Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation
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چکیده
Citation Dettmer, Ulf, Andrew J. Newman, Frank Soldner, Eric S. Luth, Nora C. Kim, Victoria E. von Saucken, John B. Sanderson, Rudolf Jaenisch, Tim Bartels, and Dennis Selkoe. 2015. “Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation.” Nature Communications 6 (1): 7314. doi:10.1038/ncomms8314. http://dx.doi.org/10.1038/ncomms8314.
منابع مشابه
Corrigendum: Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation
β-Sheet-rich α-synuclein (αS) aggregates characterize Parkinson's disease (PD). αS was long believed to be a natively unfolded monomer, but recent work suggests it also occurs in α-helix-rich tetramers. Crosslinking traps principally tetrameric αS in intact normal neurons, but not after cell lysis, suggesting a dynamic equilibrium. Here we show that freshly biopsied normal human brain contains ...
متن کاملParkinson-causing a-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation
b-Sheet-rich a-synuclein (aS) aggregates characterize Parkinson’s disease (PD). aS was long believed to be a natively unfolded monomer, but recent work suggests it also occurs in a-helix-rich tetramers. Crosslinking traps principally tetrameric aS in intact normal neurons, but not after cell lysis, suggesting a dynamic equilibrium. Here we show that freshly biopsied normal human brain contains ...
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Alpha-synuclein (α-syn) protein is abundantly expressed mainly within neurons, and exists in a number of different forms - monomers, tetramers, oligomers and fibrils. During disease, α-syn undergoes conformational changes to form oligomers and high molecular weight aggregates that tend to make the protein more insoluble. Abnormally aggregated α-syn is a neuropathological feature of Parkinson's ...
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