| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10872471 | FEBS Letters | 2009 | 6 Pages |
Abstract
Protein misfolding and aggregation are pathognomic for a number of the most common age-related degenerative diseases. Great progress has been made in studying protein aggregation in the test tube and also in replicating protein aggregation in vertebrate animal models of these diseases. However, we argue here that the development and effective integration of emerging techniques such as the methods of nanoscience and the use of invertebrate models are now providing powerful new opportunities to advance our current understanding of the fundamental origins of these disorders.
Keywords
AFMTCCDSECsHSPD. melanogasterAβFRAPC. elegansAPPSDS–PAGEAmyloidsodium dodecyl sulfate–polyacrylamide gel electrophoresisamyloid betaAlzheimer’s diseaseNeurodegenerationNanosciencefluorescence recovery after photobleachingquartz crystal microbalanceQCMatomic force microscopysmall heat shock proteinamyloid precursor proteinSize exclusion chromatography
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Authors
Leila M. Luheshi, Christopher M. Dobson,