Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar α-synuclein assemblies by mass spectrometry.
Identifieur interne : 000189 ( PubMed/Corpus ); précédent : 000188; suivant : 000190Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar α-synuclein assemblies by mass spectrometry.
Auteurs : Amulya Nidhi Shrivastava ; Virginie Redeker ; Nicolas Fritz ; Laura Pieri ; Leandro G. Almeida ; Maria Spolidoro ; Thomas Liebmann ; Luc Bousset ; Marianne Renner ; Clément Léna ; Anita Aperia ; Ronald Melki ; Antoine TrillerSource :
- Data in brief ; 2016.
Abstract
α-Synuclein (α-syn) is the principal component of Lewy bodies, the pathophysiological hallmark of individuals affected by Parkinson disease (PD). This neuropathologic form of α-syn contributes to PD progression and propagation of α-syn assemblies between neurons. The data we present here support the proteomic analysis used to identify neuronal proteins that specifically interact with extracellularly applied oligomeric or fibrillar α-syn assemblies (conditions 1 and 2, respectively) (doi: 10.15252/embj.201591397[1]). α-syn assemblies and their cellular partner proteins were pulled down from neuronal cell lysed shortly after exposure to exogenous α-syn assemblies and the associated proteins were identified by mass spectrometry using a shotgun proteomic-based approach. We also performed experiments on pure cultures of astrocytes to identify astrocyte-specific proteins interacting with oligomeric or fibrillar α-syn (conditions 3 and 4, respectively). For each condition, proteins interacting selectively with α-syn assemblies were identified by comparison to proteins pulled-down from untreated cells used as controls. The mass spectrometry data, the database search and the peak lists have been deposited to the ProteomeXchange Consortium database via the PRIDE partner repository with the dataset identifiers PRIDE: PXD002256 to PRIDE: PXD002263 and doi: 10.6019/PXD002256 to 10.6019/PXD002263.
DOI: 10.1016/j.dib.2016.02.018
PubMed: 26958642
Links to Exploration step
pubmed:26958642Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar α-synuclein assemblies by mass spectrometry.</title><author><name sortKey="Shrivastava, Amulya Nidhi" sort="Shrivastava, Amulya Nidhi" uniqKey="Shrivastava A" first="Amulya Nidhi" last="Shrivastava">Amulya Nidhi Shrivastava</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author><author><name sortKey="Redeker, Virginie" sort="Redeker, Virginie" uniqKey="Redeker V" first="Virginie" last="Redeker">Virginie Redeker</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</nlm:affiliation></affiliation></author><author><name sortKey="Fritz, Nicolas" sort="Fritz, Nicolas" uniqKey="Fritz N" first="Nicolas" last="Fritz">Nicolas Fritz</name><affiliation><nlm:affiliation>Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Pieri, Laura" sort="Pieri, Laura" uniqKey="Pieri L" first="Laura" last="Pieri">Laura Pieri</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</nlm:affiliation></affiliation></author><author><name sortKey="Almeida, Leandro G" sort="Almeida, Leandro G" uniqKey="Almeida L" first="Leandro G" last="Almeida">Leandro G. Almeida</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author><author><name sortKey="Spolidoro, Maria" sort="Spolidoro, Maria" uniqKey="Spolidoro M" first="Maria" last="Spolidoro">Maria Spolidoro</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author><author><name sortKey="Liebmann, Thomas" sort="Liebmann, Thomas" uniqKey="Liebmann T" first="Thomas" last="Liebmann">Thomas Liebmann</name><affiliation><nlm:affiliation>Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</nlm:affiliation></affiliation></author><author><name sortKey="Renner, Marianne" sort="Renner, Marianne" uniqKey="Renner M" first="Marianne" last="Renner">Marianne Renner</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author><author><name sortKey="Lena, Clement" sort="Lena, Clement" uniqKey="Lena C" first="Clément" last="Léna">Clément Léna</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author><author><name sortKey="Aperia, Anita" sort="Aperia, Anita" uniqKey="Aperia A" first="Anita" last="Aperia">Anita Aperia</name><affiliation><nlm:affiliation>Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</nlm:affiliation></affiliation></author><author><name sortKey="Triller, Antoine" sort="Triller, Antoine" uniqKey="Triller A" first="Antoine" last="Triller">Antoine Triller</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:26958642</idno><idno type="pmid">26958642</idno><idno type="doi">10.1016/j.dib.2016.02.018</idno><idno type="wicri:Area/PubMed/Corpus">000189</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000189</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar α-synuclein assemblies by mass spectrometry.</title><author><name sortKey="Shrivastava, Amulya Nidhi" sort="Shrivastava, Amulya Nidhi" uniqKey="Shrivastava A" first="Amulya Nidhi" last="Shrivastava">Amulya Nidhi Shrivastava</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author><author><name sortKey="Redeker, Virginie" sort="Redeker, Virginie" uniqKey="Redeker V" first="Virginie" last="Redeker">Virginie Redeker</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</nlm:affiliation></affiliation></author><author><name sortKey="Fritz, Nicolas" sort="Fritz, Nicolas" uniqKey="Fritz N" first="Nicolas" last="Fritz">Nicolas Fritz</name><affiliation><nlm:affiliation>Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Pieri, Laura" sort="Pieri, Laura" uniqKey="Pieri L" first="Laura" last="Pieri">Laura Pieri</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</nlm:affiliation></affiliation></author><author><name sortKey="Almeida, Leandro G" sort="Almeida, Leandro G" uniqKey="Almeida L" first="Leandro G" last="Almeida">Leandro G. Almeida</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author><author><name sortKey="Spolidoro, Maria" sort="Spolidoro, Maria" uniqKey="Spolidoro M" first="Maria" last="Spolidoro">Maria Spolidoro</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author><author><name sortKey="Liebmann, Thomas" sort="Liebmann, Thomas" uniqKey="Liebmann T" first="Thomas" last="Liebmann">Thomas Liebmann</name><affiliation><nlm:affiliation>Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</nlm:affiliation></affiliation></author><author><name sortKey="Renner, Marianne" sort="Renner, Marianne" uniqKey="Renner M" first="Marianne" last="Renner">Marianne Renner</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author><author><name sortKey="Lena, Clement" sort="Lena, Clement" uniqKey="Lena C" first="Clément" last="Léna">Clément Léna</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author><author><name sortKey="Aperia, Anita" sort="Aperia, Anita" uniqKey="Aperia A" first="Anita" last="Aperia">Anita Aperia</name><affiliation><nlm:affiliation>Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</nlm:affiliation></affiliation></author><author><name sortKey="Triller, Antoine" sort="Triller, Antoine" uniqKey="Triller A" first="Antoine" last="Triller">Antoine Triller</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Data in brief</title><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">α-Synuclein (α-syn) is the principal component of Lewy bodies, the pathophysiological hallmark of individuals affected by Parkinson disease (PD). This neuropathologic form of α-syn contributes to PD progression and propagation of α-syn assemblies between neurons. The data we present here support the proteomic analysis used to identify neuronal proteins that specifically interact with extracellularly applied oligomeric or fibrillar α-syn assemblies (conditions 1 and 2, respectively) (doi: 10.15252/embj.201591397[1]). α-syn assemblies and their cellular partner proteins were pulled down from neuronal cell lysed shortly after exposure to exogenous α-syn assemblies and the associated proteins were identified by mass spectrometry using a shotgun proteomic-based approach. We also performed experiments on pure cultures of astrocytes to identify astrocyte-specific proteins interacting with oligomeric or fibrillar α-syn (conditions 3 and 4, respectively). For each condition, proteins interacting selectively with α-syn assemblies were identified by comparison to proteins pulled-down from untreated cells used as controls. The mass spectrometry data, the database search and the peak lists have been deposited to the ProteomeXchange Consortium database via the PRIDE partner repository with the dataset identifiers PRIDE: PXD002256 to PRIDE: PXD002263 and doi: 10.6019/PXD002256 to 10.6019/PXD002263.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">26958642</PMID><DateCreated><Year>2016</Year><Month>03</Month><Day>09</Day></DateCreated><DateCompleted><Year>2016</Year><Month>03</Month><Day>09</Day></DateCompleted><DateRevised><Year>2016</Year><Month>03</Month><Day>11</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><JournalIssue CitedMedium="Print"><Volume>7</Volume><PubDate><Year>2016</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Data in brief</Title><ISOAbbreviation>Data Brief</ISOAbbreviation></Journal><ArticleTitle>Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar α-synuclein assemblies by mass spectrometry.</ArticleTitle><Pagination><MedlinePgn>221-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.dib.2016.02.018</ELocationID><Abstract><AbstractText>α-Synuclein (α-syn) is the principal component of Lewy bodies, the pathophysiological hallmark of individuals affected by Parkinson disease (PD). This neuropathologic form of α-syn contributes to PD progression and propagation of α-syn assemblies between neurons. The data we present here support the proteomic analysis used to identify neuronal proteins that specifically interact with extracellularly applied oligomeric or fibrillar α-syn assemblies (conditions 1 and 2, respectively) (doi: 10.15252/embj.201591397[1]). α-syn assemblies and their cellular partner proteins were pulled down from neuronal cell lysed shortly after exposure to exogenous α-syn assemblies and the associated proteins were identified by mass spectrometry using a shotgun proteomic-based approach. We also performed experiments on pure cultures of astrocytes to identify astrocyte-specific proteins interacting with oligomeric or fibrillar α-syn (conditions 3 and 4, respectively). For each condition, proteins interacting selectively with α-syn assemblies were identified by comparison to proteins pulled-down from untreated cells used as controls. The mass spectrometry data, the database search and the peak lists have been deposited to the ProteomeXchange Consortium database via the PRIDE partner repository with the dataset identifiers PRIDE: PXD002256 to PRIDE: PXD002263 and doi: 10.6019/PXD002256 to 10.6019/PXD002263.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shrivastava</LastName><ForeName>Amulya Nidhi</ForeName><Initials>AN</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Redeker</LastName><ForeName>Virginie</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fritz</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pieri</LastName><ForeName>Laura</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Almeida</LastName><ForeName>Leandro G</ForeName><Initials>LG</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Spolidoro</LastName><ForeName>Maria</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liebmann</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bousset</LastName><ForeName>Luc</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Renner</LastName><ForeName>Marianne</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Léna</LastName><ForeName>Clément</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aperia</LastName><ForeName>Anita</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Women and Children׳s Health, Karolinska Institutet, 171 76 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Melki</LastName><ForeName>Ronald</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Gif-sur-Yvette 91198, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Triller</LastName><ForeName>Antoine</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS), INSERM, CNRS, PSL Research University, 46 Rue d׳Ulm, Paris 75005, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>02</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Data Brief</MedlineTA><NlmUniqueID>101654995</NlmUniqueID><ISSNLinking>2352-3409</ISSNLinking></MedlineJournalInfo><OtherID Source="NLM">PMC4773484</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Alpha-synuclein assemblies</Keyword><Keyword MajorTopicYN="N">Parkinson׳s disease</Keyword><Keyword MajorTopicYN="N">Proteomic Analysis</Keyword><Keyword MajorTopicYN="N">Pull down</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>10</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>12</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>02</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>3</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>3</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>3</Month><Day>10</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26958642</ArticleId><ArticleId IdType="doi">10.1016/j.dib.2016.02.018</ArticleId><ArticleId IdType="pii">S2352-3409(16)30040-3</ArticleId><ArticleId IdType="pmc">PMC4773484</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonFranceV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000189 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 000189 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Sante
|area= ParkinsonFranceV1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:26958642
|texte= Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar α-synuclein assemblies by mass spectrometry.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:26958642" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a ParkinsonFranceV1
| This area was generated with Dilib version V0.6.29. |  |