THIS ARTICLE HAS BEEN RETRACTED: Pathological biochemistry of α‐synucleinopathy
Identifieur interne : 001778 ( Main/Corpus ); précédent : 001777; suivant : 001779THIS ARTICLE HAS BEEN RETRACTED: Pathological biochemistry of α‐synucleinopathy
Auteurs : Takeshi IwatsuboSource :
- Neuropathology [ 0919-6544 ] ; 2007-10.
English descriptors
Abstract
Lewy bodies (LBs) are hallmark lesions in the brains of patients with Parkinson's disease (PD) and dementia with Lewy bodies (DLB). We raised a monoclonal antibody LB509 against purified LBs from the brains of patients with DLB that strongly immuolabled LBs, and found that α‐synuclein is one of the major components of LBs. Thus, the deposition of α‐synuclein, an abundant presynaptic brain protein, as fibrillary aggregates in affected neurons or glial cells, was highlighted as a hallmark lesion of a subset of neurodegenerative disorders, including PD, DLB and multiple system atrophy collectively referred to as synucleinopathies. Importantly, the identification of missense mutations in and multiplication of α‐synuclein gene in some pedigrees of familial PD has strongly implicated α‐synuclein in the pathogenesis of PD and other synucleinopathies. We then examined the specific post‐translational modifications that characterize and underlie the aggregation of α‐synuclein in synucleinopathy brains by mass spectrometry and using a specific antibody, and found that serine 129 of α‐synuclein deposited in synucleinopathy lesions is selectively and extensively phosphorylated. Furthermore we generated transgenic C. elegans overexpressing α‐synuclein in neurons, and found that overexpression of familial PD‐linked mutant form of α‐synuclein impairs functions of dopamine neurons. These findings collectively underscore the importance of deposition of α‐synuclein as well as its phosphorylation in the pathogenesis of α‐synucleinopathies.
Url:
DOI: 10.1111/j.1440-1789.2007.00785.x
Links to Exploration step
ISTEX:CEFE215F3C31B33E6499C02EA19A025CDB247A75Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">THIS ARTICLE HAS BEEN RETRACTED: Pathological biochemistry of α‐synucleinopathy</title><author><name sortKey="Iwatsubo, Takeshi" sort="Iwatsubo, Takeshi" uniqKey="Iwatsubo T" first="Takeshi" last="Iwatsubo">Takeshi Iwatsubo</name><affiliation><mods:affiliation>Department of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:CEFE215F3C31B33E6499C02EA19A025CDB247A75</idno><date when="2007" year="2007">2007</date><idno type="doi">10.1111/j.1440-1789.2007.00785.x</idno><idno type="url">https://api.istex.fr/document/CEFE215F3C31B33E6499C02EA19A025CDB247A75/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">001778</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">THIS ARTICLE HAS BEEN RETRACTED: Pathological biochemistry of α‐synucleinopathy</title><author><name sortKey="Iwatsubo, Takeshi" sort="Iwatsubo, Takeshi" uniqKey="Iwatsubo T" first="Takeshi" last="Iwatsubo">Takeshi Iwatsubo</name><affiliation><mods:affiliation>Department of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Neuropathology</title><idno type="ISSN">0919-6544</idno><idno type="eISSN">1440-1789</idno><imprint><publisher>Blackwell Publishing Asia</publisher><pubPlace>Melbourne, Australia</pubPlace><date type="published" when="2007-10">2007-10</date><biblScope unit="volume">27</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="474">474</biblScope><biblScope unit="page" to="478">478</biblScope></imprint><idno type="ISSN">0919-6544</idno></series><idno type="istex">CEFE215F3C31B33E6499C02EA19A025CDB247A75</idno><idno type="DOI">10.1111/j.1440-1789.2007.00785.x</idno><idno type="ArticleID">NEUP785</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0919-6544</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Lewy body</term><term>Parkinson's disease</term><term>synucleinopathy</term><term>transgenic C. elegans</term><term>α‐synuclein</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lewy bodies (LBs) are hallmark lesions in the brains of patients with Parkinson's disease (PD) and dementia with Lewy bodies (DLB). We raised a monoclonal antibody LB509 against purified LBs from the brains of patients with DLB that strongly immuolabled LBs, and found that α‐synuclein is one of the major components of LBs. Thus, the deposition of α‐synuclein, an abundant presynaptic brain protein, as fibrillary aggregates in affected neurons or glial cells, was highlighted as a hallmark lesion of a subset of neurodegenerative disorders, including PD, DLB and multiple system atrophy collectively referred to as synucleinopathies. Importantly, the identification of missense mutations in and multiplication of α‐synuclein gene in some pedigrees of familial PD has strongly implicated α‐synuclein in the pathogenesis of PD and other synucleinopathies. We then examined the specific post‐translational modifications that characterize and underlie the aggregation of α‐synuclein in synucleinopathy brains by mass spectrometry and using a specific antibody, and found that serine 129 of α‐synuclein deposited in synucleinopathy lesions is selectively and extensively phosphorylated. Furthermore we generated transgenic C. elegans overexpressing α‐synuclein in neurons, and found that overexpression of familial PD‐linked mutant form of α‐synuclein impairs functions of dopamine neurons. These findings collectively underscore the importance of deposition of α‐synuclein as well as its phosphorylation in the pathogenesis of α‐synucleinopathies.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Takeshi Iwatsubo</name><affiliations><json:string>Department of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>α‐synuclein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Lewy body</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>synucleinopathy</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>transgenic C. elegans</value></json:item></subject><articleId><json:string>NEUP785</json:string></articleId><language><json:string>eng</json:string></language><abstract>Lewy bodies (LBs) are hallmark lesions in the brains of patients with Parkinson's disease (PD) and dementia with Lewy bodies (DLB). We raised a monoclonal antibody LB509 against purified LBs from the brains of patients with DLB that strongly immuolabled LBs, and found that α‐synuclein is one of the major components of LBs. Thus, the deposition of α‐synuclein, an abundant presynaptic brain protein, as fibrillary aggregates in affected neurons or glial cells, was highlighted as a hallmark lesion of a subset of neurodegenerative disorders, including PD, DLB and multiple system atrophy collectively referred to as synucleinopathies. Importantly, the identification of missense mutations in and multiplication of α‐synuclein gene in some pedigrees of familial PD has strongly implicated α‐synuclein in the pathogenesis of PD and other synucleinopathies. We then examined the specific post‐translational modifications that characterize and underlie the aggregation of α‐synuclein in synucleinopathy brains by mass spectrometry and using a specific antibody, and found that serine 129 of α‐synuclein deposited in synucleinopathy lesions is selectively and extensively phosphorylated. Furthermore we generated transgenic C. elegans overexpressing α‐synuclein in neurons, and found that overexpression of familial PD‐linked mutant form of α‐synuclein impairs functions of dopamine neurons. These findings collectively underscore the importance of deposition of α‐synuclein as well as its phosphorylation in the pathogenesis of α‐synucleinopathies.</abstract><qualityIndicators><score>6.479</score><pdfVersion>1.6</pdfVersion><pdfPageSize>595.276 x 779.528 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>5</keywordCount><abstractCharCount>1545</abstractCharCount><pdfWordCount>2423</pdfWordCount><pdfCharCount>16145</pdfCharCount><pdfPageCount>5</pdfPageCount><abstractWordCount>213</abstractWordCount></qualityIndicators><title>THIS ARTICLE HAS BEEN RETRACTED: Pathological biochemistry of α‐synucleinopathy</title><genre><json:string>other</json:string></genre><host><volume>27</volume><publisherId><json:string>NEUP</json:string></publisherId><pages><total>5</total><last>478</last><first>474</first></pages><issn><json:string>0919-6544</json:string></issn><issue>5</issue><subject><json:item><value>Symposium: Synucleinopathies: Update</value></json:item></subject><genre><json:string>Journal</json:string></genre><language><json:string>unknown</json:string></language><eissn><json:string>1440-1789</json:string></eissn><title>Neuropathology</title><doi><json:string>10.1111/(ISSN)1440-1789</json:string></doi></host><publicationDate>2007</publicationDate><copyrightDate>2007</copyrightDate><doi><json:string>10.1111/j.1440-1789.2007.00785.x</json:string></doi><id>CEFE215F3C31B33E6499C02EA19A025CDB247A75</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/CEFE215F3C31B33E6499C02EA19A025CDB247A75/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/CEFE215F3C31B33E6499C02EA19A025CDB247A75/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/CEFE215F3C31B33E6499C02EA19A025CDB247A75/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">THIS ARTICLE HAS BEEN RETRACTED: Pathological biochemistry of α‐synucleinopathy</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Blackwell Publishing Asia</publisher><pubPlace>Melbourne, Australia</pubPlace><availability><p>WILEY</p></availability><date>2007</date></publicationStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">THIS ARTICLE HAS BEEN RETRACTED: Pathological biochemistry of α‐synucleinopathy</title><author><persName><forename type="first">Takeshi</forename><surname>Iwatsubo</surname></persName><affiliation>Department of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan</affiliation></author></analytic><monogr><title level="j">Neuropathology</title><idno type="pISSN">0919-6544</idno><idno type="eISSN">1440-1789</idno><idno type="DOI">10.1111/(ISSN)1440-1789</idno><imprint><publisher>Blackwell Publishing Asia</publisher><pubPlace>Melbourne, Australia</pubPlace><date type="published" when="2007-10"></date><biblScope unit="volume">27</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="474">474</biblScope><biblScope unit="page" to="478">478</biblScope></imprint></monogr><idno type="istex">CEFE215F3C31B33E6499C02EA19A025CDB247A75</idno><idno type="DOI">10.1111/j.1440-1789.2007.00785.x</idno><idno type="ArticleID">NEUP785</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2007</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Lewy bodies (LBs) are hallmark lesions in the brains of patients with Parkinson's disease (PD) and dementia with Lewy bodies (DLB). We raised a monoclonal antibody LB509 against purified LBs from the brains of patients with DLB that strongly immuolabled LBs, and found that α‐synuclein is one of the major components of LBs. Thus, the deposition of α‐synuclein, an abundant presynaptic brain protein, as fibrillary aggregates in affected neurons or glial cells, was highlighted as a hallmark lesion of a subset of neurodegenerative disorders, including PD, DLB and multiple system atrophy collectively referred to as synucleinopathies. Importantly, the identification of missense mutations in and multiplication of α‐synuclein gene in some pedigrees of familial PD has strongly implicated α‐synuclein in the pathogenesis of PD and other synucleinopathies. We then examined the specific post‐translational modifications that characterize and underlie the aggregation of α‐synuclein in synucleinopathy brains by mass spectrometry and using a specific antibody, and found that serine 129 of α‐synuclein deposited in synucleinopathy lesions is selectively and extensively phosphorylated. Furthermore we generated transgenic C. elegans overexpressing α‐synuclein in neurons, and found that overexpression of familial PD‐linked mutant form of α‐synuclein impairs functions of dopamine neurons. These findings collectively underscore the importance of deposition of α‐synuclein as well as its phosphorylation in the pathogenesis of α‐synucleinopathies.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>α‐synuclein</term></item><item><term>Lewy body</term></item><item><term>Parkinson's disease</term></item><item><term>synucleinopathy</term></item><item><term>transgenic C. elegans</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>article category</head><item><term>Symposium: Synucleinopathies: Update</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2007-10">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/CEFE215F3C31B33E6499C02EA19A025CDB247A75/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Blackwell Publishing Asia</publisherName><publisherLoc>Melbourne, Australia</publisherLoc></publisherInfo><doi origin="wiley" registered="yes">10.1111/(ISSN)1440-1789</doi><issn type="print">0919-6544</issn><issn type="electronic">1440-1789</issn><idGroup><id type="product" value="NEUP"></id><id type="publisherDivision" value="ST"></id></idGroup><titleGroup><title type="main" sort="NEUROPATHOLOGY">Neuropathology</title></titleGroup></publicationMeta><publicationMeta level="part" position="10105"><doi origin="wiley">10.1111/neu.2007.27.issue-5</doi><numberingGroup><numbering type="journalVolume" number="27">27</numbering><numbering type="journalIssue" number="5">5</numbering></numberingGroup><coverDate startDate="2007-10">October 2007</coverDate></publicationMeta><publicationMeta level="unit" type="miscellaneous" position="12" status="forIssue"><doi origin="wiley">10.1111/j.1440-1789.2007.00785.x</doi><idGroup><id type="unit" value="NEUP785"></id></idGroup><countGroup><count type="pageTotal" number="5"></count></countGroup><titleGroup><title type="tocHeading1">SYMPOSIUM: SYNUCLEINOPATHIES: UPDATE</title><title type="articleCategory">Symposium: Synucleinopathies: Update</title></titleGroup><copyright>2007 Japanese Society of Neuropathology</copyright><eventGroup><event type="firstOnline" date="2007-09-18"></event><event type="publishedOnlineFinalForm" date="2007-09-18"></event><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:3.1.3 standalone mode:FullText" date="2012-03-08"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-02-03"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-31"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="474">474</numbering><numbering type="pageLast" number="478">478</numbering></numberingGroup><correspondenceTo>Takeshi Iwatsubo, MD, Department of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7‐3‐1 Hongo Bunkyoku, Tokyo 113‐0033, Japan. Email: <email normalForm="iwatsubo@mol.f.u-tokyo.ac.jp">iwatsubo@mol.f.u‐tokyo.ac.jp</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:NEUP.NEUP785.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 17 October 2006; revised and accepted 6 November 2006.</unparsedEditorialHistory><countGroup><count type="figureTotal" number="4"></count><count type="tableTotal" number="0"></count><count type="formulaTotal" number="0"></count><count type="referenceTotal" number="14"></count><count type="wordTotal" number="2367"></count><count type="linksPubMed" number="0"></count><count type="linksCrossRef" number="0"></count></countGroup><titleGroup><title type="main">THIS ARTICLE HAS BEEN RETRACTED: Pathological biochemistry of α‐synucleinopathy</title><title type="shortAuthors">T Iwatsubo</title><title type="short">Pathobiochemistry of α‐synucleinopathy</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#aff-1-1"><personName><givenNames>Takeshi</givenNames><familyName>Iwatsubo</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="aff-1-1" countryCode="JP"><unparsedAffiliation>Department of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">α‐synuclein</keyword><keyword xml:id="k2">Lewy body</keyword><keyword xml:id="k3">Parkinson's disease</keyword><keyword xml:id="k4">synucleinopathy</keyword><keyword xml:id="k5">transgenic <i>C. elegans</i></keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><p>Lewy bodies (LBs) are hallmark lesions in the brains of patients with Parkinson's disease (PD) and dementia with Lewy bodies (DLB). We raised a monoclonal antibody LB509 against purified LBs from the brains of patients with DLB that strongly immuolabled LBs, and found that α‐synuclein is one of the major components of LBs. Thus, the deposition of α‐synuclein, an abundant presynaptic brain protein, as fibrillary aggregates in affected neurons or glial cells, was highlighted as a hallmark lesion of a subset of neurodegenerative disorders, including PD, DLB and multiple system atrophy collectively referred to as synucleinopathies. Importantly, the identification of missense mutations in and multiplication of α‐synuclein gene in some pedigrees of familial PD has strongly implicated α‐synuclein in the pathogenesis of PD and other synucleinopathies. We then examined the specific post‐translational modifications that characterize and underlie the aggregation of α‐synuclein in synucleinopathy brains by mass spectrometry and using a specific antibody, and found that serine 129 of α‐synuclein deposited in synucleinopathy lesions is selectively and extensively phosphorylated. Furthermore we generated transgenic <i>C. elegans</i> overexpressing α‐synuclein in neurons, and found that overexpression of familial PD‐linked mutant form of α‐synuclein impairs functions of dopamine neurons. These findings collectively underscore the importance of deposition of α‐synuclein as well as its phosphorylation in the pathogenesis of α‐synucleinopathies.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>THIS ARTICLE HAS BEEN RETRACTED: Pathological biochemistry of α‐synucleinopathy</title></titleInfo><titleInfo type="abbreviated"><title>Pathobiochemistry of α‐synucleinopathy</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>THIS ARTICLE HAS BEEN RETRACTED: Pathological biochemistry of α‐synucleinopathy</title></titleInfo><name type="personal"><namePart type="given">Takeshi</namePart><namePart type="family">Iwatsubo</namePart><affiliation>Department of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="other" displayLabel="miscellaneous"></genre><originInfo><publisher>Blackwell Publishing Asia</publisher><place><placeTerm type="text">Melbourne, Australia</placeTerm></place><dateIssued encoding="w3cdtf">2007-10</dateIssued><edition>Received 17 October 2006; revised and accepted 6 November 2006.</edition><copyrightDate encoding="w3cdtf">2007</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="references">14</extent><extent unit="words">2367</extent></physicalDescription><abstract lang="en">Lewy bodies (LBs) are hallmark lesions in the brains of patients with Parkinson's disease (PD) and dementia with Lewy bodies (DLB). We raised a monoclonal antibody LB509 against purified LBs from the brains of patients with DLB that strongly immuolabled LBs, and found that α‐synuclein is one of the major components of LBs. Thus, the deposition of α‐synuclein, an abundant presynaptic brain protein, as fibrillary aggregates in affected neurons or glial cells, was highlighted as a hallmark lesion of a subset of neurodegenerative disorders, including PD, DLB and multiple system atrophy collectively referred to as synucleinopathies. Importantly, the identification of missense mutations in and multiplication of α‐synuclein gene in some pedigrees of familial PD has strongly implicated α‐synuclein in the pathogenesis of PD and other synucleinopathies. We then examined the specific post‐translational modifications that characterize and underlie the aggregation of α‐synuclein in synucleinopathy brains by mass spectrometry and using a specific antibody, and found that serine 129 of α‐synuclein deposited in synucleinopathy lesions is selectively and extensively phosphorylated. Furthermore we generated transgenic C. elegans overexpressing α‐synuclein in neurons, and found that overexpression of familial PD‐linked mutant form of α‐synuclein impairs functions of dopamine neurons. These findings collectively underscore the importance of deposition of α‐synuclein as well as its phosphorylation in the pathogenesis of α‐synucleinopathies.</abstract><subject lang="en"><genre>Keywords</genre><topic>α‐synuclein</topic><topic>Lewy body</topic><topic>Parkinson's disease</topic><topic>synucleinopathy</topic><topic>transgenic C. elegans</topic></subject><relatedItem type="host"><titleInfo><title>Neuropathology</title></titleInfo><genre type="Journal">journal</genre><subject><genre>article category</genre><topic>Symposium: Synucleinopathies: Update</topic></subject><identifier type="ISSN">0919-6544</identifier><identifier type="eISSN">1440-1789</identifier><identifier type="DOI">10.1111/(ISSN)1440-1789</identifier><identifier type="PublisherID">NEUP</identifier><part><date>2007</date><detail type="volume"><caption>vol.</caption><number>27</number></detail><detail type="issue"><caption>no.</caption><number>5</number></detail><extent unit="pages"><start>474</start><end>478</end><total>5</total></extent></part></relatedItem><identifier type="istex">CEFE215F3C31B33E6499C02EA19A025CDB247A75</identifier><identifier type="DOI">10.1111/j.1440-1789.2007.00785.x</identifier><identifier type="ArticleID">NEUP785</identifier><accessCondition type="use and reproduction" contentType="copyright">2007 Japanese Society of Neuropathology</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Blackwell Publishing Asia</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001778 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 001778 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Sante
|area= ParkinsonV1
|flux= Main
|étape= Corpus
|type= RBID
|clé= ISTEX:CEFE215F3C31B33E6499C02EA19A025CDB247A75
|texte= THIS ARTICLE HAS BEEN RETRACTED: Pathological biochemistry of α‐synucleinopathy
}}
| This area was generated with Dilib version V0.6.23. |  |