Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation.
about
Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)The role of lipid peroxidation in neurological disordersAlpha-Synuclein Oligomers-Neurotoxic Molecules in Parkinson's Disease and Other Lewy Body DisordersMitochondrial lipids in neurodegenerationProtein adducts of aldehydic lipid peroxidation products identification and characterization of protein adducts using an aldehyde/keto-reactive probe in combination with mass spectrometryMethionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions.Next-generation active immunization approach for synucleinopathies: implications for Parkinson's disease clinical trials.Rapamycin improves motor function, reduces 4-hydroxynonenal adducted protein in brain, and attenuates synaptic injury in a mouse model of synucleinopathyBiophysics of Parkinson's disease: structure and aggregation of alpha-synuclein.Caenorhabditis elegans: a model to investigate oxidative stress and metal dyshomeostasis in Parkinson's diseasePathological correlations between traumatic brain injury and chronic neurodegenerative diseases.Neurodegeneration and motor dysfunction in mice lacking cytosolic and mitochondrial aldehyde dehydrogenases: implications for Parkinson's disease.Air pollution: mechanisms of neuroinflammation and CNS disease.Protective Action of Neurotrophic Factors and Estrogen against Oxidative Stress-Mediated NeurodegenerationActive immunization against alpha-synuclein ameliorates the degenerative pathology and prevents demyelination in a model of multiple system atrophyEffects of impaired membrane interactions on α-synuclein aggregation and neurotoxicityInteractions of glutathione transferases with 4-hydroxynonenal.Oligomerization and Membrane-binding Properties of Covalent Adducts Formed by the Interaction of α-Synuclein with the Toxic Dopamine Metabolite 3,4-Dihydroxyphenylacetaldehyde (DOPAL).Structural and functional properties of prefibrillar α-synuclein oligomersDopamine prevents lipid peroxidation-induced accumulation of toxic α-synuclein oligomers by preserving autophagy-lysosomal function.Effects of 4-hydroxynonenal on vascular endothelial and smooth muscle cell redox signaling and function in health and disease.The interplay between lipids and dopamine on α-synuclein oligomerization and membrane binding.Oxidative stress in Parkinson's disease: a mechanism of pathogenic and therapeutic significance.α-Synuclein in Parkinson's disease.Oxidative and nitrative alpha-synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies.4-Hydroxynonenal in the pathogenesis and progression of human diseases.Involvement of 4-hydroxy-2-nonenal accumulation in multiple system atrophy.Structural, morphological, and functional diversity of amyloid oligomers.Oxidative Modification and Its Implications for the Neurodegeneration of Parkinson's Disease.Dopamine and Cu+/2+ can induce oligomerization of α-synuclein in the absence of oxygen: Two types of oligomerization mechanisms for α-synuclein and related cell toxicity studies.Off-pathway α-synuclein oligomers seem to alter α-synuclein turnover in a cell model but lack seeding capability in vivo.Structural and morphological characterization of aggregated species of α-synuclein induced by docosahexaenoic acid.Site-specific effects of peptide lipidation on beta-amyloid aggregation and cytotoxicity.The impact of genetic research on our understanding of Parkinson's diseaseInhibition of aminoacylase 3 protects rat brain cortex neuronal cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and 4-hydroxy-2-nonenal.The Aggregation of Huntingtin and α-Synuclein.Lipid peroxidation product 4-hydroxy-2-nonenal promotes seeding-capable oligomer formation and cell-to-cell transfer of α-synuclein.FOXO3 determines the accumulation of α-synuclein and controls the fate of dopaminergic neurons in the substantia nigra.Posttranslational modifications of blood-derived alpha-synuclein as biochemical markers for Parkinson's disease.Do mtDNA Mutations Participate in the Pathogenesis of Sporadic Parkinson's Disease?
P2860
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P2860
Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation.
description
2006 nî lūn-bûn
@nan
2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
name
Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation.
@ast
Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation.
@en
type
label
Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation.
@ast
Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation.
@en
prefLabel
Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation.
@ast
Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation.
@en
P2093
P2860
P356
P1476
Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation.
@en
P2093
Anthony L Fink
Donato A Di Monte
Dongmei Hu
Stephen H Reaney
Zhijie Qin
P2860
P304
P356
10.1074/JBC.M608126200
P407
P577
2006-12-21T00:00:00Z