonium quaternaire, Inositol 1,4,5-trisphosphate, Ornithine, Ornithine carbamoyltransferase, Phosphotransferases (Alcohol Group Acceptor), Phosphotransferases (Carboxyl Group Acceptor), Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- pharmacologie : Arginine, Composés d'ammonium quaternaire, Ornithine.
- Biocatalyse, Facteurs temps, Humains, Mutation, Techniques de knock-out de gènes, Test de complémentation.
English descriptors
- KwdEn :
- Aldehyde Oxidoreductases (genetics), Aldehyde Oxidoreductases (metabolism), Arginine (metabolism), Arginine (pharmacology), Biocatalysis (MeSH), Gene Expression Regulation, Fungal (drug effects), Gene Knockout Techniques (MeSH), Genetic Complementation Test (MeSH), Humans (MeSH), Inositol 1,4,5-Trisphosphate (metabolism), Inositol Phosphates (biosynthesis), Multienzyme Complexes (genetics), Multienzyme Complexes (metabolism), Mutation (MeSH), Ornithine (metabolism), Ornithine (pharmacology), Ornithine Carbamoyltransferase (genetics), Ornithine Carbamoyltransferase (metabolism), Phosphotransferases (Alcohol Group Acceptor) (genetics), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Phosphotransferases (Carboxyl Group Acceptor) (genetics), Phosphotransferases (Carboxyl Group Acceptor) (metabolism), Promoter Regions, Genetic (genetics), Quaternary Ammonium Compounds (metabolism), Quaternary Ammonium Compounds (pharmacology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Time Factors (MeSH), Transcription, Genetic (genetics).
- MESH :
- chemical , biosynthesis : Inositol Phosphates.
- chemical , genetics : Aldehyde Oxidoreductases, Multienzyme Complexes, Ornithine Carbamoyltransferase, Phosphotransferases (Alcohol Group Acceptor), Phosphotransferases (Carboxyl Group Acceptor), Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Aldehyde Oxidoreductases, Arginine, Inositol 1,4,5-Trisphosphate, Multienzyme Complexes, Ornithine, Ornithine Carbamoyltransferase, Phosphotransferases (Alcohol Group Acceptor), Phosphotransferases (Carboxyl Group Acceptor), Quaternary Ammonium Compounds, Saccharomyces cerevisiae Proteins.
- chemical , pharmacology : Arginine, Ornithine, Quaternary Ammonium Compounds.
- drug effects : Gene Expression Regulation, Fungal.
- genetics : Promoter Regions, Genetic, Saccharomyces cerevisiae, Transcription, Genetic.
- growth & development : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Biocatalysis, Gene Knockout Techniques, Genetic Complementation Test, Humans, Mutation, Time Factors.
Abstract
Inositol phosphates are key signaling molecules affecting a large variety of cellular processes. Inositol-polyphosphate multikinase (IPMK) is a central component of the inositol phosphate biosynthetic routes, playing essential roles during development. IPMK phosphorylates inositol 1,4,5-trisphosphate to inositol tetrakisphosphate and subsequently to inositol pentakisphosphate and has also been described to function as a lipid kinase. Recently, a catalytically inactive mammalian IPMK was reported to be involved in nutrient signaling by way of mammalian target of rapamycin and AMP-activated protein kinase. In yeast, the IPMK homologue, Arg82, is the sole inositol-trisphosphate kinase. Arg82 has been extensively studied as part of the transcriptional complex regulating nitrogen sensing, in particular arginine metabolism. Whether this role requires Arg82 catalytic activity has long been a matter of contention. In this study, we developed a novel method for the real time study of promoter strength in vivo and used it to demonstrate that catalytically inactive Arg82 fully restored the arginine-dependent transcriptional response. We also showed that expression in yeast of catalytically active, but structurally very different, mammalian or plant IPMK homologue failed to restore arginine regulation. Our work indicates that inositol phosphates do not regulate arginine-dependent gene expression.
DOI: 10.1074/jbc.M112.384255
PubMed: 22992733
PubMed Central: PMC3488103
Affiliations:
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Le document en format XML
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(genetics)</term><term>Phosphotransferases (Alcohol Group Acceptor) (metabolism)</term><term>Phosphotransferases (Carboxyl Group Acceptor) (genetics)</term><term>Phosphotransferases (Carboxyl Group Acceptor) (metabolism)</term><term>Promoter Regions, Genetic (genetics)</term><term>Quaternary Ammonium Compounds (metabolism)</term><term>Quaternary Ammonium Compounds (pharmacology)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (growth & development)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Time Factors (MeSH)</term><term>Transcription, Genetic (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aldehyde oxidoreductases (génétique)</term><term>Aldehyde oxidoreductases (métabolisme)</term><term>Arginine (métabolisme)</term><term>Arginine (pharmacologie)</term><term>Biocatalyse (MeSH)</term><term>Complexes multienzymatiques (génétique)</term><term>Complexes multienzymatiques (métabolisme)</term><term>Composés d'ammonium quaternaire (métabolisme)</term><term>Composés d'ammonium quaternaire (pharmacologie)</term><term>Facteurs temps (MeSH)</term><term>Humains (MeSH)</term><term>Inositol 1,4,5-trisphosphate (métabolisme)</term><term>Inositol phosphates (biosynthèse)</term><term>Mutation (MeSH)</term><term>Ornithine (métabolisme)</term><term>Ornithine (pharmacologie)</term><term>Ornithine carbamoyltransferase (génétique)</term><term>Ornithine carbamoyltransferase (métabolisme)</term><term>Phosphotransferases (Alcohol Group Acceptor) (génétique)</term><term>Phosphotransferases (Alcohol Group Acceptor) (métabolisme)</term><term>Phosphotransferases (Carboxyl Group Acceptor) (génétique)</term><term>Phosphotransferases (Carboxyl Group Acceptor) (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Régions promotrices (génétique) (génétique)</term><term>Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (croissance et développement)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Techniques de knock-out de gènes (MeSH)</term><term>Test de complémentation (MeSH)</term><term>Transcription génétique (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Inositol Phosphates</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Aldehyde Oxidoreductases</term><term>Multienzyme Complexes</term><term>Ornithine Carbamoyltransferase</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Phosphotransferases (Carboxyl Group Acceptor)</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aldehyde Oxidoreductases</term><term>Arginine</term><term>Inositol 1,4,5-Trisphosphate</term><term>Multienzyme Complexes</term><term>Ornithine</term><term>Ornithine Carbamoyltransferase</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Phosphotransferases (Carboxyl Group Acceptor)</term><term>Quaternary Ammonium Compounds</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Arginine</term><term>Ornithine</term><term>Quaternary Ammonium Compounds</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Inositol phosphates</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Gene Expression Regulation, Fungal</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Régulation de l'expression des gènes fongiques</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Promoter Regions, Genetic</term><term>Saccharomyces cerevisiae</term><term>Transcription, Genetic</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Aldehyde oxidoreductases</term><term>Complexes multienzymatiques</term><term>Ornithine carbamoyltransferase</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Phosphotransferases (Carboxyl Group Acceptor)</term><term>Protéines de Saccharomyces cerevisiae</term><term>Régions promotrices (génétique)</term><term>Saccharomyces cerevisiae</term><term>Transcription génétique</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aldehyde oxidoreductases</term><term>Arginine</term><term>Complexes multienzymatiques</term><term>Composés d'ammonium quaternaire</term><term>Inositol 1,4,5-trisphosphate</term><term>Ornithine</term><term>Ornithine carbamoyltransferase</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Phosphotransferases (Carboxyl Group Acceptor)</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Arginine</term><term>Composés d'ammonium quaternaire</term><term>Ornithine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biocatalysis</term><term>Gene Knockout Techniques</term><term>Genetic Complementation Test</term><term>Humans</term><term>Mutation</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biocatalyse</term><term>Facteurs temps</term><term>Humains</term><term>Mutation</term><term>Techniques de knock-out de gènes</term><term>Test de complémentation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Inositol phosphates are key signaling molecules affecting a large variety of cellular processes. Inositol-polyphosphate multikinase (IPMK) is a central component of the inositol phosphate biosynthetic routes, playing essential roles during development. IPMK phosphorylates inositol 1,4,5-trisphosphate to inositol tetrakisphosphate and subsequently to inositol pentakisphosphate and has also been described to function as a lipid kinase. Recently, a catalytically inactive mammalian IPMK was reported to be involved in nutrient signaling by way of mammalian target of rapamycin and AMP-activated protein kinase. In yeast, the IPMK homologue, Arg82, is the sole inositol-trisphosphate kinase. Arg82 has been extensively studied as part of the transcriptional complex regulating nitrogen sensing, in particular arginine metabolism. Whether this role requires Arg82 catalytic activity has long been a matter of contention. In this study, we developed a novel method for the real time study of promoter strength in vivo and used it to demonstrate that catalytically inactive Arg82 fully restored the arginine-dependent transcriptional response. We also showed that expression in yeast of catalytically active, but structurally very different, mammalian or plant IPMK homologue failed to restore arginine regulation. Our work indicates that inositol phosphates do not regulate arginine-dependent gene expression.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22992733</PMID><DateCompleted><Year>2013</Year><Month>01</Month><Day>23</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>287</Volume><Issue>45</Issue><PubDate><Year>2012</Year><Month>Nov</Month><Day>02</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Arginine transcriptional response does not require inositol phosphate synthesis.</ArticleTitle><Pagination><MedlinePgn>38347-55</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M112.384255</ELocationID><Abstract><AbstractText>Inositol phosphates are key signaling molecules affecting a large variety of cellular processes. Inositol-polyphosphate multikinase (IPMK) is a central component of the inositol phosphate biosynthetic routes, playing essential roles during development. IPMK phosphorylates inositol 1,4,5-trisphosphate to inositol tetrakisphosphate and subsequently to inositol pentakisphosphate and has also been described to function as a lipid kinase. Recently, a catalytically inactive mammalian IPMK was reported to be involved in nutrient signaling by way of mammalian target of rapamycin and AMP-activated protein kinase. In yeast, the IPMK homologue, Arg82, is the sole inositol-trisphosphate kinase. Arg82 has been extensively studied as part of the transcriptional complex regulating nitrogen sensing, in particular arginine metabolism. Whether this role requires Arg82 catalytic activity has long been a matter of contention. In this study, we developed a novel method for the real time study of promoter strength in vivo and used it to demonstrate that catalytically inactive Arg82 fully restored the arginine-dependent transcriptional response. We also showed that expression in yeast of catalytically active, but structurally very different, mammalian or plant IPMK homologue failed to restore arginine regulation. Our work indicates that inositol phosphates do not regulate arginine-dependent gene expression.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bosch</LastName><ForeName>Daniel</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Cell Biology Unit, Medical Research Council Laboratory for Molecular Cell Biology, University College London, Gower Street, London WC1E 6BT, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Saiardi</LastName><ForeName>Adolfo</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>MC_U122680443</GrantID><Agency>Medical 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>2012</Year><Month>09</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C492864">Arg5,6 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007295">Inositol Phosphates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009097">Multienzyme Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000644">Quaternary Ammonium Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>85166-31-0</RegistryNumber><NameOfSubstance UI="D015544">Inositol 1,4,5-Trisphosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>94ZLA3W45F</RegistryNumber><NameOfSubstance UI="D001120">Arginine</NameOfSubstance></Chemical><Chemical><RegistryNumber>E524N2IXA3</RegistryNumber><NameOfSubstance UI="D009952">Ornithine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.2.-</RegistryNumber><NameOfSubstance UI="D000445">Aldehyde Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.3.3</RegistryNumber><NameOfSubstance UI="D009954">Ornithine Carbamoyltransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.3.3</RegistryNumber><NameOfSubstance UI="C451259">arg3 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="C425775">ARG82 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D017853">Phosphotransferases (Alcohol Group Acceptor)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="C434257">inositol polyphosphate multikinase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.2.-</RegistryNumber><NameOfSubstance UI="D017851">Phosphotransferases (Carboxyl Group Acceptor)</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000445" MajorTopicYN="N">Aldehyde Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001120" MajorTopicYN="N">Arginine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055162" MajorTopicYN="N">Biocatalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055786" MajorTopicYN="N">Gene Knockout Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005816" MajorTopicYN="N">Genetic Complementation Test</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015544" MajorTopicYN="N">Inositol 1,4,5-Trisphosphate</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007295" MajorTopicYN="N">Inositol Phosphates</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009097" MajorTopicYN="N">Multienzyme Complexes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009952" MajorTopicYN="N">Ornithine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009954" MajorTopicYN="N">Ornithine Carbamoyltransferase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017853" MajorTopicYN="N">Phosphotransferases (Alcohol Group Acceptor)</DescriptorName><QualifierName UI="Q000235" 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IdType="pubmed">15939867</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Grand Londres</li></region><settlement><li>Londres</li></settlement><orgName><li>University College de Londres</li></orgName></list><tree><noCountry><name sortKey="Saiardi, Adolfo" sort="Saiardi, Adolfo" uniqKey="Saiardi A" first="Adolfo" last="Saiardi">Adolfo Saiardi</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Bosch, Daniel" sort="Bosch, Daniel" uniqKey="Bosch D" first="Daniel" last="Bosch">Daniel Bosch</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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