Neurodegenerative disease Amyloid pores from pathogenic mutations
Alzheimer's and Parkinson's diseases are associated with the formation in the brain of amyloid fibrils from β-amyloid and α-synuclein proteins, respectively. It is likely that oligomeric fibrillization intermediates (protofibrils), rather than the fibrils themselves, are pathogenic, but th...
Gespeichert in:
| Veröffentlicht in: | Nature (London) 2002-07, Vol.418 (6895), p.291-291 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 291 |
|---|---|
| container_issue | 6895 |
| container_start_page | 291 |
| container_title | Nature (London) |
| container_volume | 418 |
| creator | Lansbury, Peter T Lashuel, Hilal A Hartley, Dean Petre, Benjamin M Walz, Thomas |
| description | Alzheimer's and Parkinson's diseases are associated with the formation in the brain of amyloid fibrils from β-amyloid and α-synuclein proteins, respectively. It is likely that oligomeric fibrillization intermediates (protofibrils), rather than the fibrils themselves, are pathogenic, but the mechanism by which they cause neuronal death remains a mystery. We show here that mutant amyloid proteins associated with familial Alzheimer's and Parkinson's diseases form morphologically indistinguishable annular protofibrils that resemble a class of pore-forming bacterial toxins, suggesting that inappropriate membrane permeabilization might be the cause of cell dysfunction and even cell death in amyloid diseases. |
| doi_str_mv | 10.1038/418291a |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_743337830</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A187545917</galeid><sourcerecordid>A187545917</sourcerecordid><originalsourceid>FETCH-LOGICAL-g462t-729ec50317389c506838d60c654eb9813c77a42651154476c9e7efc7b6cb26443</originalsourceid><addsrcrecordid>eNp10u9L3DAYB_AgG3o68S9wFN_IGHX51SR9WY45BbnB5tjLkkufnpG2qUkqu__ewN3EEyUvEsInX548CUInBF8QzNQ3ThQtid5DM8KlyLlQ8gOaYUxVjhUTB-gwhHuMcUEk30cHhBLKBWEzVC1g8q6BFQzgdbSPkDU2gA6QVf26c7bJRuchZK13fTbqeOcStSbrp5i4G8In9LHVXYDj7XyE_lx-v51f5Tc_f1zPq5t8xQWNuaQlmAIzIpkq00IophqBjSg4LEtFmJFScyoKQgqe7mBKkNAauRRmSQXn7Aidb3JH7x4mCLHubTDQdXoAN4VacsaYVAwnefZK3rvJD6m4mmJeYCwESyjfoJXuoLZD66LXZtOGzg3Q2rRdESULXpSp6OfQHW9G-1C_RBdvoDQa6K15M_XLzoFkIvyLKz2FUF___rVrv75vq9u_88Wu_rxtwrTsoalHb3vt1_X_p0_gdAMGHScPz2D7ldgTG7KyrA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>204500663</pqid></control><display><type>article</type><title>Neurodegenerative disease Amyloid pores from pathogenic mutations</title><source>MEDLINE</source><source>Nature</source><source>Alma/SFX Local Collection</source><creator>Lansbury, Peter T ; Lashuel, Hilal A ; Hartley, Dean ; Petre, Benjamin M ; Walz, Thomas</creator><creatorcontrib>Lansbury, Peter T ; Lashuel, Hilal A ; Hartley, Dean ; Petre, Benjamin M ; Walz, Thomas</creatorcontrib><description>Alzheimer's and Parkinson's diseases are associated with the formation in the brain of amyloid fibrils from β-amyloid and α-synuclein proteins, respectively. It is likely that oligomeric fibrillization intermediates (protofibrils), rather than the fibrils themselves, are pathogenic, but the mechanism by which they cause neuronal death remains a mystery. We show here that mutant amyloid proteins associated with familial Alzheimer's and Parkinson's diseases form morphologically indistinguishable annular protofibrils that resemble a class of pore-forming bacterial toxins, suggesting that inappropriate membrane permeabilization might be the cause of cell dysfunction and even cell death in amyloid diseases.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/418291a</identifier><identifier>PMID: 12124613</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>England: Nature Publishing Group</publisher><subject>alpha-Synuclein ; Alzheimer Disease - genetics ; Alzheimer Disease - metabolism ; Alzheimer Disease - pathology ; Alzheimer's disease ; Amyloid beta-Peptides - chemistry ; Amyloid beta-Peptides - genetics ; Amyloid beta-Peptides - metabolism ; Amyloid beta-Peptides - toxicity ; Cell Membrane Permeability - drug effects ; Chromatography, Gel ; Circular Dichroism ; Diabetes ; Disease ; Humans ; Models, Biological ; Molecular Weight ; Mortality ; Mutation ; Mutation - genetics ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Nerve Tissue Proteins - toxicity ; Parkinson Disease - genetics ; Parkinson Disease - metabolism ; Parkinson Disease - pathology ; Parkinson's disease ; Plaque, Amyloid - genetics ; Plaque, Amyloid - metabolism ; Plaque, Amyloid - pathology ; Porins - chemistry ; Porins - genetics ; Porins - metabolism ; Porins - toxicity ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Proteins ; Synucleins ; Toxicity ; Toxins</subject><ispartof>Nature (London), 2002-07, Vol.418 (6895), p.291-291</ispartof><rights>COPYRIGHT 2002 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jul 18, 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12124613$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lansbury, Peter T</creatorcontrib><creatorcontrib>Lashuel, Hilal A</creatorcontrib><creatorcontrib>Hartley, Dean</creatorcontrib><creatorcontrib>Petre, Benjamin M</creatorcontrib><creatorcontrib>Walz, Thomas</creatorcontrib><title>Neurodegenerative disease Amyloid pores from pathogenic mutations</title><title>Nature (London)</title><addtitle>Nature</addtitle><description>Alzheimer's and Parkinson's diseases are associated with the formation in the brain of amyloid fibrils from β-amyloid and α-synuclein proteins, respectively. It is likely that oligomeric fibrillization intermediates (protofibrils), rather than the fibrils themselves, are pathogenic, but the mechanism by which they cause neuronal death remains a mystery. We show here that mutant amyloid proteins associated with familial Alzheimer's and Parkinson's diseases form morphologically indistinguishable annular protofibrils that resemble a class of pore-forming bacterial toxins, suggesting that inappropriate membrane permeabilization might be the cause of cell dysfunction and even cell death in amyloid diseases.</description><subject>alpha-Synuclein</subject><subject>Alzheimer Disease - genetics</subject><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer Disease - pathology</subject><subject>Alzheimer's disease</subject><subject>Amyloid beta-Peptides - chemistry</subject><subject>Amyloid beta-Peptides - genetics</subject><subject>Amyloid beta-Peptides - metabolism</subject><subject>Amyloid beta-Peptides - toxicity</subject><subject>Cell Membrane Permeability - drug effects</subject><subject>Chromatography, Gel</subject><subject>Circular Dichroism</subject><subject>Diabetes</subject><subject>Disease</subject><subject>Humans</subject><subject>Models, Biological</subject><subject>Molecular Weight</subject><subject>Mortality</subject><subject>Mutation</subject><subject>Mutation - genetics</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Nerve Tissue Proteins - toxicity</subject><subject>Parkinson Disease - genetics</subject><subject>Parkinson Disease - metabolism</subject><subject>Parkinson Disease - pathology</subject><subject>Parkinson's disease</subject><subject>Plaque, Amyloid - genetics</subject><subject>Plaque, Amyloid - metabolism</subject><subject>Plaque, Amyloid - pathology</subject><subject>Porins - chemistry</subject><subject>Porins - genetics</subject><subject>Porins - metabolism</subject><subject>Porins - toxicity</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Synucleins</subject><subject>Toxicity</subject><subject>Toxins</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp10u9L3DAYB_AgG3o68S9wFN_IGHX51SR9WY45BbnB5tjLkkufnpG2qUkqu__ewN3EEyUvEsInX548CUInBF8QzNQ3ThQtid5DM8KlyLlQ8gOaYUxVjhUTB-gwhHuMcUEk30cHhBLKBWEzVC1g8q6BFQzgdbSPkDU2gA6QVf26c7bJRuchZK13fTbqeOcStSbrp5i4G8In9LHVXYDj7XyE_lx-v51f5Tc_f1zPq5t8xQWNuaQlmAIzIpkq00IophqBjSg4LEtFmJFScyoKQgqe7mBKkNAauRRmSQXn7Aidb3JH7x4mCLHubTDQdXoAN4VacsaYVAwnefZK3rvJD6m4mmJeYCwESyjfoJXuoLZD66LXZtOGzg3Q2rRdESULXpSp6OfQHW9G-1C_RBdvoDQa6K15M_XLzoFkIvyLKz2FUF___rVrv75vq9u_88Wu_rxtwrTsoalHb3vt1_X_p0_gdAMGHScPz2D7ldgTG7KyrA</recordid><startdate>20020718</startdate><enddate>20020718</enddate><creator>Lansbury, Peter T</creator><creator>Lashuel, Hilal A</creator><creator>Hartley, Dean</creator><creator>Petre, Benjamin M</creator><creator>Walz, Thomas</creator><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>ATWCN</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7SC</scope><scope>7SP</scope><scope>7SR</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>F28</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope></search><sort><creationdate>20020718</creationdate><title>Neurodegenerative disease Amyloid pores from pathogenic mutations</title><author>Lansbury, Peter T ; Lashuel, Hilal A ; Hartley, Dean ; Petre, Benjamin M ; Walz, Thomas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-g462t-729ec50317389c506838d60c654eb9813c77a42651154476c9e7efc7b6cb26443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>alpha-Synuclein</topic><topic>Alzheimer Disease - genetics</topic><topic>Alzheimer Disease - metabolism</topic><topic>Alzheimer Disease - pathology</topic><topic>Alzheimer's disease</topic><topic>Amyloid beta-Peptides - chemistry</topic><topic>Amyloid beta-Peptides - genetics</topic><topic>Amyloid beta-Peptides - metabolism</topic><topic>Amyloid beta-Peptides - toxicity</topic><topic>Cell Membrane Permeability - drug effects</topic><topic>Chromatography, Gel</topic><topic>Circular Dichroism</topic><topic>Diabetes</topic><topic>Disease</topic><topic>Humans</topic><topic>Models, Biological</topic><topic>Molecular Weight</topic><topic>Mortality</topic><topic>Mutation</topic><topic>Mutation - genetics</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Nerve Tissue Proteins - toxicity</topic><topic>Parkinson Disease - genetics</topic><topic>Parkinson Disease - metabolism</topic><topic>Parkinson Disease - pathology</topic><topic>Parkinson's disease</topic><topic>Plaque, Amyloid - genetics</topic><topic>Plaque, Amyloid - metabolism</topic><topic>Plaque, Amyloid - pathology</topic><topic>Porins - chemistry</topic><topic>Porins - genetics</topic><topic>Porins - metabolism</topic><topic>Porins - toxicity</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Synucleins</topic><topic>Toxicity</topic><topic>Toxins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lansbury, Peter T</creatorcontrib><creatorcontrib>Lashuel, Hilal A</creatorcontrib><creatorcontrib>Hartley, Dean</creatorcontrib><creatorcontrib>Petre, Benjamin M</creatorcontrib><creatorcontrib>Walz, Thomas</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Gale In Context: Middle School</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Psychology Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Research Library (Corporate)</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest One Psychology</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>University of Michigan</collection><collection>Genetics Abstracts</collection><collection>SIRS Editorial</collection><collection>Environment Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lansbury, Peter T</au><au>Lashuel, Hilal A</au><au>Hartley, Dean</au><au>Petre, Benjamin M</au><au>Walz, Thomas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Neurodegenerative disease Amyloid pores from pathogenic mutations</atitle><jtitle>Nature (London)</jtitle><addtitle>Nature</addtitle><date>2002-07-18</date><risdate>2002</risdate><volume>418</volume><issue>6895</issue><spage>291</spage><epage>291</epage><pages>291-291</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>Alzheimer's and Parkinson's diseases are associated with the formation in the brain of amyloid fibrils from β-amyloid and α-synuclein proteins, respectively. It is likely that oligomeric fibrillization intermediates (protofibrils), rather than the fibrils themselves, are pathogenic, but the mechanism by which they cause neuronal death remains a mystery. We show here that mutant amyloid proteins associated with familial Alzheimer's and Parkinson's diseases form morphologically indistinguishable annular protofibrils that resemble a class of pore-forming bacterial toxins, suggesting that inappropriate membrane permeabilization might be the cause of cell dysfunction and even cell death in amyloid diseases.</abstract><cop>England</cop><pub>Nature Publishing Group</pub><pmid>12124613</pmid><doi>10.1038/418291a</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 2002-07, Vol.418 (6895), p.291-291 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743337830 |
| source | MEDLINE; Nature; Alma/SFX Local Collection |
| subjects | alpha-Synuclein Alzheimer Disease - genetics Alzheimer Disease - metabolism Alzheimer Disease - pathology Alzheimer's disease Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - genetics Amyloid beta-Peptides - metabolism Amyloid beta-Peptides - toxicity Cell Membrane Permeability - drug effects Chromatography, Gel Circular Dichroism Diabetes Disease Humans Models, Biological Molecular Weight Mortality Mutation Mutation - genetics Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Nerve Tissue Proteins - toxicity Parkinson Disease - genetics Parkinson Disease - metabolism Parkinson Disease - pathology Parkinson's disease Plaque, Amyloid - genetics Plaque, Amyloid - metabolism Plaque, Amyloid - pathology Porins - chemistry Porins - genetics Porins - metabolism Porins - toxicity Protein Structure, Quaternary Protein Structure, Secondary Proteins Synucleins Toxicity Toxins |
| title | Neurodegenerative disease Amyloid pores from pathogenic mutations |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T02%3A35%3A44IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Neurodegenerative%20disease%20Amyloid%20pores%20from%20pathogenic%20mutations&rft.jtitle=Nature%20(London)&rft.au=Lansbury,%20Peter%20T&rft.date=2002-07-18&rft.volume=418&rft.issue=6895&rft.spage=291&rft.epage=291&rft.pages=291-291&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/418291a&rft_dat=%3Cgale_proqu%3EA187545917%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=204500663&rft_id=info:pmid/12124613&rft_galeid=A187545917&rfr_iscdi=true |