PINK1 is selectively stabilized on impaired mitochondria to activate Parkin - Test2 - elhamkhani - TriplyDB

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

http://www.wikidata.org/entity/Q21145802

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Brain region specific mitophagy capacity could contribute to selective neuronal vulnerability in Parkinson's disease The phosphorylation-dependent regulation of mitochondrial proteins in stress responses Parkinson's disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria Genetic perspective on the role of the autophagy-lysosome pathway in Parkinson disease Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65 ULK1 translocates to mitochondria and phosphorylates FUNDC1 to regulate mitophagy Functional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's disease Ubiquitin is phosphorylated by PINK1 to activate parkin PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin Genome-wide RNAi screen identifies the Parkinson disease GWAS risk locus SREBF1 as a regulator of mitophagy Mitochondrial Parkin recruitment is impaired in neurons derived from mutant PINK1 induced pluripotent stem cells p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells AMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62/SQSTM1 Short mitochondrial ARF triggers Parkin/PINK1-dependent mitophagy Phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1)-dependent ubiquitination of endogenous Parkin attenuates mitophagy: study in human primary fibroblasts and induced pluripotent stem cell-derived neurons Autoregulation of Parkin activity through its ubiquitin-like domain The role of oxidative stress in Parkinson's disease High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402 PINK1 cleavage at position A103 by the mitochondrial protease PARL.Cytosolic cleaved PINK1 represses Parkin translocation to mitochondria and mitophagy Inactivation of Pink1 gene in vivo sensitizes dopamine-producing neurons to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and can be rescued by autosomal recessive Parkinson disease genes, Parkin or DJ-1 Adaptor proteins MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission.USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria The Parkinson's disease-linked proteins Fbxo7 and Parkin interact to mediate mitophagy Hexokinase activity is required for recruitment of parkin to depolarized mitochondria Genome-wide RNAi screen identifies ATPase inhibitory factor 1 (ATPIF1) as essential for PARK2 recruitment and mitophagy Hsp90-Cdc37 chaperone complex regulates Ulk1- and Atg13-mediated mitophagy Oxidative stress-induced signaling pathways implicated in the pathogenesis of Parkinson's disease Glucocerebrosidase is shaking up the synucleinopathies G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy Identification of the ubiquitin-like domain of midnolin as a new glucokinase interaction partner Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection Neurological surgery at the National Institutes of Health.

P2860

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P2860

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

http://www.wikidata.org/entity/Q21145802

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@ast

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@en

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@en-gb

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@nl

type

label

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@ast

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@en

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@en-gb

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@nl

altLabel

PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin

@en

prefLabel

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@ast

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@en

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@en-gb

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@nl

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JOURNAL.PBIO.1000298

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P1476

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

@en

P2093

Atsushi Tanaka

http://www.w3.org/2001/XMLSchema#string

Clement A Gautier

http://www.w3.org/2001/XMLSchema#string

Der-Fen Suen

http://www.w3.org/2001/XMLSchema#string

Derek P Narendra

http://www.w3.org/2001/XMLSchema#string

Jie Shen

http://www.w3.org/2001/XMLSchema#string

Richard J Youle

http://www.w3.org/2001/XMLSchema#string

Seok Min Jin

http://www.w3.org/2001/XMLSchema#string

P2860

Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis

Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RING

Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability

Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission

The kinase domain of mitochondrial PINK1 faces the cytoplasm

Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins

Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease

Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy.

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e1000298

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scholarly article

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5521

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10.1371/JOURNAL.PBIO.1000298

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1

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8

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2010-01-01T00:00:00Z

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41401266

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20126261

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2811155

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