Redox-dependent regulation of the Na⁺-K⁺ pump: new twists to an old target for treatment of heart failure.
Identifieur interne : 000720 ( Main/Exploration ); précédent : 000719; suivant : 000721Redox-dependent regulation of the Na⁺-K⁺ pump: new twists to an old target for treatment of heart failure.
Auteurs : Chia-Chi Liu [Australie] ; Natasha A S. Fry ; Elisha J. Hamilton ; Karin K M. Chia ; Alvaro Garcia ; Keyvan Karimi Galougahi ; Gemma A. Figtree ; Ronald J. Clarke ; Henning Bundgaard ; Helge H. RasmussenSource :
- Journal of molecular and cellular cardiology [ 1095-8584 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cardiotoniques (pharmacologie), Cardiotoniques (usage thérapeutique), Données de séquences moléculaires (MeSH), Défaillance cardiaque (enzymologie), Défaillance cardiaque (traitement médicamenteux), Humains (MeSH), Inhibiteurs de protéines kinases (pharmacologie), Inhibiteurs de protéines kinases (usage thérapeutique), Maturation post-traductionnelle des protéines (MeSH), Oxydoréduction (MeSH), Phosphoprotéines (composition chimique), Phosphorylation (MeSH), Protein kinases (métabolisme), Protéines membranaires (composition chimique), Sodium-Potassium-Exchanging ATPase (antagonistes et inhibiteurs), Sodium-Potassium-Exchanging ATPase (métabolisme), Séquence d'acides aminés (MeSH), Transduction du signal (MeSH).
- MESH :
- antagonistes et inhibiteurs : Sodium-Potassium-Exchanging ATPase.
- composition chimique : Phosphoprotéines, Protéines membranaires.
- enzymologie : Défaillance cardiaque.
- métabolisme : Protein kinases, Sodium-Potassium-Exchanging ATPase.
- pharmacologie : Cardiotoniques, Inhibiteurs de protéines kinases.
- traitement médicamenteux : Défaillance cardiaque.
- usage thérapeutique : Cardiotoniques, Inhibiteurs de protéines kinases.
- Animaux, Données de séquences moléculaires, Humains, Maturation post-traductionnelle des protéines, Oxydoréduction, Phosphorylation, Séquence d'acides aminés, Transduction du signal.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Cardiotonic Agents (pharmacology), Cardiotonic Agents (therapeutic use), Heart Failure (drug therapy), Heart Failure (enzymology), Humans (MeSH), Membrane Proteins (chemistry), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Phosphoproteins (chemistry), Phosphorylation (MeSH), Protein Kinase Inhibitors (pharmacology), Protein Kinase Inhibitors (therapeutic use), Protein Kinases (metabolism), Protein Processing, Post-Translational (MeSH), Signal Transduction (MeSH), Sodium-Potassium-Exchanging ATPase (antagonists & inhibitors), Sodium-Potassium-Exchanging ATPase (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Sodium-Potassium-Exchanging ATPase.
- chemical , chemistry : Membrane Proteins, Phosphoproteins.
- chemical , metabolism : Protein Kinases, Sodium-Potassium-Exchanging ATPase.
- chemical , pharmacology : Cardiotonic Agents, Protein Kinase Inhibitors.
- chemical , therapeutic use : Cardiotonic Agents, Protein Kinase Inhibitors.
- drug therapy : Heart Failure.
- enzymology : Heart Failure.
- Amino Acid Sequence, Animals, Humans, Molecular Sequence Data, Oxidation-Reduction, Phosphorylation, Protein Processing, Post-Translational, Signal Transduction.
Abstract
By the time it was appreciated that the positive inotropic effect of cardiac glycosides is due to inhibition of the membrane Na(+)-K(+) pump, glycosides had been used for treatment of heart failure on an empiric basis for ~200 years. The subsequent documentation of their lack of clinical efficacy and possible harmful effect largely coincided with the discovery that a raised Na(+) concentration in cardiac myocytes plays an important role in the electromechanical phenotype of heart failure syndromes. Consistent with this, efficacious pharmacological treatments for heart failure have been found to stimulate the Na(+)-K(+) pump, effectively the only export route for intracellular Na(+) in the heart failure. A paradigm has emerged that implicates pump inhibition in the raised Na(+) levels in heart failure. It invokes protein kinase-dependent activation of nicotinamide adenine dinucleotide phosphate oxidase (NADPH oxidase) and glutathionylation, a reversible oxidative modification, of the Na(+)-K(+) pump molecular complex that inhibits its activity. Since treatments of proven efficacy reverse the oxidative Na(+)-K(+) pump inhibition, the pump retains its status as a key pharmacological target in heart failure. Its role as a target is well integrated with the paradigms of neurohormonal abnormalities, raised myocardial oxidative stress and energy deficiency implicated in the pathophysiology of the failing heart. We propose that targeting oxidative inhibition of the pump is useful for the exploration of future treatment strategies. This article is part of a Special Issue entitled "Na(+)Regulation in Cardiac Myocytes".
DOI: 10.1016/j.yjmcc.2013.05.013
PubMed: 23727392
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Clarke</name></author><author><name sortKey="Bundgaard, Henning" sort="Bundgaard, Henning" uniqKey="Bundgaard H" first="Henning" last="Bundgaard">Henning Bundgaard</name></author><author><name sortKey="Rasmussen, Helge H" sort="Rasmussen, Helge H" uniqKey="Rasmussen H" first="Helge H" last="Rasmussen">Helge H. Rasmussen</name></author></analytic><series><title level="j">Journal of molecular and cellular cardiology</title><idno type="eISSN">1095-8584</idno><imprint><date when="2013" type="published">2013</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>Cardiotonic Agents (pharmacology)</term><term>Cardiotonic Agents (therapeutic use)</term><term>Heart Failure (drug therapy)</term><term>Heart Failure (enzymology)</term><term>Humans (MeSH)</term><term>Membrane Proteins (chemistry)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Phosphoproteins (chemistry)</term><term>Phosphorylation (MeSH)</term><term>Protein Kinase Inhibitors (pharmacology)</term><term>Protein Kinase Inhibitors (therapeutic use)</term><term>Protein Kinases (metabolism)</term><term>Protein Processing, Post-Translational (MeSH)</term><term>Signal Transduction (MeSH)</term><term>Sodium-Potassium-Exchanging ATPase (antagonists & inhibitors)</term><term>Sodium-Potassium-Exchanging ATPase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cardiotoniques (pharmacologie)</term><term>Cardiotoniques (usage thérapeutique)</term><term>Données de séquences moléculaires (MeSH)</term><term>Défaillance cardiaque (enzymologie)</term><term>Défaillance cardiaque (traitement médicamenteux)</term><term>Humains (MeSH)</term><term>Inhibiteurs de protéines kinases (pharmacologie)</term><term>Inhibiteurs de protéines kinases (usage thérapeutique)</term><term>Maturation post-traductionnelle des protéines (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Phosphoprotéines (composition chimique)</term><term>Phosphorylation (MeSH)</term><term>Protein kinases (métabolisme)</term><term>Protéines membranaires (composition chimique)</term><term>Sodium-Potassium-Exchanging ATPase (antagonistes et inhibiteurs)</term><term>Sodium-Potassium-Exchanging ATPase (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Sodium-Potassium-Exchanging ATPase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Proteins</term><term>Phosphoproteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Protein Kinases</term><term>Sodium-Potassium-Exchanging ATPase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cardiotonic Agents</term><term>Protein Kinase Inhibitors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>Cardiotonic Agents</term><term>Protein Kinase Inhibitors</term></keywords><keywords scheme="MESH" 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scheme="MESH" qualifier="usage thérapeutique" xml:lang="fr"><term>Cardiotoniques</term><term>Inhibiteurs de protéines kinases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Humans</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Phosphorylation</term><term>Protein Processing, Post-Translational</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Maturation post-traductionnelle des protéines</term><term>Oxydoréduction</term><term>Phosphorylation</term><term>Séquence d'acides aminés</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">By the time it was appreciated that the positive inotropic effect of cardiac glycosides is due to inhibition of the membrane Na(+)-K(+) pump, glycosides had been used for treatment of heart failure on an empiric basis for ~200 years. The subsequent documentation of their lack of clinical efficacy and possible harmful effect largely coincided with the discovery that a raised Na(+) concentration in cardiac myocytes plays an important role in the electromechanical phenotype of heart failure syndromes. Consistent with this, efficacious pharmacological treatments for heart failure have been found to stimulate the Na(+)-K(+) pump, effectively the only export route for intracellular Na(+) in the heart failure. A paradigm has emerged that implicates pump inhibition in the raised Na(+) levels in heart failure. It invokes protein kinase-dependent activation of nicotinamide adenine dinucleotide phosphate oxidase (NADPH oxidase) and glutathionylation, a reversible oxidative modification, of the Na(+)-K(+) pump molecular complex that inhibits its activity. Since treatments of proven efficacy reverse the oxidative Na(+)-K(+) pump inhibition, the pump retains its status as a key pharmacological target in heart failure. Its role as a target is well integrated with the paradigms of neurohormonal abnormalities, raised myocardial oxidative stress and energy deficiency implicated in the pathophysiology of the failing heart. We propose that targeting oxidative inhibition of the pump is useful for the exploration of future treatment strategies. This article is part of a Special Issue entitled "Na(+)Regulation in Cardiac Myocytes".</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23727392</PMID><DateCompleted><Year>2014</Year><Month>02</Month><Day>13</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1095-8584</ISSN><JournalIssue CitedMedium="Internet"><Volume>61</Volume><PubDate><Year>2013</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Journal of molecular and cellular cardiology</Title><ISOAbbreviation>J Mol Cell Cardiol</ISOAbbreviation></Journal><ArticleTitle>Redox-dependent regulation of the Na⁺-K⁺ pump: new twists to an old target for treatment of heart failure.</ArticleTitle><Pagination><MedlinePgn>94-101</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.yjmcc.2013.05.013</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0022-2828(13)00181-8</ELocationID><Abstract><AbstractText>By the time it was appreciated that the positive inotropic effect of cardiac glycosides is due to inhibition of the membrane Na(+)-K(+) pump, glycosides had been used for treatment of heart failure on an empiric basis for ~200 years. The subsequent documentation of their lack of clinical efficacy and possible harmful effect largely coincided with the discovery that a raised Na(+) concentration in cardiac myocytes plays an important role in the electromechanical phenotype of heart failure syndromes. Consistent with this, efficacious pharmacological treatments for heart failure have been found to stimulate the Na(+)-K(+) pump, effectively the only export route for intracellular Na(+) in the heart failure. A paradigm has emerged that implicates pump inhibition in the raised Na(+) levels in heart failure. It invokes protein kinase-dependent activation of nicotinamide adenine dinucleotide phosphate oxidase (NADPH oxidase) and glutathionylation, a reversible oxidative modification, of the Na(+)-K(+) pump molecular complex that inhibits its activity. Since treatments of proven efficacy reverse the oxidative Na(+)-K(+) pump inhibition, the pump retains its status as a key pharmacological target in heart failure. Its role as a target is well integrated with the paradigms of neurohormonal abnormalities, raised myocardial oxidative stress and energy deficiency implicated in the pathophysiology of the failing heart. We propose that targeting oxidative inhibition of the pump is useful for the exploration of future treatment strategies. This article is part of a Special Issue entitled "Na(+)Regulation in Cardiac Myocytes".</AbstractText><CopyrightInformation>Copyright © 2013 The Authors. Published by Elsevier Ltd.. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Chia-Chi</ForeName><Initials>CC</Initials><AffiliationInfo><Affiliation>North Shore Heart Research Group, Kolling Medical Research Institute, University of Sydney, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fry</LastName><ForeName>Natasha A S</ForeName><Initials>NA</Initials></Author><Author ValidYN="Y"><LastName>Hamilton</LastName><ForeName>Elisha J</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Chia</LastName><ForeName>Karin K M</ForeName><Initials>KK</Initials></Author><Author ValidYN="Y"><LastName>Garcia</LastName><ForeName>Alvaro</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Karimi Galougahi</LastName><ForeName>Keyvan</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Figtree</LastName><ForeName>Gemma A</ForeName><Initials>GA</Initials></Author><Author ValidYN="Y"><LastName>Clarke</LastName><ForeName>Ronald J</ForeName><Initials>RJ</Initials></Author><Author ValidYN="Y"><LastName>Bundgaard</LastName><ForeName>Henning</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Rasmussen</LastName><ForeName>Helge H</ForeName><Initials>HH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>05</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Mol Cell Cardiol</MedlineTA><NlmUniqueID>0262322</NlmUniqueID><ISSNLinking>0022-2828</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002316">Cardiotonic Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008565">Membrane Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010750">Phosphoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D047428">Protein Kinase Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>135541-82-1</RegistryNumber><NameOfSubstance UI="C069141">phospholemman</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 7.2.2.13</RegistryNumber><NameOfSubstance UI="D000254">Sodium-Potassium-Exchanging ATPase</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="D002316" MajorTopicYN="N">Cardiotonic Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006333" MajorTopicYN="N">Heart Failure</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="Y">drug therapy</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008565" MajorTopicYN="N">Membrane Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></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="D010750" MajorTopicYN="N">Phosphoproteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047428" MajorTopicYN="N">Protein Kinase Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000254" MajorTopicYN="N">Sodium-Potassium-Exchanging ATPase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">ACE</Keyword><Keyword MajorTopicYN="N">AR</Keyword><Keyword MajorTopicYN="N">Ang II</Keyword><Keyword MajorTopicYN="N">GSH</Keyword><Keyword MajorTopicYN="N">Grx1</Keyword><Keyword MajorTopicYN="N">Heart failure</Keyword><Keyword MajorTopicYN="N">I(p)</Keyword><Keyword MajorTopicYN="N">NADPH oxidase</Keyword><Keyword MajorTopicYN="N">NO</Keyword><Keyword MajorTopicYN="N">Na(+)–K(+) pump</Keyword><Keyword MajorTopicYN="N">ONOO(−)</Keyword><Keyword MajorTopicYN="N">PKA</Keyword><Keyword MajorTopicYN="N">PKC</Keyword><Keyword MajorTopicYN="N">PKG</Keyword><Keyword MajorTopicYN="N">PP2A</Keyword><Keyword MajorTopicYN="N">Redox regulation</Keyword><Keyword MajorTopicYN="N">[Na(+)](i)</Keyword><Keyword MajorTopicYN="N">adrenergic receptor</Keyword><Keyword MajorTopicYN="N">angiotensin II</Keyword><Keyword MajorTopicYN="N">angiotensin converting enzyme</Keyword><Keyword MajorTopicYN="N">cAMP</Keyword><Keyword MajorTopicYN="N">cyclic adenosine monophosphate, πGST, π isoform of glutathione S-transferase</Keyword><Keyword MajorTopicYN="N">electrogenic Na(+)–K(+) pump current</Keyword><Keyword MajorTopicYN="N">glutaredoxin 1</Keyword><Keyword MajorTopicYN="N">glutathione</Keyword><Keyword MajorTopicYN="N">intracellular Na(+) concentration</Keyword><Keyword MajorTopicYN="N">nicotinamide adenine dinucleotide phosphate-oxidase</Keyword><Keyword MajorTopicYN="N">nitric oxide</Keyword><Keyword MajorTopicYN="N">peroxynitrite</Keyword><Keyword MajorTopicYN="N">protein kinase A</Keyword><Keyword MajorTopicYN="N">protein kinase C</Keyword><Keyword MajorTopicYN="N">protein kinase G</Keyword><Keyword MajorTopicYN="N">protein phosphatase 2A</Keyword><Keyword MajorTopicYN="N">sGC</Keyword><Keyword MajorTopicYN="N">soluble guanylyl cyclase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>01</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>05</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>05</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>6</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>6</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>2</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23727392</ArticleId><ArticleId IdType="pii">S0022-2828(13)00181-8</ArticleId><ArticleId IdType="doi">10.1016/j.yjmcc.2013.05.013</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li></country><region><li>Nouvelle-Galles du Sud</li></region><settlement><li>Sydney</li></settlement><orgName><li>Université de Sydney</li></orgName></list><tree><noCountry><name sortKey="Bundgaard, Henning" sort="Bundgaard, Henning" uniqKey="Bundgaard H" first="Henning" last="Bundgaard">Henning Bundgaard</name><name sortKey="Chia, Karin K M" sort="Chia, Karin K M" uniqKey="Chia K" first="Karin K M" last="Chia">Karin K M. Chia</name><name sortKey="Clarke, Ronald J" sort="Clarke, Ronald J" uniqKey="Clarke R" first="Ronald J" last="Clarke">Ronald J. Clarke</name><name sortKey="Figtree, Gemma A" sort="Figtree, Gemma A" uniqKey="Figtree G" first="Gemma A" last="Figtree">Gemma A. Figtree</name><name sortKey="Fry, Natasha A S" sort="Fry, Natasha A S" uniqKey="Fry N" first="Natasha A S" last="Fry">Natasha A S. Fry</name><name sortKey="Garcia, Alvaro" sort="Garcia, Alvaro" uniqKey="Garcia A" first="Alvaro" last="Garcia">Alvaro Garcia</name><name sortKey="Hamilton, Elisha J" sort="Hamilton, Elisha J" uniqKey="Hamilton E" first="Elisha J" last="Hamilton">Elisha J. Hamilton</name><name sortKey="Karimi Galougahi, Keyvan" sort="Karimi Galougahi, Keyvan" uniqKey="Karimi Galougahi K" first="Keyvan" last="Karimi Galougahi">Keyvan Karimi Galougahi</name><name sortKey="Rasmussen, Helge H" sort="Rasmussen, Helge H" uniqKey="Rasmussen H" first="Helge H" last="Rasmussen">Helge H. Rasmussen</name></noCountry><country name="Australie"><region name="Nouvelle-Galles du Sud"><name sortKey="Liu, Chia Chi" sort="Liu, Chia Chi" uniqKey="Liu C" first="Chia-Chi" last="Liu">Chia-Chi Liu</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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