Loading…
The Amyloid State of Proteins in Human Diseases
Amyloid fibers and oligomers are associated with a great variety of human diseases including Alzheimer's disease and the prion conditions. Here we attempt to connect recent discoveries on the molecular properties of proteins in the amyloid state with observations about pathological tissues and...
Saved in:
| Published in: | Cell 2012-03, Vol.148 (6), p.1188-1203 |
|---|---|
| Main Authors: | , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c511t-881e60e32090a75834b0a61c63c6e9e9fa7bd43beb5da918e6ac343ffd33a1f13 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c511t-881e60e32090a75834b0a61c63c6e9e9fa7bd43beb5da918e6ac343ffd33a1f13 |
| container_end_page | 1203 |
| container_issue | 6 |
| container_start_page | 1188 |
| container_title | Cell |
| container_volume | 148 |
| creator | Eisenberg, David Jucker, Mathias |
| description | Amyloid fibers and oligomers are associated with a great variety of human diseases including Alzheimer's disease and the prion conditions. Here we attempt to connect recent discoveries on the molecular properties of proteins in the amyloid state with observations about pathological tissues and disease states. We summarize studies of structure and nucleation of amyloid and relate these to observations on amyloid polymorphism, prion strains, coaggregation of pathogenic proteins in tissues, and mechanisms of toxicity and transmissibility. Molecular studies have also led to numerous strategies for biological and chemical interventions against amyloid diseases. |
| doi_str_mv | 10.1016/j.cell.2012.02.022 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3353745</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S009286741200222X</els_id><sourcerecordid>929123445</sourcerecordid><originalsourceid>FETCH-LOGICAL-c511t-881e60e32090a75834b0a61c63c6e9e9fa7bd43beb5da918e6ac343ffd33a1f13</originalsourceid><addsrcrecordid>eNp9kV9L5TAQxcOyy3pX9wv4oH1zX3qdZJq2gUUQ94-CoKA-hzSdai5to0mv4Lc33euKvkgG8jC_c5iZw9guhyUHXh6ulpb6fimAiyXMJT6xBQdV5QWvxGe2AFAir8uq2GLfYlwBQC2l_Mq2hCjSE2rBDq_vKDsennrv2uxqMhNlvssug5_IjTFzY3a6HsyY_XKRTKS4w750po_0_eXfZjd_fl-fnObnF3_PTo7Pcys5n_K65lQCoQAFppI1Fg2YktsSbUmKVGeqpi2woUa2RvGaSmOxwK5rEQ3vOG6zo43v_boZqLU0TsH0-j64wYQn7Y3T7zuju9O3_lEjSqwKmQwOXgyCf1hTnPTg4nwvM5JfR62E4gKLf-SPD0mOAmsQlVQJFRvUBh9joO51IA56zkSv9KzUcyYa5hJJtPd2lVfJ_xASsL8BOuO1uQ0u6pur5FCmwEBhhYn4uSEonfzRUdDROhottS6QnXTr3UcTPAO086V-</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1323802759</pqid></control><display><type>article</type><title>The Amyloid State of Proteins in Human Diseases</title><source>ScienceDirect - Connect here FIRST to enable access</source><creator>Eisenberg, David ; Jucker, Mathias</creator><creatorcontrib>Eisenberg, David ; Jucker, Mathias</creatorcontrib><description>Amyloid fibers and oligomers are associated with a great variety of human diseases including Alzheimer's disease and the prion conditions. Here we attempt to connect recent discoveries on the molecular properties of proteins in the amyloid state with observations about pathological tissues and disease states. We summarize studies of structure and nucleation of amyloid and relate these to observations on amyloid polymorphism, prion strains, coaggregation of pathogenic proteins in tissues, and mechanisms of toxicity and transmissibility. Molecular studies have also led to numerous strategies for biological and chemical interventions against amyloid diseases.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/j.cell.2012.02.022</identifier><identifier>PMID: 22424229</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Alzheimer disease ; Alzheimer's disease ; Amyloid ; Amyloid beta-Protein Precursor - chemistry ; Amyloid beta-Protein Precursor - metabolism ; Animals ; Disease Models, Animal ; diseases ; Fibers ; Gene polymorphism ; human diseases ; Humans ; Models, Molecular ; Neurodegenerative diseases ; Neurodegenerative Diseases - metabolism ; Nucleation ; Plaque, Amyloid - chemistry ; Prion protein ; prions ; Protein Structure, Secondary ; Reviews ; tissues ; Toxicity</subject><ispartof>Cell, 2012-03, Vol.148 (6), p.1188-1203</ispartof><rights>2012 Elsevier Inc.</rights><rights>Copyright © 2012 Elsevier Inc. All rights reserved.</rights><rights>2012 Elsevier Inc. All rights reserved. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c511t-881e60e32090a75834b0a61c63c6e9e9fa7bd43beb5da918e6ac343ffd33a1f13</citedby><cites>FETCH-LOGICAL-c511t-881e60e32090a75834b0a61c63c6e9e9fa7bd43beb5da918e6ac343ffd33a1f13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S009286741200222X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22424229$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Eisenberg, David</creatorcontrib><creatorcontrib>Jucker, Mathias</creatorcontrib><title>The Amyloid State of Proteins in Human Diseases</title><title>Cell</title><addtitle>Cell</addtitle><description>Amyloid fibers and oligomers are associated with a great variety of human diseases including Alzheimer's disease and the prion conditions. Here we attempt to connect recent discoveries on the molecular properties of proteins in the amyloid state with observations about pathological tissues and disease states. We summarize studies of structure and nucleation of amyloid and relate these to observations on amyloid polymorphism, prion strains, coaggregation of pathogenic proteins in tissues, and mechanisms of toxicity and transmissibility. Molecular studies have also led to numerous strategies for biological and chemical interventions against amyloid diseases.</description><subject>Alzheimer disease</subject><subject>Alzheimer's disease</subject><subject>Amyloid</subject><subject>Amyloid beta-Protein Precursor - chemistry</subject><subject>Amyloid beta-Protein Precursor - metabolism</subject><subject>Animals</subject><subject>Disease Models, Animal</subject><subject>diseases</subject><subject>Fibers</subject><subject>Gene polymorphism</subject><subject>human diseases</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Neurodegenerative diseases</subject><subject>Neurodegenerative Diseases - metabolism</subject><subject>Nucleation</subject><subject>Plaque, Amyloid - chemistry</subject><subject>Prion protein</subject><subject>prions</subject><subject>Protein Structure, Secondary</subject><subject>Reviews</subject><subject>tissues</subject><subject>Toxicity</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNp9kV9L5TAQxcOyy3pX9wv4oH1zX3qdZJq2gUUQ94-CoKA-hzSdai5to0mv4Lc33euKvkgG8jC_c5iZw9guhyUHXh6ulpb6fimAiyXMJT6xBQdV5QWvxGe2AFAir8uq2GLfYlwBQC2l_Mq2hCjSE2rBDq_vKDsennrv2uxqMhNlvssug5_IjTFzY3a6HsyY_XKRTKS4w750po_0_eXfZjd_fl-fnObnF3_PTo7Pcys5n_K65lQCoQAFppI1Fg2YktsSbUmKVGeqpi2woUa2RvGaSmOxwK5rEQ3vOG6zo43v_boZqLU0TsH0-j64wYQn7Y3T7zuju9O3_lEjSqwKmQwOXgyCf1hTnPTg4nwvM5JfR62E4gKLf-SPD0mOAmsQlVQJFRvUBh9joO51IA56zkSv9KzUcyYa5hJJtPd2lVfJ_xASsL8BOuO1uQ0u6pur5FCmwEBhhYn4uSEonfzRUdDROhottS6QnXTr3UcTPAO086V-</recordid><startdate>20120316</startdate><enddate>20120316</enddate><creator>Eisenberg, David</creator><creator>Jucker, Mathias</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20120316</creationdate><title>The Amyloid State of Proteins in Human Diseases</title><author>Eisenberg, David ; Jucker, Mathias</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c511t-881e60e32090a75834b0a61c63c6e9e9fa7bd43beb5da918e6ac343ffd33a1f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Alzheimer disease</topic><topic>Alzheimer's disease</topic><topic>Amyloid</topic><topic>Amyloid beta-Protein Precursor - chemistry</topic><topic>Amyloid beta-Protein Precursor - metabolism</topic><topic>Animals</topic><topic>Disease Models, Animal</topic><topic>diseases</topic><topic>Fibers</topic><topic>Gene polymorphism</topic><topic>human diseases</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>Neurodegenerative diseases</topic><topic>Neurodegenerative Diseases - metabolism</topic><topic>Nucleation</topic><topic>Plaque, Amyloid - chemistry</topic><topic>Prion protein</topic><topic>prions</topic><topic>Protein Structure, Secondary</topic><topic>Reviews</topic><topic>tissues</topic><topic>Toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Eisenberg, David</creatorcontrib><creatorcontrib>Jucker, Mathias</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Eisenberg, David</au><au>Jucker, Mathias</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Amyloid State of Proteins in Human Diseases</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2012-03-16</date><risdate>2012</risdate><volume>148</volume><issue>6</issue><spage>1188</spage><epage>1203</epage><pages>1188-1203</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Amyloid fibers and oligomers are associated with a great variety of human diseases including Alzheimer's disease and the prion conditions. Here we attempt to connect recent discoveries on the molecular properties of proteins in the amyloid state with observations about pathological tissues and disease states. We summarize studies of structure and nucleation of amyloid and relate these to observations on amyloid polymorphism, prion strains, coaggregation of pathogenic proteins in tissues, and mechanisms of toxicity and transmissibility. Molecular studies have also led to numerous strategies for biological and chemical interventions against amyloid diseases.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22424229</pmid><doi>10.1016/j.cell.2012.02.022</doi><tpages>16</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0092-8674 |
| ispartof | Cell, 2012-03, Vol.148 (6), p.1188-1203 |
| issn | 0092-8674 1097-4172 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3353745 |
| source | ScienceDirect - Connect here FIRST to enable access |
| subjects | Alzheimer disease Alzheimer's disease Amyloid Amyloid beta-Protein Precursor - chemistry Amyloid beta-Protein Precursor - metabolism Animals Disease Models, Animal diseases Fibers Gene polymorphism human diseases Humans Models, Molecular Neurodegenerative diseases Neurodegenerative Diseases - metabolism Nucleation Plaque, Amyloid - chemistry Prion protein prions Protein Structure, Secondary Reviews tissues Toxicity |
| title | The Amyloid State of Proteins in Human Diseases |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T17%3A51%3A03IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Amyloid%20State%20of%20Proteins%20in%20Human%20Diseases&rft.jtitle=Cell&rft.au=Eisenberg,%20David&rft.date=2012-03-16&rft.volume=148&rft.issue=6&rft.spage=1188&rft.epage=1203&rft.pages=1188-1203&rft.issn=0092-8674&rft.eissn=1097-4172&rft_id=info:doi/10.1016/j.cell.2012.02.022&rft_dat=%3Cproquest_pubme%3E929123445%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c511t-881e60e32090a75834b0a61c63c6e9e9fa7bd43beb5da918e6ac343ffd33a1f13%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1323802759&rft_id=info:pmid/22424229&rfr_iscdi=true |