Divalent metal ions enhance DOPAL-induced oligomerization of alpha-synuclein.
about
Catecholamine autotoxicity. Implications for pharmacology and therapeutics of Parkinson disease and related disordersA vesicular sequestration to oxidative deamination shift in myocardial sympathetic nerves in Parkinson's disease.Rotenone decreases intracellular aldehyde dehydrogenase activity: implications for the pathogenesis of Parkinson's disease.Decreased vesicular storage and aldehyde dehydrogenase activity in multiple system atrophy.Deficient vesicular storage: A common theme in catecholaminergic neurodegeneration.The serotonin aldehyde, 5-HIAL, oligomerizes alpha-synuclein.DOPAL derived alpha-synuclein oligomers impair synaptic vesicles physiological function.Insights on the interaction of alpha-synuclein and metals in the pathophysiology of Parkinson's disease.Alpha-synuclein: relating metals to structure, function and inhibition.α-Synuclein Over-Expression Induces Increased Iron Accumulation and Redistribution in Iron-Exposed Neurons.Coherent and Contradictory Facts, Feats and Fictions Associated with Metal Accumulation in Parkinson's Disease: Epicenter or Outcome, Yet a Demigod Question.Metals in Alzheimer's and Parkinson's Disease: Relevance to Dementia with Lewy Bodies.Impulse control disorder, lysosomal malfunction and ATP13A2 insufficiency in Parkinsonism.Elevated cerebrospinal fluid ratios of cysteinyl-dopamine/3,4-dihydroxyphenylacetic acid in parkinsonian synucleinopathies.Individual Amino Acid Supplementation Can Improve Energy Metabolism and Decrease ROS Production in Neuronal Cells Overexpressing Alpha-Synuclein.Superoxide is the critical driver of DOPAL autoxidation, lysyl adduct formation, and crosslinking of α-synuclein.Inactivation of glyceraldehyde-3-phosphate dehydrogenase by the dopamine metabolite, 3,4-dihydroxyphenylacetaldehyde.Isoindole Linkages Provide a Pathway for DOPAL-Mediated Cross-Linking of α-Synuclein.3,4-Dihydroxyphenylacetaldehyde-Induced Protein Modifications and Their Mitigation by N-Acetylcysteine.
P2860
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P2860
Divalent metal ions enhance DOPAL-induced oligomerization of alpha-synuclein.
description
2014 nî lūn-bûn
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2014 թուականի Մարտին հրատարակուած գիտական յօդուած
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2014 թվականի մարտին հրատարակված գիտական հոդված
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
@zh-hk
2014年論文
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2014年論文
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2014年论文
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name
Divalent metal ions enhance DOPAL-induced oligomerization of alpha-synuclein.
@ast
Divalent metal ions enhance DOPAL-induced oligomerization of alpha-synuclein.
@en
type
label
Divalent metal ions enhance DOPAL-induced oligomerization of alpha-synuclein.
@ast
Divalent metal ions enhance DOPAL-induced oligomerization of alpha-synuclein.
@en
prefLabel
Divalent metal ions enhance DOPAL-induced oligomerization of alpha-synuclein.
@ast
Divalent metal ions enhance DOPAL-induced oligomerization of alpha-synuclein.
@en
P2093
P2860
P1433
P1476
Divalent metal ions enhance DOPAL-induced oligomerization of alpha-synuclein
@en
P2093
Adele Cooney
David S Goldstein
Patricia Sullivan
Yehonatan Sharabi
Yunden Jinsmaa
P2860
P356
10.1016/J.NEULET.2014.03.016
P407
P50
P577
2014-03-23T00:00:00Z