Inhibition of bacterial thioredoxin reductase: an antibiotic mechanism targeting bacteria lacking glutathione.
Identifieur interne : 000749 ( Main/Exploration ); précédent : 000748; suivant : 000750Inhibition of bacterial thioredoxin reductase: an antibiotic mechanism targeting bacteria lacking glutathione.
Auteurs : Jun Lu [Suède] ; Alexios Vlamis-Gardikas ; Karuppasamy Kandasamy ; Rong Zhao ; Tomas N. Gustafsson ; Lars Engstrand ; Sven Hoffner ; Lars Engman ; Arne HolmgrenSource :
- FASEB journal : official publication of the Federation of American Societies for Experimental Biology [ 1530-6860 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Antioxydants (pharmacologie), Azoles (pharmacologie), Cellules cultivées (MeSH), Composés organiques du sélénium (pharmacologie), Escherichia coli (MeSH), Glutathion (déficit), Glutathion (métabolisme), NADP (métabolisme), Stress oxydatif (effets des médicaments et des substances chimiques), Stress oxydatif (physiologie), Thioredoxin-disulfide reductase (antagonistes et inhibiteurs), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (métabolisme), Transduction du signal (effets des médicaments et des substances chimiques), Transduction du signal (physiologie).
- MESH :
- antagonistes et inhibiteurs : Thioredoxin-disulfide reductase.
- déficit : Glutathion.
- effets des médicaments et des substances chimiques : Stress oxydatif, Transduction du signal.
- métabolisme : Glutathion, NADP, Thioredoxin-disulfide reductase, Thiorédoxines.
- pharmacologie : Antioxydants, Azoles, Composés organiques du sélénium.
- physiologie : Stress oxydatif, Transduction du signal.
- Animaux, Cellules cultivées, Escherichia coli.
English descriptors
- KwdEn :
- Animals (MeSH), Antioxidants (pharmacology), Azoles (pharmacology), Cells, Cultured (MeSH), Escherichia coli (MeSH), Glutathione (deficiency), Glutathione (metabolism), NADP (metabolism), Organoselenium Compounds (pharmacology), Oxidative Stress (drug effects), Oxidative Stress (physiology), Signal Transduction (drug effects), Signal Transduction (physiology), Thioredoxin-Disulfide Reductase (antagonists & inhibitors), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Thioredoxin-Disulfide Reductase.
- chemical , deficiency : Glutathione.
- chemical , metabolism : Glutathione, NADP, Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical , pharmacology : Antioxidants, Azoles, Organoselenium Compounds.
- drug effects : Oxidative Stress, Signal Transduction.
- physiology : Oxidative Stress, Signal Transduction.
- Animals, Cells, Cultured, Escherichia coli.
Abstract
Increasing antibiotic resistance makes the identification of new antibacterial principles an urgent task. The thioredoxin system including thioredoxin reductase (TrxR), thioredoxin (Trx), and NADPH plays critical roles in cellular DNA synthesis and defense against oxidative stress. Notably, TrxR is very different in structure and mechanism in mammals and bacteria. Ebselen [2-phenyl-1,2 benzisoselenazol-3(2H)-one], a well-known antioxidant and a substrate for mammalian TrxR and Trx, is rapidly bacteriocidal for methicillin-resistant Staphylococcus aureus by an unknown mechanism. We have discovered that ebselen is a competitive inhibitor of Escherichia coli TrxR with a Ki of 0.52 ± 0.13 μM, through reaction with the active site dithiol of the enzyme. Bacteria lacking glutathione (GSH) and glutaredoxin, in which TrxR and Trx are essential for DNA synthesis, were particularly sensitive to ebselen. In growth-inhibited E. coli strains, Trx1 and Trx2 were oxidized, demonstrating that electron transfer via thioredoxin was blocked. Ebselen and its sulfur analog ebsulfur were bactericidal for GSH-negative pathogens. Ebsulfur inhibited a clinically isolated Helicobacter pylori strain with a minimum inhibitory concentration value as low as 0.39 μg/ml. These results demonstrate that bacterial Trx and TrxR are viable antibacterial drug targets using benzisoselenazol and benzisothiazol derivates.
DOI: 10.1096/fj.12-223305
PubMed: 23248236
Affiliations:
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Gustafsson</name></author><author><name sortKey="Engstrand, Lars" sort="Engstrand, Lars" uniqKey="Engstrand L" first="Lars" last="Engstrand">Lars Engstrand</name></author><author><name sortKey="Hoffner, Sven" sort="Hoffner, Sven" uniqKey="Hoffner S" first="Sven" last="Hoffner">Sven Hoffner</name></author><author><name sortKey="Engman, Lars" sort="Engman, Lars" uniqKey="Engman L" first="Lars" last="Engman">Lars Engman</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23248236</idno><idno type="pmid">23248236</idno><idno type="doi">10.1096/fj.12-223305</idno><idno type="wicri:Area/Main/Corpus">000780</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000780</idno><idno type="wicri:Area/Main/Curation">000780</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000780</idno><idno type="wicri:Area/Main/Exploration">000780</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Inhibition of bacterial thioredoxin reductase: an antibiotic mechanism targeting bacteria lacking glutathione.</title><author><name sortKey="Lu, Jun" sort="Lu, Jun" uniqKey="Lu J" first="Jun" last="Lu">Jun Lu</name><affiliation wicri:level="3"><nlm:affiliation>Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author><author><name sortKey="Vlamis Gardikas, Alexios" sort="Vlamis Gardikas, Alexios" uniqKey="Vlamis Gardikas A" first="Alexios" last="Vlamis-Gardikas">Alexios Vlamis-Gardikas</name></author><author><name sortKey="Kandasamy, Karuppasamy" sort="Kandasamy, Karuppasamy" uniqKey="Kandasamy K" first="Karuppasamy" last="Kandasamy">Karuppasamy Kandasamy</name></author><author><name sortKey="Zhao, Rong" sort="Zhao, Rong" uniqKey="Zhao R" first="Rong" last="Zhao">Rong Zhao</name></author><author><name sortKey="Gustafsson, Tomas N" sort="Gustafsson, Tomas N" uniqKey="Gustafsson T" first="Tomas N" last="Gustafsson">Tomas N. Gustafsson</name></author><author><name sortKey="Engstrand, Lars" sort="Engstrand, Lars" uniqKey="Engstrand L" first="Lars" last="Engstrand">Lars Engstrand</name></author><author><name sortKey="Hoffner, Sven" sort="Hoffner, Sven" uniqKey="Hoffner S" first="Sven" last="Hoffner">Sven Hoffner</name></author><author><name sortKey="Engman, Lars" sort="Engman, Lars" uniqKey="Engman L" first="Lars" last="Engman">Lars Engman</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author></analytic><series><title level="j">FASEB journal : official publication of the Federation of American Societies for Experimental Biology</title><idno type="eISSN">1530-6860</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Antioxidants (pharmacology)</term><term>Azoles (pharmacology)</term><term>Cells, Cultured (MeSH)</term><term>Escherichia coli (MeSH)</term><term>Glutathione (deficiency)</term><term>Glutathione (metabolism)</term><term>NADP (metabolism)</term><term>Organoselenium Compounds (pharmacology)</term><term>Oxidative Stress (drug effects)</term><term>Oxidative Stress (physiology)</term><term>Signal Transduction (drug effects)</term><term>Signal Transduction (physiology)</term><term>Thioredoxin-Disulfide Reductase (antagonists & inhibitors)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Antioxydants (pharmacologie)</term><term>Azoles (pharmacologie)</term><term>Cellules cultivées (MeSH)</term><term>Composés organiques du sélénium (pharmacologie)</term><term>Escherichia coli (MeSH)</term><term>Glutathion (déficit)</term><term>Glutathion (métabolisme)</term><term>NADP (métabolisme)</term><term>Stress oxydatif (effets des médicaments et des substances chimiques)</term><term>Stress oxydatif (physiologie)</term><term>Thioredoxin-disulfide reductase (antagonistes et inhibiteurs)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term><term>Thiorédoxines (métabolisme)</term><term>Transduction du signal (effets des médicaments et des substances chimiques)</term><term>Transduction du signal (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Glutathione</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>NADP</term><term>Thioredoxin-Disulfide Reductase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antioxidants</term><term>Azoles</term><term>Organoselenium Compounds</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Oxidative Stress</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Glutathion</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Stress oxydatif</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>NADP</term><term>Thioredoxin-disulfide reductase</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antioxydants</term><term>Azoles</term><term>Composés organiques du sélénium</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Stress oxydatif</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Oxidative Stress</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Escherichia coli</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules cultivées</term><term>Escherichia coli</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Increasing antibiotic resistance makes the identification of new antibacterial principles an urgent task. The thioredoxin system including thioredoxin reductase (TrxR), thioredoxin (Trx), and NADPH plays critical roles in cellular DNA synthesis and defense against oxidative stress. Notably, TrxR is very different in structure and mechanism in mammals and bacteria. Ebselen [2-phenyl-1,2 benzisoselenazol-3(2H)-one], a well-known antioxidant and a substrate for mammalian TrxR and Trx, is rapidly bacteriocidal for methicillin-resistant Staphylococcus aureus by an unknown mechanism. We have discovered that ebselen is a competitive inhibitor of Escherichia coli TrxR with a Ki of 0.52 ± 0.13 μM, through reaction with the active site dithiol of the enzyme. Bacteria lacking glutathione (GSH) and glutaredoxin, in which TrxR and Trx are essential for DNA synthesis, were particularly sensitive to ebselen. In growth-inhibited E. coli strains, Trx1 and Trx2 were oxidized, demonstrating that electron transfer via thioredoxin was blocked. Ebselen and its sulfur analog ebsulfur were bactericidal for GSH-negative pathogens. Ebsulfur inhibited a clinically isolated Helicobacter pylori strain with a minimum inhibitory concentration value as low as 0.39 μg/ml. These results demonstrate that bacterial Trx and TrxR are viable antibacterial drug targets using benzisoselenazol and benzisothiazol derivates.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23248236</PMID><DateCompleted><Year>2013</Year><Month>06</Month><Day>17</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1530-6860</ISSN><JournalIssue CitedMedium="Internet"><Volume>27</Volume><Issue>4</Issue><PubDate><Year>2013</Year><Month>Apr</Month></PubDate></JournalIssue><Title>FASEB journal : official publication of the Federation of American Societies for Experimental Biology</Title><ISOAbbreviation>FASEB J</ISOAbbreviation></Journal><ArticleTitle>Inhibition of bacterial thioredoxin reductase: an antibiotic mechanism targeting bacteria lacking glutathione.</ArticleTitle><Pagination><MedlinePgn>1394-403</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1096/fj.12-223305</ELocationID><Abstract><AbstractText>Increasing antibiotic resistance makes the identification of new antibacterial principles an urgent task. The thioredoxin system including thioredoxin reductase (TrxR), thioredoxin (Trx), and NADPH plays critical roles in cellular DNA synthesis and defense against oxidative stress. Notably, TrxR is very different in structure and mechanism in mammals and bacteria. Ebselen [2-phenyl-1,2 benzisoselenazol-3(2H)-one], a well-known antioxidant and a substrate for mammalian TrxR and Trx, is rapidly bacteriocidal for methicillin-resistant Staphylococcus aureus by an unknown mechanism. We have discovered that ebselen is a competitive inhibitor of Escherichia coli TrxR with a Ki of 0.52 ± 0.13 μM, through reaction with the active site dithiol of the enzyme. Bacteria lacking glutathione (GSH) and glutaredoxin, in which TrxR and Trx are essential for DNA synthesis, were particularly sensitive to ebselen. In growth-inhibited E. coli strains, Trx1 and Trx2 were oxidized, demonstrating that electron transfer via thioredoxin was blocked. Ebselen and its sulfur analog ebsulfur were bactericidal for GSH-negative pathogens. Ebsulfur inhibited a clinically isolated Helicobacter pylori strain with a minimum inhibitory concentration value as low as 0.39 μg/ml. These results demonstrate that bacterial Trx and TrxR are viable antibacterial drug targets using benzisoselenazol and benzisothiazol derivates.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>Jun</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vlamis-Gardikas</LastName><ForeName>Alexios</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Kandasamy</LastName><ForeName>Karuppasamy</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Zhao</LastName><ForeName>Rong</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Gustafsson</LastName><ForeName>Tomas N</ForeName><Initials>TN</Initials></Author><Author ValidYN="Y"><LastName>Engstrand</LastName><ForeName>Lars</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Hoffner</LastName><ForeName>Sven</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Engman</LastName><ForeName>Lars</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>Arne</ForeName><Initials>A</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>2012</Year><Month>12</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>FASEB J</MedlineTA><NlmUniqueID>8804484</NlmUniqueID><ISSNLinking>0892-6638</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000975">Antioxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001393">Azoles</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016566">Organoselenium Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>40X2P7DPGH</RegistryNumber><NameOfSubstance UI="C042986">ebselen</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000975" MajorTopicYN="N">Antioxidants</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001393" MajorTopicYN="N">Azoles</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000172" MajorTopicYN="N">deficiency</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016566" MajorTopicYN="N">Organoselenium Compounds</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>12</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>12</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>6</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23248236</ArticleId><ArticleId IdType="pii">fj.12-223305</ArticleId><ArticleId IdType="doi">10.1096/fj.12-223305</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><noCountry><name sortKey="Engman, Lars" sort="Engman, Lars" uniqKey="Engman L" first="Lars" last="Engman">Lars Engman</name><name sortKey="Engstrand, Lars" sort="Engstrand, Lars" uniqKey="Engstrand L" first="Lars" last="Engstrand">Lars Engstrand</name><name sortKey="Gustafsson, Tomas N" sort="Gustafsson, Tomas N" uniqKey="Gustafsson T" first="Tomas N" last="Gustafsson">Tomas N. Gustafsson</name><name sortKey="Hoffner, Sven" sort="Hoffner, Sven" uniqKey="Hoffner S" first="Sven" last="Hoffner">Sven Hoffner</name><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name><name sortKey="Kandasamy, Karuppasamy" sort="Kandasamy, Karuppasamy" uniqKey="Kandasamy K" first="Karuppasamy" last="Kandasamy">Karuppasamy Kandasamy</name><name sortKey="Vlamis Gardikas, Alexios" sort="Vlamis Gardikas, Alexios" uniqKey="Vlamis Gardikas A" first="Alexios" last="Vlamis-Gardikas">Alexios Vlamis-Gardikas</name><name sortKey="Zhao, Rong" sort="Zhao, Rong" uniqKey="Zhao R" first="Rong" last="Zhao">Rong Zhao</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Lu, Jun" sort="Lu, Jun" uniqKey="Lu J" first="Jun" last="Lu">Jun Lu</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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