Membrane bound α-synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain.
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Conformational heterogeneity of α-synuclein in membrane.Structural and dynamical insights into the membrane-bound α-synuclein.Molecular details of α-synuclein membrane association revealed by neutrons and photons.α-Synuclein interferes with the ESCRT-III complex contributing to the pathogenesis of Lewy body disease.The function of α-synuclein.Interactions between calcium and alpha-synuclein in neurodegeneration.Loss of native α-synuclein multimerization by strategically mutating its amphipathic helix causes abnormal vesicle interactions in neuronal cells.Rationally Designed Variants of α-Synuclein Illuminate Its Structural Properties in Health and Disease
P2860
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P2860
Membrane bound α-synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain.
description
2013 nî lūn-bûn
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2013年の論文
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2013年学术文章
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name
Membrane bound α-synuclein is ...... ith higher flexibility remain.
@en
Membrane bound α-synuclein is ...... ith higher flexibility remain.
@nl
type
label
Membrane bound α-synuclein is ...... ith higher flexibility remain.
@en
Membrane bound α-synuclein is ...... ith higher flexibility remain.
@nl
prefLabel
Membrane bound α-synuclein is ...... ith higher flexibility remain.
@en
Membrane bound α-synuclein is ...... ith higher flexibility remain.
@nl
P2093
P2860
P1433
P1476
Membrane bound α-synuclein is ...... with higher flexibility remain
@en
P2093
Andreas Herrmann
Aouefa Amoussouvi
Ivan Haralampiev
Martin Stöckl
P2860
P304
P356
10.1016/J.FEBSLET.2013.06.034
P407
P50
P577
2013-07-03T00:00:00Z