Deacetylation of nuclear LC3 drives autophagy initiation under starvation - Test2 - elhamkhani - TriplyDB

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

http://www.wikidata.org/entity/Q28255696

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)SIRT1: A Novel Target for the Treatment of Muscular Dystrophies Age-Associated Weight Gain, Leptin, and SIRT1: A Possible Role for Hypothalamic SIRT1 in the Prevention of Weight Gain and Aging through Modulation of Leptin Sensitivity Role of SIRT1 in the growth and regulation of normal hematopoietic and leukemia stem cells Autophagy mediates degradation of nuclear lamina Nuclear LC3 Associates with Slowly Diffusing Complexes that Survey the Nucleolus Nuclear DNA damage signalling to mitochondria in ageing Resveratrol ameliorates diet-induced dysregulation of lipid metabolism in zebrafish (Danio rerio).Pharmaceutical screen identifies novel target processes for activation of autophagy with a broad translational potential.A functional endosomal pathway is necessary for lysosome biogenesis in Drosophila.Neuroprotective effect of cellular prion protein (PrPC) is related with activation of alpha7 nicotinic acetylcholine receptor (α7nAchR)-mediated autophagy flux.c-Jun N-terminal kinase activation by nitrobenzoxadiazoles leads to late-stage autophagy inhibition Nucleolin antagonist triggers autophagic cell death in human glioblastoma primary cells and decreased in vivo tumor growth in orthotopic brain tumor model.Role of the phosphatidylinositol-3-kinase/Akt/target of rapamycin pathway during ambidensovirus infection of insect cells.Autophagy in Ischemic Livers: A Critical Role of Sirtuin 1/Mitofusin 2 Axis in Autophagy Induction.Aldehyde dehydrogenase 2 activation in aged heart improves the autophagy by reducing the carbonyl modification on SIRT1.Mechanisms of Selective Autophagy in Normal Physiology and Cancer Caloric restriction blocks neuropathology and motor deficits in Machado-Joseph disease mouse models through SIRT1 pathway.MAP1LC3B overexpression protects against Hermansky-Pudlak syndrome type-1-induced defective autophagy in vitro Functional role of autophagy in gastric cancer.Galangin Induces Autophagy via Deacetylation of LC3 by SIRT1 in HepG2 Cells.TP53INP2/DOR, a mediator of cell autophagy, promotes rDNA transcription via facilitating the assembly of the POLR1/RNA polymerase I preinitiation complex at rDNA promoters.Role of the mammalian ATG8/LC3 family in autophagy: differential and compensatory roles in the spatiotemporal regulation of autophagy.Size, organization, and dynamics of soluble SQSTM1 and LC3-SQSTM1 complexes in living cells The protective role of Sirt1 in vascular tissue: its relationship to vascular aging and atherosclerosis.Differential control of muscle mass in type 1 and type 2 diabetes mellitus.Autophagy at the crossroads of catabolism and anabolism.Sunitinib induces genomic instability of renal carcinoma cells through affecting the interaction of LC3-II and PARP-1.Nicotinamide phosphoribosyltransferase (Nampt) in carcinogenesis: new clinical opportunities.Fine-tuning autophagy: from transcriptional to posttranslational regulation.Nuclear autophagy: An evolutionarily conserved mechanism of nuclear degradation in the cytoplasm.HDACs and HDAC Inhibitors in Cancer Development and Therapy.Emerging connections between RNA and autophagy.Tenovin-6 inhibits proliferation and survival of diffuse large B-cell lymphoma cells by blocking autophagy.The pharmacological regulation of cellular mitophagy.Nicotinamide is an inhibitor of SIRT1 in vitro, but can be a stimulator in cells.Regulating Autophagy as a Therapeutic Target for Diabetic Nephropathy.Standard Immunohistochemical Assays to Assess Autophagy in Mammalian Tissue.Assays to Monitor Autophagy Progression in Cell Cultures.Quo vadis? Interferon-inducible GTPases go to their target membranes via the LC3-conjugation system of autophagy.

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P2860

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

http://www.wikidata.org/entity/Q28255696

description

2015 nî lūn-bûn

@nan

2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

@ast

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

@en

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

@nl

type

label

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

@ast

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

@en

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

@nl

prefLabel

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

@ast

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

@en

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

@nl

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J.MOLCEL.2014.12.013

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P1476

Deacetylation of nuclear LC3 drives autophagy initiation under starvation

@en

P2093

Bo Liu

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

Chunmei Chang

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

Jiali Qian

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

Rui Huang

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

Tianhua Zhou

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

Wei Liu

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

Wei Wan

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

Xin Shou

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

Yinfeng Xu

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

Zhiyuan You

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456-66

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scholarly article

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1688595

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10.1016/J.MOLCEL.2014.12.013

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3

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57

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Jennifer Lippincott-Schwartz

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2015-02-05T00:00:00Z

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25601754

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