6-Hydroxydopamine but not 1-methyl-4-phenylpyridinium abolishes alpha-synuclein anti-apoptotic phenotype by inhibiting its proteasomal degradation and by promoting its aggregation.
Identifieur interne : 000E08 ( PubMed/Checkpoint ); précédent : 000E07; suivant : 000E096-Hydroxydopamine but not 1-methyl-4-phenylpyridinium abolishes alpha-synuclein anti-apoptotic phenotype by inhibiting its proteasomal degradation and by promoting its aggregation.
Auteurs : Cristine Alves Da Costa [France] ; Julie Dunys ; Frédéric Brau ; Sherwin Wilk ; Roberto Cappai ; Frédéric CheclerSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2006.
English descriptors
- KwdEn :
- 1-Methyl-4-phenylpyridinium (metabolism), Animals, Apoptosis (drug effects), Disease Models, Animal, Herbicides (metabolism), Humans, Neuroblastoma (pathology), Neurons (physiology), Oxidopamine (pharmacology), Parkinson Disease (physiopathology), Phenotype, Proteasome Endopeptidase Complex (metabolism), Tumor Cells, Cultured, alpha-Synuclein (drug effects), alpha-Synuclein (metabolism).
- MESH :
- chemical , drug effects : alpha-Synuclein.
- chemical , metabolism : 1-Methyl-4-phenylpyridinium, Herbicides, Proteasome Endopeptidase Complex, alpha-Synuclein.
- drug effects : Apoptosis.
- pathology : Neuroblastoma.
- chemical , pharmacology : Oxidopamine.
- physiology : Neurons.
- physiopathology : Parkinson Disease.
- Animals, Disease Models, Animal, Humans, Phenotype, Tumor Cells, Cultured.
Abstract
We established previously that alpha-synuclein displayed a protective anti-apoptotic phenotype in neurons, mainly by down-regulating p53-dependent caspase-3 activation (Alves da Costa, C., Ancolio, K., and Checler, F. (2000) J. Biol. Chem. 275, 24065-24069; Alves da Costa, C., Paitel, E., Vincent, B., and Checler, F. (2002) J. Biol. Chem. 277, 50980-50984). This function was abolished by Parkinson disease-linked pathogenic mutations and by the dopaminergic toxin, 6-hydroxydopamine (6OH-DOPA) (Alves da Costa, C., Paitel, E., Vincent, B., and Checler, F. (2002) J. Biol. Chem. 277, 50980-50984). However, the mechanisms by which 6OH-DOPA interfered with alpha-synuclein function remained unclear. Here we showed that 6OH-DOPA prevents alpha-synuclein-mediated anti-apoptotic function by altering its degradation. Thus, 6OH-DOPA treatment of TSM1 neurons and SH-SY5Y neuroblastoma cells enhances endogenous alpha-synuclein-like immunoreactivity and inhibits the catabolism of endogenous and recombinant alpha-synucleins by purified 20 S proteasome. Furthermore, we demonstrated that 6OH-DOPA directly inhibits endogenous proteasomal activity in TSM1 and SH-SY5Y cells and also blocks purified proteasome activity in vitro. This inhibitory effect can be prevented by the anti-oxidant phenyl-N-butylnitrone. We also established that 6OH-DOPA triggers the aggregation of recombinant alpha-synuclein in vitro. Therefore, we conclude that 6OH-DOPA abolishes alpha-synuclein anti-apoptotic phenotype by inhibiting its proteasomal degradation, thereby increasing its intracellular concentration and potential propensity to aggregation, the latter phenomenon being directly exacerbated by 6OH-DOPA itself. Interestingly, 1-methyl-4-phenylpyridinium (MPP(+)), another toxin inducer of Parkinson disease-like pathology, does not affect alpha-synuclein protective function and fails to trigger aggregation of recombinant alpha-synuclein. Furthermore, MPP(+) does not alter cellular proteasomal activity, and only high concentrations of the toxin affect purified 20 S proteasome by a mechanism that remains insensitive to phenyl-N-butylnitrone. The drastically distinct effects of 6OH-DOPA and MPP(+) on alpha-synuclein function are discussed with respect to Parkinson disease pathology and animal models mimicking this pathology.
DOI: 10.1074/jbc.M513903200
PubMed: 16464850
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:16464850Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">6-Hydroxydopamine but not 1-methyl-4-phenylpyridinium abolishes alpha-synuclein anti-apoptotic phenotype by inhibiting its proteasomal degradation and by promoting its aggregation.</title>
<author><name sortKey="Alves Da Costa, Cristine" sort="Alves Da Costa, Cristine" uniqKey="Alves Da Costa C" first="Cristine" last="Alves Da Costa">Cristine Alves Da Costa</name>
<affiliation wicri:level="3"><nlm:affiliation>IPMC du CNRS, UMR6097, Equipe Labellisée FRM, 660 Route des Lucioles, 06560 Valbonne, France. acosta@ipmc.cnrs.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>IPMC du CNRS, UMR6097, Equipe Labellisée FRM, 660 Route des Lucioles, 06560 Valbonne</wicri:regionArea>
<placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region>
<settlement type="city">Valbonne</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Dunys, Julie" sort="Dunys, Julie" uniqKey="Dunys J" first="Julie" last="Dunys">Julie Dunys</name>
</author>
<author><name sortKey="Brau, Frederic" sort="Brau, Frederic" uniqKey="Brau F" first="Frédéric" last="Brau">Frédéric Brau</name>
</author>
<author><name sortKey="Wilk, Sherwin" sort="Wilk, Sherwin" uniqKey="Wilk S" first="Sherwin" last="Wilk">Sherwin Wilk</name>
</author>
<author><name sortKey="Cappai, Roberto" sort="Cappai, Roberto" uniqKey="Cappai R" first="Roberto" last="Cappai">Roberto Cappai</name>
</author>
<author><name sortKey="Checler, Frederic" sort="Checler, Frederic" uniqKey="Checler F" first="Frédéric" last="Checler">Frédéric Checler</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2006">2006</date>
<idno type="RBID">pubmed:16464850</idno>
<idno type="pmid">16464850</idno>
<idno type="doi">10.1074/jbc.M513903200</idno>
<idno type="wicri:Area/PubMed/Corpus">000E76</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000E76</idno>
<idno type="wicri:Area/PubMed/Curation">000E36</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000E36</idno>
<idno type="wicri:Area/PubMed/Checkpoint">000E36</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000E36</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">6-Hydroxydopamine but not 1-methyl-4-phenylpyridinium abolishes alpha-synuclein anti-apoptotic phenotype by inhibiting its proteasomal degradation and by promoting its aggregation.</title>
<author><name sortKey="Alves Da Costa, Cristine" sort="Alves Da Costa, Cristine" uniqKey="Alves Da Costa C" first="Cristine" last="Alves Da Costa">Cristine Alves Da Costa</name>
<affiliation wicri:level="3"><nlm:affiliation>IPMC du CNRS, UMR6097, Equipe Labellisée FRM, 660 Route des Lucioles, 06560 Valbonne, France. acosta@ipmc.cnrs.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>IPMC du CNRS, UMR6097, Equipe Labellisée FRM, 660 Route des Lucioles, 06560 Valbonne</wicri:regionArea>
<placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region>
<settlement type="city">Valbonne</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Dunys, Julie" sort="Dunys, Julie" uniqKey="Dunys J" first="Julie" last="Dunys">Julie Dunys</name>
</author>
<author><name sortKey="Brau, Frederic" sort="Brau, Frederic" uniqKey="Brau F" first="Frédéric" last="Brau">Frédéric Brau</name>
</author>
<author><name sortKey="Wilk, Sherwin" sort="Wilk, Sherwin" uniqKey="Wilk S" first="Sherwin" last="Wilk">Sherwin Wilk</name>
</author>
<author><name sortKey="Cappai, Roberto" sort="Cappai, Roberto" uniqKey="Cappai R" first="Roberto" last="Cappai">Roberto Cappai</name>
</author>
<author><name sortKey="Checler, Frederic" sort="Checler, Frederic" uniqKey="Checler F" first="Frédéric" last="Checler">Frédéric Checler</name>
</author>
</analytic>
<series><title level="j">The Journal of biological chemistry</title>
<idno type="ISSN">0021-9258</idno>
<imprint><date when="2006" type="published">2006</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>1-Methyl-4-phenylpyridinium (metabolism)</term>
<term>Animals</term>
<term>Apoptosis (drug effects)</term>
<term>Disease Models, Animal</term>
<term>Herbicides (metabolism)</term>
<term>Humans</term>
<term>Neuroblastoma (pathology)</term>
<term>Neurons (physiology)</term>
<term>Oxidopamine (pharmacology)</term>
<term>Parkinson Disease (physiopathology)</term>
<term>Phenotype</term>
<term>Proteasome Endopeptidase Complex (metabolism)</term>
<term>Tumor Cells, Cultured</term>
<term>alpha-Synuclein (drug effects)</term>
<term>alpha-Synuclein (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>alpha-Synuclein</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>1-Methyl-4-phenylpyridinium</term>
<term>Herbicides</term>
<term>Proteasome Endopeptidase Complex</term>
<term>alpha-Synuclein</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Apoptosis</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Neuroblastoma</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Oxidopamine</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Neurons</term>
</keywords>
<keywords scheme="MESH" qualifier="physiopathology" xml:lang="en"><term>Parkinson Disease</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Disease Models, Animal</term>
<term>Humans</term>
<term>Phenotype</term>
<term>Tumor Cells, Cultured</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">We established previously that alpha-synuclein displayed a protective anti-apoptotic phenotype in neurons, mainly by down-regulating p53-dependent caspase-3 activation (Alves da Costa, C., Ancolio, K., and Checler, F. (2000) J. Biol. Chem. 275, 24065-24069; Alves da Costa, C., Paitel, E., Vincent, B., and Checler, F. (2002) J. Biol. Chem. 277, 50980-50984). This function was abolished by Parkinson disease-linked pathogenic mutations and by the dopaminergic toxin, 6-hydroxydopamine (6OH-DOPA) (Alves da Costa, C., Paitel, E., Vincent, B., and Checler, F. (2002) J. Biol. Chem. 277, 50980-50984). However, the mechanisms by which 6OH-DOPA interfered with alpha-synuclein function remained unclear. Here we showed that 6OH-DOPA prevents alpha-synuclein-mediated anti-apoptotic function by altering its degradation. Thus, 6OH-DOPA treatment of TSM1 neurons and SH-SY5Y neuroblastoma cells enhances endogenous alpha-synuclein-like immunoreactivity and inhibits the catabolism of endogenous and recombinant alpha-synucleins by purified 20 S proteasome. Furthermore, we demonstrated that 6OH-DOPA directly inhibits endogenous proteasomal activity in TSM1 and SH-SY5Y cells and also blocks purified proteasome activity in vitro. This inhibitory effect can be prevented by the anti-oxidant phenyl-N-butylnitrone. We also established that 6OH-DOPA triggers the aggregation of recombinant alpha-synuclein in vitro. Therefore, we conclude that 6OH-DOPA abolishes alpha-synuclein anti-apoptotic phenotype by inhibiting its proteasomal degradation, thereby increasing its intracellular concentration and potential propensity to aggregation, the latter phenomenon being directly exacerbated by 6OH-DOPA itself. Interestingly, 1-methyl-4-phenylpyridinium (MPP(+)), another toxin inducer of Parkinson disease-like pathology, does not affect alpha-synuclein protective function and fails to trigger aggregation of recombinant alpha-synuclein. Furthermore, MPP(+) does not alter cellular proteasomal activity, and only high concentrations of the toxin affect purified 20 S proteasome by a mechanism that remains insensitive to phenyl-N-butylnitrone. The drastically distinct effects of 6OH-DOPA and MPP(+) on alpha-synuclein function are discussed with respect to Parkinson disease pathology and animal models mimicking this pathology.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16464850</PMID>
<DateCreated><Year>2006</Year>
<Month>04</Month>
<Day>03</Day>
</DateCreated>
<DateCompleted><Year>2006</Year>
<Month>05</Month>
<Day>30</Day>
</DateCompleted>
<DateRevised><Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN>
<JournalIssue CitedMedium="Print"><Volume>281</Volume>
<Issue>14</Issue>
<PubDate><Year>2006</Year>
<Month>Apr</Month>
<Day>07</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation>
</Journal>
<ArticleTitle>6-Hydroxydopamine but not 1-methyl-4-phenylpyridinium abolishes alpha-synuclein anti-apoptotic phenotype by inhibiting its proteasomal degradation and by promoting its aggregation.</ArticleTitle>
<Pagination><MedlinePgn>9824-31</MedlinePgn>
</Pagination>
<Abstract><AbstractText>We established previously that alpha-synuclein displayed a protective anti-apoptotic phenotype in neurons, mainly by down-regulating p53-dependent caspase-3 activation (Alves da Costa, C., Ancolio, K., and Checler, F. (2000) J. Biol. Chem. 275, 24065-24069; Alves da Costa, C., Paitel, E., Vincent, B., and Checler, F. (2002) J. Biol. Chem. 277, 50980-50984). This function was abolished by Parkinson disease-linked pathogenic mutations and by the dopaminergic toxin, 6-hydroxydopamine (6OH-DOPA) (Alves da Costa, C., Paitel, E., Vincent, B., and Checler, F. (2002) J. Biol. Chem. 277, 50980-50984). However, the mechanisms by which 6OH-DOPA interfered with alpha-synuclein function remained unclear. Here we showed that 6OH-DOPA prevents alpha-synuclein-mediated anti-apoptotic function by altering its degradation. Thus, 6OH-DOPA treatment of TSM1 neurons and SH-SY5Y neuroblastoma cells enhances endogenous alpha-synuclein-like immunoreactivity and inhibits the catabolism of endogenous and recombinant alpha-synucleins by purified 20 S proteasome. Furthermore, we demonstrated that 6OH-DOPA directly inhibits endogenous proteasomal activity in TSM1 and SH-SY5Y cells and also blocks purified proteasome activity in vitro. This inhibitory effect can be prevented by the anti-oxidant phenyl-N-butylnitrone. We also established that 6OH-DOPA triggers the aggregation of recombinant alpha-synuclein in vitro. Therefore, we conclude that 6OH-DOPA abolishes alpha-synuclein anti-apoptotic phenotype by inhibiting its proteasomal degradation, thereby increasing its intracellular concentration and potential propensity to aggregation, the latter phenomenon being directly exacerbated by 6OH-DOPA itself. Interestingly, 1-methyl-4-phenylpyridinium (MPP(+)), another toxin inducer of Parkinson disease-like pathology, does not affect alpha-synuclein protective function and fails to trigger aggregation of recombinant alpha-synuclein. Furthermore, MPP(+) does not alter cellular proteasomal activity, and only high concentrations of the toxin affect purified 20 S proteasome by a mechanism that remains insensitive to phenyl-N-butylnitrone. The drastically distinct effects of 6OH-DOPA and MPP(+) on alpha-synuclein function are discussed with respect to Parkinson disease pathology and animal models mimicking this pathology.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Alves da Costa</LastName>
<ForeName>Cristine</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>IPMC du CNRS, UMR6097, Equipe Labellisée FRM, 660 Route des Lucioles, 06560 Valbonne, France. acosta@ipmc.cnrs.fr</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dunys</LastName>
<ForeName>Julie</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Brau</LastName>
<ForeName>Frédéric</ForeName>
<Initials>F</Initials>
</Author>
<Author ValidYN="Y"><LastName>Wilk</LastName>
<ForeName>Sherwin</ForeName>
<Initials>S</Initials>
</Author>
<Author ValidYN="Y"><LastName>Cappai</LastName>
<ForeName>Roberto</ForeName>
<Initials>R</Initials>
</Author>
<Author ValidYN="Y"><LastName>Checler</LastName>
<ForeName>Frédéric</ForeName>
<Initials>F</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2006</Year>
<Month>02</Month>
<Day>07</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Biol Chem</MedlineTA>
<NlmUniqueID>2985121R</NlmUniqueID>
<ISSNLinking>0021-9258</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D006540">Herbicides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>8HW4YBZ748</RegistryNumber>
<NameOfSubstance UI="D016627">Oxidopamine</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.25.1</RegistryNumber>
<NameOfSubstance UI="D046988">Proteasome Endopeptidase Complex</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>R865A5OY8J</RegistryNumber>
<NameOfSubstance UI="D015655">1-Methyl-4-phenylpyridinium</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>J Biol Chem. 2013 Jul 19;288(29):21208</RefSource>
</CommentsCorrections>
</CommentsCorrectionsList>
<MeshHeadingList><MeshHeading><DescriptorName UI="D015655" MajorTopicYN="N">1-Methyl-4-phenylpyridinium</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017209" MajorTopicYN="N">Apoptosis</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006540" MajorTopicYN="N">Herbicides</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009447" MajorTopicYN="N">Neuroblastoma</DescriptorName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016627" MajorTopicYN="N">Oxidopamine</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName>
<QualifierName UI="Q000503" MajorTopicYN="N">physiopathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D046988" MajorTopicYN="N">Proteasome Endopeptidase Complex</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014407" MajorTopicYN="N">Tumor Cells, Cultured</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year>
<Month>2</Month>
<Day>9</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2006</Year>
<Month>5</Month>
<Day>31</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2006</Year>
<Month>2</Month>
<Day>9</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">16464850</ArticleId>
<ArticleId IdType="pii">M513903200</ArticleId>
<ArticleId IdType="doi">10.1074/jbc.M513903200</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>France</li>
</country>
<region><li>Provence-Alpes-Côte d'Azur</li>
</region>
<settlement><li>Valbonne</li>
</settlement>
</list>
<tree><noCountry><name sortKey="Brau, Frederic" sort="Brau, Frederic" uniqKey="Brau F" first="Frédéric" last="Brau">Frédéric Brau</name>
<name sortKey="Cappai, Roberto" sort="Cappai, Roberto" uniqKey="Cappai R" first="Roberto" last="Cappai">Roberto Cappai</name>
<name sortKey="Checler, Frederic" sort="Checler, Frederic" uniqKey="Checler F" first="Frédéric" last="Checler">Frédéric Checler</name>
<name sortKey="Dunys, Julie" sort="Dunys, Julie" uniqKey="Dunys J" first="Julie" last="Dunys">Julie Dunys</name>
<name sortKey="Wilk, Sherwin" sort="Wilk, Sherwin" uniqKey="Wilk S" first="Sherwin" last="Wilk">Sherwin Wilk</name>
</noCountry>
<country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Alves Da Costa, Cristine" sort="Alves Da Costa, Cristine" uniqKey="Alves Da Costa C" first="Cristine" last="Alves Da Costa">Cristine Alves Da Costa</name>
</region>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonFranceV1/Data/PubMed/Checkpoint
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000E08 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd -nk 000E08 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Sante |area= ParkinsonFranceV1 |flux= PubMed |étape= Checkpoint |type= RBID |clé= pubmed:16464850 |texte= 6-Hydroxydopamine but not 1-methyl-4-phenylpyridinium abolishes alpha-synuclein anti-apoptotic phenotype by inhibiting its proteasomal degradation and by promoting its aggregation. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/RBID.i -Sk "pubmed:16464850" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd \ | NlmPubMed2Wicri -a ParkinsonFranceV1
![]() | This area was generated with Dilib version V0.6.29. | ![]() |