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Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases Kelly JWStructure 1997[May]; 5 (5): 595-600The 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.|Amyloid/*chemistry[MESH]|Amyloidosis/*etiology[MESH]|Humans[MESH]|Models, Chemical[MESH]|Prealbumin/*chemistry[MESH]|Prion Diseases/*etiology[MESH]|Protein Conformation[MESH]|Protein Denaturation[MESH]|Protein Folding[MESH] |
