The E46K mutation in alpha-synuclein increases amyloid fibril formation. - Wikidata - wikimedia - TriplyDB

The E46K mutation in alpha-synuclein increases amyloid fibril formation.

The E46K mutation in alpha-synuclein increases amyloid fibril formation.

http://www.wikidata.org/entity/Q30349931

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Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein protein Pre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease models Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases Residual structure, backbone dynamics, and interactions within the synuclein family Definition of a molecular pathway mediating α-synuclein neurotoxicity Systematic mutagenesis of α-synuclein reveals distinct sequence requirements for physiological and pathological activities Dynamic structural flexibility of α-synuclein Exploring the accessible conformations of N-terminal acetylated α-synuclein Propagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.Distinct α-synuclein strains differentially promote tau inclusions in neurons Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46K Amyloid oligomer neurotoxicity, calcium dysregulation, and lipid rafts Antibodies against alpha-synuclein reduce oligomerization in living cells Effects of Mutations on the Reconfiguration Rate of α-Synuclein Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation Clustering of alpha-synuclein on supported lipid bilayers: role of anionic lipid, protein, and divalent ion concentration Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae α-Synuclein-induced tubule formation in lipid bilayers Peptide ligand screening of alpha-synuclein aggregation modulators by in silico panning Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein.Role of small oligomers on the amyloidogenic aggregation free-energy landscape Residue Glu83 plays a major role in negatively regulating alpha-synuclein amyloid formation Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy Distinct region-specific alpha-synuclein oligomers in A53T transgenic mice: implications for neurodegeneration.Quantitative measurement of intact alpha-synuclein proteoforms from post-mortem control and Parkinson's disease brain tissue by intact protein mass spectrometry.Structure activity relationship of phenolic acid inhibitors of α-synuclein fibril formation and toxicity A novel, high-efficiency cellular model of fibrillar alpha-synuclein inclusions and the examination of mutations that inhibit amyloid formation Baicalein reduces E46K alpha-synuclein aggregation in vitro and protects cells against E46K alpha-synuclein toxicity in cell models of familiar Parkinsonism.Distinct hydration properties of wild-type and familial point mutant A53T of α-synuclein associated with Parkinson's disease.Residue histidine 50 plays a key role in protecting α-synuclein from aggregation at physiological pH.Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein.Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level.Unravelling the role of defective genes.The genetics of Parkinson disease.Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation.Induction of intracellular tau aggregation is promoted by α-synuclein seeds and provides novel insights into the hyperphosphorylation of tau.α-Synuclein, leucine-rich repeat kinase-2, and manganese in the pathogenesis of Parkinson disease Aggregation of α-synuclein in S. cerevisiae is associated with defects in endosomal trafficking and phospholipid biosynthesis.Familial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein.

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P2860

The E46K mutation in alpha-synuclein increases amyloid fibril formation.

http://www.wikidata.org/entity/Q30349931

description

2005 nî lūn-bûn

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2005 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2005 թվականի հունվարին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

The E46K mutation in alpha-synuclein increases amyloid fibril formation.

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The E46K mutation in alpha-synuclein increases amyloid fibril formation.

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type

label

The E46K mutation in alpha-synuclein increases amyloid fibril formation.

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The E46K mutation in alpha-synuclein increases amyloid fibril formation.

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prefLabel

The E46K mutation in alpha-synuclein increases amyloid fibril formation.

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The E46K mutation in alpha-synuclein increases amyloid fibril formation.

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P1476

The E46K mutation in alpha-synuclein increases amyloid fibril formation.

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P2093

Amanda J Mishizen-Eberz

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Benoit I Giasson

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Charles L Graves

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David R Lynch

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Eric A Greenbaum

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Michael A Lupoli

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Paul H Axelsen

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S Walter Englander

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7800-7807

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scholarly article

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10.1074/JBC.M411638200

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9

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280

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2005-01-04T00:00:00Z

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15632170

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