NR ACSL
AU Cohen,F.E.; Prusiner,S.B.
TI Pathologic conformations of prion proteins
QU Annual Review of Biochemistry 1998; 67: 793-819
PT journal article; review; review, academic
AB While many aspects of prion disease biology are unorthodox, perhaps the most fundamental paradox is posed by the coexistence of inherited, sporadic, and infectious forms of these diseases. Sensible molecular mechanisms for prion propagation must explain all three forms of prion diseases in a manner that is compatible with the formidable array of experimental data derived from histopathological, biochemical, biophysical, human genetic, and transgenetic studies. In this review, we explore prion disease pathogenesis initially from the perspective of an autosomal dominant inherited disease. Subsequently, we examine how an intrinsically inherited disease could present in sporadic and infectious forms. Finally, we explore the phenomenologic constraints on models of prion replication with a specific emphasis on biophysical studies of prion protein structures.
ZR 139
MH Human; Models, Theoretical; Prion Diseases/*etiology; Prions/*chemistry; Protein Conformation; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.
AD Fred E. Cohen (cohen@cgl.ucsf.edu), Stanley B. Prusiner, Department of Biochemistry and Biophysics, University of California, San Francisco 94143, USA
SP englisch
PO USA