Phylogenetic and in silico structural analysis of the Parkinson disease‐related kinase PINK1
Identifieur interne : 002F63 ( Main/Corpus ); précédent : 002F62; suivant : 002F64Phylogenetic and in silico structural analysis of the Parkinson disease‐related kinase PINK1
Auteurs : Fernando Cardona ; Jose Vicente Sánchez-Mut ; Hernán Dopazo ; Jordi Pérez-TurSource :
- Human Mutation [ 1059-7794 ] ; 2011-04.
English descriptors
- KwdEn :
Abstract
Parkinson disease (PD) is the second most common neurodegenerative disorder and is characterized by the loss of dopaminergic neurons in the substantia nigra. Mutations in PINK1 were shown to cause recessive familial PD, and today are proposed to be associated with the disease via mitochondrial dysfunction and oxidative damage. The PINK1 gene comprises eight exons, which encode a ubiquitously expressed 581 amino acid protein that contains an N‐terminal mitochondrial targeting domain and a serine/threonine protein kinase. To better understand the relationship between PINK1 and PD we have first analyzed the evolutionary history of the gene showing its late emergence in evolution. In addition, we have modeled the three‐dimensional structure of PINK1 and found some evidences that help to explain the effect of some PD‐related mutations in this protein's function. Hum Mutat 32:369–378, 2011. © 2011 Wiley‐Liss, Inc.
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DOI: 10.1002/humu.21444
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ISTEX:1B14321FFF6639FB4227A437AA32988E6971D7E7Le document en format XML
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Mutations in PINK1 were shown to cause recessive familial PD, and today are proposed to be associated with the disease via mitochondrial dysfunction and oxidative damage. The PINK1 gene comprises eight exons, which encode a ubiquitously expressed 581 amino acid protein that contains an N‐terminal mitochondrial targeting domain and a serine/threonine protein kinase. To better understand the relationship between PINK1 and PD we have first analyzed the evolutionary history of the gene showing its late emergence in evolution. In addition, we have modeled the three‐dimensional structure of PINK1 and found some evidences that help to explain the effect of some PD‐related mutations in this protein's function. Hum Mutat 32:369–378, 2011. © 2011 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Fernando Cardona</name><affiliations><json:string>Unitat de Genètica Molecular, Institut de Biomedicina de València‐CSIC, Valencia, Spain</json:string><json:string>CiberNed, Spain</json:string></affiliations></json:item><json:item><name>Jose Vicente Sánchez‐Mut</name><affiliations><json:string>Unitat de Genètica Molecular, Institut de Biomedicina de València‐CSIC, Valencia, Spain</json:string><json:string>Current Address: Programa d'Epigenètica y Biologia del Càncer, Insitut d'Investigació Biomèdica de Bellvitge (IDIBELL), Barcelona, Spain</json:string></affiliations></json:item><json:item><name>Hernán Dopazo</name><affiliations><json:string>Bioinformatics and Genomics Department, Centro de Investigación Príncipe Felipe, Valencia, Spain</json:string></affiliations></json:item><json:item><name>Jordi Pérez‐Tur</name><affiliations><json:string>Unitat de Genètica Molecular, Institut de Biomedicina de València‐CSIC, Valencia, Spain</json:string><json:string>CiberNed, Spain</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>PINK1</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CaMKI</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CaMKII</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>DMPK</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>kinase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Parkinson disease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>phylogeny</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>pathogenic mutations</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>structure</value></json:item></subject><articleId><json:string>HUMU21444</json:string></articleId><language><json:string>eng</json:string></language><abstract>Parkinson disease (PD) is the second most common neurodegenerative disorder and is characterized by the loss of dopaminergic neurons in the substantia nigra. 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href="urn-x:wiley:10597794:media:humu21444:humu_21444_sm_SuppInfo"></mediaResource><caption>Supporting Information</caption></supportingInfoItem></supportingInformation><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Parkinson disease (PD) is the second most common neurodegenerative disorder and is characterized by the loss of dopaminergic neurons in the substantia nigra. Mutations in <i>PINK1</i> were shown to cause recessive familial PD, and today are proposed to be associated with the disease via mitochondrial dysfunction and oxidative damage. The <i>PINK1</i> gene comprises eight exons, which encode a ubiquitously expressed 581 amino acid protein that contains an N‐terminal mitochondrial targeting domain and a serine/threonine protein kinase. To better understand the relationship between PINK1 and PD we have first analyzed the evolutionary history of the gene showing its late emergence in evolution. In addition, we have modeled the three‐dimensional structure of PINK1 and found some evidences that help to explain the effect of some PD‐related mutations in this protein's function. Hum Mutat 32:369–378, 2011. © 2011 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><p>Communicated by Mauno Vihinen</p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Phylogenetic and in silico structural analysis of the Parkinson disease‐related kinase PINK1</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Phylogenetic and in silico structural analysis of the Parkinson disease‐related kinase PINK1</title></titleInfo><name type="personal"><namePart type="given">Fernando</namePart><namePart type="family">Cardona</namePart><affiliation>Unitat de Genètica Molecular, Institut de Biomedicina de València‐CSIC, Valencia, Spain</affiliation><affiliation>CiberNed, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jose Vicente</namePart><namePart type="family">Sánchez‐Mut</namePart><affiliation>Unitat de Genètica Molecular, Institut de Biomedicina de València‐CSIC, Valencia, Spain</affiliation><affiliation>Current Address: Programa d'Epigenètica y Biologia del Càncer, Insitut d'Investigació Biomèdica de Bellvitge (IDIBELL), Barcelona, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hernán</namePart><namePart type="family">Dopazo</namePart><affiliation>Bioinformatics and Genomics Department, Centro de Investigación Príncipe Felipe, Valencia, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jordi</namePart><namePart type="family">Pérez‐Tur</namePart><affiliation>Unitat de Genètica Molecular, Institut de Biomedicina de València‐CSIC, Valencia, Spain</affiliation><affiliation>CiberNed, Spain</affiliation><description>Correspondence: Institut de Biomedicina de València‐CSIC, Jaime Roig 11, E46010 València, Spain</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="other" displayLabel="miscellaneous"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2011-04</dateIssued><dateCaptured encoding="w3cdtf">2010-07-23</dateCaptured><dateValid encoding="w3cdtf">2010-12-08</dateValid><copyrightDate encoding="w3cdtf">2011</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">5</extent><extent unit="tables">1</extent><extent unit="references">53</extent></physicalDescription><abstract lang="en">Parkinson disease (PD) is the second most common neurodegenerative disorder and is characterized by the loss of dopaminergic neurons in the substantia nigra. Mutations in PINK1 were shown to cause recessive familial PD, and today are proposed to be associated with the disease via mitochondrial dysfunction and oxidative damage. The PINK1 gene comprises eight exons, which encode a ubiquitously expressed 581 amino acid protein that contains an N‐terminal mitochondrial targeting domain and a serine/threonine protein kinase. To better understand the relationship between PINK1 and PD we have first analyzed the evolutionary history of the gene showing its late emergence in evolution. In addition, we have modeled the three‐dimensional structure of PINK1 and found some evidences that help to explain the effect of some PD‐related mutations in this protein's function. Hum Mutat 32:369–378, 2011. © 2011 Wiley‐Liss, Inc.</abstract><note type="content">*Communicated by Mauno Vihinen</note><note type="funding">The Ministerio de Ciencia e Innovación, Spain - No. SAF2009‐10434; </note><note type="funding">Generalitat Valenciana - No. ACOMP/2010/096; </note><subject lang="en"><genre>Keywords</genre><topic>PINK1</topic><topic>CaMKI</topic><topic>CaMKII</topic><topic>DMPK</topic><topic>kinase</topic><topic>Parkinson disease</topic><topic>phylogeny</topic><topic>pathogenic mutations</topic><topic>structure</topic></subject><relatedItem type="host"><titleInfo><title>Human Mutation</title></titleInfo><titleInfo type="abbreviated"><title>Hum. Mutat.</title></titleInfo><genre type="Journal">journal</genre><note type="content"> Additional Supporting Information may be found in the online version of this articleSupporting Info Item: Supporting Information - </note><subject><genre>article category</genre><topic>Informatics</topic></subject><identifier type="ISSN">1059-7794</identifier><identifier type="eISSN">1098-1004</identifier><identifier type="DOI">10.1002/(ISSN)1098-1004</identifier><identifier type="PublisherID">HUMU</identifier><part><date>2011</date><detail type="volume"><caption>vol.</caption><number>32</number></detail><detail type="issue"><caption>no.</caption><number>4</number></detail><extent unit="pages"><start>369</start><end>378</end><total>10</total></extent></part></relatedItem><identifier type="istex">1B14321FFF6639FB4227A437AA32988E6971D7E7</identifier><identifier type="DOI">10.1002/humu.21444</identifier><identifier type="ArticleID">HUMU21444</identifier><accessCondition type="use and reproduction" contentType="copyright">© 2011 Wiley‐Liss, Inc.</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)
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