Prions and prion-like proteins.
Identifieur interne : 000714 ( PubMed/Curation ); précédent : 000713; suivant : 000715Prions and prion-like proteins.
Auteurs : Paul E. Fraser [Canada]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 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.
DOI: 10.1074/jbc.R114.583492
PubMed: 24860092
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Fraser</name><affiliation wicri:level="1"><nlm:affiliation>From the Tanz Centre for Research in Neurodegenerative Diseases and the Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5T 2S8, Canada pfraser@asbmb.org.</nlm:affiliation><country>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></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:24860092</idno><idno type="pmid">24860092</idno><idno type="doi">10.1074/jbc.R114.583492</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></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">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="1"><nlm:affiliation>From the Tanz Centre for Research in Neurodegenerative Diseases and the Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5T 2S8, Canada pfraser@asbmb.org.</nlm:affiliation><country>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></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2014" type="published">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">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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24860092</PMID><DateCreated><Year>2014</Year><Month>07</Month><Day>29</Day></DateCreated><DateCompleted><Year>2014</Year><Month>10</Month><Day>06</Day></DateCompleted><DateRevised><Year>2015</Year><Month>08</Month><Day>05</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>289</Volume><Issue>29</Issue><PubDate><Year>2014</Year><Month>Jul</Month><Day>18</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Prions and prion-like proteins.</ArticleTitle><Pagination><MedlinePgn>19839-40</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.R114.583492</ELocationID><Abstract><AbstractText>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.</AbstractText><CopyrightInformation>© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fraser</LastName><ForeName>Paul E</ForeName><Initials>PE</Initials><AffiliationInfo><Affiliation>From the Tanz Centre for Research in Neurodegenerative Diseases and the Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5T 2S8, Canada pfraser@asbmb.org.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>05</Month><Day>23</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="C054369">MAPT protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011328">Prions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016875">tau Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Science. 2004 Jul 30;305(5684):673-6</RefSource><PMID Version="1">15286374</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2014 Jul 18;289(29):19862-8</RefSource><PMID 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18;289(29):19855-61</RefSource><PMID Version="1">24860099</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nature. 1967 Sep 2;215(5105):1043-4</RefSource><PMID Version="1">4964084</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000544" MajorTopicYN="N">Alzheimer Disease</DescriptorName><QualifierName UI="Q000209" MajorTopicYN="N">etiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000209" MajorTopicYN="N">etiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017096" MajorTopicYN="N">Prion Diseases</DescriptorName><QualifierName UI="Q000209" MajorTopicYN="Y">etiology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000635" MajorTopicYN="N">transmission</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011328" MajorTopicYN="N">Prions</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016875" MajorTopicYN="N">tau Proteins</DescriptorName><QualifierName UI="Q000737" 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