PerspectiveCell Biology

A Unifying Role for Prions in Neurodegenerative Diseases

See allHide authors and affiliations

Science  22 Jun 2012:
Vol. 336, Issue 6088, pp. 1511-1513
DOI: 10.1126/science.1222951

You are currently viewing the figures only.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

  1. Modeling neurodegeneration caused by prions.

    (A) Wild-type (WT) prions multiply through self-propagating cycles of posttranslational modification; generally, an increase in β-sheet content accompanies prion formation. Pathogenic prions are most toxic as oligomers and less toxic after polymerization into amyloid fibrils. Depending on the protein, the fibrils coalesce into amyloid plaques, neurofibrillary tangles, or intracellular inclusions such as Lewy or Pick bodies. Drug targets for the development of therapeutics (black circles): (i) lowering precursor protein, (ii) inhibiting prion formation, and (iii) enhancing prion clearance. (B) Late-onset heritable neurodegeneration argues for two discrete events (squares): (i) mutant protein synthesis and (ii) prion formation.

    PHOTO CREDITS: STEPHEN J. DEARMOND/UNIVERSITY OF CALIFORNIA, SAN FRANCISCO, AND JEFFREY H. KORDOWER/RUSH UNIVERSITY

Stay Connected to Science