(Q40603171)

22 September 2017

title

Tyrosine-to-cysteine modification of human alpha-synuclein enhances protein aggregation and cellular toxicity (English)

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22 September 2017

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Wenbo Zhou

1

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22 September 2017

Curt R Freed

series ordinal

2

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22 September 2017

language of work or name

English

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publication date

29 December 2003

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Journal of Biological Chemistry

22 September 2017

published in

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22 September 2017

volume

279

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22 September 2017

issue

11

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22 September 2017

page(s)

10128-10135

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Animal models of PD: pieces of the same puzzle?

22 September 2017

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Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation

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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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Tyrosine 125 of alpha-synuclein plays a critical role for dimerization following nitrative stress.

21 January 2018

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Effects of oxidative and nitrative challenges on alpha-synuclein fibrillogenesis involve distinct mechanisms of protein modifications

21 January 2018

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alpha-synuclein promotes mitochondrial deficit and oxidative stress

21 January 2018

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Human alpha-synuclein over-expression increases intracellular reactive oxygen species levels and susceptibility to dopamine.

21 January 2018

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21 January 2018

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Expression of mutant alpha-synuclein causes increased susceptibility to dopamine toxicity

21 January 2018

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Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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

21 January 2018

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Dityrosine cross-linking promotes formation of stable alpha -synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies

21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M307563200

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22 September 2017

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