Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
about
A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's diseaseMalin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)Laforin, the most common protein mutated in Lafora disease, regulates autophagyLaforin is required for the functional activation of malin in endoplasmic reticulum stress resistance in neuronal cellsStructure of human PIR1, an atypical dual-specificity phosphataseProtein tyrosine phosphatases--from housekeeping enzymes to master regulators of signal transductionGenetics of Lafora progressive myoclonic epilepsy: current perspectivesAre there errors in glycogen biosynthesis and is laforin a repair enzyme?Structural and functional characterization of a novel phosphatase from the Arabidopsis thaliana gene locus At1g05000Structural basis for the glucan phosphatase activity of Starch Excess4Structural and functional analysis of PTPMT1, a phosphatase required for cardiolipin synthesisStructure of the Arabidopsis Glucan Phosphatase LIKE SEX FOUR2 Reveals a Unique Mechanism for Starch DephosphorylationPhosphoglucan-bound structure of starch phosphatase Starch Excess4 reveals the mechanism for C6 specificityVoltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function researchThe carbohydrate-binding domain of overexpressed STBD1 is important for its stability and protein-protein interactionsEngineering Potato Starch with a Higher Phosphate ContentPTG depletion removes Lafora bodies and rescues the fatal epilepsy of Lafora diseaseMitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesisConservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glucan metabolism of the organismDimeric quaternary structure of human laforin.Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease.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 complexLaforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo.Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial beta-amylases.Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforinAbnormal glycogen chain length pattern, not hyperphosphorylation, is critical in Lafora disease.Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activityThe 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 laforinInsights into the mechanism of polysaccharide dephosphorylation by a glucan phosphataseIncreased oxidative stress and impaired antioxidant response in Lafora disease.Several dual specificity phosphatases coordinate to control the magnitude and duration of JNK activation in signaling response to oxidative stress.An Update on Jacalin-Like Lectins and Their Role in Plant Defense.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.Relationship between glycogen accumulation and the laforin dual specificity phosphatase.Laforin, a dual-specificity phosphatase involved in Lafora disease, is phosphorylated at Ser25 by AMP-activated protein kinase.Laforin, a protein with many faces: glucan phosphatase, adapter protein, et alii.Muscle glycogen remodeling and glycogen phosphate metabolism following exhaustive exercise of wild type and laforin knockout mice.
P2860
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P2860
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
description
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2006
@ast
im Oktober 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2006/10/13)
@sk
vědecký článek publikovaný v roce 2006
@cs
wetenschappelijk artikel (gepubliceerd op 2006/10/13)
@nl
наукова стаття, опублікована в жовтні 2006
@uk
name
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
@ast
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
@en
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
@nl
type
label
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
@ast
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
@en
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
@nl
prefLabel
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
@ast
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
@en
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
@nl
P2093
P2860
P3181
P356
P1476
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
@en
P2093
Carolyn A. Worby
Jack E. Dixon
Matthew S. Gentry
P2860
P304
30412–30418
P3181
P356
10.1074/JBC.M606117200
P407
P577
2006-10-13T00:00:00Z