C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1.
about
Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation updatePINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagyBiochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1)PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signalingPINK1 cleavage at position A103 by the mitochondrial protease PARL.Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fissionPINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neuronsBAG5 protects against mitochondrial oxidative damage through regulating PINK1 degradationStructure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of NeuroprotectionRegulation of mitochondrial functions by protein phosphorylation and dephosphorylationMitochondrial impairment increases FL-PINK1 levels by calcium-dependent gene expressionLoss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stressThe PINK1/Parkin pathway regulates mitochondrial morphologyPINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagyMicrotubule affinity-regulating kinase 2 (MARK2) turns on phosphatase and tensin homolog (PTEN)-induced kinase 1 (PINK1) at Thr-313, a mutation site in Parkinson disease: effects on mitochondrial transportMitochondrial cell death control in familial Parkinson disease.Significance of the parkin and PINK1 gene in Jordanian families with incidences of young-onset and juvenile parkinsonismSilencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells.DJ-1, PINK1, and their effects on mitochondrial pathwaysPINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondriaPINK1 expression increases during brain development and stem cell differentiation, and affects the development of GFAP-positive astrocytes.PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy.In Vitro Comparison of the Activity Requirements and Substrate Specificity of Human and Triboleum castaneum PINK1 Orthologues.Rescue of PINK1 protein null-specific mitochondrial complex IV deficits by ginsenoside Re activation of nitric oxide signalingCharacterization of PINK1 (PTEN-induced putative kinase 1) mutations associated with Parkinson disease in mammalian cells and DrosophilaCharacterization of PINK1 processing, stability, and subcellular localization.PINK1 deficiency attenuates astrocyte proliferation through mitochondrial dysfunction, reduced AKT and increased p38 MAPK activation, and downregulation of EGFR.Kinase signaling pathways as potential targets in the treatment of Parkinson's disease.Review: Familial Parkinson's disease--genetics, clinical phenotype and neuropathology in relation to the common sporadic form of the disease.Identification of direct tyrosine kinase substrates based on protein kinase assay-linked phosphoproteomicsThe role of PTEN-induced kinase 1 in mitochondrial dysfunction and dynamics.Oxidative stress mechanisms underlying Parkinson's disease-associated neurodegeneration in C. elegans.Tickled PINK1: mitochondrial homeostasis and autophagy in recessive Parkinsonism.A critical evaluation of the ubiquitin-proteasome system in Parkinson's diseaseOxidative modifications, mitochondrial dysfunction, and impaired protein degradation in Parkinson's disease: how neurons are lost in the Bermuda triangle.PINK1-dependent phosphorylation of PINK1 and Parkin is essential for mitochondrial quality control.Mitochondrial medicine for neurodegenerative diseases.Molecular mechanisms of PINK1-related neurodegeneration.
P2860
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P2860
C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
C-terminal truncation and Park ...... vity of PTEN-induced kinase-1.
@en
type
label
C-terminal truncation and Park ...... vity of PTEN-induced kinase-1.
@en
prefLabel
C-terminal truncation and Park ...... vity of PTEN-induced kinase-1.
@en
P2093
P50
P356
P1476
C-terminal truncation and Park ...... vity of PTEN-induced kinase-1.
@en
P2093
Chou Hung Sim
Daisy Sio Seng Lio
Janetta G Culvenor
Su San Mok
P304
P356
10.1093/HMG/DDL398
P577
2006-09-25T00:00:00Z