Ontology highlight
ABSTRACT:
SUBMITTER: Tsemekhman K
PROVIDER: S-EPMC2203343 | biostudies-literature | 2007 Apr
REPOSITORIES: biostudies-literature
Tsemekhman Kiril K Goldschmidt Lukasz L Eisenberg David D Baker David D
Protein science : a publication of the Protein Society 20070227 4
Amyloid diseases, including Alzheimer's and prion diseases, are each associated with unbranched protein fibrils. Each fibril is made of a particular protein, yet they share common properties. One such property is nucleation-dependent fibril growth. Monomers of amyloid-forming proteins can remain in dissolved form for long periods, before rapidly assembly into fibrils. The lag before growth has been attributed to slow kinetics of formation of a nucleus, on which other molecules can deposit to for ...[more]