Biochemical characterization of the core structure of alpha-synuclein filaments. - Wikidata - awgldk - TriplyDB

Biochemical characterization of the core structure of alpha-synuclein filaments.

Biochemical characterization of the core structure of alpha-synuclein filaments.

http://www.wikidata.org/entity/Q30827075

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The synaptic pathology of alpha-synuclein aggregation in dementia with Lewy bodies, Parkinson's disease and Parkinson's disease dementia Acceleration of alpha-synuclein aggregation by homologous peptides Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies Characterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1 Prediction of "hot spots" of aggregation in disease-linked polypeptides Versatile Structures of α-Synuclein Molecular Pathological Classification of Neurodegenerative Diseases: Turning towards Precision Medicine Gut Feelings About α-Synuclein in Gastrointestinal Biopsies: Biomarker in the Making?Is Cell Death Primary or Secondary in the Pathophysiology of Idiopathic Parkinson's Disease?Behavioral characterization of A53T mice reveals early and late stage deficits related to Parkinson's disease.Distinct α-synuclein strains differentially promote tau inclusions in neurons Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions.AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.Residue Glu83 plays a major role in negatively regulating alpha-synuclein amyloid formation Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level.Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR.Direct observation of the interconversion of normal and toxic forms of α-synuclein Novel one-step immunoassays to quantify α-synuclein: applications for biomarker development and high-throughput screening.Covalent α-synuclein dimers: chemico-physical and aggregation properties.Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregation Alpha-synuclein aggregation induced by brief ischemia negatively impacts neuronal survival in vivo: a study in [A30P]alpha-synuclein transgenic mouse Sumoylation inhibits alpha-synuclein aggregation and toxicity.Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites.Highly amyloidogenic two-chain peptide fragments are released upon partial digestion of insulin with pepsin.Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.A guide to neurotoxic animal models of Parkinson's disease Aggregation of αSynuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons Aggregated Alpha-Synuclein Transfer Efficiently between Cultured Human Neuron-Like Cells and Localize to Lysosomes α-Synuclein Amyloid Fibrils with Two Entwined, Asymmetrically Associated Protofibrils.Calcium(II) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domain Structure of the toxic core of α-synuclein from invisible crystals The fold of alpha-synuclein fibrils.Effects of Serine 129 Phosphorylation on α-Synuclein Aggregation, Membrane Association, and Internalization.Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease Modulating the Amyloidogenesis of α-Synuclein Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy.α-Synuclein Fibrils Exhibit Gain of Toxic Function, Promoting Tau Aggregation and Inhibiting Microtubule Assembly Conversion of wild-type alpha-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant.Interactive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins.

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P2860

Biochemical characterization of the core structure of alpha-synuclein filaments.

http://www.wikidata.org/entity/Q30827075

description

2002 nî lūn-bûn

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2002 թուականի Մարտին հրատարակուած գիտական յօդուած

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2002 թվականի մարտին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Biochemical characterization of the core structure of alpha-synuclein filaments.

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Biochemical characterization of the core structure of alpha-synuclein filaments.

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type

label

Biochemical characterization of the core structure of alpha-synuclein filaments.

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Biochemical characterization of the core structure of alpha-synuclein filaments.

@en

prefLabel

Biochemical characterization of the core structure of alpha-synuclein filaments.

@ast

Biochemical characterization of the core structure of alpha-synuclein filaments.

@en

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P1433

Journal of Biological Chemistry

P1476

Biochemical characterization of the core structure of alpha-synuclein filaments.

@en

P2093

Hidehiro Mizusawa

http://www.w3.org/2001/XMLSchema#string

Hirotomo Miake

http://www.w3.org/2001/XMLSchema#string

Masato Hasegawa

http://www.w3.org/2001/XMLSchema#string

Takeshi Iwatsubo

http://www.w3.org/2001/XMLSchema#string

P2860

alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies

Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

Alpha-synuclein in Lewy bodies

Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease

Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease

Widespread alterations of alpha-synuclein in multiple system atrophy

Characterisation of isolated alpha-synuclein filaments from substantia nigra of Parkinson's disease brain.

Membrane association and protein conformation of alpha-synuclein in intact neurons. Effect of Parkinson's disease-linked mutations.

alpha-Synuclein is phosphorylated in synucleinopathy lesions.

The significance of tau and alpha-synuclein inclusions in neurodegenerative diseases.

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19213-19219

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scholarly article

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10.1074/JBC.M110551200

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21

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277

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2002-03-13T00:00:00Z

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11893734

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