Expression of Lewy body protein septin 4 in postmortem brain of Parkinson's disease and control subjects
Identifieur interne : 001037 ( Istex/Corpus ); précédent : 001036; suivant : 001038Expression of Lewy body protein septin 4 in postmortem brain of Parkinson's disease and control subjects
Auteurs : Lina Shehadeh ; Georgia Mitsi ; Nikhil Adi ; Nanette Bishopric ; Spyridon PapapetropoulosSource :
- Movement Disorders [ 0885-3185 ] ; 2009-01-30.
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Abstract
In Parkinson's disease (PD) neuronal degeneration is associated with abnormal protein aggregation in various forms including Lewy bodies (LBs). A major component of LBs is α‐synuclein; septin 4 (SEPT4), a polymerizing GTP‐binding protein that serves as scaffold for diverse molecules has been found to colocalize with α‐synuclein in LBs. The central role of SEPT4 in the etiopathogenesis of PD has been suggested since SEPT4 also shows a physiological association with α‐synuclein and serves as a substrate for parkin. To this end, we studied the expression of septin 4 and α‐synuclein in postmortem human substantia nigra (SN) and amygdala from patients with PD and healthy controls. Twenty patients (14 men : 6 women, onset 63.0 ± 11.4 years, age 77.3 ± 7.6 years, Hoehn and Yahr 4.05/5) and 9 neurologically healthy controls (4 men/5 women, age at death 80.1 ± 8.6 years) were studied. Sporadic PD cases showed a statistically significant decrease of the fold change (FC) of SNCA (FC = 0.31, P = 0.00001) and SEPT4 (FC = 0.67, P = 0.054) gene expressions in the SN and the amygdala (SNCA: FC = 0.49, P = 0.02; SEPT4: FC = 0.32, P = 0.007) versus healthy controls. However, an increase of both proteins in PD versus control subjects was observed with immunoblotting. The semi‐quantitative protein ratio calculations revealed more than 10‐fold increases for both SEPT4 and α‐synuclein in PD versus control subjects. We present for the first time similar signal expression patterns and parallel accumulation of SEPT4 and α‐synuclein in well‐characterized postmortem PD brain. Considering the heterogeneous etiology of sporadic PD and the variability of individual human samples, SEPT4 accumulation may be regarded as one of the common pathological changes in PD and should therefore be further explored. © 2008 Movement Disorder Society
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DOI: 10.1002/mds.22306
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Disord.</title><idno type="ISSN">0885-3185</idno><idno type="eISSN">1531-8257</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2009-01-30">2009-01-30</date><biblScope unit="vol">24</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="204">204</biblScope><biblScope unit="page" to="210">210</biblScope></imprint><idno type="ISSN">0885-3185</idno></series><idno type="istex">B660860B55A8094845BE234AE20CD200EBC5E21E</idno><idno type="DOI">10.1002/mds.22306</idno><idno type="ArticleID">MDS22306</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0885-3185</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Parkinson's disease</term><term>alpha‐synuclein</term><term>amygdala</term><term>gene expression</term><term>mRNA</term><term>postmortem brain</term><term>protein</term><term>septin 4</term><term>substantia nigra</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In Parkinson's disease (PD) neuronal degeneration is associated with abnormal protein aggregation in various forms including Lewy bodies (LBs). A major component of LBs is α‐synuclein; septin 4 (SEPT4), a polymerizing GTP‐binding protein that serves as scaffold for diverse molecules has been found to colocalize with α‐synuclein in LBs. The central role of SEPT4 in the etiopathogenesis of PD has been suggested since SEPT4 also shows a physiological association with α‐synuclein and serves as a substrate for parkin. To this end, we studied the expression of septin 4 and α‐synuclein in postmortem human substantia nigra (SN) and amygdala from patients with PD and healthy controls. Twenty patients (14 men : 6 women, onset 63.0 ± 11.4 years, age 77.3 ± 7.6 years, Hoehn and Yahr 4.05/5) and 9 neurologically healthy controls (4 men/5 women, age at death 80.1 ± 8.6 years) were studied. Sporadic PD cases showed a statistically significant decrease of the fold change (FC) of SNCA (FC = 0.31, P = 0.00001) and SEPT4 (FC = 0.67, P = 0.054) gene expressions in the SN and the amygdala (SNCA: FC = 0.49, P = 0.02; SEPT4: FC = 0.32, P = 0.007) versus healthy controls. However, an increase of both proteins in PD versus control subjects was observed with immunoblotting. The semi‐quantitative protein ratio calculations revealed more than 10‐fold increases for both SEPT4 and α‐synuclein in PD versus control subjects. We present for the first time similar signal expression patterns and parallel accumulation of SEPT4 and α‐synuclein in well‐characterized postmortem PD brain. Considering the heterogeneous etiology of sporadic PD and the variability of individual human samples, SEPT4 accumulation may be regarded as one of the common pathological changes in PD and should therefore be further explored. © 2008 Movement Disorder Society</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Lina Shehadeh PhD</name><affiliations><json:string>Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, Florida, USA</json:string><json:string>Center for Complex Systems and Brain Sciences, Florida Atlantic University, Miami, Florida, USA</json:string></affiliations></json:item><json:item><name>Georgia Mitsi PhD</name><affiliations><json:string>University of Miami‐Humana Health Services Research Center, Miami, Florida, USA</json:string></affiliations></json:item><json:item><name>Nikhil Adi PhD</name><affiliations><json:string>Department of Neurology, University of Miami Miller School of Medicine, Miami, Florida, USA</json:string></affiliations></json:item><json:item><name>Nanette Bishopric MD</name><affiliations><json:string>Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, Florida, USA</json:string></affiliations></json:item><json:item><name>Spyridon Papapetropoulos MD, PhD</name><affiliations><json:string>Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, Florida, USA</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>alpha‐synuclein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>septin 4</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>gene expression</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>mRNA</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>protein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Parkinson's disease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>postmortem brain</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>substantia nigra</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>amygdala</value></json:item></subject><language><json:string>eng</json:string></language><abstract>In Parkinson's disease (PD) neuronal degeneration is associated with abnormal protein aggregation in various forms including Lewy bodies (LBs). A major component of LBs is α‐synuclein; septin 4 (SEPT4), a polymerizing GTP‐binding protein that serves as scaffold for diverse molecules has been found to colocalize with α‐synuclein in LBs. The central role of SEPT4 in the etiopathogenesis of PD has been suggested since SEPT4 also shows a physiological association with α‐synuclein and serves as a substrate for parkin. To this end, we studied the expression of septin 4 and α‐synuclein in postmortem human substantia nigra (SN) and amygdala from patients with PD and healthy controls. Twenty patients (14 men : 6 women, onset 63.0 ± 11.4 years, age 77.3 ± 7.6 years, Hoehn and Yahr 4.05/5) and 9 neurologically healthy controls (4 men/5 women, age at death 80.1 ± 8.6 years) were studied. Sporadic PD cases showed a statistically significant decrease of the fold change (FC) of SNCA (FC = 0.31, P = 0.00001) and SEPT4 (FC = 0.67, P = 0.054) gene expressions in the SN and the amygdala (SNCA: FC = 0.49, P = 0.02; SEPT4: FC = 0.32, P = 0.007) versus healthy controls. However, an increase of both proteins in PD versus control subjects was observed with immunoblotting. The semi‐quantitative protein ratio calculations revealed more than 10‐fold increases for both SEPT4 and α‐synuclein in PD versus control subjects. We present for the first time similar signal expression patterns and parallel accumulation of SEPT4 and α‐synuclein in well‐characterized postmortem PD brain. Considering the heterogeneous etiology of sporadic PD and the variability of individual human samples, SEPT4 accumulation may be regarded as one of the common pathological changes in PD and should therefore be further explored. © 2008 Movement Disorder Society</abstract><qualityIndicators><score>6.607</score><pdfVersion>1.3</pdfVersion><pdfPageSize>612 x 810 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractCharCount>1836</abstractCharCount><pdfWordCount>3607</pdfWordCount><pdfCharCount>23834</pdfCharCount><pdfPageCount>7</pdfPageCount><abstractWordCount>293</abstractWordCount></qualityIndicators><title>Expression of Lewy body protein septin 4 in postmortem brain of Parkinson's disease and control subjects</title><genre><json:string>Serial article</json:string></genre><host><volume>24</volume><pages><total>7</total><last>210</last><first>204</first></pages><issn><json:string>0885-3185</json:string></issn><issue>2</issue><subject><json:item><value>Research Article</value></json:item></subject><genre></genre><language><json:string>unknown</json:string></language><title>Movement Disorders</title><doi><json:string>10.1002/(ISSN)1531-8257</json:string></doi></host><publicationDate>2009</publicationDate><copyrightDate>2009</copyrightDate><doi><json:string>10.1002/mds.22306</json:string></doi><id>B660860B55A8094845BE234AE20CD200EBC5E21E</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/B660860B55A8094845BE234AE20CD200EBC5E21E/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/B660860B55A8094845BE234AE20CD200EBC5E21E/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/B660860B55A8094845BE234AE20CD200EBC5E21E/fulltext/tei"><teiHeader type="text"><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Expression of Lewy body protein septin 4 in postmortem brain of Parkinson's disease and control subjects</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><availability><p>Wiley Subscription Services, Inc., A Wiley Company</p></availability><date>2009</date></publicationStmt><notesStmt><note type="content">*Potential conflict of interest: None reported.</note><note>Stanley Glaser Foundation - No. NIMH 5R03MH074059‐02;</note><note>National Parkinson Foundation Inc.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Expression of Lewy body protein septin 4 in postmortem brain of Parkinson's disease and control subjects</title><author><persName><forename type="first">Lina</forename><surname>Shehadeh</surname><roleName type="degree">PhD</roleName></persName><affiliation>Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, Florida, USA</affiliation><affiliation>Center for Complex Systems and Brain Sciences, Florida Atlantic University, Miami, Florida, USA</affiliation></author><author><persName><forename type="first">Georgia</forename><surname>Mitsi</surname><roleName type="degree">PhD</roleName></persName><affiliation>University of Miami‐Humana Health Services Research Center, Miami, Florida, USA</affiliation></author><author><persName><forename type="first">Nikhil</forename><surname>Adi</surname><roleName type="degree">PhD</roleName></persName><affiliation>Department of Neurology, University of Miami Miller School of Medicine, Miami, Florida, USA</affiliation></author><author><persName><forename type="first">Nanette</forename><surname>Bishopric</surname><roleName type="degree">MD</roleName></persName><affiliation>Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, Florida, USA</affiliation></author><author><persName><forename type="first">Spyridon</forename><surname>Papapetropoulos</surname><roleName type="degree">MD, PhD</roleName></persName><note type="correspondence"><p>Correspondence: Division of Movement Disorders, Department of Neurology, University of Miami, Miller School of Medicine, Clinical Research Building, 1120 N.W. 14th Street, 13th Floor, Room 1349, Miami, FL 33136</p></note><affiliation>Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, Florida, USA</affiliation></author></analytic><monogr><title level="j">Movement Disorders</title><title level="j" type="sub">Official Journal of the Movement Disorder Society</title><title level="j" type="abbrev">Mov. 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A major component of LBs is α‐synuclein; septin 4 (SEPT4), a polymerizing GTP‐binding protein that serves as scaffold for diverse molecules has been found to colocalize with α‐synuclein in LBs. The central role of SEPT4 in the etiopathogenesis of PD has been suggested since SEPT4 also shows a physiological association with α‐synuclein and serves as a substrate for parkin. To this end, we studied the expression of septin 4 and α‐synuclein in postmortem human substantia nigra (SN) and amygdala from patients with PD and healthy controls. Twenty patients (14 men : 6 women, onset 63.0 ± 11.4 years, age 77.3 ± 7.6 years, Hoehn and Yahr 4.05/5) and 9 neurologically healthy controls (4 men/5 women, age at death 80.1 ± 8.6 years) were studied. Sporadic PD cases showed a statistically significant decrease of the fold change (FC) of SNCA (FC = 0.31, P = 0.00001) and SEPT4 (FC = 0.67, P = 0.054) gene expressions in the SN and the amygdala (SNCA: FC = 0.49, P = 0.02; SEPT4: FC = 0.32, P = 0.007) versus healthy controls. However, an increase of both proteins in PD versus control subjects was observed with immunoblotting. The semi‐quantitative protein ratio calculations revealed more than 10‐fold increases for both SEPT4 and α‐synuclein in PD versus control subjects. We present for the first time similar signal expression patterns and parallel accumulation of SEPT4 and α‐synuclein in well‐characterized postmortem PD brain. 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type="organization"><unparsedAffiliation>Center for Complex Systems and Brain Sciences, Florida Atlantic University, Miami, Florida, USA</unparsedAffiliation></affiliation><affiliation xml:id="af3" countryCode="US" type="organization"><unparsedAffiliation>University of Miami‐Humana Health Services Research Center, Miami, Florida, USA</unparsedAffiliation></affiliation><affiliation xml:id="af4" countryCode="US" type="organization"><unparsedAffiliation>Department of Neurology, University of Miami Miller School of Medicine, Miami, Florida, USA</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">alpha‐synuclein</keyword><keyword xml:id="kwd2">septin 4</keyword><keyword xml:id="kwd3">gene expression</keyword><keyword xml:id="kwd4">mRNA</keyword><keyword xml:id="kwd5">protein</keyword><keyword xml:id="kwd6">Parkinson's disease</keyword><keyword xml:id="kwd7">postmortem brain</keyword><keyword xml:id="kwd8">substantia nigra</keyword><keyword xml:id="kwd9">amygdala</keyword></keywordGroup><fundingInfo><fundingAgency>Stanley Glaser Foundation</fundingAgency><fundingNumber>NIMH 5R03MH074059‐02</fundingNumber></fundingInfo><fundingInfo><fundingAgency>National Parkinson Foundation Inc.</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>In Parkinson's disease (PD) neuronal degeneration is associated with abnormal protein aggregation in various forms including Lewy bodies (LBs). A major component of LBs is α‐synuclein; septin 4 (SEPT4), a polymerizing GTP‐binding protein that serves as scaffold for diverse molecules has been found to colocalize with α‐synuclein in LBs. The central role of SEPT4 in the etiopathogenesis of PD has been suggested since SEPT4 also shows a physiological association with α‐synuclein and serves as a substrate for parkin. To this end, we studied the expression of septin 4 and α‐synuclein in postmortem human substantia nigra (SN) and amygdala from patients with PD and healthy controls. Twenty patients (14 men : 6 women, onset 63.0 ± 11.4 years, age 77.3 ± 7.6 years, Hoehn and Yahr 4.05/5) and 9 neurologically healthy controls (4 men/5 women, age at death 80.1 ± 8.6 years) were studied. Sporadic PD cases showed a statistically significant decrease of the fold change (FC) of <i>SNCA</i> (FC = 0.31, <i>P =</i> 0.00001) and <i>SEPT4</i> (FC = 0.67, <i>P =</i> 0.054) gene expressions in the SN and the amygdala (<i>SNCA</i>: FC = 0.49, <i>P =</i> 0.02; <i>SEPT4</i>: FC = 0.32<i>, P =</i> 0.007) versus healthy controls. However, an increase of both proteins in PD versus control subjects was observed with immunoblotting. The semi‐quantitative protein ratio calculations revealed more than 10‐fold increases for both SEPT4 and α‐synuclein in PD versus control subjects. We present for the first time similar signal expression patterns and parallel accumulation of SEPT4 and α‐synuclein in well‐characterized postmortem PD brain. Considering the heterogeneous etiology of sporadic PD and the variability of individual human samples, SEPT4 accumulation may be regarded as one of the common pathological changes in PD and should therefore be further explored. © 2008 Movement Disorder Society</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><p>Potential conflict of interest: None reported.</p></note></noteGroup></header></component></istex:document></istex:metadataXml><!--Version 0.6 générée le 3-12-2015--><mods version="3.6"><titleInfo lang="en"><title>Expression of Lewy body protein septin 4 in postmortem brain of Parkinson's disease and control subjects</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Septin 4 in PD</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Expression of Lewy body protein septin 4 in postmortem brain of Parkinson's disease and control subjects</title></titleInfo><name type="personal"><namePart type="given">Lina</namePart><namePart type="family">Shehadeh</namePart><namePart type="termsOfAddress">PhD</namePart><affiliation>Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, Florida, USA</affiliation><affiliation>Center for Complex Systems and Brain Sciences, Florida Atlantic University, Miami, Florida, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Georgia</namePart><namePart type="family">Mitsi</namePart><namePart type="termsOfAddress">PhD</namePart><affiliation>University of Miami‐Humana Health Services Research Center, Miami, Florida, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Nikhil</namePart><namePart type="family">Adi</namePart><namePart type="termsOfAddress">PhD</namePart><affiliation>Department of Neurology, University of Miami Miller School of Medicine, Miami, Florida, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Nanette</namePart><namePart type="family">Bishopric</namePart><namePart type="termsOfAddress">MD</namePart><affiliation>Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, Florida, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Spyridon</namePart><namePart type="family">Papapetropoulos</namePart><namePart type="termsOfAddress">MD, PhD</namePart><affiliation>Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, Florida, USA</affiliation><description>Correspondence: Division of Movement Disorders, Department of Neurology, University of Miami, Miller School of Medicine, Clinical Research Building, 1120 N.W. 14th Street, 13th Floor, Room 1349, Miami, FL 33136</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre authority="originalCategForm">article</genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2009-01-30</dateIssued><dateCaptured encoding="w3cdtf">2007-11-15</dateCaptured><dateValid encoding="w3cdtf">2008-08-08</dateValid><copyrightDate encoding="w3cdtf">2009</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">4</extent><extent unit="tables">1</extent><extent unit="references">30</extent><extent unit="words">3878</extent></physicalDescription><abstract lang="en">In Parkinson's disease (PD) neuronal degeneration is associated with abnormal protein aggregation in various forms including Lewy bodies (LBs). A major component of LBs is α‐synuclein; septin 4 (SEPT4), a polymerizing GTP‐binding protein that serves as scaffold for diverse molecules has been found to colocalize with α‐synuclein in LBs. The central role of SEPT4 in the etiopathogenesis of PD has been suggested since SEPT4 also shows a physiological association with α‐synuclein and serves as a substrate for parkin. To this end, we studied the expression of septin 4 and α‐synuclein in postmortem human substantia nigra (SN) and amygdala from patients with PD and healthy controls. Twenty patients (14 men : 6 women, onset 63.0 ± 11.4 years, age 77.3 ± 7.6 years, Hoehn and Yahr 4.05/5) and 9 neurologically healthy controls (4 men/5 women, age at death 80.1 ± 8.6 years) were studied. Sporadic PD cases showed a statistically significant decrease of the fold change (FC) of SNCA (FC = 0.31, P = 0.00001) and SEPT4 (FC = 0.67, P = 0.054) gene expressions in the SN and the amygdala (SNCA: FC = 0.49, P = 0.02; SEPT4: FC = 0.32, P = 0.007) versus healthy controls. However, an increase of both proteins in PD versus control subjects was observed with immunoblotting. The semi‐quantitative protein ratio calculations revealed more than 10‐fold increases for both SEPT4 and α‐synuclein in PD versus control subjects. We present for the first time similar signal expression patterns and parallel accumulation of SEPT4 and α‐synuclein in well‐characterized postmortem PD brain. Considering the heterogeneous etiology of sporadic PD and the variability of individual human samples, SEPT4 accumulation may be regarded as one of the common pathological changes in PD and should therefore be further explored. © 2008 Movement Disorder Society</abstract><note type="content">*Potential conflict of interest: None reported.</note><note type="funding">Stanley Glaser Foundation - No. NIMH 5R03MH074059‐02; </note><note type="funding">National Parkinson Foundation Inc.</note><subject lang="en"><genre>Keywords</genre><topic>alpha‐synuclein</topic><topic>septin 4</topic><topic>gene expression</topic><topic>mRNA</topic><topic>protein</topic><topic>Parkinson's disease</topic><topic>postmortem brain</topic><topic>substantia nigra</topic><topic>amygdala</topic></subject><relatedItem type="host"><titleInfo><title>Movement Disorders</title><subTitle>Official Journal of the Movement Disorder Society</subTitle></titleInfo><titleInfo type="abbreviated"><title>Mov. Disord.</title></titleInfo><subject><genre>article category</genre><topic>Research Article</topic></subject><identifier type="ISSN">0885-3185</identifier><identifier type="eISSN">1531-8257</identifier><identifier type="DOI">10.1002/(ISSN)1531-8257</identifier><identifier type="PublisherID">MDS</identifier><part><date>2009</date><detail type="volume"><caption>vol.</caption><number>24</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>204</start><end>210</end><total>7</total></extent></part></relatedItem><identifier type="istex">B660860B55A8094845BE234AE20CD200EBC5E21E</identifier><identifier type="DOI">10.1002/mds.22306</identifier><identifier type="ArticleID">MDS22306</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2008 Movement Disorder Society</accessCondition><recordInfo><recordOrigin>Wiley Subscription Services, Inc., A Wiley Company</recordOrigin><recordContentSource>WILEY</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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