title: Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases.
abstract: The assembly and misassembly of normally soluble proteins into fibrilar structures is thought to be a causative agent in a variety of human amyloid and prion diseases. Structural and mechanistic studies of this process are beginning to elucidate the conformational changes required for the conversion of a normally soluble and functional protein into a defined quaternary structure.
authors.affiliation: Department of Chemistry, Texas A&M University, College Station, Texas, 77843-3255, USA. kelly@chemvx.tamu.edu
authors.forename: J W
authors.initials: JW
authors.lastname: Kelly
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D000686:Amyloidosis / Q000209:etiology*; D006801:Humans; D008956:Models, Chemical; D011228:Prealbumin / Q000737:chemistry*; D017096:Prion Diseases / Q000209:etiology*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding
chemical_list: D000682:Amyloid; D011228:Prealbumin