(Q40669171)

22 September 2017

title

The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease (English)

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22 September 2017

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5

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22 September 2017

1

Ronit Sharon

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22 September 2017

6

Dennis J Selkoe

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22 September 2017

3

Matthew P Frosch

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22 September 2017

Ifat Bar-Joseph

2

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22 September 2017

Dominic M Walsh

series ordinal

4

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22 September 2017

language of work or name

English

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publication date

1 February 2003

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22 September 2017

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22 September 2017

volume

37

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22 September 2017

issue

4

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22 September 2017

page(s)

583-595

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Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system

22 September 2017

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Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein

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A novel N18TG2 x mesencephalon cell hybrid expresses properties that suggest a dopaminergic cell line of substantia nigra origin

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Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes

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Sphingomyelin in Lewy inclusion bodies in Parkinson's disease

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Experimental allergic encephalomyelitis. An encephalitogenic basic protein from bovine myelin

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A Drosophila model of Parkinson's disease

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In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies

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Characterization of a novel protein regulated during the critical period for song learning in the zebra finch.

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Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein

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Transport of fatty acids across membranes by the diffusion mechanism.

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How are free fatty acids transported in membranes? Is it by proteins or by free diffusion through the lipids?

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beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor

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Selective insolubility of alpha-synuclein in human Lewy body diseases is recapitulated in a transgenic mouse model

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

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Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53 --> Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice

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Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders

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

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Allergic encephalomyelitis: Preparation of the encephalitogenic basic protein from bovine brain

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Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis.

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Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins.

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

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7 January 2021

Expression cloning and characterization of a novel adipocyte long chain fatty acid transport protein

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7 January 2021

alpha-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins

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7 January 2021

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α-Synuclein in Lewy bodies

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

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Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo

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Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease

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7 January 2021

Chronic n-3 polyunsaturated fatty acid diet-deficiency acts on dopamine metabolism in the rat frontal cortex: a microdialysis study.

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Chronic n-3 polyunsaturated fatty acid deficiency alters dopamine vesicle density in the rat frontal cortex

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7 January 2021

10.1016/S0896-6273(03)00024-2

Identifiers

DOI

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22 September 2017

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