Abnormal metabolism of glycogen phosphate as a cause for Lafora disease. - Wikidata - awgldk - TriplyDB

Abnormal metabolism of glycogen phosphate as a cause for Lafora disease.

Abnormal metabolism of glycogen phosphate as a cause for Lafora disease.

http://www.wikidata.org/entity/Q41502630

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Starch binding domain-containing protein 1/genethonin 1 is a novel participant in 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 Protein tyrosine phosphatases--from housekeeping enzymes to master regulators of signal transduction Are there errors in glycogen biosynthesis and is laforin a repair enzyme?Structural basis for the glucan phosphatase activity of Starch Excess4 Structural basis for 2'-phosphate incorporation into glycogen by glycogen synthase Phosphate incorporation during glycogen synthesis and Lafora disease Early-onset Lafora body disease The evolution of glycogen and starch metabolism in eukaryotes gives molecular clues to understand the establishment of plastid endosymbiosis Loss of GABAergic cortical neurons underlies the neuropathology of Lafora disease PTG depletion removes Lafora bodies and rescues the fatal epilepsy of Lafora disease Hexokinase 2, glycogen synthase and phosphorylase play a key role in muscle glycogen supercompensation Deficiency of a glycogen synthase-associated protein, Epm2aip1, causes decreased glycogen synthesis and hepatic insulin resistance Conservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glucan metabolism of the organism Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease.Physiological bases of the K+ and the glutamate/GABA hypotheses of epilepsy.Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin Abnormal glycogen chain length pattern, not hyperphosphorylation, is critical in Lafora disease.Protein degradation and quality control in cells from laforin and malin knockout mice.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 Insights into the mechanism of polysaccharide dephosphorylation by a glucan phosphatase Does abnormal glycogen structure contribute to increased susceptibility to seizures in epilepsy?Dimerization of the glucan phosphatase laforin requires the participation of cysteine 329.Glycogen phosphomonoester distribution in mouse models of the progressive myoclonic epilepsy, Lafora disease.Expression, purification and characterization of soluble red rooster laforin as a fusion protein in Escherichia coli.The laforin-malin complex negatively regulates glycogen synthesis by modulating cellular glucose uptake via glucose transporters.Laforin, a dual-specificity phosphatase involved in Lafora disease, is phosphorylated at Ser25 by AMP-activated protein kinase.Ontogeny of Lafora bodies and neurocytoskeleton changes in Laforin-deficient mice.Laforin, a protein with many faces: glucan phosphatase, adapter protein, et alii.Neurodegeneration and functional impairments associated with glycogen synthase accumulation in a mouse model of Lafora disease Muscle glycogen remodeling and glycogen phosphate metabolism following exhaustive exercise of wild type and laforin knockout mice.Increased laforin and laforin binding to glycogen underlie Lafora body formation in malin-deficient Lafora disease.Deciphering the role of malin in the lafora progressive myoclonus epilepsy Mechanistic Insights into Glucan Phosphatase Activity against Polyglucan Substrates Laforin prevents stress-induced polyglucosan body formation and Lafora disease progression in neurons.Structural mechanisms of plant glucan phosphatases in starch metabolism Glycogen and its metabolism: some new developments and old themes.

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P2860

Abnormal metabolism of glycogen phosphate as a cause for Lafora disease.

http://www.wikidata.org/entity/Q41502630

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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name

Abnormal metabolism of glycogen phosphate as a cause for Lafora disease.

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type

label

Abnormal metabolism of glycogen phosphate as a cause for Lafora disease.

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prefLabel

Abnormal metabolism of glycogen phosphate as a cause for Lafora disease.

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P1433

Journal of Biological Chemistry

P1476

Abnormal metabolism of glycogen phosphate as a cause for Lafora disease.

@en

P2093

Berge A Minassian

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Catalina Meyer

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Dyann Segvich

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Jean Marie Girard

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Julie Turnbull

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Peter J Roach

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Vincent S Tagliabracci

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Xiaochu Zhao

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P2860

Glycogen and its Metabolism

A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease

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

Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)

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

V-Amylose at atomic resolution: X-ray structure of a cycloamylose with 26 glucose residues (cyclomaltohexaicosaose)

Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates

The muscle-specific protein phosphatase PP1G/R(GL)(G(M))is essential for activation of glycogen synthase by exercise

Phosphorylation of C6- and C3-positions of glucosyl residues in starch is catalysed by distinct dikinases

Glycosomes--the organelles of glycogen metabolism

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33816-33825

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scholarly article

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10.1074/JBC.M807428200

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P433

49

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P478

283

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Anna A. Depaoli-Roach

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2008-10-13T00:00:00Z

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18852261

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P921

Protein phosphatase 1, regulatory subunit 3C

Epilepsy, progressive myoclonic epilepsy, type 2 gene alpha

P932

2590708

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