The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells.
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The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicityPropagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.The contribution of alpha synuclein to neuronal survival and function - Implications for Parkinson's diseasePost translational changes to α-synuclein control iron and dopamine trafficking; a concept for neuron vulnerability in Parkinson's disease.Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregationAlpha-synuclein function and dysfunction on cellular membranes.Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivoSystematic comparison of the effects of alpha-synuclein mutations on its oligomerization and aggregation.Effects of impaired membrane interactions on α-synuclein aggregation and neurotoxicityThe A53E α-synuclein pathological mutation demonstrates reduced aggregation propensity in vitro and in cell cultureThe Interplay between Alpha-Synuclein Clearance and SpreadingDistinct clinical and neuropathological features of G51D SNCA mutation cases compared with SNCA duplication and H50Q mutationshRNA-Based Screen Identifies Endocytic Recycling Pathway Components That Act as Genetic Modifiers of Alpha-Synuclein Aggregation, Secretion and Toxicity.Oligomerization and Membrane-binding Properties of Covalent Adducts Formed by the Interaction of α-Synuclein with the Toxic Dopamine Metabolite 3,4-Dihydroxyphenylacetaldehyde (DOPAL).Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutantsInduction of de novo α-synuclein fibrillization in a neuronal model for Parkinson's diseaseTRIM28 regulates the nuclear accumulation and toxicity of both alpha-synuclein and tau.The Synucleinopathies: Twenty Years On.Protein phosphorylation in neurodegeneration: friend or foe?Multiple system atrophy: genetic or epigenetic?Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies.Alpha-synuclein: relating metals to structure, function and inhibition.Protein Partners of α-Synuclein in Health and Disease.Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade?Investigational α-synuclein aggregation inhibitors: hope for Parkinson's disease.Nuclear Lipids in the Nervous System: What they do in Health and Disease.Role of neurotoxicants and traumatic brain injury in α-synuclein protein misfolding and aggregation.Cell Biology and Pathophysiology of α-Synuclein.Nanomolar oligomerization and selective co-aggregation of α-synuclein pathogenic mutants revealed by single-molecule fluorescence.From the baker to the bedside: yeast models of Parkinson's disease.Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism.Semisynthetic and in Vitro Phosphorylation of Alpha-Synuclein at Y39 Promotes Functional Partly Helical Membrane-Bound States Resembling Those Induced by PD Mutations.Comparison of the in vivo induction and transmission of α-synuclein pathology by mutant α-synuclein fibril seeds in transgenic mice.Trehalose Inhibits A53T Mutant α-Synuclein Overexpression and Neurotoxicity in Transduced PC12 Cells.Neurodegeneration and the ordered assembly of α-synuclein.Silencing Alpha Synuclein in Mature Nigral Neurons Results in Rapid Neuroinflammation and Subsequent Toxicity.The Transcellular Propagation and Intracellular Trafficking of α-Synuclein.Advancing Stem Cell Models of Alpha-Synuclein Gene Regulation in Neurodegenerative Disease.Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules.Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding.
P2860
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P2860
The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells.
description
2014 nî lūn-bûn
@nan
2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
The novel Parkinson's disease ...... nuclear localization in cells.
@ast
The novel Parkinson's disease ...... nuclear localization in cells.
@en
type
label
The novel Parkinson's disease ...... nuclear localization in cells.
@ast
The novel Parkinson's disease ...... nuclear localization in cells.
@en
prefLabel
The novel Parkinson's disease ...... nuclear localization in cells.
@ast
The novel Parkinson's disease ...... nuclear localization in cells.
@en
P2093
P2860
P356
P1476
The novel Parkinson's disease ...... nuclear localization in cells
@en
P2093
Aaron D Gitler
Ana Jovičić
Aoife Kiely
David Eliezer
Hilal A Lashuel
Janice L Holton
Martial K Mbefo
Mohamed-Bilal Fares
Nadine Ait-Bouziad
P2860
P304
P356
10.1093/HMG/DDU165
P577
2014-04-11T00:00:00Z