Explaining the Structural Plasticity of α-Synuclein
Given that α-synuclein has been implicated in the pathogenesis of several neurodegenerative disorders, deciphering the structure of this protein is of particular importance. While monomeric α-synuclein is disordered in solution, it can form aggregates rich in cross-β structure, relatively long helic...
Main Authors: | Ullman, Orly, Fisher, Charles K., Stultz, Collin M. |
---|---|
Other Authors: | Harvard University--MIT Division of Health Sciences and Technology |
Format: | Article |
Language: | en_US |
Published: |
American Chemical Society (ACS)
2012
|
Online Access: | http://hdl.handle.net/1721.1/73165 https://orcid.org/0000-0002-3415-242X |
Similar Items
-
Modeling intrinsically disordered proteins ; a comprehensive study of [alpha]-synuclein
by: Ullman, Orly
Published: (2015) -
Comparative Studies of Disordered Proteins with Similar Sequences: Application to Aβ40 and Aβ42
by: Fisher, Charles K., et al.
Published: (2014) -
EFFICIENT CONSTRUCTION OF DISORDERED PROTEIN ENSEMBLES IN A BAYESIAN FRAMEWORK WITH OPTIMAL SELECTION OF CONFORMATIONS
by: Fisher, Charles K, et al.
Published: (2017) -
A role for α-Synuclein in axon growth and its implications in corticostriatal glutamatergic plasticity in Parkinson’s disease
by: Schechter, Meir, et al.
Published: (2020) -
Calcineurin determines toxic versus beneficial responses to α-synuclein
by: Caraveo, Gabriela, et al.
Published: (2015)