Structural Intermediates during α-Synuclein Fibrillogenesis on Phospholipid Vesicles
نویسندگان
چکیده
منابع مشابه
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 helical segments when bound to micelles or lipid vesicles, and a relatively ordered helical tetramer w...
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α-Synuclein is a conserved, abundantly expressed protein that is partially localized in pre-synaptic terminals in the central nervous system. The precise biological function(s) and structure of α-synuclein are under investigation. Recently, the native conformation and the presence of naturally occurring multimeric assemblies have come under debate. These are important deliberations because α-sy...
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The normal functions and pathologic facets of the small presynaptic protein α-synuclein (α-syn) are of exceptional interest. In previous studies, we found that α-syn attenuates synaptic exo/endocytosis; however, underlying mechanisms remain unknown. More recent evidence suggests that α-syn exists as metastable multimers and not solely as a natively unfolded monomer. However, conformations of α-...
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α-Crystallin is the major protein of vertebrate lenses. It is found in the water soluble and insoluble fractions of lens fiber cells and can represent up to 50% of the total soluble protein [1,2]. α-Crystallin is a large heteromeric complex containing 30 to 40 copies of two closely related subunits, αA(αA) and αB-crystallin (αB), in roughly a 3:1 ratio in humans [2]. The αA protein is found exc...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2012
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja209019s