Induction of alpha-synuclein aggregation by intracellular nitrative insult. (Q40776570)

PubMed publication ID

11588178

23 September 2017

title

Induction of alpha-synuclein aggregation by intracellular nitrative insult (English)

1 reference

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12 May 2020

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5

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12 May 2020

author name string

E Paxinou

1

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12 May 2020

Q Chen

2

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12 May 2020

M Weisse

3

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12 May 2020

B I Giasson

4

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12 May 2020

S M Rueter

6

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12 May 2020

J Q Trojanowski

7

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12 May 2020

V M Lee

8

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12 May 2020

H Ischiropoulos

9

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12 May 2020

language of work or name

English

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publication date

1 October 2001

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PubMed publication ID

11588178

23 September 2017

published in

Journal of Neuroscience

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12 May 2020

volume

21

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12 May 2020

issue

20

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12 May 2020

page(s)

8053-8061

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describes a project that uses

12 May 2020

ImageQuant

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11 June 2022

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Effect of the overexpression of wild-type or mutant alpha-synuclein on cell susceptibility to insult

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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

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Cysteine proteinase inhibitors and ras gene products share the same biological activities including transforming activity toward NIH3T3 mouse fibroblasts and the differentiation-inducing activity toward PC12 rat pheochromocytoma cells

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Degradation of alpha-synuclein by proteasome

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Mass spectrometric quantification of 3-nitrotyrosine, ortho-tyrosine, and o,o'-dityrosine in brain tissue of 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridine-treated mice, a model of oxidative stress in Parkinson's disease.

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A panel of epitope-specific antibodies detects protein domains distributed throughout human alpha-synuclein in Lewy bodies of Parkinson's disease

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alpha-synuclein promotes mitochondrial deficit and oxidative stress

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Two distinct mechanisms of nitric oxide-mediated neuronal cell death show thiol dependency

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

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Cold-induced brain edema and infarction are reduced in transgenic mice overexpressing CuZn-Superoxide dismutase

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The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity

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Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules

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Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=PMCID:PMC6763872&resulttype=core&format=json

12 May 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=PMCID:PMC6763872&resulttype=core&format=json

12 May 2020

PubMed publication ID

11588178

1 reference