(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation - Wikidata - wikimedia - TriplyDB

(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation

(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation

http://www.wikidata.org/entity/Q36078552

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Ubiquitin modifications Ubiquitin phosphorylation in Parkinson's disease: Implications for pathogenesis and treatment Parkin Regulation and Neurodegenerative Disorders The Function of Autophagy in Neurodegenerative Diseases Expanding the ubiquitin code through post-translational modification The PINK1 p.I368N mutation affects protein stability and ubiquitin kinase activity The ubiquitin signal and autophagy: an orchestrated dance leading to mitochondrial degradation PINK1, Parkin, and Mitochondrial Quality Control: What can we Learn about Parkinson's Disease Pathobiology?Heterozygous PINK1 p.G411S increases risk of Parkinson's disease via a dominant-negative mechanism.Ubiquitin S65 phosphorylation engenders a pH-sensitive conformational switch.Parkin and PINK1 functions in oxidative stress and neurodegeneration.Ubiquitin and Parkinson's disease through the looking glass of genetics.miR-27a and miR-27b regulate autophagic clearance of damaged mitochondria by targeting PTEN-induced putative kinase 1 (PINK1).Non-radioactive in vitro PINK1 Kinase Assays Using Ubiquitin or Parkin as Substrate.PINK1 Primes Parkin-Mediated Ubiquitination of PARIS in Dopaminergic Neuronal Survival.Hexokinases link DJ-1 to the PINK1/parkin pathway.Direct Neuronal Reprogramming for Disease Modeling Studies Using Patient-Derived Neurons: What Have We Learned?S-Nitrosylation of PINK1 Attenuates PINK1/Parkin-Dependent Mitophagy in hiPSC-Based Parkinson's Disease Models.Development of phospho-specific Rab protein antibodies to monitor in vivo activity of the LRRK2 Parkinson's disease kinase.Mitochondrial targeted HSP90 inhibitor Gamitrinib-TPP (G-TPP) induces PINK1/Parkin-dependent mitophagy.The genetic architecture of mitochondrial dysfunction in Parkinson's disease.Intra- and Intercellular Quality Control Mechanisms of Mitochondria.PINK1 import regulation; a fine system to convey mitochondrial stress to the cytosol.Mechanisms, pathophysiological roles and methods for analyzing mitophagy - recent insights.Evidence that phosphorylated ubiquitin signaling is involved in the etiology of Parkinson's disease.Protein molecular modeling techniques investigating novel TAB2 variant R347X causing cardiomyopathy and congenital heart defects in multigenerational family.Generation of phospho-ubiquitin variants by orthogonal translation reveals codon skipping.Whole Exome Sequencing and Molecular Modeling of a Missense Variant in TNFAIP3 That Segregates with Disease in a Family with Chronic Urticaria and Angioedema.Deficiency of parkin and PINK1 impairs age-dependent mitophagy in Drosophila.

P2860

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P2860

(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation

http://www.wikidata.org/entity/Q36078552

description

2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

@zh-cn

name

(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation

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(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation

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label

(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation

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(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation

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prefLabel

(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation

@ast

(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation

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(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation

@en

P2093

Anneliese R Hill

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

Dennis W Dickson

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

Isidre Ferrer

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

Jeannette N Stankowski

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

José M Arbelo

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

Li Chen

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

Maya Ando

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

Monica Castanedes-Casey

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

Owen A Ross

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

Roman Hudec

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

P2860

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

Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis

Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tethering

PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila

Phosphorylation by PINK1 releases the UBL domain and initializes the conformational opening of the E3 ubiquitin ligase Parkin

Structure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13

Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture

WHAT IF: a molecular modeling and drug design program

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1114-1130

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10.15252/EMBR.201540514

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P433

9

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P478

16

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Fabienne C. Fiesel

Wolfdieter Springer

Oswaldo Lorenzo Betancor

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2015-07-10T00:00:00Z

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279988222

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26162776

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phosphorylation

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4576981

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