Similar Protein Phosphatases Control Starch Metabolism in Plants and Glycogen Metabolism in Mammals - Wikidata - awgldk - TriplyDB

Similar Protein Phosphatases Control Starch Metabolism in Plants and Glycogen Metabolism in Mammals

Similar Protein Phosphatases Control Starch Metabolism in Plants and Glycogen Metabolism in Mammals

http://www.wikidata.org/entity/Q58035365

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Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)A Tale of Two Sugars: Trehalose 6-Phosphate and Sucrose Genetics of Lafora progressive myoclonic epilepsy: current perspectives Structural basis for the glucan phosphatase activity of Starch Excess4 Structure of the Arabidopsis Glucan Phosphatase LIKE SEX FOUR2 Reveals a Unique Mechanism for Starch Dephosphorylation Phosphoglucan-bound structure of starch phosphatase Starch Excess4 reveals the mechanism for C6 specificity Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates Role of plastid protein phosphatase TAP38 in LHCII dephosphorylation and thylakoid electron flow Conservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glucan metabolism of the organism Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial beta-amylases.Specificity of RCN1-mediated protein phosphatase 2A regulation in meristem organization and stress response in roots.Articulation of three core metabolic processes in Arabidopsis: fatty acid biosynthesis, leucine catabolism and starch metabolism.Arabidopsis At5g39790 encodes a chloroplast-localized, carbohydrate-binding, coiled-coil domain-containing putative scaffold protein Circadian control of carbohydrate availability for growth in Arabidopsis plants at night.Kinetic modeling and exploratory numerical simulation of chloroplastic starch degradation.Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity Quantitative analysis of regulatory flexibility under changing environmental conditions.A redox-regulated chloroplast protein phosphatase binds to starch diurnally and functions in its accumulation Reduction of the cytosolic phosphoglucomutase in Arabidopsis reveals impact on plant growth, seed and root development, and carbohydrate partitioning Signal processing by protein tyrosine phosphorylation in plants.A plastid-localized glycogen synthase kinase 3 modulates stress tolerance and carbohydrate metabolism.Identification of Photosynthesis-Associated C4 Candidate Genes through Comparative Leaf Gradient Transcriptome in Multiple Lineages of C3 and C4 Species.Laforin, a protein with many faces: glucan phosphatase, adapter protein, et alii.The phosphatase laforin crosses evolutionary boundaries and links carbohydrate metabolism to neuronal disease.Modular evolution of phosphorylation-based signalling systems.Mechanistic Insights into Glucan Phosphatase Activity against Polyglucan Substrates Starch metabolism in Arabidopsis Early gene duplication within chloroplastida and its correspondence with relocation of starch metabolism to chloroplasts Unique carbohydrate binding platforms employed by the glucan phosphatases.Structural mechanisms of plant glucan phosphatases in starch metabolism A Survey of Chloroplast Protein Kinases and Phosphatases in Arabidopsis thaliana.Structural insights into glucan phosphatase dynamics using amide hydrogen-deuterium exchange mass spectrometry.Eukaryotic starch degradation: integration of plastidial and cytosolic pathways.The carbohydrate-binding module family 20--diversity, structure, and function.Lafora disease: insights into neurodegeneration from plant metabolism.The regulation of muscle glycogen: the granule and its proteins.Modeling human neurodegenerative diseases in transgenic systems.Mechanisms of regulation of SNF1/AMPK/SnRK1 protein kinases Role of Protein Tyrosine Phosphatases in Plants.Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.

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Similar Protein Phosphatases Control Starch Metabolism in Plants and Glycogen Metabolism in Mammals

http://www.wikidata.org/entity/Q58035365

description

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

im März 2006 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Journal of Biological Chemistry

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в березні 2006

@uk

name

Similar Protein Phosphatases C ...... Glycogen Metabolism in Mammals

@en

Similar Protein Phosphatases C ...... Glycogen Metabolism in Mammals

@nl

type

label

Similar Protein Phosphatases C ...... Glycogen Metabolism in Mammals

@en

Similar Protein Phosphatases C ...... Glycogen Metabolism in Mammals

@nl

prefLabel

Similar Protein Phosphatases C ...... Glycogen Metabolism in Mammals

@en

Similar Protein Phosphatases C ...... Glycogen Metabolism in Mammals

@nl

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Journal of Biological Chemistry

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Similar protein phosphatases c ...... glycogen metabolism in mammals

@en

P2093

Alison M Smith

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

Gaëlle Messerli

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

Jychian Chen

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

Martine Trevisan

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Michael D J Seymour

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Steven M Smith

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Sylviane Comparot-Moss

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Wei-Ling Lue

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P2860

The starch-related R1 protein is an alpha -glucan, water dikinase.

The Arabidopsis sex1 mutant is defective in the R1 protein, a general regulator of starch degradation in plants, and not in the chloroplast hexose transporter

Identification of a novel enzyme required for starch metabolism in Arabidopsis leaves. The phosphoglucan, water dikinase

Metabolic profiling allows comprehensive phenotyping of genetically or environmentally modified plant systems

Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice

Glycogen and related polysaccharides inhibit the laforin dual-specificity protein phosphatase

A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen.

The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis

alpha-Amylase is not required for breakdown of transitory starch in Arabidopsis leaves.

Lafora's disease: towards a clinical, pathologic, and molecular synthesis.

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11815-11818

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scholarly article

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10.1074/JBC.M600519200

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17

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281

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Samuel C Zeeman

John A Gatehouse

Totte Niittylä

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2006-03-02T00:00:00Z

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16513634

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