Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

R492X mutation in PTEN-induced putative kinase 1 induced cellular mitochondrial dysfunction and oxidative stress.

Brain research - 10 Sept 2010

Yuan Xiang-Li, Guo Ji-Feng, Shi Zhen-Hua, Xiao Zhi-Qian, Yan Xin-Xiang, Zhao Bao-Lu, Tang Bei-Sha

Abstract excerpt

The identification of rare monogenic forms of Parkinson's disease (PD) has provided tremendous insights into the molecular pathogenesis of the disorder. Mitochondrial dysfunction and oxidative stress are thought to play a prominent role in the pathogenesis of PD, but how the monogenic mutation ge...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Membrane
Share to Fetus
Share to Membrane Potential, Mitochondrial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondria

Share to Oxidative Stress

Share to Parkinson Disease

Share to Protein Kinases

Share to Reactive Oxygen Species

Source

Identifiers

PMID: 20547144
DOI: 10.1016/j.brainres.2010.06.005

Genes

PINK1
PTEN

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20547144-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

R492X mutation in PTEN-induced putative kinase 1 induced cellular mitochondrial dysfunction and oxidative stress.PMID 20547144Read ↗

Mechanisms Associated with PINK1 Mutations in Parkinson's DiseaseSemantic proximity Read ↗

PARK6 PINK1 mutants are defective in maintaining mitochondrial membrane potential and inhibiting ROS formation of substantia nigra dopaminergic neurons.Semantic proximity Read ↗

PINK1 function in health and disease.Semantic proximity Read ↗

Genetic Mutations and Mitochondrial Toxins Shed New Light on the Pathogenesis of Parkinson's DiseaseSemantic proximity Read ↗

Chronic treatment with the complex I inhibitor MPP+ depletes endogenous PTEN-induced kinase 1 (PINK1) via up-regulation of Bcl-2–associated athanogene 6 (BAG6)Semantic proximity Read ↗

Characterization of PINK1 (PTEN-induced putative kinase 1) mutations associated with Parkinson disease in mammalian cells and Drosophila.Semantic proximity Read ↗

The impact of reactive oxygen species and genetic mitochondrial mutations in Parkinson's disease.Semantic proximity Read ↗

Biochemical properties of the kinase PINK1 as sensor protein for mitochondrial damage signalling.Semantic proximity Read ↗

Differential effects of PINK1 nonsense and missense mutations on mitochondrial function and morphology.Semantic proximity Read ↗

A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment.Semantic proximity Read ↗

Mitochondrial-Dependent and Independent Functions of PINK1Semantic proximity Read ↗

Bioenergetic consequences of PINK1 mutations in Parkinson disease.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.