Crystal structures of a poplar thioredoxin peroxidase that exhibits the structure of glutathione peroxidases: insights into redox-driven conformational changes.
Identifieur interne : 003C17 ( Main/Exploration ); précédent : 003C16; suivant : 003C18Crystal structures of a poplar thioredoxin peroxidase that exhibits the structure of glutathione peroxidases: insights into redox-driven conformational changes.
Auteurs : Cha San Koh [France] ; Claude Didierjean ; Nicolas Navrot ; Santosh Panjikar ; Guillermo Mulliert ; Nicolas Rouhier ; Jean-Pierre Jacquot ; André Aubry ; Omar Shawkataly ; Catherine CorbierSource :
- Journal of molecular biology [ 0022-2836 ] ; 2007.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Animaux (MeSH), Cadmium (métabolisme), Cristallographie aux rayons X (MeSH), Cystéine (métabolisme), Données de séquences moléculaires (MeSH), Glutathione peroxidase (composition chimique), Glutathione peroxidase (métabolisme), Humains (MeSH), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Peroxirédoxines (MeSH), Pliage des protéines (MeSH), Populus (enzymologie), Protéines végétales (composition chimique), Protéines végétales (génétique), Protéines végétales (métabolisme), Sites de fixation (MeSH), Sous-unités de protéines (composition chimique), Sous-unités de protéines (génétique), Sous-unités de protéines (métabolisme), Structure quaternaire des protéines (MeSH), Structure secondaire des protéines (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Glutathione peroxidase, Peroxidases, Protéines végétales, Sous-unités de protéines.
- enzymologie : Populus.
- génétique : Peroxidases, Protéines végétales, Sous-unités de protéines.
- métabolisme : Cadmium, Cystéine, Glutathione peroxidase, Peroxidases, Protéines végétales, Sous-unités de protéines.
- Alignement de séquences, Animaux, Cristallographie aux rayons X, Données de séquences moléculaires, Humains, Modèles moléculaires, Oxydoréduction, Peroxirédoxines, Pliage des protéines, Sites de fixation, Structure quaternaire des protéines, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Binding Sites (MeSH), Cadmium (metabolism), Crystallography, X-Ray (MeSH), Cysteine (metabolism), Glutathione Peroxidase (chemistry), Glutathione Peroxidase (metabolism), Humans (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Peroxiredoxins (MeSH), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (metabolism), Populus (enzymology), Protein Folding (MeSH), Protein Structure, Quaternary (MeSH), Protein Structure, Secondary (MeSH), Protein Structure, Tertiary (MeSH), Protein Subunits (chemistry), Protein Subunits (genetics), Protein Subunits (metabolism), Sequence Alignment (MeSH).
- MESH :
- chemical , chemistry : Glutathione Peroxidase, Peroxidases, Plant Proteins, Protein Subunits.
- chemical , genetics : Peroxidases, Plant Proteins, Protein Subunits.
- chemical , metabolism : Cadmium, Cysteine, Glutathione Peroxidase, Peroxidases, Plant Proteins, Protein Subunits.
- enzymology : Populus.
- Amino Acid Sequence, Animals, Binding Sites, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Peroxiredoxins, Protein Folding, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment.
Abstract
Glutathione peroxidases (GPXs) are a group of enzymes that regulate the levels of reactive oxygen species in cells and tissues, and protect them against oxidative damage. Contrary to most of their counterparts in animal cells, the higher plant GPX homologues identified so far possess cysteine instead of selenocysteine in their active site. Interestingly, the plant GPXs are not dependent on glutathione but rather on thioredoxin as their in vitro electron donor. We have determined the crystal structures of the reduced and oxidized form of Populus trichocarpaxdeltoides GPX5 (PtGPX5), using a selenomethionine derivative. PtGPX5 exhibits an overall structure similar to that of the known animal GPXs. PtGPX5 crystallized in the assumed physiological dimeric form, displaying a pseudo ten-stranded beta sheet core. Comparison of both redox structures indicates that a drastic conformational change is necessary to bring the two distant cysteine residues together to form an intramolecular disulfide bond. In addition, a computer model of a complex of PtGPX5 and its in vitro recycling partner thioredoxin h1 is proposed on the basis of the crystal packing of the oxidized form enzyme. A possible role of PtGPX5 as a heavy-metal sink is also discussed.
DOI: 10.1016/j.jmb.2007.04.031
PubMed: 17531267
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></author><author><name sortKey="Aubry, Andre" sort="Aubry, Andre" uniqKey="Aubry A" first="André" last="Aubry">André Aubry</name></author><author><name sortKey="Shawkataly, Omar" sort="Shawkataly, Omar" uniqKey="Shawkataly O" first="Omar" last="Shawkataly">Omar Shawkataly</name></author><author><name sortKey="Corbier, Catherine" sort="Corbier, Catherine" uniqKey="Corbier C" first="Catherine" last="Corbier">Catherine Corbier</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="ISSN">0022-2836</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Binding Sites (MeSH)</term><term>Cadmium (metabolism)</term><term>Crystallography, X-Ray (MeSH)</term><term>Cysteine (metabolism)</term><term>Glutathione Peroxidase (chemistry)</term><term>Glutathione Peroxidase (metabolism)</term><term>Humans (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Peroxiredoxins (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (metabolism)</term><term>Populus (enzymology)</term><term>Protein Folding (MeSH)</term><term>Protein Structure, Quaternary (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Protein Subunits (chemistry)</term><term>Protein Subunits (genetics)</term><term>Protein Subunits (metabolism)</term><term>Sequence Alignment (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Animaux (MeSH)</term><term>Cadmium (métabolisme)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Cystéine (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutathione peroxidase (composition chimique)</term><term>Glutathione peroxidase (métabolisme)</term><term>Humains (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Peroxirédoxines (MeSH)</term><term>Pliage des protéines (MeSH)</term><term>Populus (enzymologie)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (génétique)</term><term>Protéines végétales (métabolisme)</term><term>Sites de fixation (MeSH)</term><term>Sous-unités de protéines (composition chimique)</term><term>Sous-unités de protéines (génétique)</term><term>Sous-unités de protéines (métabolisme)</term><term>Structure quaternaire des protéines (MeSH)</term><term>Structure secondaire des protéines (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione Peroxidase</term><term>Peroxidases</term><term>Plant Proteins</term><term>Protein Subunits</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peroxidases</term><term>Plant Proteins</term><term>Protein Subunits</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cadmium</term><term>Cysteine</term><term>Glutathione Peroxidase</term><term>Peroxidases</term><term>Plant Proteins</term><term>Protein Subunits</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutathione peroxidase</term><term>Peroxidases</term><term>Protéines végétales</term><term>Sous-unités de protéines</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peroxidases</term><term>Protéines végétales</term><term>Sous-unités de protéines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cadmium</term><term>Cystéine</term><term>Glutathione peroxidase</term><term>Peroxidases</term><term>Protéines végétales</term><term>Sous-unités de protéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Crystallography, X-Ray</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Peroxiredoxins</term><term>Protein Folding</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Peroxirédoxines</term><term>Pliage des protéines</term><term>Sites de fixation</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutathione peroxidases (GPXs) are a group of enzymes that regulate the levels of reactive oxygen species in cells and tissues, and protect them against oxidative damage. Contrary to most of their counterparts in animal cells, the higher plant GPX homologues identified so far possess cysteine instead of selenocysteine in their active site. Interestingly, the plant GPXs are not dependent on glutathione but rather on thioredoxin as their in vitro electron donor. We have determined the crystal structures of the reduced and oxidized form of Populus trichocarpaxdeltoides GPX5 (PtGPX5), using a selenomethionine derivative. PtGPX5 exhibits an overall structure similar to that of the known animal GPXs. PtGPX5 crystallized in the assumed physiological dimeric form, displaying a pseudo ten-stranded beta sheet core. Comparison of both redox structures indicates that a drastic conformational change is necessary to bring the two distant cysteine residues together to form an intramolecular disulfide bond. In addition, a computer model of a complex of PtGPX5 and its in vitro recycling partner thioredoxin h1 is proposed on the basis of the crystal packing of the oxidized form enzyme. A possible role of PtGPX5 as a heavy-metal sink is also discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17531267</PMID><DateCompleted><Year>2007</Year><Month>09</Month><Day>17</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0022-2836</ISSN><JournalIssue CitedMedium="Print"><Volume>370</Volume><Issue>3</Issue><PubDate><Year>2007</Year><Month>Jul</Month><Day>13</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Crystal structures of a poplar thioredoxin peroxidase that exhibits the structure of glutathione peroxidases: insights into redox-driven conformational changes.</ArticleTitle><Pagination><MedlinePgn>512-29</MedlinePgn></Pagination><Abstract><AbstractText>Glutathione peroxidases (GPXs) are a group of enzymes that regulate the levels of reactive oxygen species in cells and tissues, and protect them against oxidative damage. Contrary to most of their counterparts in animal cells, the higher plant GPX homologues identified so far possess cysteine instead of selenocysteine in their active site. Interestingly, the plant GPXs are not dependent on glutathione but rather on thioredoxin as their in vitro electron donor. We have determined the crystal structures of the reduced and oxidized form of Populus trichocarpaxdeltoides GPX5 (PtGPX5), using a selenomethionine derivative. PtGPX5 exhibits an overall structure similar to that of the known animal GPXs. PtGPX5 crystallized in the assumed physiological dimeric form, displaying a pseudo ten-stranded beta sheet core. Comparison of both redox structures indicates that a drastic conformational change is necessary to bring the two distant cysteine residues together to form an intramolecular disulfide bond. In addition, a computer model of a complex of PtGPX5 and its in vitro recycling partner thioredoxin h1 is proposed on the basis of the crystal packing of the oxidized form enzyme. A possible role of PtGPX5 as a heavy-metal sink is also discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Koh</LastName><ForeName>Cha San</ForeName><Initials>CS</Initials><AffiliationInfo><Affiliation>LCM3B, Equipe Biocristallographie, UMR 7036 CNRS-UHP, Faculté des Sciences et Techniques, Nancy Université, BP 239, 54506 Vandoeuvre-lès-Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Didierjean</LastName><ForeName>Claude</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Navrot</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Panjikar</LastName><ForeName>Santosh</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Mulliert</LastName><ForeName>Guillermo</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Aubry</LastName><ForeName>André</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Shawkataly</LastName><ForeName>Omar</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Corbier</LastName><ForeName>Catherine</ForeName><Initials>C</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><ArticleDate DateType="Electronic"><Year>2007</Year><Month>04</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Mol Biol</MedlineTA><NlmUniqueID>2985088R</NlmUniqueID><ISSNLinking>0022-2836</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D021122">Protein Subunits</NameOfSubstance></Chemical><Chemical><RegistryNumber>00BH33GNGH</RegistryNumber><NameOfSubstance UI="D002104">Cadmium</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="D005979">Glutathione Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002104" MajorTopicYN="N">Cadmium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005979" MajorTopicYN="N">Glutathione Peroxidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><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></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020836" MajorTopicYN="N">Protein Structure, Quaternary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="Y">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021122" MajorTopicYN="N">Protein Subunits</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2007</Year><Month>02</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2007</Year><Month>04</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>04</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>5</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>9</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>5</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17531267</ArticleId><ArticleId IdType="pii">S0022-2836(07)00502-5</ArticleId><ArticleId IdType="doi">10.1016/j.jmb.2007.04.031</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Vandœuvre-lès-Nancy</li></settlement><orgName><li>Nancy-Université</li></orgName></list><tree><noCountry><name sortKey="Aubry, Andre" sort="Aubry, Andre" uniqKey="Aubry A" first="André" last="Aubry">André Aubry</name><name sortKey="Corbier, Catherine" sort="Corbier, Catherine" uniqKey="Corbier C" first="Catherine" last="Corbier">Catherine Corbier</name><name sortKey="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Mulliert, Guillermo" sort="Mulliert, Guillermo" uniqKey="Mulliert G" first="Guillermo" last="Mulliert">Guillermo Mulliert</name><name sortKey="Navrot, Nicolas" sort="Navrot, Nicolas" uniqKey="Navrot N" first="Nicolas" last="Navrot">Nicolas Navrot</name><name sortKey="Panjikar, Santosh" sort="Panjikar, Santosh" uniqKey="Panjikar S" first="Santosh" last="Panjikar">Santosh Panjikar</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Shawkataly, Omar" sort="Shawkataly, Omar" uniqKey="Shawkataly O" first="Omar" last="Shawkataly">Omar Shawkataly</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Koh, Cha San" sort="Koh, Cha San" uniqKey="Koh C" first="Cha San" last="Koh">Cha San Koh</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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