Identification of a novel Zn2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parkin. - Wikidata - wikimedia - TriplyDB

Identification of a novel Zn2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parkin.

Identification of a novel Zn2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parkin.

http://www.wikidata.org/entity/Q43123357

about

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin Autoregulation of Parkin activity through its ubiquitin-like domain Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection Chaperone-Mediated Autophagy and Mitochondrial Homeostasis in Parkinson's Disease Deconvoluting the complexity of autophagy and Parkinson's disease for potential therapeutic purpose RBR E3 ubiquitin ligases: new structures, new insights, new questions Parkin structure and function Pathologic and therapeutic implications for the cell biology of parkin Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tethering Selective Recruitment of an E2 Ubiquitin Complex by an E3 Ubiquitin Ligase Structure of the human Parkin ligase domain in an autoinhibited state Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases A molecular explanation for the recessive nature of parkin-linked Parkinson’s disease Structure of parkin reveals mechanisms for ubiquitin ligase activation Targeting Pink1-Parkin-mediated mitophagy for treating liver injury Mutant Parkin impairs mitochondrial function and morphology in human fibroblasts PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy The Monoamine Brainstem Reticular Formation as a Paradigm for Re-Defining Various Phenotypes of Parkinson's Disease Owing Genetic and Anatomical Specificity.Parkin disease: a clinicopathologic entity?Decreased circulating Zinc levels in Parkinson's disease: a meta-analysis study Following Ariadne's thread: a new perspective on RBR ubiquitin ligases Identification and molecular characterization of Parkin in Clonorchis sinensis.Parkinson's Disease in Saudi Patients: A Genetic Study The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease Genome-wide analysis of copy number variations identifies PARK2 as a candidate gene for autism spectrum disorder.Covalent ISG15 conjugation positively regulates the ubiquitin E3 ligase activity of parkin Genome-wide identification and characterization of RBR ubiquitin ligase genes in soybean.Parkin, A Top Level Manager in the Cell's Sanitation Department.Parkin, PINK1 and mitochondrial integrity: emerging concepts of mitochondrial dysfunction in Parkinson's disease.Regulation of Parkin E3 ubiquitin ligase activity.Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences.Ubiquitin in regulation of spindle apparatus and its positioning: implications in development and disease.Structural studies of parkin and sacsin: Mitochondrial dynamics in neurodegenerative diseases.Alterations in the E3 ligases Parkin and CHIP result in unique metabolic signaling defects and mitochondrial quality control issues.Reduced expression of PARK2 in manganese-exposed smelting workers.Phospho-ubiquitin: upending the PINK-Parkin-ubiquitin cascade Specificity and disease in the ubiquitin system The Effects of Variants in the Parkin, PINK1, and DJ-1 Genes along with Evidence for their Pathogenicity.Parkin-phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activity.Dyrk1A phosphorylates parkin at Ser-131 and negatively regulates its ubiquitin E3 ligase activity.

P2860

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P2860

Identification of a novel Zn2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parkin.

http://www.wikidata.org/entity/Q43123357

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

@wuu

2009年学术文章

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2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh-hant

name

Identification of a novel Zn2+ ...... nson-related E3 ligase parkin.

@en

Identification of a novel Zn2+ ...... nson-related E3 ligase parkin.

@nl

type

label

Identification of a novel Zn2+ ...... nson-related E3 ligase parkin.

@en

Identification of a novel Zn2+ ...... nson-related E3 ligase parkin.

@nl

prefLabel

Identification of a novel Zn2+ ...... nson-related E3 ligase parkin.

@en

Identification of a novel Zn2+ ...... nson-related E3 ligase parkin.

@nl

P1433

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P1433

Journal of Biological Chemistry

P1476

Identification of a novel Zn2+ ...... inson-related E3 ligase parkin

@en

P2093

Steven A Beasley

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

Ventzislava A Hristova

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

P2860

The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity

Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1

A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity

Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7

Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation

Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2

Parkin ubiquitinates and promotes the degradation of RanBP2

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

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14978-14986

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24250939

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19339245

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Parkinson's disease

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2685680

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