Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal death (Q24323228)

9

object named as

Zbigniew K Wszolek

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Eng-King Tan

11

object named as

Eng-King Tan

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Matthew J. Farrer

8

object named as

Matt Farrer

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author name string

Dario C Angeles

1

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Bong-Hwa Gan

2

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Luisa Onstead

3

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Yi Zhao

4

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Kah-Leong Lim

5

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Justus Dachsel

6

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Heather Melrose

Localization of LRRK2 to membranous and vesicular structures in mammalian brain

7

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language of work or name

English

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publication date

December 2011

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published in

Human Mutation

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volume

32

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issue

12

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page(s)

1390-7

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cites work

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Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin

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Parkinson's disease: mechanisms and models

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Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium.

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Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein

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LRRK2 expression linked to dopamine-innervated areas

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The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity

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The Parkinson's disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase that stimulates kinase activity

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Mitochondrial peroxiredoxin-3 protects hippocampal neurons from excitotoxic injury in vivo

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Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product

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Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila

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LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity

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Parkin protects human dopaminergic neuroblastoma cells against dopamine-induced apoptosis

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Identification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: evidence of a common founder across European populations

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Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha.

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Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors

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Increased susceptibility of MER5 (peroxiredoxin III) knockout mice to LPS-induced oxidative stress

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Wild-type LRRK2 but not its mutant attenuates stress-induced cell death via ERK pathway

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Microperoxisome distribution in the central nervous system of the rat

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Anatomical localization of leucine-rich repeat kinase 2 in mouse brain

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Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease

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Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis

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PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1

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Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling

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Mitochondria and dopamine: new insights into recessive parkinsonism

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Kinase activity of mutant LRRK2 mediates neuronal toxicity

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Pathogenic mutations in Parkinson disease

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4-Hydroxy-2-nonenal-modified glyceraldehyde-3-phosphate dehydrogenase is degraded by cathepsin G.

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The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2.

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Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity

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Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology

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Cytosolic peroxiredoxin attenuates the activation of Jnk and p38 but potentiates that of Erk in Hela cells stimulated with tumor necrosis factor-alpha

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inferred from DOI database lookup

7 January 2021

based on heuristic

Intense oxidative DNA damage promoted by L-dopa and its metabolites. Implications for neurodegenerative disease

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1002/HUMU.21582

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

21850687

1 reference

Consolidated OpenCitations Corpus – April 2017