N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation.
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The Synaptic Function of α-SynucleinThe biological functions of Naa10 - From amino-terminal acetylation to human diseaseTotal α-synuclein levels in human blood cells, CSF, and saliva determined by a lipid-ELISA.A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicityAlpha-synuclein function and dysfunction on cellular membranes.Purification of α-synuclein from human brain reveals an instability of endogenous multimers as the protein approaches purity.The Interplay between Alpha-Synuclein Clearance and SpreadingOligomerization and Membrane-binding Properties of Covalent Adducts Formed by the Interaction of α-Synuclein with the Toxic Dopamine Metabolite 3,4-Dihydroxyphenylacetaldehyde (DOPAL).The mechanism of sirtuin 2-mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease.The influence of N-terminal acetylation on micelle-induced conformational changes and aggregation of α-Synuclein.Nuclear Magnetic Resonance Observation of α-Synuclein Membrane Interaction by Monitoring the Acetylation Reactivity of Its Lysine Side Chains.Insight into conformational modification of alpha-synuclein in the presence of neuronal whole cells and of their isolated membranes.Cell Biology and Pathophysiology of α-Synuclein.The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease.The Impact of N-terminal Acetylation of α-Synuclein on Phospholipid Membrane Binding and Fibril Structure.Alpha-, Beta-, and Gamma-synuclein Quantification in Cerebrospinal Fluid by Multiple Reaction Monitoring Reveals Increased Concentrations in Alzheimer's and Creutzfeldt-Jakob Disease but No Alteration in SynucleinopathiesFactors affecting the physical stability (aggregation) of peptide therapeutics.Acetylome in Human Fibroblasts From Parkinson's Disease Patients.Altered expression of genes involved in ganglioside biosynthesis in substantia nigra neurons in Parkinson's disease.Investigating the functionality of a ribosome-binding mutant of NAA15 using Saccharomyces cerevisiae.Minimotifs dysfunction is pervasive in neurodegenerative disorders
P2860
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P2860
N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation.
description
2014 nî lūn-bûn
@nan
2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2014年の論文
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年學術文章
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name
N-alpha-acetylation of α-synuc ...... and resistance to aggregation.
@ast
N-alpha-acetylation of α-synuc ...... and resistance to aggregation.
@en
type
label
N-alpha-acetylation of α-synuc ...... and resistance to aggregation.
@ast
N-alpha-acetylation of α-synuc ...... and resistance to aggregation.
@en
prefLabel
N-alpha-acetylation of α-synuc ...... and resistance to aggregation.
@ast
N-alpha-acetylation of α-synuc ...... and resistance to aggregation.
@en
P2093
P2860
P1433
P1476
N-alpha-acetylation of α-synuc ...... and resistance to aggregation.
@en
P2093
Dennis J Selkoe
Eric S Luth
Nora C Kim
P2860
P304
P356
10.1371/JOURNAL.PONE.0103727
P407
P50
P577
2014-07-30T00:00:00Z