| Literature DB >> 21825020 |
Michele Vendruscolo1, Tuomas P J Knowles, Christopher M Dobson.
Abstract
According to the "generic view" of protein aggregation, the ability to self-assemble into stable and highly organized structures such as amyloid fibrils is not an unusual feature exhibited by a small group of peptides and proteins with special sequence or structural properties, but rather a property shared by most proteins. At the same time, through a wide variety of techniques, many of which were originally devised for applications in other disciplines, it has also been established that the maintenance of proteins in a soluble state is a fundamental aspect of protein homeostasis. Taken together, these advances offer a unified framework for understanding the molecular basis of protein aggregation and for the rational development of therapeutic strategies based on the biological and chemical regulation of protein solubility.Entities:
Mesh:
Year: 2011 PMID: 21825020 PMCID: PMC3225949 DOI: 10.1101/cshperspect.a010454
Source DB: PubMed Journal: Cold Spring Harb Perspect Biol ISSN: 1943-0264 Impact factor: 10.005