Prions and Prion-like Proteins
Identifieur interne : 000962 ( Main/Exploration ); précédent : 000961; suivant : 000963Prions and Prion-like Proteins
Auteurs : Paul E. Fraser [Canada]Source :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2014.
English descriptors
- KwdEn :
- Alzheimer Disease (etiology), Animals, Humans, Multiprotein Complexes (chemistry), Multiprotein Complexes (metabolism), Parkinson Disease (etiology), Prion Diseases (etiology), Prion Diseases (metabolism), Prion Diseases (transmission), Prions (chemistry), Prions (metabolism), Protein Conformation, Protein Multimerization, tau Proteins (chemistry), tau Proteins (metabolism).
- MESH :
- chemical , chemistry : Multiprotein Complexes, Prions, tau Proteins.
- etiology : Alzheimer Disease, Parkinson Disease, Prion Diseases.
- chemical , metabolism : Multiprotein Complexes, Prion Diseases, Prions, tau Proteins.
- transmission : Prion Diseases.
- Animals, Humans, Protein Conformation, Protein Multimerization.
Abstract
Prions are self-replicating protein aggregates and are the primary causative factor in a number of neurological diseases in mammals. The prion protein (PrP) undergoes a conformational transformation leading to aggregation into an infectious cellular pathogen. Prion-like protein spreading and transmission of aggregates between cells have also been demonstrated for other proteins associated with Alzheimer disease and Parkinson disease. This protein-only phenomenon may therefore have broader implications in neurodegenerative disorders. The minireviews in this thematic series highlight the recent advances in prion biology and the roles these unique proteins play in disease.
Url:
DOI: 10.1074/jbc.R114.583492
PubMed: 24860092
PubMed Central: 4106303
Affiliations:
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Le document en format XML
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Fraser</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Tanz Centre for Research in Neurodegenerative Diseases and the Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5T 2S8, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>From the Tanz Centre for Research in Neurodegenerative Diseases and the Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5T 2S8</wicri:regionArea><orgName type="university">Université de Toronto</orgName><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">24860092</idno><idno type="pmc">4106303</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4106303</idno><idno type="RBID">PMC:4106303</idno><idno type="doi">10.1074/jbc.R114.583492</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000B84</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000B84</idno><idno type="wicri:Area/Pmc/Curation">000B84</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000B84</idno><idno type="wicri:Area/Pmc/Checkpoint">000421</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000421</idno><idno type="wicri:source">PubMed</idno><idno type="wicri:Area/PubMed/Corpus">000714</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000714</idno><idno type="wicri:Area/PubMed/Curation">000714</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000714</idno><idno type="wicri:Area/PubMed/Checkpoint">000714</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000714</idno><idno type="wicri:Area/Ncbi/Merge">001771</idno><idno type="wicri:Area/Ncbi/Curation">001771</idno><idno type="wicri:Area/Ncbi/Checkpoint">001771</idno><idno type="wicri:doubleKey">0021-9258:2014:Fraser P:prions:and:prion</idno><idno type="wicri:Area/Main/Merge">000964</idno><idno type="wicri:Area/Main/Curation">000962</idno><idno type="wicri:Area/Main/Exploration">000962</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Prions and Prion-like Proteins</title><author><name sortKey="Fraser, Paul E" sort="Fraser, Paul E" uniqKey="Fraser P" first="Paul E." last="Fraser">Paul E. Fraser</name><affiliation wicri:level="4"><nlm:aff id="aff1">From the Tanz Centre for Research in Neurodegenerative Diseases and the Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5T 2S8, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>From the Tanz Centre for Research in Neurodegenerative Diseases and the Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5T 2S8</wicri:regionArea><orgName type="university">Université de Toronto</orgName><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alzheimer Disease (etiology)</term><term>Animals</term><term>Humans</term><term>Multiprotein Complexes (chemistry)</term><term>Multiprotein Complexes (metabolism)</term><term>Parkinson Disease (etiology)</term><term>Prion Diseases (etiology)</term><term>Prion Diseases (metabolism)</term><term>Prion Diseases (transmission)</term><term>Prions (chemistry)</term><term>Prions (metabolism)</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>tau Proteins (chemistry)</term><term>tau Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Multiprotein Complexes</term><term>Prions</term><term>tau Proteins</term></keywords><keywords scheme="MESH" qualifier="etiology" xml:lang="en"><term>Alzheimer Disease</term><term>Parkinson Disease</term><term>Prion Diseases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Multiprotein Complexes</term><term>Prion Diseases</term><term>Prions</term><term>tau Proteins</term></keywords><keywords scheme="MESH" qualifier="transmission" xml:lang="en"><term>Prion Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Protein Conformation</term><term>Protein Multimerization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Prions are self-replicating protein aggregates and are the primary causative factor in a number of neurological diseases in mammals. The prion protein (PrP) undergoes a conformational transformation leading to aggregation into an infectious cellular pathogen. Prion-like protein spreading and transmission of aggregates between cells have also been demonstrated for other proteins associated with Alzheimer disease and Parkinson disease. This protein-only phenomenon may therefore have broader implications in neurodegenerative disorders. The minireviews in this thematic series highlight the recent advances in prion biology and the roles these unique proteins play in disease.</p></div></front></TEI><affiliations><list><country><li>Canada</li></country><region><li>Ontario</li></region><settlement><li>Toronto</li></settlement><orgName><li>Université de Toronto</li></orgName></list><tree><country name="Canada"><region name="Ontario"><name sortKey="Fraser, Paul E" sort="Fraser, Paul E" uniqKey="Fraser P" first="Paul E." last="Fraser">Paul E. 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