Use of cysteine-reactive cross-linkers to probe conformational flexibility of human DJ-1 demonstrates that Glu18 mutations are dimers (Q27683814)

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Language	Label	Description	Also known as
English	Use of cysteine-reactive cross-linkers to probe conformational flexibility of human DJ-1 demonstrates that Glu18 mutations are dimers	scientific article

Statements

scholarly article

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Use of cysteine-reactive cross-linkers to probe conformational flexibility of human DJ-1 demonstrates that Glu18 mutations are dimers (English)

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object named as

David N Hauser

2

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4

object named as

Mark R Cookson

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author name string

Janani Prahlad

1

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Nicole M Milkovic

3

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Mark A Wilson

5

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language of work or name

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publication date

September 2014

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Journal of Neurochemistry

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130

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6

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839-53

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Conservation of oxidative protein stabilization in an insect homologue of parkinsonism-associated protein DJ-1

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Formation of a Stabilized Cysteine Sulfinic Acid Is Critical for the Mitochondrial Function of the Parkinsonism Protein DJ-1

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Cysteine p K a Depression by a Protonated Glutamic Acid in Human DJ-1

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20 March 2017

Structural Impact of Three Parkinsonism-Associated Missense Mutations on Human DJ-1 † , ‡

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Sensitivity to oxidative stress in DJ-1-deficient dopamine neurons: an ES- derived cell model of primary Parkinsonism

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Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition

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Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain

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Crystal structure of DJ-1/RS and implication on familial 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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The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease

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Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease

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Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism

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Using NMRView to visualize and analyze the NMR spectra of macromolecules

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20 March 2017

L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4156530

20 March 2017

DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras

1 reference

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20 March 2017

Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1

1 reference

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DJ-1-dependent regulation of oxidative stress in the retinal pigment epithelium (RPE)

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Monomer DJ-1 and its N-terminal sequence are necessary for mitochondrial localization of DJ-1 mutants

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Parkinson's disease-associated mutations in DJ-1 modulate its dimerization in living cells.

1 reference

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Mitochondrial dysfunction and oxidative stress in Parkinson's disease and monogenic parkinsonism

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ROS-dependent regulation of Parkin and DJ-1 localization during oxidative stress in neurons.

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Loss of DJ-1 does not affect mitochondrial respiration but increases ROS production and mitochondrial permeability transition pore opening

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DJ-1 knock-down impairs astrocyte mitochondrial function

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L10p and P158DEL DJ‐1 mutations cause protein instability, aggregation, and dimerization impairments

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Loss of the Parkinson's disease-linked gene DJ-1 perturbs mitochondrial dynamics

1 reference

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DJ-1 is critical for mitochondrial function and rescues PINK1 loss of function

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Parkinson's disease: insights from pathways

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DJ-1 protects against oxidative damage by regulating the thioredoxin/ASK1 complex.

1 reference

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Structural effects of Parkinson's disease linked DJ-1 mutations.

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1 reference

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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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A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization.

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

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12 December 2020

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10.1111/JNC.12763

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