The amyloid state and its association with protein misfolding diseases.
The phenomenon of protein aggregation and amyloid formation has become the subject of rapidly increasing research activities across a wide range of scientific disciplines. Such activities have been stimulated by the association of amyloid deposition with a range of debilitating medical disorders, from Alzheimer's disease to type II diabetes, many of which are major threats to human health and welfare in the modern world. It has become clear, however, that the ability to form the amyloid state is more general than previously imagined, and that its study can provide unique insights into the nature of the functional forms of peptides and proteins, as well as understanding the means by which protein homeostasis can be maintained and protein metastasis avoided.
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Tuomas P J
TP
Knowles
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Michele
M
Vendruscolo
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Christopher M
CM
Dobson
D000544:Alzheimer Disease / Q000209:etiology* / Q000473:pathology; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D000686:Amyloidosis / Q000209:etiology* / Q000473:pathology; D000818:Animals; D006801:Humans; D011487:Protein Conformation; D017510:Protein Folding
D000682:Amyloid