[Infectious properties of protein aggregates involved in neurodegenerative diseases].
Identifieur interne : 000785 ( PubMed/Corpus ); précédent : 000784; suivant : 000786[Infectious properties of protein aggregates involved in neurodegenerative diseases].
Auteurs : Luc Bousset ; Ronald MelkiSource :
- Biologie aujourd'hui [ 2105-0686 ] ; 2013.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Proteins.
- metabolism : Neurodegenerative Diseases.
- Cell Communication, Humans, Protein Folding, Protein Multimerization.
Abstract
Several progressive neurodegenerative disorders, e.g. Alzheimer, Parkinson and Huntington diseases, cerebro-spinal ataxia and amyotrophic lateral sclerosis, are the consequence of protein misfolding and aggregation. Recent data indicates that some of these diseases are not cell autonomous as previously thought. We and others have shown that protein assemblies involved in the aforementioned diseases propagate from cell to cell in a manner akin prion high molecular weight assemblies propagation in Creutzfeldt-Jacob disease. The mechanism of propagation and amplification of protein assemblies involved in neurodegenerative diseases and its physiopathological consequences are discussed hereafter.
DOI: 10.1051/jbio/2013004
PubMed: 23694725
Links to Exploration step
pubmed:23694725Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">[Infectious properties of protein aggregates involved in neurodegenerative diseases].</title><author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name><affiliation><nlm:affiliation>Laboratoire d'Enzymologie et Biochimie Structurale, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.</nlm:affiliation></affiliation></author><author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23694725</idno><idno type="pmid">23694725</idno><idno type="doi">10.1051/jbio/2013004</idno><idno type="wicri:Area/PubMed/Corpus">000785</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000785</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">[Infectious properties of protein aggregates involved in neurodegenerative diseases].</title><author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name><affiliation><nlm:affiliation>Laboratoire d'Enzymologie et Biochimie Structurale, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.</nlm:affiliation></affiliation></author><author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name></author></analytic><series><title level="j">Biologie aujourd'hui</title><idno type="eISSN">2105-0686</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Communication</term><term>Humans</term><term>Neurodegenerative Diseases (metabolism)</term><term>Protein Folding</term><term>Protein Multimerization</term><term>Proteins (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Neurodegenerative Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Communication</term><term>Humans</term><term>Protein Folding</term><term>Protein Multimerization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Several progressive neurodegenerative disorders, e.g. Alzheimer, Parkinson and Huntington diseases, cerebro-spinal ataxia and amyotrophic lateral sclerosis, are the consequence of protein misfolding and aggregation. Recent data indicates that some of these diseases are not cell autonomous as previously thought. We and others have shown that protein assemblies involved in the aforementioned diseases propagate from cell to cell in a manner akin prion high molecular weight assemblies propagation in Creutzfeldt-Jacob disease. The mechanism of propagation and amplification of protein assemblies involved in neurodegenerative diseases and its physiopathological consequences are discussed hereafter.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23694725</PMID><DateCreated><Year>2013</Year><Month>05</Month><Day>22</Day></DateCreated><DateCompleted><Year>2014</Year><Month>01</Month><Day>06</Day></DateCompleted><DateRevised><Year>2013</Year><Month>05</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2105-0686</ISSN><JournalIssue CitedMedium="Internet"><Volume>207</Volume><Issue>1</Issue><PubDate><Year>2013</Year></PubDate></JournalIssue><Title>Biologie aujourd'hui</Title><ISOAbbreviation>Biol Aujourdhui</ISOAbbreviation></Journal><ArticleTitle>[Infectious properties of protein aggregates involved in neurodegenerative diseases].</ArticleTitle><Pagination><MedlinePgn>55-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1051/jbio/2013004</ELocationID><Abstract><AbstractText>Several progressive neurodegenerative disorders, e.g. Alzheimer, Parkinson and Huntington diseases, cerebro-spinal ataxia and amyotrophic lateral sclerosis, are the consequence of protein misfolding and aggregation. Recent data indicates that some of these diseases are not cell autonomous as previously thought. We and others have shown that protein assemblies involved in the aforementioned diseases propagate from cell to cell in a manner akin prion high molecular weight assemblies propagation in Creutzfeldt-Jacob disease. The mechanism of propagation and amplification of protein assemblies involved in neurodegenerative diseases and its physiopathological consequences are discussed hereafter.</AbstractText><CopyrightInformation>© Société de Biologie, 2013.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bousset</LastName><ForeName>Luc</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Laboratoire d'Enzymologie et Biochimie Structurale, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Melki</LastName><ForeName>Ronald</ForeName><Initials>R</Initials></Author></AuthorList><Language>fre</Language><PublicationTypeList><PublicationType UI="D004740">English Abstract</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><VernacularTitle>Propriétés infectieuses des agrégats de protéines impliquées dans des maladies neurodégénératives.</VernacularTitle><ArticleDate DateType="Electronic"><Year>2013</Year><Month>05</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>France</Country><MedlineTA>Biol Aujourdhui</MedlineTA><NlmUniqueID>101544020</NlmUniqueID><ISSNLinking>2105-0678</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002450" MajorTopicYN="N">Cell Communication</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019636" MajorTopicYN="N">Neurodegenerative Diseases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="Y">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="Y">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>01</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>5</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>5</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>1</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23694725</ArticleId><ArticleId IdType="doi">10.1051/jbio/2013004</ArticleId><ArticleId IdType="pii">jbio2013004</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 000785 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 000785 | 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:23694725
|texte= [Infectious properties of protein aggregates involved in neurodegenerative diseases].
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:23694725" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a ParkinsonFranceV1
| This area was generated with Dilib version V0.6.29. |  |