Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation. - Wikidata - wikimedia - TriplyDB

Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation.

Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation.

http://www.wikidata.org/entity/Q42071947

about

Ubiquitin modifications Myosins, Actin and Autophagy Ubiquitin phosphorylation in Parkinson's disease: Implications for pathogenesis and treatment Expanding the ubiquitin code through post-translational modification GDNF-Ret signaling in midbrain dopaminergic neurons and its implication for Parkinson disease Probes of ubiquitin E3 ligases enable systematic dissection of parkin activation Site-specific Interaction Mapping of Phosphorylated Ubiquitin to Uncover Parkin Activation.Structure-guided mutagenesis reveals a hierarchical mechanism of Parkin activation.Quantitative proteomic analysis of Parkin substrates in Drosophila neurons.A Ubl/ubiquitin switch in the activation of Parkin The ubiquitin signal and autophagy: an orchestrated dance leading to mitochondrial degradation Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria.Covalent ISG15 conjugation positively regulates the ubiquitin E3 ligase activity of parkin PINK1, Parkin, and Mitochondrial Quality Control: What can we Learn about Parkinson's Disease Pathobiology?Specificity and disease in the ubiquitin system Parkin-phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activity.The mitochondrial kinase PINK1: functions beyond mitophagy.Structural insights into the catalysis and regulation of E3 ubiquitin ligases.Parkin and mitophagy in cancer.Rabs, Membrane Dynamics, and Parkinson's Disease.Parkin and PINK1 functions in oxidative stress and neurodegeneration.Post translational modification of Parkin.Ubiquitin and Parkinson's disease through the looking glass of genetics.Mitophagy Transcriptome: Mechanistic Insights into Polyphenol-Mediated Mitophagy.Mitochondrial quality control in amyotrophic lateral sclerosis: towards a common pathway?pUBLically unzipping Parkin: how phosphorylation exposes a ligase bit by bit.Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1.PINK1 Primes Parkin-Mediated Ubiquitination of PARIS in Dopaminergic Neuronal Survival.Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis.Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations.Regulation of mitophagy by the ubiquitin pathway in neurodegenerative diseases.AMPKα2 Protects Against the Development of Heart Failure by Enhancing Mitophagy via PINK1 Phosphorylation.The Anthelmintic Drug Niclosamide and its Analogues Activate the Parkinson's Disease Associated Protein Kinase PINK1.Structure of PINK1 in complex with its substrate ubiquitin.An invisible ubiquitin conformation is required for efficient phosphorylation by PINK1.Knockdown of the mitochondria-localized protein p13 protects against experimental parkinsonism.Mechanism and regulation of the Lys6-selective deubiquitinase USP30.RING-Between-RING E3 Ligases: Emerging Themes amid the Variations.UbMES and UbFluor: Novel probes for ring-between-ring (RBR) E3 ubiquitin ligase PARKIN.CDK5-Mediated Phosphorylation-Dependent Ubiquitination and Degradation of E3 Ubiquitin Ligases GP78 Accelerates Neuronal Death in Parkinson's Disease.

P2860

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P2860

Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation.

http://www.wikidata.org/entity/Q42071947

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年学术文章

@wuu

2015年学术文章

@zh-cn

2015年学术文章

@zh-hans

2015年学术文章

@zh-my

2015年学术文章

@zh-sg

2015年學術文章

@yue

2015年學術文章

@zh

2015年學術文章

@zh-hant

name

Binding to serine 65-phosphory ...... hosphorylation and activation.

@en

Binding to serine 65-phosphory ...... hosphorylation and activation.

@nl

type

label

Binding to serine 65-phosphory ...... hosphorylation and activation.

@en

Binding to serine 65-phosphory ...... hosphorylation and activation.

@nl

prefLabel

Binding to serine 65-phosphory ...... hosphorylation and activation.

@en

Binding to serine 65-phosphory ...... hosphorylation and activation.

@nl

P1433

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P2860

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P1433

P1476

Binding to serine 65-phosphory ...... phosphorylation and activation

@en

P2093

Alan R Prescott

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

Alba Gonzalez

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

Anthony G Hope

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

Axel Knebel

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

Clare Johnson

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

Daan M F van Aalten

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

Dario R Alessi

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

Helen Walden

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

Jinwei Zhang

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

Julien Peltier

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

P2860

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65

Ubiquitin is phosphorylated by PINK1 to activate parkin

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Autoregulation of Parkin activity through its ubiquitin-like domain

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis

Hereditary early-onset Parkinson's disease caused by mutations in PINK1

PINK1 and Parkin – mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson's disease

Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tethering

P304

939-954

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scholarly article

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10.15252/EMBR.201540352

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P433

8

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P478

16

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P50

Agne Kazlauskaite

P577

2015-06-25T00:00:00Z

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P5875

279278262

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26116755

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P921

phosphorylation

P932

4552487

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