Binding Interactions of Dopamine and Apomorphine in D2High and D2Low States of Human Dopamine D2 Receptor Using Computational and Experimental Techniques.
Identifieur interne : 000293 ( PubMed/Curation ); précédent : 000292; suivant : 000294Binding Interactions of Dopamine and Apomorphine in D2High and D2Low States of Human Dopamine D2 Receptor Using Computational and Experimental Techniques.
Auteurs : Serdar Durdagi [Turquie] ; Ramin Ekhteiari Salmas [Turquie] ; Matthias Stein [Allemagne] ; Mine Yurtsever [Turquie] ; Philip SeemanSource :
- ACS chemical neuroscience [ 1948-7193 ] ; 2016.
English descriptors
- KwdEn :
- Apomorphine (metabolism), Apomorphine (pharmacology), Binding, Competitive (drug effects), Dopamine (metabolism), Dopamine (pharmacology), Dopamine Agonists (pharmacology), Dose-Response Relationship, Drug, Humans, Models, Molecular, Molecular Docking Simulation (methods), Protein Binding (drug effects), Protein Engineering, Receptors, Dopamine D2 (chemistry), Receptors, Dopamine D2 (drug effects), Receptors, Dopamine D2 (metabolism).
- MESH :
- chemical , chemistry : Receptors, Dopamine D2.
- chemical , drug effects : Receptors, Dopamine D2.
- chemical , metabolism : Apomorphine, Dopamine, Receptors, Dopamine D2.
- chemical , pharmacology : Apomorphine, Dopamine, Dopamine Agonists.
- drug effects : Binding, Competitive, Protein Binding.
- methods : Molecular Docking Simulation.
- Dose-Response Relationship, Drug, Humans, Models, Molecular, Protein Engineering.
Abstract
We have recently reported G-protein coupled receptor (GPCR) model structures for the active and inactive states of the human dopamine D2 receptor (D2R) using adrenergic crystal structures as templates. Since the therapeutic concentrations of dopamine agonists that suppress the release of prolactin are the same as those that act at the high-affinity state of the D2 receptor (D2High), D2High in the anterior pituitary gland is considered to be the functional state of the receptor. In addition, the therapeutic concentrations of anti-Parkinson drugs are also related to the dissociation constants in the D2High form of the receptor. The discrimination between the high- and low-affinity (D2Low) components of the D2R is not obvious and requires advanced computer-assisted structural biology investigations. Therefore, in this work, the derived D2High and D2Low receptor models (GPCR monomer and dimer three-dimensional structures) are used as drug-binding targets to investigate binding interactions of dopamine and apomorphine. The study reveals a match between the experimental dissociation constants of dopamine and apomorphine at their high- and low-affinity sites of the D2 receptor in monomer and dimer and their calculated dissociation constants. The allosteric receptor-receptor interaction for dopamine D2R dimer is associated with the accessibility of adjacent residues of transmembrane region 4. The measured negative cooperativity between agonist ligand at dopamine D2 receptor is also correctly predicted using the D2R homodimerization model.
DOI: 10.1021/acschemneuro.5b00271
PubMed: 26645629
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000293
Links to Exploration step
pubmed:26645629Curation
No country items
Philip Seeman<affiliation><nlm:affiliation>Departments of Pharmacology and Psychiatry, University of Toronto , 260 Heath Street West, Unit 605, M5P 3L6, Toronto, Ontario Canada.</nlm:affiliation>
<wicri:noCountry code="subField">Ontario Canada</wicri:noCountry>
</affiliation>
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Binding Interactions of Dopamine and Apomorphine in D2High and D2Low States of Human Dopamine D2 Receptor Using Computational and Experimental Techniques.</title>
<author><name sortKey="Durdagi, Serdar" sort="Durdagi, Serdar" uniqKey="Durdagi S" first="Serdar" last="Durdagi">Serdar Durdagi</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Biophysics, School of Medicine, Bahcesehir University , 34349 Istanbul, Turkey.</nlm:affiliation>
<country xml:lang="fr">Turquie</country>
<wicri:regionArea>Department of Biophysics, School of Medicine, Bahcesehir University , 34349 Istanbul</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Salmas, Ramin Ekhteiari" sort="Salmas, Ramin Ekhteiari" uniqKey="Salmas R" first="Ramin Ekhteiari" last="Salmas">Ramin Ekhteiari Salmas</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Biophysics, School of Medicine, Bahcesehir University , 34349 Istanbul, Turkey.</nlm:affiliation>
<country xml:lang="fr">Turquie</country>
<wicri:regionArea>Department of Biophysics, School of Medicine, Bahcesehir University , 34349 Istanbul</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Stein, Matthias" sort="Stein, Matthias" uniqKey="Stein M" first="Matthias" last="Stein">Matthias Stein</name>
<affiliation wicri:level="1"><nlm:affiliation>Molecular Simulations and Design Group, Max-Planck Institute for Dynamics of Complex Technical Systems , Sandtorstrasse 1, 39106, Magdeburg, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Molecular Simulations and Design Group, Max-Planck Institute for Dynamics of Complex Technical Systems , Sandtorstrasse 1, 39106, Magdeburg</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Yurtsever, Mine" sort="Yurtsever, Mine" uniqKey="Yurtsever M" first="Mine" last="Yurtsever">Mine Yurtsever</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Istanbul Technical University , 34469 Istanbul, Turkey.</nlm:affiliation>
<country xml:lang="fr">Turquie</country>
<wicri:regionArea>Department of Chemistry, Istanbul Technical University , 34469 Istanbul</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Seeman, Philip" sort="Seeman, Philip" uniqKey="Seeman P" first="Philip" last="Seeman">Philip Seeman</name>
<affiliation><nlm:affiliation>Departments of Pharmacology and Psychiatry, University of Toronto , 260 Heath Street West, Unit 605, M5P 3L6, Toronto, Ontario Canada.</nlm:affiliation>
<wicri:noCountry code="subField">Ontario Canada</wicri:noCountry>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2016">2016</date>
<idno type="RBID">pubmed:26645629</idno>
<idno type="pmid">26645629</idno>
<idno type="doi">10.1021/acschemneuro.5b00271</idno>
<idno type="wicri:Area/PubMed/Corpus">000293</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000293</idno>
<idno type="wicri:Area/PubMed/Curation">000293</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000293</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Binding Interactions of Dopamine and Apomorphine in D2High and D2Low States of Human Dopamine D2 Receptor Using Computational and Experimental Techniques.</title>
<author><name sortKey="Durdagi, Serdar" sort="Durdagi, Serdar" uniqKey="Durdagi S" first="Serdar" last="Durdagi">Serdar Durdagi</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Biophysics, School of Medicine, Bahcesehir University , 34349 Istanbul, Turkey.</nlm:affiliation>
<country xml:lang="fr">Turquie</country>
<wicri:regionArea>Department of Biophysics, School of Medicine, Bahcesehir University , 34349 Istanbul</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Salmas, Ramin Ekhteiari" sort="Salmas, Ramin Ekhteiari" uniqKey="Salmas R" first="Ramin Ekhteiari" last="Salmas">Ramin Ekhteiari Salmas</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Biophysics, School of Medicine, Bahcesehir University , 34349 Istanbul, Turkey.</nlm:affiliation>
<country xml:lang="fr">Turquie</country>
<wicri:regionArea>Department of Biophysics, School of Medicine, Bahcesehir University , 34349 Istanbul</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Stein, Matthias" sort="Stein, Matthias" uniqKey="Stein M" first="Matthias" last="Stein">Matthias Stein</name>
<affiliation wicri:level="1"><nlm:affiliation>Molecular Simulations and Design Group, Max-Planck Institute for Dynamics of Complex Technical Systems , Sandtorstrasse 1, 39106, Magdeburg, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Molecular Simulations and Design Group, Max-Planck Institute for Dynamics of Complex Technical Systems , Sandtorstrasse 1, 39106, Magdeburg</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Yurtsever, Mine" sort="Yurtsever, Mine" uniqKey="Yurtsever M" first="Mine" last="Yurtsever">Mine Yurtsever</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Istanbul Technical University , 34469 Istanbul, Turkey.</nlm:affiliation>
<country xml:lang="fr">Turquie</country>
<wicri:regionArea>Department of Chemistry, Istanbul Technical University , 34469 Istanbul</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Seeman, Philip" sort="Seeman, Philip" uniqKey="Seeman P" first="Philip" last="Seeman">Philip Seeman</name>
<affiliation><nlm:affiliation>Departments of Pharmacology and Psychiatry, University of Toronto , 260 Heath Street West, Unit 605, M5P 3L6, Toronto, Ontario Canada.</nlm:affiliation>
<wicri:noCountry code="subField">Ontario Canada</wicri:noCountry>
</affiliation>
</author>
</analytic>
<series><title level="j">ACS chemical neuroscience</title>
<idno type="eISSN">1948-7193</idno>
<imprint><date when="2016" type="published">2016</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Apomorphine (metabolism)</term>
<term>Apomorphine (pharmacology)</term>
<term>Binding, Competitive (drug effects)</term>
<term>Dopamine (metabolism)</term>
<term>Dopamine (pharmacology)</term>
<term>Dopamine Agonists (pharmacology)</term>
<term>Dose-Response Relationship, Drug</term>
<term>Humans</term>
<term>Models, Molecular</term>
<term>Molecular Docking Simulation (methods)</term>
<term>Protein Binding (drug effects)</term>
<term>Protein Engineering</term>
<term>Receptors, Dopamine D2 (chemistry)</term>
<term>Receptors, Dopamine D2 (drug effects)</term>
<term>Receptors, Dopamine D2 (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Receptors, Dopamine D2</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Receptors, Dopamine D2</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Apomorphine</term>
<term>Dopamine</term>
<term>Receptors, Dopamine D2</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Apomorphine</term>
<term>Dopamine</term>
<term>Dopamine Agonists</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Binding, Competitive</term>
<term>Protein Binding</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Molecular Docking Simulation</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Dose-Response Relationship, Drug</term>
<term>Humans</term>
<term>Models, Molecular</term>
<term>Protein Engineering</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">We have recently reported G-protein coupled receptor (GPCR) model structures for the active and inactive states of the human dopamine D2 receptor (D2R) using adrenergic crystal structures as templates. Since the therapeutic concentrations of dopamine agonists that suppress the release of prolactin are the same as those that act at the high-affinity state of the D2 receptor (D2High), D2High in the anterior pituitary gland is considered to be the functional state of the receptor. In addition, the therapeutic concentrations of anti-Parkinson drugs are also related to the dissociation constants in the D2High form of the receptor. The discrimination between the high- and low-affinity (D2Low) components of the D2R is not obvious and requires advanced computer-assisted structural biology investigations. Therefore, in this work, the derived D2High and D2Low receptor models (GPCR monomer and dimer three-dimensional structures) are used as drug-binding targets to investigate binding interactions of dopamine and apomorphine. The study reveals a match between the experimental dissociation constants of dopamine and apomorphine at their high- and low-affinity sites of the D2 receptor in monomer and dimer and their calculated dissociation constants. The allosteric receptor-receptor interaction for dopamine D2R dimer is associated with the accessibility of adjacent residues of transmembrane region 4. The measured negative cooperativity between agonist ligand at dopamine D2 receptor is also correctly predicted using the D2R homodimerization model.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26645629</PMID>
<DateCreated><Year>2016</Year>
<Month>02</Month>
<Day>17</Day>
</DateCreated>
<DateCompleted><Year>2016</Year>
<Month>12</Month>
<Day>13</Day>
</DateCompleted>
<DateRevised><Year>2016</Year>
<Month>12</Month>
<Day>30</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1948-7193</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>7</Volume>
<Issue>2</Issue>
<PubDate><Year>2016</Year>
<Month>Feb</Month>
<Day>17</Day>
</PubDate>
</JournalIssue>
<Title>ACS chemical neuroscience</Title>
<ISOAbbreviation>ACS Chem Neurosci</ISOAbbreviation>
</Journal>
<ArticleTitle>Binding Interactions of Dopamine and Apomorphine in D2High and D2Low States of Human Dopamine D2 Receptor Using Computational and Experimental Techniques.</ArticleTitle>
<Pagination><MedlinePgn>185-95</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1021/acschemneuro.5b00271</ELocationID>
<Abstract><AbstractText>We have recently reported G-protein coupled receptor (GPCR) model structures for the active and inactive states of the human dopamine D2 receptor (D2R) using adrenergic crystal structures as templates. Since the therapeutic concentrations of dopamine agonists that suppress the release of prolactin are the same as those that act at the high-affinity state of the D2 receptor (D2High), D2High in the anterior pituitary gland is considered to be the functional state of the receptor. In addition, the therapeutic concentrations of anti-Parkinson drugs are also related to the dissociation constants in the D2High form of the receptor. The discrimination between the high- and low-affinity (D2Low) components of the D2R is not obvious and requires advanced computer-assisted structural biology investigations. Therefore, in this work, the derived D2High and D2Low receptor models (GPCR monomer and dimer three-dimensional structures) are used as drug-binding targets to investigate binding interactions of dopamine and apomorphine. The study reveals a match between the experimental dissociation constants of dopamine and apomorphine at their high- and low-affinity sites of the D2 receptor in monomer and dimer and their calculated dissociation constants. The allosteric receptor-receptor interaction for dopamine D2R dimer is associated with the accessibility of adjacent residues of transmembrane region 4. The measured negative cooperativity between agonist ligand at dopamine D2 receptor is also correctly predicted using the D2R homodimerization model.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Durdagi</LastName>
<ForeName>Serdar</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Biophysics, School of Medicine, Bahcesehir University , 34349 Istanbul, Turkey.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Salmas</LastName>
<ForeName>Ramin Ekhteiari</ForeName>
<Initials>RE</Initials>
<AffiliationInfo><Affiliation>Department of Biophysics, School of Medicine, Bahcesehir University , 34349 Istanbul, Turkey.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Chemistry, Istanbul Technical University , 34469 Istanbul, Turkey.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Stein</LastName>
<ForeName>Matthias</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Molecular Simulations and Design Group, Max-Planck Institute for Dynamics of Complex Technical Systems , Sandtorstrasse 1, 39106, Magdeburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yurtsever</LastName>
<ForeName>Mine</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry, Istanbul Technical University , 34469 Istanbul, Turkey.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Seeman</LastName>
<ForeName>Philip</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Departments of Pharmacology and Psychiatry, University of Toronto , 260 Heath Street West, Unit 605, M5P 3L6, Toronto, Ontario Canada.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><Agency>Canadian Institutes of Health Research</Agency>
<Country>Canada</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>2015</Year>
<Month>12</Month>
<Day>22</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>ACS Chem Neurosci</MedlineTA>
<NlmUniqueID>101525337</NlmUniqueID>
<ISSNLinking>1948-7193</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D018491">Dopamine Agonists</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D017448">Receptors, Dopamine D2</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>N21FAR7B4S</RegistryNumber>
<NameOfSubstance UI="D001058">Apomorphine</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>VTD58H1Z2X</RegistryNumber>
<NameOfSubstance UI="D004298">Dopamine</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D001058" MajorTopicYN="N">Apomorphine</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001667" MajorTopicYN="N">Binding, Competitive</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004298" MajorTopicYN="N">Dopamine</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018491" MajorTopicYN="N">Dopamine Agonists</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D062105" MajorTopicYN="N">Molecular Docking Simulation</DescriptorName>
<QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015202" MajorTopicYN="N">Protein Engineering</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017448" MajorTopicYN="N">Receptors, Dopamine D2</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">D2High and D2Low states of dopamine</Keyword>
<Keyword MajorTopicYN="N">Dopamine D2 receptor</Keyword>
<Keyword MajorTopicYN="N">GPCR dimerization</Keyword>
<Keyword MajorTopicYN="N">molecular docking</Keyword>
<Keyword MajorTopicYN="N">protein engineering</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year>
<Month>12</Month>
<Day>10</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2015</Year>
<Month>12</Month>
<Day>10</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2016</Year>
<Month>12</Month>
<Day>15</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">26645629</ArticleId>
<ArticleId IdType="doi">10.1021/acschemneuro.5b00271</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Canada/explor/ParkinsonCanadaV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000293 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 000293 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Canada |area= ParkinsonCanadaV1 |flux= PubMed |étape= Curation |type= RBID |clé= pubmed:26645629 |texte= Binding Interactions of Dopamine and Apomorphine in D2High and D2Low States of Human Dopamine D2 Receptor Using Computational and Experimental Techniques. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:26645629" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \ | NlmPubMed2Wicri -a ParkinsonCanadaV1
![]() | This area was generated with Dilib version V0.6.29. | ![]() |