Indoleamine 2,3 Dioxygenase as a Potential Therapeutic Target in Huntington's Disease.
Identifieur interne : 000487 ( PubMed/Checkpoint ); précédent : 000486; suivant : 000488Indoleamine 2,3 Dioxygenase as a Potential Therapeutic Target in Huntington's Disease.
Auteurs : Gelareh Mazarei [Canada] ; Blair R. Leavitt [Canada]Source :
- Journal of Huntington's disease [ 1879-6400 ] ; 2015.
English descriptors
- KwdEn :
- Alzheimer Disease (enzymology), Animals, Humans, Huntington Disease (drug therapy), Huntington Disease (enzymology), Huntington Disease (prevention & control), Indoleamine-Pyrrole 2,3,-Dioxygenase (antagonists & inhibitors), Kynurenine (metabolism), Parkinson Disease (enzymology), Signal Transduction, Tryptophan (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Indoleamine-Pyrrole 2,3,-Dioxygenase.
- drug therapy : Huntington Disease.
- enzymology : Alzheimer Disease, Huntington Disease, Parkinson Disease.
- chemical , metabolism : Kynurenine, Tryptophan.
- prevention & control : Huntington Disease.
- Animals, Humans, Signal Transduction.
Abstract
Within the past decade, there has been increasing interest in the role of tryptophan (Trp) metabolites and the kynurenine pathway (KP) in diseases of the brain such as Huntington's disease (HD). Evidence is accumulating to suggest that this pathway is imbalanced in neurologic disease states. The KP diverges into two branches that can lead to production of either neuroprotective or neurotoxic metabolites. In one branch, kynurenine (Kyn) produced as a result of tryptophan (Trp) catabolism is further metabolized to neurotoxic metabolites such as 3-hydroxykunurenine (3-HK) and quinolinic acid (QA). In the other branch, Kyn is converted to the neuroprotective metabolite kynurenic acid (KA). The enzyme Indoleamine 2,3 dioxygenase (IDO1) catalyzes the conversion of Trp into Kyn, the first and rate-limiting enzymatic step of the KP. This reaction takes place throughout the body in multiple cell types as a required step in the degradation of the essential amino acid Trp. Studies of IDO1 in brain have focused primarily on a potential role in depression, immune tolerance associated with brain tumours, and multiple sclerosis; however the role of this enzyme in neurodegenerative disease has garnered significant attention in recent years. This review will provide a summary of the current understanding of the role of IDO1 in Huntington's disease and will assess this enzyme as a potential therapeutic target for HD.
DOI: 10.3233/JHD-159003
PubMed: 26397892
Affiliations:
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pubmed:26397892Le document en format XML
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Leavitt</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Molecular Medicine & Therapeutics and Department of Medical Genetics, University of British Columbia, Vancouver, BC, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Centre for Molecular Medicine & Therapeutics and Department of Medical Genetics, University of British Columbia, Vancouver, BC</wicri:regionArea><wicri:noRegion>BC</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26397892</idno><idno type="pmid">26397892</idno><idno type="doi">10.3233/JHD-159003</idno><idno type="wicri:Area/PubMed/Corpus">000597</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000597</idno><idno type="wicri:Area/PubMed/Curation">000597</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000597</idno><idno type="wicri:Area/PubMed/Checkpoint">000597</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000597</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Indoleamine 2,3 Dioxygenase as a Potential Therapeutic Target in Huntington's Disease.</title><author><name sortKey="Mazarei, Gelareh" sort="Mazarei, Gelareh" uniqKey="Mazarei G" first="Gelareh" last="Mazarei">Gelareh Mazarei</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Molecular Medicine & Therapeutics and Department of Medical Genetics, University of British Columbia, Vancouver, BC, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Centre for Molecular Medicine & Therapeutics and Department of Medical Genetics, University of British Columbia, Vancouver, BC</wicri:regionArea><wicri:noRegion>BC</wicri:noRegion></affiliation></author><author><name sortKey="Leavitt, Blair R" sort="Leavitt, Blair R" uniqKey="Leavitt B" first="Blair R" last="Leavitt">Blair R. Leavitt</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Molecular Medicine & Therapeutics and Department of Medical Genetics, University of British Columbia, Vancouver, BC, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Centre for Molecular Medicine & Therapeutics and Department of Medical Genetics, University of British Columbia, Vancouver, BC</wicri:regionArea><wicri:noRegion>BC</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of Huntington's disease</title><idno type="eISSN">1879-6400</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alzheimer Disease (enzymology)</term><term>Animals</term><term>Humans</term><term>Huntington Disease (drug therapy)</term><term>Huntington Disease (enzymology)</term><term>Huntington Disease (prevention & control)</term><term>Indoleamine-Pyrrole 2,3,-Dioxygenase (antagonists & inhibitors)</term><term>Kynurenine (metabolism)</term><term>Parkinson Disease (enzymology)</term><term>Signal Transduction</term><term>Tryptophan (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Indoleamine-Pyrrole 2,3,-Dioxygenase</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Huntington Disease</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Alzheimer Disease</term><term>Huntington Disease</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Kynurenine</term><term>Tryptophan</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Huntington Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Signal Transduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Within the past decade, there has been increasing interest in the role of tryptophan (Trp) metabolites and the kynurenine pathway (KP) in diseases of the brain such as Huntington's disease (HD). Evidence is accumulating to suggest that this pathway is imbalanced in neurologic disease states. The KP diverges into two branches that can lead to production of either neuroprotective or neurotoxic metabolites. In one branch, kynurenine (Kyn) produced as a result of tryptophan (Trp) catabolism is further metabolized to neurotoxic metabolites such as 3-hydroxykunurenine (3-HK) and quinolinic acid (QA). In the other branch, Kyn is converted to the neuroprotective metabolite kynurenic acid (KA). The enzyme Indoleamine 2,3 dioxygenase (IDO1) catalyzes the conversion of Trp into Kyn, the first and rate-limiting enzymatic step of the KP. This reaction takes place throughout the body in multiple cell types as a required step in the degradation of the essential amino acid Trp. Studies of IDO1 in brain have focused primarily on a potential role in depression, immune tolerance associated with brain tumours, and multiple sclerosis; however the role of this enzyme in neurodegenerative disease has garnered significant attention in recent years. This review will provide a summary of the current understanding of the role of IDO1 in Huntington's disease and will assess this enzyme as a potential therapeutic target for HD.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26397892</PMID><DateCreated><Year>2015</Year><Month>09</Month><Day>24</Day></DateCreated><DateCompleted><Year>2016</Year><Month>06</Month><Day>15</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1879-6400</ISSN><JournalIssue CitedMedium="Internet"><Volume>4</Volume><Issue>2</Issue><PubDate><Year>2015</Year></PubDate></JournalIssue><Title>Journal of Huntington's disease</Title><ISOAbbreviation>J Huntingtons Dis</ISOAbbreviation></Journal><ArticleTitle>Indoleamine 2,3 Dioxygenase as a Potential Therapeutic Target in Huntington's Disease.</ArticleTitle><Pagination><MedlinePgn>109-18</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3233/JHD-159003</ELocationID><Abstract><AbstractText>Within the past decade, there has been increasing interest in the role of tryptophan (Trp) metabolites and the kynurenine pathway (KP) in diseases of the brain such as Huntington's disease (HD). Evidence is accumulating to suggest that this pathway is imbalanced in neurologic disease states. The KP diverges into two branches that can lead to production of either neuroprotective or neurotoxic metabolites. In one branch, kynurenine (Kyn) produced as a result of tryptophan (Trp) catabolism is further metabolized to neurotoxic metabolites such as 3-hydroxykunurenine (3-HK) and quinolinic acid (QA). In the other branch, Kyn is converted to the neuroprotective metabolite kynurenic acid (KA). The enzyme Indoleamine 2,3 dioxygenase (IDO1) catalyzes the conversion of Trp into Kyn, the first and rate-limiting enzymatic step of the KP. This reaction takes place throughout the body in multiple cell types as a required step in the degradation of the essential amino acid Trp. Studies of IDO1 in brain have focused primarily on a potential role in depression, immune tolerance associated with brain tumours, and multiple sclerosis; however the role of this enzyme in neurodegenerative disease has garnered significant attention in recent years. This review will provide a summary of the current understanding of the role of IDO1 in Huntington's disease and will assess this enzyme as a potential therapeutic target for HD.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mazarei</LastName><ForeName>Gelareh</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Centre for Molecular Medicine & Therapeutics and Department of Medical Genetics, University of British Columbia, Vancouver, BC, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Leavitt</LastName><ForeName>Blair R</ForeName><Initials>BR</Initials><AffiliationInfo><Affiliation>Centre for Molecular Medicine & Therapeutics and Department of Medical Genetics, University of British Columbia, Vancouver, BC, Canada.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><Agency>Canadian Institutes of Health 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Version="1">15939737</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Clin Invest. 2007 May;117(5):1147-54</RefSource><PMID Version="1">17476344</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Psychoneuroendocrinology. 2006 Apr;31(3):407-13</RefSource><PMID Version="1">16303256</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2013 Dec;127(6):852-67</RefSource><PMID Version="1">23786539</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Behav Brain Res. 2010 Jun 26;210(1):84-91</RefSource><PMID Version="1">20153778</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Science. 1998 Aug 21;281(5380):1191-3</RefSource><PMID Version="1">9712583</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Clin Invest. 2012 Aug;122(8):2940-54</RefSource><PMID Version="1">22751107</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Exp Neurol. 2006 Jan;197(1):31-40</RefSource><PMID Version="1">16099455</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Prog Neurobiol. 2010 Feb 9;90(2):230-45</RefSource><PMID Version="1">19394403</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nature. 1986 May 8-14;321(6066):168-71</RefSource><PMID Version="1">2422561</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Trends Immunol. 2013 Mar;34(3):137-43</RefSource><PMID Version="1">23103127</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Cancer Res. 2012 Nov 15;72(22):5649-57</RefSource><PMID Version="1">23144293</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neurobiol Dis. 2006 Jul;23(1):190-7</RefSource><PMID Version="1">16697652</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Mol Med (Berl). 2007 Dec;85(12):1351-9</RefSource><PMID Version="1">17594069</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Redox Rep. 2010;15(4):161-8</RefSource><PMID Version="1">20663292</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mol Brain. 2009 Mar 27;2:8</RefSource><PMID Version="1">19323847</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Infect Immun. 2005 Aug;73(8):5249-51</RefSource><PMID Version="1">16041050</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2009 Aug;110(3):791-800</RefSource><PMID Version="1">19457071</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Science. 2005 Nov 4;310(5749):850-5</RefSource><PMID Version="1">16272121</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 1990 Oct;55(4):1327-39</RefSource><PMID Version="1">2144582</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Arch Biochem Biophys. 1967 May;120(2):397-403</RefSource><PMID Version="1">4291827</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 1998 Jan;70(1):299-307</RefSource><PMID Version="1">9422375</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Med Microbiol. 1998 Feb;47(2):141-9</RefSource><PMID Version="1">9879957</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Exp Neurol. 2013 Nov;249:144-8</RefSource><PMID Version="1">23994717</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Curr Biol. 2011 Jun 7;21(11):961-6</RefSource><PMID Version="1">21636279</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Science. 1983 Jan 21;219(4582):316-8</RefSource><PMID Version="1">6849138</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Schizophr Bull. 2011 Nov;37(6):1147-56</RefSource><PMID Version="1">21036897</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neurotox Res. 2010 Aug;18(2):132-42</RefSource><PMID Version="1">19921535</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Leukoc Biol. 2006 Mar;79(3):596-610</RefSource><PMID Version="1">16365156</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2005 May;93(3):611-23</RefSource><PMID Version="1">15836620</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neurology. 1992 Sep;42(9):1702-6</RefSource><PMID Version="1">1513457</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nat Rev Neurosci. 2008 Jan;9(1):46-56</RefSource><PMID Version="1">18073775</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Clin Chem. 1998 Apr;44(4):858-62</RefSource><PMID Version="1">9554499</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neuroimmunol. 2002 Aug;129(1-2):186-96</RefSource><PMID Version="1">12161035</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neuroinflammation. 2011 Aug 02;8:88</RefSource><PMID Version="1">21810259</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neural Transm (Vienna). 2002 Feb;109(2):181-9</RefSource><PMID Version="1">12075858</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2002 Mar;80(6):1071-8</RefSource><PMID Version="1">11953457</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neural Transm (Vienna). 2000;107(10):1127-38</RefSource><PMID Version="1">11129102</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Curr Opin Struct Biol. 2008 Dec;18(6):748-55</RefSource><PMID Version="1">18950711</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>CNS Neurol Disord Drug Targets. 2010 Dec;9(6):791-800</RefSource><PMID Version="1">20942784</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Int J Biochem Cell Biol. 2009 Mar;41(3):467-71</RefSource><PMID Version="1">18282734</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Adv Exp Med Biol. 2003;527:105-12</RefSource><PMID Version="1">15206722</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Hum Mol Genet. 2010 Feb 15;19(4):609-22</RefSource><PMID Version="1">19934114</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Brain Behav Immun. 2008 Oct;22(7):1087-95</RefSource><PMID Version="1">18479887</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurol Sci. 2011 Nov 15;310(1-2):256-60</RefSource><PMID Version="1">21824629</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2012 Mar 6;109(10):3909-14</RefSource><PMID Version="1">22355111</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 1984 Feb;81(3):908-12</RefSource><PMID Version="1">6422465</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Eur J Neurosci. 2007 Oct;26(8):2211-21</RefSource><PMID Version="1">17892481</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Immunol. 2009 Mar 1;182(5):3202-12</RefSource><PMID Version="1">19234218</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neuropathol Appl Neurobiol. 2005 Aug;31(4):395-404</RefSource><PMID Version="1">16008823</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neurosci Biobehav Rev. 2012 Feb;36(2):764-85</RefSource><PMID Version="1">22197082</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Comp Biochem Physiol B Biochem Mol Biol. 2009 Jun;153(2):137-44</RefSource><PMID Version="1">19402226</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Adv Exp Med Biol. 2003;527:167-76</RefSource><PMID Version="1">15206729</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neurobiol Dis. 2004 Dec;17(3):455-61</RefSource><PMID Version="1">15571981</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Curr Med Chem. 2012;19(13):1899-920</RefSource><PMID Version="1">22429096</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 1986 Jul;47(1):23-30</RefSource><PMID Version="1">2940338</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2012 Sep 11;109(37):14912-7</RefSource><PMID Version="1">22927396</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 1995 Feb;64(2):932-5</RefSource><PMID Version="1">7830088</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2013 Dec 20;288(51):36554-66</RefSource><PMID Version="1">24189070</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neuroreport. 2003 Dec 19;14(18):2311-5</RefSource><PMID Version="1">14663182</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000544" MajorTopicYN="N">Alzheimer Disease</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006816" MajorTopicYN="N">Huntington Disease</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000517" MajorTopicYN="Y">prevention & 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MajorTopicYN="N">Huntington’s disease</Keyword><Keyword MajorTopicYN="N">huntingtin</Keyword><Keyword MajorTopicYN="N">indoleamine 2,3 dioxygenase</Keyword><Keyword MajorTopicYN="N">kynurenine pathway</Keyword><Keyword MajorTopicYN="N">quinolinic acid</Keyword><Keyword MajorTopicYN="N">tryptophan</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>9</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>9</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>6</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26397892</ArticleId><ArticleId IdType="pii">JHD159003</ArticleId><ArticleId IdType="doi">10.3233/JHD-159003</ArticleId><ArticleId 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| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd \
| NlmPubMed2Wicri -a ParkinsonCanadaV1
| This area was generated with Dilib version V0.6.29. |  |