Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells. - Wikidata - wikimedia - TriplyDB

Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells.

Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells.

http://www.wikidata.org/entity/Q35208410

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Genome-wide RNAi screen identifies the Parkinson disease GWAS risk locus SREBF1 as a regulator of 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 Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection Hepatocellular carcinoma mouse models: Hepatitis B virus-associated hepatocarcinogenesis and haploinsufficient tumor suppressor genes A Mechanistic Review of Mitophagy and Its Role in Protection against Alcoholic Liver Disease Endogenous Parkin Preserves Dopaminergic Substantia Nigral Neurons following Mitochondrial DNA Mutagenic Stress Evidence for a common biological pathway linking three Parkinson's disease-causing genes: parkin, PINK1 and DJ-1 Molecular mechanisms of mitochondrial autophagy/mitophagy in the heart Mitochondria: in sickness and in health A Rab5 endosomal pathway mediates Parkin-dependent mitochondrial clearance.PINK1/Parkin-Dependent Mitochondrial Surveillance: From Pleiotropy to Parkinson's Disease.Increased hepatic CD36 expression with age is associated with enhanced susceptibility to nonalcoholic fatty liver disease.Mitochondrial dysfunction and decrease in body weight of a transgenic knock-in mouse model for TDP-43.Parkin regulation of CHOP modulates susceptibility to cardiac endoplasmic reticulum stress.Parkin in the regulation of fat uptake and mitochondrial biology: emerging links in the pathophysiology of Parkinson's disease.Inhibition of neuronal cell mitochondrial complex I with rotenone increases lipid β-oxidation, supporting acetyl-coenzyme A levels.Mitochondrial quality control mediated by PINK1 and Parkin: links to parkinsonism.A genome wide association study for backfat thickness in Italian Large White pigs highlights new regions affecting fat deposition including neuronal genes.Mfge8 promotes obesity by mediating the uptake of dietary fats and serum fatty acids.Mitophagy and cancer.Parkin mutations reduce the complexity of neuronal processes in iPSC-derived human neurons Convergence of Parkin, PINK1, and α-Synuclein on Stress-induced Mitochondrial Morphological Remodeling PINK1 Is Dispensable for Mitochondrial Recruitment of Parkin and Activation of Mitophagy in Cardiac Myocytes.Parkinsonism due to mutations in PINK1, parkin, and DJ-1 and oxidative stress and mitochondrial pathways.Ranbp2 haploinsufficiency mediates distinct cellular and biochemical phenotypes in brain and retinal dopaminergic and glia cells elicited by the Parkinsonian neurotoxin, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP).Lipid profiling of parkin-mutant human skin fibroblasts.Loss of parkin promotes lipid rafts-dependent endocytosis through accumulating caveolin-1: implications for Parkinson's disease Copy number variations associated with obesity-related traits in African Americans: a joint analysis between GENOA and HyperGEN.Glycogen synthase kinase-3-mediated phosphorylation of serine 73 targets sterol response element binding protein-1c (SREBP-1c) for proteasomal degradation Parkin protein deficiency exacerbates cardiac injury and reduces survival following myocardial infarction Parkin-mediated mitophagy directs perinatal cardiac metabolic maturation in mice HIF-driven SF3B1 induces KHK-C to enforce fructolysis and heart disease.Integration of cellular bioenergetics with mitochondrial quality control and autophagy.Aging and Autophagy in the Heart Declines in Drp1 and parkin expression underlie DNA damage-induced changes in mitochondrial length and neuronal death.Reduced intestinal lipid absorption and body weight-independent improvements in insulin sensitivity in high-fat diet-fed Park2 knockout mice.Association of a PARK2 Germline Variant and Epithelial Ovarian Cancer in a Southern Brazilian Population.Pathways to neurodegeneration: mechanistic insights from GWAS in Alzheimer's disease, Parkinson's disease, and related disorders Mfge8 regulates enterocyte lipid storage by promoting enterocyte triglyceride hydrolase activity.The ubiquitin ligase parkin mediates resistance to intracellular pathogens

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P2860

Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells.

http://www.wikidata.org/entity/Q35208410

description

2011 nî lūn-bûn

@nan

2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells.

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Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells.

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type

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Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells.

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Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells.

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Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells.

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Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells.

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Journal of Clinical Investigation

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Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells.

@en

P2093

Alan T Remaley

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Alexander V Bocharov

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Alexandra Cohen

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Audrey Noguchi

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Danielle Springer

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Der-Fen Suen

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Kye-Young Kim

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M Hasina Akter

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Marcelo Amar

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Mark V Stevens

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P2860

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

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

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

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

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

Defective fatty acid uptake modulates insulin responsiveness and metabolic responses to diet in CD36-null mice

LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor

Protein-protein interactions in the mammalian brain

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

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3701-3712

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10.1172/JCI44736

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9

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121

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2011-08-25T00:00:00Z

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21865652

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3171101

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