Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress.
about
Functional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's diseaseBiochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1)Phosphorylation 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.Cytosolic cleaved PINK1 represses Parkin translocation to mitochondria and mitophagyThe kinase domain of mitochondrial PINK1 faces the cytoplasmPINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neuronsBAG5 protects against mitochondrial oxidative damage through regulating PINK1 degradationUbiquitin phosphorylation in Parkinson's disease: Implications for pathogenesis and treatmentRecruitment of the oncoprotein v-ErbA to aggresomes.Role of glucose metabolism and ATP in maintaining PINK1 levels during Parkin-mediated mitochondrial damage responses.Mitochondrial regulation of β-cell function: maintaining the momentum for insulin releaseMitochondrial impairment increases FL-PINK1 levels by calcium-dependent gene expressionBeyond mitophagy: cytosolic PINK1 as a messenger of mitochondrial healthThe Parkinson's gene PINK1 regulates cell cycle progression and promotes cancer-associated phenotypesMitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARLPINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65Proteomic characterization of an isolated fraction of synthetic proteasome inhibitor (PSI)-induced inclusions in PC12 cells might offer clues to aggresomes as a cellular defensive response against proteasome inhibition by PSI.Hyperexcitable substantia nigra dopamine neurons in PINK1- and HtrA2/Omi-deficient mice.The PINK1 p.I368N mutation affects protein stability and ubiquitin kinase activityThe human PINK1 locus is regulated in vivo by a non-coding natural antisense RNA during modulation of mitochondrial function.PINK1 defect causes mitochondrial dysfunction, proteasomal deficit and alpha-synuclein aggregation in cell culture models of Parkinson's disease.Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells.PINK1 is degraded through the N-end rule pathwayPathogenic p62/SQSTM1 mutations impair energy metabolism through limitation of mitochondrial substrates.DJ-1, PINK1, and their effects on mitochondrial pathwaysMutations in valosin-containing protein (VCP) decrease ADP/ATP translocation across the mitochondrial membrane and impair energy metabolism in human neurons.Structural determinants of PINK1 topology and dual subcellular distributionUpregulation of human PINK1 gene expression by NFκB signallingRhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin.The ubiquitin-conjugating enzyme UBE2E3 and its import receptor importin-11 regulate the localization and activity of the antioxidant transcription factor NRF2.Epithelial cell mitochondrial dysfunction and PINK1 are induced by transforming growth factor-beta1 in pulmonary fibrosisCytosolic PTEN-induced Putative Kinase 1 Is Stabilized by the NF-κB Pathway and Promotes Non-selective Mitophagy.Pink1 kinase and its membrane potential (Deltaψ)-dependent cleavage product both localize to outer mitochondrial membrane by unique targeting mode.Differential submitochondrial localization of PINK1 as a molecular switch for mediating distinct mitochondrial signaling pathways.Characterization of PINK1 (PTEN-induced putative kinase 1) mutations associated with Parkinson disease in mammalian cells and DrosophilaMitochondrial protein quality control by the proteasome involves ubiquitination and the protease OmiCharacterization of PINK1 processing, stability, and subcellular localization.Cytosolic PINK1 promotes the targeting of ubiquitinated proteins to the aggresome-autophagy pathway during proteasomal stress.PINK1- and Parkin-mediated mitophagy at a glance.
P2860
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P2860
Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress.
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
Altered cleavage and localizat ...... resence of proteasomal stress.
@en
type
label
Altered cleavage and localizat ...... resence of proteasomal stress.
@en
prefLabel
Altered cleavage and localizat ...... resence of proteasomal stress.
@en
P2093
P2860
P50
P1476
Altered cleavage and localizat ...... resence of proteasomal stress.
@en
P2093
Daniel G Healy
David S Latchman
Janice Holton
Kerrie Venner
Kirsten Harvey
Martin D Payne Smith
Miratul M K Muqit
Patrick M Abou-Sleiman
Simon Eaton
P2860
P304
P356
10.1111/J.1471-4159.2006.03845.X
P407
P50
P577
2006-07-01T00:00:00Z