(Q44214168)

30 November 2017

title

Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T. (English)

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30 November 2017

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2

Vladimir N Uversky

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30 November 2017

Jie Li

1

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30 November 2017

Anthony L Fink

series ordinal

3

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30 November 2017

publication date

1 October 2002

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30 November 2017

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30 November 2017

volume

23

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30 November 2017

issue

4-5

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30 November 2017

page(s)

553-567

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Aluminum-containing antacids as a cause of idiopathic Parkinson's disease

30 November 2017

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Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy

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Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro

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Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein

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The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: paraquat and alpha-synuclein

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7 January 2021

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7 January 2021

Pesticides directly accelerate the rate of alpha-synuclein fibril formation: a possible factor in Parkinson's disease

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7 January 2021

Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure

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7 January 2021

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7 January 2021

NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded

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7 January 2021

alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease

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7 January 2021

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Identifiers

DOI

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30 November 2017

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