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Looking At The Recent Advances In Understanding Α-Synuclein And Its Aggregation Through The Proteoform Prism, Vladimir N. Uversky
Looking At The Recent Advances In Understanding Α-Synuclein And Its Aggregation Through The Proteoform Prism, Vladimir N. Uversky
Molecular Medicine Faculty Publications
Despite attracting the close attention of multiple researchers for the past 25 years, α-synuclein continues to be an enigma, hiding sacred truth related to its structure, function, and dysfunction, concealing mechanisms of its pathological spread within the affected brain during disease progression, and, above all, covering up the molecular mechanisms of its multipathogenicity, i.e. the ability to be associated with the pathogenesis of various diseases. The goal of this article is to present the most recent advances in understanding of this protein and its aggregation and to show that the remarkable structural, functional, and dysfunctional multifaceted nature of α-synuclein can …
Calbindin-D28k Acts As A Calcium-Dependent Chaperone Suppressing Α-Synuclein Fibrillation In Vitro, Wenbo Zhou, Chunmei Long, Anthony L. Fink, Vladimir N. Uversky
Calbindin-D28k Acts As A Calcium-Dependent Chaperone Suppressing Α-Synuclein Fibrillation In Vitro, Wenbo Zhou, Chunmei Long, Anthony L. Fink, Vladimir N. Uversky
Molecular Medicine Faculty Publications
α-Synuclein, a natively unfolded protein aggregation which is implicated in the pathogenesis of Parkinson’s disease and several other neurodegenerative diseases, is known to interact with a great number of unrelated proteins. Some of these proteins, such as ß-synuclein and DJ-1, were shown to inhibit α-synuclein aggregation in vitro and in vivo therefore acting as chaperones. Since calbindin-D28K is co-localized with Ca2+ neuronal membrane pumps, and since α-synuclein is also found in the membrane proximity, these two proteins can potentially interact in vivo. Here we show that calbindin-D28K interacts with α-synuclein and inhibits its fibrillation in a calcium-dependent manner, therefore potentially …