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Review
. 1997 May 15;5(5):595-600.
doi: 10.1016/s0969-2126(97)00215-3.

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

J W Kelly  1
Affiliations
Review

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

J W Kelly. Structure. .

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.

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