The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
about
Alpha-synuclein Toxicity in the Early Secretory Pathway: How It Drives Neurodegeneration in Parkinsons DiseasePropagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.α-Synuclein structural features inhibit harmful polyunsaturated fatty acid oxidation, suggesting roles in neuroprotectionMutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregationAlpha-synuclein function and dysfunction on cellular membranes.The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein.Systematic comparison of the effects of alpha-synuclein mutations on its oligomerization and aggregation.The Interplay between Alpha-Synuclein Clearance and SpreadingInteraction between Neuromelanin and Alpha-Synuclein in Parkinson's Disease.Distinct clinical and neuropathological features of G51D SNCA mutation cases compared with SNCA duplication and H50Q mutationAlpha-Synuclein Proteins Promote Pro-Inflammatory Cascades in Microglia: Stronger Effects of the A53T MutantO-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's diseaseBent out of shape: α-Synuclein misfolding and the convergence of pathogenic pathways in Parkinson's disease.Induction of de novo α-synuclein fibrillization in a neuronal model for Parkinson's diseaseAFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species.Interactions between calcium and alpha-synuclein in neurodegeneration.Multiple system atrophy: genetic or epigenetic?Insights on the interaction of alpha-synuclein and metals in the pathophysiology of Parkinson's disease.Genetic Variants in SNCA and the Risk of Sporadic Parkinson's Disease and Clinical Outcomes: A ReviewLumbee traditional medicine: Neuroprotective activities of medicinal plants used to treat Parkinson's disease-related symptoms.Role of neurotoxicants and traumatic brain injury in α-synuclein protein misfolding and aggregation.Nanomolar oligomerization and selective co-aggregation of α-synuclein pathogenic mutants revealed by single-molecule fluorescence.Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism.Insights into the mechanisms of copper dyshomeostasis in amyotrophic lateral sclerosis.Amyloid single-cell cytotoxicity assays by nanomotion detection.Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets genetics.Mitophagy in Parkinson's Disease: Pathogenic and Therapeutic Implications.Posttranslational modification and mutation of histidine 50 trigger alpha synuclein aggregation and toxicity.A sensitive assay reveals structural requirements for α-synuclein fibril growth.Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules.Unconventional Secretion and Intercellular Transfer of Mutant Huntingtin.Rationally Designed Variants of α-Synuclein Illuminate Its Structural Properties in Health and DiseaseMicrofluidic deposition for resolving single-molecule protein architecture and heterogeneityIdentification and nanomechanical characterization of the fundamental single-strand protofilaments of amyloid α-synuclein fibrilsQuality Over Quantity: Advantages of Using Alpha-Synuclein Preformed Fibril Triggered Synucleinopathy to Model Idiopathic Parkinson's Disease
P2860
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P2860
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
description
2014 nî lūn-bûn
@nan
2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի օգոստոսին 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 H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@ast
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@en
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@en-gb
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@nl
type
label
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@ast
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@en
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@en-gb
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@nl
prefLabel
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@ast
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@en
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@en-gb
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@nl
P2093
P2860
P50
P921
P3181
P356
P1476
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity
@en
P2093
Anne-Laure Mahul-Mellier
Bruno Fauvet
David Eliezer
Filip Vercruysse
Giovanni Dietler
Hilal A Lashuel
Igor Dikiy
Martial K Mbefo
P2860
P304
21856-21876
P3181
P356
10.1074/JBC.M114.553297
P407
P577
2014-08-08T00:00:00Z