Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway. - Wikidata - awgldk - TriplyDB

Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway.

Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway.

http://www.wikidata.org/entity/Q40047094

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Lafora progressive myoclonus epilepsy: NHLRC1 mutations affect glycogen metabolism Laforin, the most common protein mutated in Lafora disease, regulates autophagy Laforin is required for the functional activation of malin in endoplasmic reticulum stress resistance in neuronal cells Early-onset Lafora body disease Loss of GABAergic cortical neurons underlies the neuropathology of Lafora disease AMP-activated kinase AMPK is expressed in boar spermatozoa and regulates motility AMP-activated protein kinase phosphorylates R5/PTG, the glycogen targeting subunit of the R5/PTG-protein phosphatase 1 holoenzyme, and accelerates its down-regulation by the laforin-malin complex Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin Co-chaperone CHIP stabilizes aggregate-prone malin, a ubiquitin ligase mutated in Lafora disease.A PTG variant contributes to a milder phenotype in Lafora disease Lafora disease E3-ubiquitin ligase malin is related to TRIM32 at both the phylogenetic and functional level Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity The laforin-malin complex, involved in Lafora disease, promotes the incorporation of K63-linked ubiquitin chains into AMP-activated protein kinase beta subunits.Genetic depletion of the malin E3 ubiquitin ligase in mice leads to lafora bodies and the accumulation of insoluble laforin Minireview: hey U(PS): metabolic and proteolytic homeostasis linked via AMPK and the ubiquitin proteasome system.Increased oxidative stress and impaired antioxidant response in Lafora disease.Dimerization of the glucan phosphatase laforin requires the participation of cysteine 329.PaCS is a novel cytoplasmic structure containing functional proteasome and inducible by cytokines/trophic factors.The laforin-malin complex negatively regulates glycogen synthesis by modulating cellular glucose uptake via glucose transporters.The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.Laforin, a dual-specificity phosphatase involved in Lafora disease, is phosphorylated at Ser25 by AMP-activated protein kinase.Malin regulates Wnt signaling pathway through degradation of dishevelled2 Laforin, a protein with many faces: glucan phosphatase, adapter protein, et alii.Loss of protein targeting to glycogen sensitizes human hepatocellular carcinoma cells towards glucose deprivation mediated oxidative stress and cell death Deciphering the role of malin in the lafora progressive myoclonus epilepsy Neuronatin-mediated aberrant calcium signaling and endoplasmic reticulum stress underlie neuropathology in Lafora disease Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity.Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease.Glycogen and its metabolism: some new developments and old themes.Deletions and missense mutations of EPM2A exacerbate unfolded protein response and apoptosis of neuronal cells induced by endoplasm reticulum stress Hyperphosphorylation and aggregation of Tau in laforin-deficient mice, an animal model for Lafora disease.Novel mutation in the NHLRC1 gene in a Malian family with a severe phenotype of Lafora disease.Structural insights into glucan phosphatase dynamics using amide hydrogen-deuterium exchange mass spectrometry.Lafora disease: insights into neurodegeneration from plant metabolism.Laforin-malin complex degrades polyglucosan bodies in concert with glycogen debranching enzyme and brain isoform glycogen phosphorylase The regulation of muscle glycogen: the granule and its proteins.Phenotype variations in Lafora progressive myoclonus epilepsy: possible involvement of genetic modifiers?Glycogen phosphorylation and Lafora disease.Pathogenesis of Lafora Disease: Transition of Soluble Glycogen to Insoluble Polyglucosan.Regulation of Carbohydrate Metabolism, Lipid Metabolism, and Protein Metabolism by AMPK.

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P2860

Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway.

http://www.wikidata.org/entity/Q40047094

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2007 nî lūn-bûn

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Regulation of glycogen synthes ...... ivated protein kinase pathway.

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Regulation of glycogen synthes ...... ivated protein kinase pathway.

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Human Molecular Genetics

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Regulation of glycogen synthes ...... ivated protein kinase pathway.

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P2093

Belen Garcia-Fojeda

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Carmen Aguado

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Erwin Knecht

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Joan Josep Guinovart

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Jorge Dominguez

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Jose Serratosa

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José Vicente Gimeno-Alcañiz

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Mar Garcia-Rocha

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Maria Carmen Solaz-Fuster

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Maria Elena Fernandez-Sanchez

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P2860

Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade

A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2)

Organizing glucose disposal: emerging roles of the glycogen targeting subunits of protein phosphatase-1

Glycogen and its Metabolism

Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation

Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin.

The Lafora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain

The regulation of AMP-activated protein kinase by phosphorylation

Characterization of Gac1p, a regulatory subunit of protein phosphatase type I involved in glycogen accumulation in Saccharomyces cerevisiae.

Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates

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667-678

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10.1093/HMG/DDM339

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5

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17

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Santiago Rodriguez de Córdoba

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2007-11-20T00:00:00Z

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5818677

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18029386

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