Ubiquitin–proteasome system and Parkinson's disease
Identifieur interne : 002792 ( Main/Corpus ); précédent : 002791; suivant : 002793Ubiquitin–proteasome system and Parkinson's disease
Auteurs : C. Warren Olanow ; Kevin St. P. McnaughtSource :
- Movement Disorders [ 0885-3185 ] ; 2006-11.
English descriptors
Abstract
Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin–proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body–like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age‐related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD. © 2006 Movement Disorder Society
Url:
DOI: 10.1002/mds.21013
Links to Exploration step
ISTEX:57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Ubiquitin–proteasome system and Parkinson's disease</title><author><name sortKey="Olanow, C Warren" sort="Olanow, C Warren" uniqKey="Olanow C" first="C. Warren" last="Olanow">C. Warren Olanow</name><affiliation><mods:affiliation>Department of Neurology, Mount Sinai School of Medicine, New York, New York, USA</mods:affiliation></affiliation></author><author><name sortKey="Mcnaught, Kevin St P" sort="Mcnaught, Kevin St P" uniqKey="Mcnaught K" first="Kevin St. P." last="Mcnaught">Kevin St. P. Mcnaught</name><affiliation><mods:affiliation>Department of Neurology, Mount Sinai School of Medicine, New York, New York, USA</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4</idno><date when="2006" year="2006">2006</date><idno type="doi">10.1002/mds.21013</idno><idno type="url">https://api.istex.fr/document/57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">002792</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Ubiquitin–proteasome system and Parkinson's disease</title><author><name sortKey="Olanow, C Warren" sort="Olanow, C Warren" uniqKey="Olanow C" first="C. Warren" last="Olanow">C. Warren Olanow</name><affiliation><mods:affiliation>Department of Neurology, Mount Sinai School of Medicine, New York, New York, USA</mods:affiliation></affiliation></author><author><name sortKey="Mcnaught, Kevin St P" sort="Mcnaught, Kevin St P" uniqKey="Mcnaught K" first="Kevin St. P." last="Mcnaught">Kevin St. P. Mcnaught</name><affiliation><mods:affiliation>Department of Neurology, Mount Sinai School of Medicine, New York, New York, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><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. 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="2006-11">2006-11</date><biblScope unit="volume">21</biblScope><biblScope unit="issue">11</biblScope><biblScope unit="page" from="1806">1806</biblScope><biblScope unit="page" to="1823">1823</biblScope></imprint><idno type="ISSN">0885-3185</idno></series><idno type="istex">57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4</idno><idno type="DOI">10.1002/mds.21013</idno><idno type="ArticleID">MDS21013</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>proteasome</term><term>protein accumulation</term><term>ubiquitin</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin–proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body–like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age‐related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD. © 2006 Movement Disorder Society</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>C. Warren Olanow MD</name><affiliations><json:string>Department of Neurology, Mount Sinai School of Medicine, New York, New York, USA</json:string></affiliations></json:item><json:item><name>Kevin St. P. McNaught PhD</name><affiliations><json:string>Department of Neurology, Mount Sinai School of Medicine, New York, New York, USA</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>ubiquitin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>proteasome</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>protein accumulation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>alpha‐synuclein</value></json:item></subject><articleId><json:string>MDS21013</json:string></articleId><language><json:string>eng</json:string></language><abstract>Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin–proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body–like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age‐related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD. © 2006 Movement Disorder Society</abstract><qualityIndicators><score>6.476</score><pdfVersion>1.3</pdfVersion><pdfPageSize>594 x 792 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>5</keywordCount><abstractCharCount>862</abstractCharCount><pdfWordCount>12945</pdfWordCount><pdfCharCount>87246</pdfCharCount><pdfPageCount>18</pdfPageCount><abstractWordCount>123</abstractWordCount></qualityIndicators><title>Ubiquitin–proteasome system and Parkinson's disease</title><genre><json:string>review-article</json:string></genre><host><volume>21</volume><publisherId><json:string>MDS</json:string></publisherId><pages><total>18</total><last>1823</last><first>1806</first></pages><issn><json:string>0885-3185</json:string></issn><issue>11</issue><subject><json:item><value>Review</value></json:item></subject><genre><json:string>Journal</json:string></genre><language><json:string>unknown</json:string></language><eissn><json:string>1531-8257</json:string></eissn><title>Movement Disorders</title><doi><json:string>10.1002/(ISSN)1531-8257</json:string></doi></host><publicationDate>2006</publicationDate><copyrightDate>2006</copyrightDate><doi><json:string>10.1002/mds.21013</json:string></doi><id>57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Ubiquitin–proteasome system and Parkinson's disease</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><availability><p>WILEY</p></availability><date>2006</date></publicationStmt><notesStmt><note>National Institutes of Health/National Institute of Neurological Disorders and Stroke - No. 1 RO1 NS045999‐01;</note><note>Bachmann‐Strauss Dystonia and Parkinson Foundation, Inc.</note><note>Bendheim Parkinson's Disease Center</note><note>Morris and Alma Schapiro Fund</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Ubiquitin–proteasome system and Parkinson's disease</title><author><persName><forename type="first">C. Warren</forename><surname>Olanow</surname></persName><roleName type="degree">MD</roleName><note type="correspondence"><p>Correspondence: Department of Neurology, Mount Sinai School of Medicine, Annenberg 14‐73, One Gustave L. Levy Place, New York, NY 10029</p></note><affiliation>Department of Neurology, Mount Sinai School of Medicine, New York, New York, USA</affiliation></author><author><persName><forename type="first">Kevin St. P.</forename><surname>McNaught</surname></persName><roleName type="degree">PhD</roleName><affiliation>Department of Neurology, Mount Sinai School of Medicine, New York, New York, 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. Disord.</title><idno type="pISSN">0885-3185</idno><idno type="eISSN">1531-8257</idno><idno type="DOI">10.1002/(ISSN)1531-8257</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2006-11"></date><biblScope unit="volume">21</biblScope><biblScope unit="issue">11</biblScope><biblScope unit="page" from="1806">1806</biblScope><biblScope unit="page" to="1823">1823</biblScope></imprint></monogr><idno type="istex">57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4</idno><idno type="DOI">10.1002/mds.21013</idno><idno type="ArticleID">MDS21013</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2006</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin–proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body–like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age‐related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD. © 2006 Movement Disorder Society</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>ubiquitin</term></item><item><term>proteasome</term></item><item><term>Parkinson's disease</term></item><item><term>protein accumulation</term></item><item><term>alpha‐synuclein</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>article category</head><item><term>Review</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2005-11-04">Received</change><change when="2006-03-12">Registration</change><change when="2006-11">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4/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>Wiley Subscription Services, Inc., A Wiley Company</publisherName><publisherLoc>Hoboken</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1531-8257</doi><issn type="print">0885-3185</issn><issn type="electronic">1531-8257</issn><idGroup><id type="product" value="MDS"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="MOVEMENT DISORDERS">Movement Disorders</title><title type="subtitle">Official Journal of the Movement Disorder Society</title><title type="short">Mov. Disord.</title></titleGroup></publicationMeta><publicationMeta level="part" position="110"><doi origin="wiley" registered="yes">10.1002/mds.v21:11</doi><numberingGroup><numbering type="journalVolume" number="21">21</numbering><numbering type="journalIssue">11</numbering></numberingGroup><coverDate startDate="2006-11">November 2006</coverDate></publicationMeta><publicationMeta level="unit" type="reviewArticle" position="30" status="forIssue"><doi origin="wiley" registered="yes">10.1002/mds.21013</doi><idGroup><id type="unit" value="MDS21013"></id></idGroup><countGroup><count type="pageTotal" number="18"></count></countGroup><titleGroup><title type="articleCategory">Review</title><title type="tocHeading1">Reviews</title></titleGroup><copyright ownership="thirdParty">Copyright © 2006 Movement Disorder Society</copyright><eventGroup><event type="manuscriptReceived" date="2005-11-04"></event><event type="manuscriptRevised" date="2006-03-09"></event><event type="manuscriptAccepted" date="2006-03-12"></event><event type="publishedOnlineEarlyUnpaginated" date="2006-09-13"></event><event type="firstOnline" date="2006-09-13"></event><event type="publishedOnlineFinalForm" date="2006-11-08"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.2 mode:FullText source:FullText result:FullText" date="2010-03-09"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-02-02"></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">1806</numbering><numbering type="pageLast">1823</numbering></numberingGroup><correspondenceTo>Department of Neurology, Mount Sinai School of Medicine, Annenberg 14‐73, One Gustave L. Levy Place, New York, NY 10029</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:MDS.MDS21013.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="3"></count><count type="tableTotal" number="2"></count><count type="referenceTotal" number="232"></count><count type="wordTotal" number="14426"></count></countGroup><titleGroup><title type="main" xml:lang="en">Ubiquitin–proteasome system and Parkinson's disease</title><title type="short" xml:lang="en">Ubiquitin‐Proteasome System</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>C. Warren</givenNames><familyName>Olanow</familyName><degrees>MD</degrees></personName><contactDetails><email>warren.olanow@mssm.edu</email></contactDetails></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Kevin St. P.</givenNames><familyName>McNaught</familyName><degrees>PhD</degrees></personName></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="US" type="organization"><unparsedAffiliation>Department of Neurology, Mount Sinai School of Medicine, New York, New York, USA</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">ubiquitin</keyword><keyword xml:id="kwd2">proteasome</keyword><keyword xml:id="kwd3">Parkinson's disease</keyword><keyword xml:id="kwd4">protein accumulation</keyword><keyword xml:id="kwd5">alpha‐synuclein</keyword></keywordGroup><fundingInfo><fundingAgency>National Institutes of Health/National Institute of Neurological Disorders and Stroke</fundingAgency><fundingNumber>1 RO1 NS045999‐01</fundingNumber></fundingInfo><fundingInfo><fundingAgency>Bachmann‐Strauss Dystonia and Parkinson Foundation, Inc.</fundingAgency></fundingInfo><fundingInfo><fundingAgency>Bendheim Parkinson's Disease Center</fundingAgency></fundingInfo><fundingInfo><fundingAgency>Morris and Alma Schapiro Fund</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin–proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body–like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age‐related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD. © 2006 Movement Disorder Society</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Ubiquitin–proteasome system and Parkinson's disease</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Ubiquitin‐Proteasome System</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Ubiquitin–proteasome system and Parkinson's disease</title></titleInfo><name type="personal"><namePart type="given">C. Warren</namePart><namePart type="family">Olanow</namePart><namePart type="termsOfAddress">MD</namePart><affiliation>Department of Neurology, Mount Sinai School of Medicine, New York, New York, USA</affiliation><description>Correspondence: Department of Neurology, Mount Sinai School of Medicine, Annenberg 14‐73, One Gustave L. Levy Place, New York, NY 10029</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Kevin St. P.</namePart><namePart type="family">McNaught</namePart><namePart type="termsOfAddress">PhD</namePart><affiliation>Department of Neurology, Mount Sinai School of Medicine, New York, New York, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="reviewArticle"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2006-11</dateIssued><dateCaptured encoding="w3cdtf">2005-11-04</dateCaptured><dateValid encoding="w3cdtf">2006-03-12</dateValid><copyrightDate encoding="w3cdtf">2006</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">3</extent><extent unit="tables">2</extent><extent unit="references">232</extent><extent unit="words">14426</extent></physicalDescription><abstract lang="en">Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin–proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body–like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age‐related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD. © 2006 Movement Disorder Society</abstract><note type="funding">National Institutes of Health/National Institute of Neurological Disorders and Stroke - No. 1 RO1 NS045999‐01; </note><note type="funding">Bachmann‐Strauss Dystonia and Parkinson Foundation, Inc.</note><note type="funding">Bendheim Parkinson's Disease Center</note><note type="funding">Morris and Alma Schapiro Fund</note><subject lang="en"><genre>Keywords</genre><topic>ubiquitin</topic><topic>proteasome</topic><topic>Parkinson's disease</topic><topic>protein accumulation</topic><topic>alpha‐synuclein</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><genre type="Journal">journal</genre><subject><genre>article category</genre><topic>Review</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>2006</date><detail type="volume"><caption>vol.</caption><number>21</number></detail><detail type="issue"><caption>no.</caption><number>11</number></detail><extent unit="pages"><start>1806</start><end>1823</end><total>18</total></extent></part></relatedItem><identifier type="istex">57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4</identifier><identifier type="DOI">10.1002/mds.21013</identifier><identifier type="ArticleID">MDS21013</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2006 Movement Disorder Society</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Wiley Subscription Services, Inc., A Wiley Company</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 002792 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 002792 | 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:57BF90C0AACEB88C954E99CBB94BAAC6F18F5FD4
|texte= Ubiquitin–proteasome system and Parkinson's disease
}}
| This area was generated with Dilib version V0.6.23. |  |