Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases

Kelly, J.W.

Structure 5(5): 595-600

1997


ISSN/ISBN: 0969-2126
PMID: 9195890
DOI: 10.1016/s0969-2126(97)00215-3
Accession: 029998213

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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.