Role of alpha-synuclein carboxy-terminus on fibril formation in vitro. - Wikidata - awgldk - TriplyDB

Role of alpha-synuclein carboxy-terminus on fibril formation in vitro.

Role of alpha-synuclein carboxy-terminus on fibril formation in vitro.

http://www.wikidata.org/entity/Q47762431

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Redistribution of DAT/α-synuclein complexes visualized by "in situ" proximity ligation assay in transgenic mice modelling early Parkinson's disease Parkinsonian neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and alpha-synuclein mutations promote Tau protein phosphorylation at Ser262 and destabilize microtubule cytoskeleton in vitro Secondary structure and dynamics of micelle bound beta- and gamma-synuclein Residual structure, backbone dynamics, and interactions within the synuclein family Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)The Synaptic Function of α-Synuclein Distinct α-synuclein strains differentially promote tau inclusions in neurons Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice Value of genetic models in understanding the cause and mechanisms of Parkinson's disease Enrichment and site mapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry.Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions.Assessing the subcellular dynamics of alpha-synuclein using photoactivation microscopy.Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species.GTPase activity plays a key role in the pathobiology of LRRK2.The first N-terminal amino acids of alpha-synuclein are essential for alpha-helical structure formation in vitro and membrane binding in yeast.Residue Glu83 plays a major role in negatively regulating alpha-synuclein amyloid formation N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42 Quantitative analysis of phospholipids containing arachidonate and docosahexaenoate chains in microdissected regions of mouse brain.The chaperone-like activity of α-synuclein attenuates aggregation of its alternatively spliced isoform, 112-synuclein in vitro: plausible cross-talk between isoforms in protein aggregation.The clustering and spatial arrangement of beta-sheet sequence, but not order, govern alpha-synuclein fibrillogenesis Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations Reducing C-terminal-truncated alpha-synuclein by immunotherapy attenuates neurodegeneration and propagation in Parkinson's disease-like models.Identification of novel α-synuclein isoforms in human brain tissue by using an online nanoLC-ESI-FTICR-MS method A novel, high-efficiency cellular model of fibrillar alpha-synuclein inclusions and the examination of mutations that inhibit amyloid formation Residue histidine 50 plays a key role in protecting α-synuclein from aggregation at physiological pH.Neurodegenerative models in Drosophila: polyglutamine disorders, Parkinson disease, and amyotrophic lateral sclerosis.Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level.Quantitative analysis of α-synuclein solubility in living cells using split GFP complementation α-Synuclein Transgenic Drosophila As a Model of Parkinson's Disease and Related Synucleinopathies.A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synuclein Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation.The bacterial curli system possesses a potent and selective inhibitor of amyloid formation.Familial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein.Addition of exogenous α-synuclein preformed fibrils to primary neuronal cultures to seed recruitment of endogenous α-synuclein to Lewy body and Lewy neurite-like aggregates.Exogenous α-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death Role of α-synuclein in inducing innate and adaptive immunity in Parkinson disease.Accelerated formation of alpha-synuclein oligomers by concerted action of the 20S proteasome and familial Parkinson mutations.Calpain-cleavage of alpha-synuclein: connecting proteolytic processing to disease-linked aggregation.

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Role of alpha-synuclein carboxy-terminus on fibril formation in vitro.

http://www.wikidata.org/entity/Q47762431

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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2003年學術文章

@zh-hant

name

Role of alpha-synuclein carboxy-terminus on fibril formation in vitro.

@en

Role of alpha-synuclein carboxy-terminus on fibril formation in vitro.

@nl

type

label

Role of alpha-synuclein carboxy-terminus on fibril formation in vitro.

@en

Role of alpha-synuclein carboxy-terminus on fibril formation in vitro.

@nl

prefLabel

Role of alpha-synuclein carboxy-terminus on fibril formation in vitro.

@en

Role of alpha-synuclein carboxy-terminus on fibril formation in vitro.

@nl

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Role of alpha-synuclein carboxy-terminus on fibril formation in vitro.

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Benoit I Giasson

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Harry Ischiropoulos

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Ian V J Murray

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John Q Trojanowski

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Paul H Axelsen

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Shawn M Quinn

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Virginia M-Y Lee

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Vishwanath Koppaka

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8530-8540

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scholarly article

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10.1021/BI027363R

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28

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42

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2003-07-01T00:00:00Z

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10663467

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12859200

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