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dc.contributor.authorAlberti, Simon
dc.contributor.authorHalfmann, Randal Arthur
dc.contributor.authorLindquist, Susan
dc.date.accessioned2011-11-03T19:07:43Z
dc.date.available2011-11-03T19:07:43Z
dc.date.issued2010-01
dc.identifier.isbn978-0-12-385118-5
dc.identifier.urihttp://hdl.handle.net/1721.1/66916
dc.description.abstractProtein aggregates are associated with a variety of debilitating human diseases, but they can have functional roles as well. Both pathological and nonpathological protein aggregates display tremendous diversity, with substantial differences in aggregate size, morphology, and structure. Among the different aggregation types, amyloids are particularly remarkable, because of their high degree of order and their ability to form self-perpetuating conformational states. Amyloids form the structural basis for a group of proteins called prions, which have the ability to generate new phenotypes by a simple switch in protein conformation that does not involve changes in the sequence of the DNA. Although protein aggregates are notoriously difficult to study, recent technological developments and, in particular, the use of yeast prions as model systems, have been very instrumental in understanding fundamental aspects of aggregation. Here, we provide a range of biochemical, cell biological and yeast genetic methods that are currently used in our laboratory to study protein aggregation and the formation of amyloids and prions.en_US
dc.language.isoen_US
dc.publisherElsevier Inc.en_US
dc.relation.isversionofhttp://dx.doi.org/10.1016/s0076-6879(10)70030-6en_US
dc.rightsCreative Commons Attribution-Noncommercial-Share Alike 3.0en_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/en_US
dc.sourceLindquisten_US
dc.titleBiochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeasten_US
dc.typeBook chapteren_US
dc.identifier.citationAlberti, Simon, Randal Halfmann, and Susan Lindquist. “Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast.” Methods in Enzymology. Vol. 470. Elsevier, 2010. 709-734. Web. 3 Nov. 2011. © 2011 Elsevier Inc.en_US
dc.contributor.departmentmove to dc.description.sponsorshipen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.departmentWhitehead Institute for Biomedical Researchen_US
dc.contributor.approverLindquist, Susan
dc.contributor.mitauthorAlberti, Simon
dc.contributor.mitauthorHalfmann, Randal Arthur
dc.contributor.mitauthorLindquist, Susan
dc.relation.journalMethods in Enzymologyen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/BookItemen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsAlberti, Simon; Halfmann, Randal; Lindquist, Susanen
dc.identifier.orcidhttps://orcid.org/0000-0003-1307-882X
mit.licenseOPEN_ACCESS_POLICYen_US


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