Work

Deadly Conformations—Protein Misfolding in Prion Disease

Year: 1997

Type: review

Abstract: Novel infectious particles, termed prions, composed largely and perhaps solely of a single protein, are the likely causative agents of a group of transmissible spongiform encephalopathies that produce lethal decline of cognitive and motor function. As if the notion of a transmissible pathogenic protein is not jarring enough, evidence indicates that the responsible protein arrives at a pathogenic state by misfolding from a normal form that has ubiquitous tissue distribution. The remarkable nature of these diseases and the nature of the prion protein conversion process as we currently understand it are reviewed below.

Source: Cell

DOI: 10.1016/s0092-8674(00)80232-9

Authors: Arthur L Horwich, Jonathan S Weissman

Institutions: Howard Hughes Medical Institute, Yale University, University of California, San Francisco

Language: English

Topic: Prion Diseases and Protein Misfolding

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $11,400