On the oligomeric state of DJ-1 protein and its mutants associated with Parkinson Disease. A combined computational and in vitro study. (Q40132686)

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30 December 2019

title

On the oligomeric state of DJ-1 protein and its mutants associated with Parkinson Disease. A combined computational and in vitro study (English)

1 reference

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30 December 2019

main subject

computational biology

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1 reference

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30 December 2019

Paolo Carloni

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30 December 2019

Stefano Gustincich

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30 December 2019

Aneta Jezierska

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30 December 2019

Fernando E Herrera

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30 December 2019

Zeno Scotto Lavina

series ordinal

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30 December 2019

language of work or name

English

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publication date

15 May 2007

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Journal of Biological Chemistry

30 December 2019

published in

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30 December 2019

volume

282

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30 December 2019

issue

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30 December 2019

page(s)

24905-24914

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Molecular pathophysiology of Parkinson's disease

30 December 2019

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The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease

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The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease

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Dimerization of Parkinson's disease-causing DJ-1 and formation of high molecular weight complexes in human brain

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The role of pathogenic DJ-1 mutations in Parkinson's disease.

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PARK7 DJ-1 protects against degeneration of nigral dopaminergic neurons in Parkinson's disease rat model

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Increased level of DJ-1 in the cerebrospinal fluids of sporadic Parkinson's disease

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The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein

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The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis

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The expression of DJ-1 (PARK7) in normal human CNS and idiopathic Parkinson's disease

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Oxidative damage of DJ-1 is linked to sporadic Parkinson and Alzheimer diseases

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Mutational analysis of DJ-1 in Drosophila implicates functional inactivation by oxidative damage and aging

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Nigrostriatal dopaminergic deficits and hypokinesia caused by inactivation of the familial Parkinsonism-linked gene DJ-1

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Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress.

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Reduced anti-oxidative stress activities of DJ-1 mutants found in Parkinson's disease patients

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Cysteine-106 of DJ-1 is the most sensitive cysteine residue to hydrogen peroxide-mediated oxidation in vivo in human umbilical vein endothelial cells

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The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization

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The DJ-1L166P mutant protein associated with early onset Parkinson's disease is unstable and forms higher-order protein complexes

21 January 2018

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Association of DJ-1 and parkin mediated by pathogenic DJ-1 mutations and oxidative stress

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Familial Parkinson's disease-associated L166P mutation disrupts DJ-1 protein folding and function

21 January 2018

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21 January 2018

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Identifiers

DOI

10.1074/JBC.M701013200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17504761%20AND%20SRC:MED&resulttype=core&format=json

30 December 2019

1 reference

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