Amyloid ion channels: A common structural link for protein-misfolding disease
University of California, Santa Barbara · University of California, Los Angeles · +2 more institutions
Abstract
Protein conformational diseases, including Alzheimer's, Huntington's, and Parkinson's diseases, result from protein misfolding, giving a distinct fibrillar feature termed amyloid. Recent studies show that only the globular (not fibrillar) conformation of amyloid proteins is sufficient to induce cellular pathophysiology. However, the 3D structural conformations of these globular structures, a key missing link in designing effective prevention and treatment, remain undefined as of yet. By using atomic force microscopy, circular dichroism, gel electrophoresis, and electrophysiological recordings, we show here that an array of amyloid molecules, including amyloid-beta(1-40), alpha-synuclein, ABri, ADan, serum…
Citation impact
- FWCI
- 20.82
- Percentile
- 100%
- References
- 39
Authors
9- APArjan P. QuistCorresponding
University of California, Santa Barbara, University of California, Los Angeles, University of Pittsburgh, New York University
- IDIvo Doudevski
University of California, Santa Barbara, University of California, Los Angeles, University of Pittsburgh, New York University
- HLHai Lin
University of California, Santa Barbara, University of California, Los Angeles, University of Pittsburgh, New York University
- RARushana Azimova
University of California, Santa Barbara, University of California, Los Angeles, University of Pittsburgh, New York University
- DNDouglas Ng
University of California, Santa Barbara, University of California, Los Angeles, University of Pittsburgh, New York University
Topics & keywords
- Amyloid (mycology)
- Ion channel
- Chemistry
- Biophysics
- Protein folding
- Thioflavin
- Globular protein
- Biochemistry
- Good health and well-being