NR AGHP
AU Kelly,J.W.
TI Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases.
QU Structure (London, England) 1997 May 15; 5(5): 595-600
PT journal article; review; review literature
AB 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.
ZR 73
MH Amyloid/*chemistry; Amyloidosis/*etiology; Human; Models, Chemical; Prealbumin/*chemistry; Prion Diseases/*etiology; Protein Conformation; Protein Denaturation; Protein Folding; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.
AD Department of Chemistry, Texas A&M University, College Station, Texas, 77843-3255, USA. kelly@chemvx.tamu.edu
SP englisch
PO England