Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism [version 1; referees: 2 approved]

F1000Research

Vladimir N. Uversky¹ 

[1] Laboratory of Structural Dynamics, Stability and Folding Of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Av., 194064 St. Petersburg, Russian Federation;

关键词: Autoimmunity;    Biocatalysis;    Cognitive Neurology & Dementia;    Cognitive Neuroscience;    Cytoskeleton;    Innate Immunity;    Medical Genetics;    Membranes & Sorting;    Motor Systems;    Movement Disorders;    Neurobiology of Disease & Regeneration;    Neuronal & Glial Cell Biology;    Neuronal Signaling Mechanisms;    Protein Chemistry & Proteomics;    Protein Folding;   

DOI  :  10.12688/f1000research.10536.1

来源: DOAJ

【 摘 要 】

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 be understood using the proteoform concept.

【 授权许可】

Unknown