Ontology highlight
ABSTRACT:
SUBMITTER: Garcia-Pardo J
PROVIDER: S-EPMC4256313 | biostudies-literature | 2014 Dec
REPOSITORIES: biostudies-literature
Garcia-Pardo Javier J Graña-Montes Ricardo R Fernandez-Mendez Marc M Ruyra Angels A Roher Nerea N Aviles Francesc X FX Lorenzo Julia J Ventura Salvador S
The Journal of biological chemistry 20141007 49
Protein aggregation is linked to a growing list of diseases, but it is also an intrinsic property of polypeptides, because the formation of functional globular proteins comes at the expense of an inherent aggregation propensity. Certain proteins can access aggregation-prone states from native-like conformations without the need to cross the energy barrier for unfolding. This is the case of transthyretin (TTR), a homotetrameric protein whose dissociation into its monomers initiates the aggregatio ...[more]