A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen.
about
A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's diseaseStarch binding domain-containing protein 1/genethonin 1 is a novel participant in glycogen metabolismMalin 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.Laforin is required for the functional activation of malin in endoplasmic reticulum stress resistance in neuronal cellsAre there errors in glycogen biosynthesis and is laforin a repair enzyme?Evidence that family 35 carbohydrate binding modules display conserved specificity but divergent functionProcessivity and Subcellular Localization of Glycogen Synthase Depend on a Non-catalytic High Affinity Glycogen-binding SiteMultiple Glycogen-binding Sites in Eukaryotic Glycogen Synthase Are Required for High Catalytic Efficiency toward GlycogenVoltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function researchLaforin, a dual specificity phosphatase that dephosphorylates complex carbohydratesConservation 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.Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo.Brain glycogen re-awakened.Sequence and structural features of carbohydrate binding in proteins and assessment of predictability using a neural networkIncreased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforinA PTG variant contributes to a milder phenotype in Lafora diseaseLaforin, 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.Minireview: hey U(PS): metabolic and proteolytic homeostasis linked via AMPK and the ubiquitin proteasome system.The minimal essential core of a cysteine-based protein-tyrosine phosphatase revealed by a novel 16-kDa VH1-like phosphatase, VHZ.Increased oxidative stress and impaired antioxidant response in Lafora disease.Dimerization of the glucan phosphatase laforin requires the participation of cysteine 329.Expression, purification and characterization of soluble red rooster laforin as a fusion protein in Escherichia coli.Genetic mapping of a new Lafora progressive myoclonus epilepsy locus (EPM2B) on 6p22The laforin-malin complex negatively regulates glycogen synthesis by modulating cellular glucose uptake via glucose transporters.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.Ontogeny of Lafora bodies and neurocytoskeleton changes in Laforin-deficient mice.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.Increased laforin and laforin binding to glycogen underlie Lafora body formation in malin-deficient Lafora disease.Modular evolution of phosphorylation-based signalling systems.Mechanistic Insights into Glucan Phosphatase Activity against Polyglucan SubstratesTargeting the PTPome in human disease.Carbohydrate binding modules: biochemical properties and novel applications.Laforin prevents stress-induced polyglucosan body formation and Lafora disease progression in neurons.Glycogen and its metabolism: some new developments and old themes.
P2860
Q24295313-DF9E451E-C9FF-41FD-8C5C-9F6F8659B380Q24298333-8A3BF00B-F5B6-4CC4-B2DB-5BA58CFD72DBQ24302550-8259EF6E-1C02-4C3D-8AA5-C034504FBC49Q24304324-FE6B6E7D-8A24-4B43-8FA0-D3CF13700CE6Q24320315-7A09626D-A07F-4DBA-A9E1-B8BB1EBA78ACQ27027530-DBC53945-ADE0-486F-AEBB-60E07977A530Q27653810-FA010243-0B0D-40C5-861D-9F0823F4DE38Q27667417-90E6090A-6850-42C6-8E42-8D0EF8549A12Q27671693-F846993E-1AAA-43C1-8B14-3B7B6FE1AB34Q28086901-F1870C49-FCBA-4240-923B-08600C2642BCQ28116113-6E2C2B81-73F0-4362-88E6-3359D23CCAFBQ28752185-2C60F702-0572-4B25-93E1-BF7DB7C4855DQ29347551-87EA68E4-E489-4F0B-B2B8-9DD336876051Q29465784-30B85742-EDDC-4029-BCCE-CFB4462C9B36Q30441600-E8D31D7D-6A08-4849-8767-EDD553C71583Q30921812-D174A42C-8291-41DF-92E0-B7C86FB291CFQ33268099-D7D45B67-283A-4B0E-8B88-851E383F84B9Q33468448-1FBEB41E-DA2E-4045-BFB7-216D00D4DD8AQ33954771-6472CB52-E046-43BE-BED6-4D002952B870Q34009801-40775118-84B3-4C4C-8C41-626D2A81CF16Q34029315-C884E9C8-B94C-43F4-A9CF-1B2326D47C1DQ34265028-DC6A290B-3FD3-4269-8445-D7A04508FB41Q34327426-63696951-E300-4961-997A-94F1E7FA5F91Q34420455-CC863325-ADAA-4B5E-B5E7-5CFE846D8668Q34902869-A5E12352-9AC9-4BEB-A21F-3D3B7F7C16CAQ35137007-328DE201-5456-4BE9-8BC6-3FE1B4518D33Q35443679-CC28FD32-D595-4D65-84C6-C2E4B1BEEE19Q35697789-133CBCAE-5CCA-4E90-B0A4-0F21A6E12E86Q35745616-0C8BD82E-5461-41EE-9797-E58E2A260FE0Q35821706-3F6F85F1-A169-4A21-B291-A5E69931F333Q36009599-14819EF3-DA19-4761-81FA-5503F42C20EBQ36020483-6FC21447-D71A-40F1-813A-ACC0B1735125Q36119725-2E6E32E7-C2DF-4F54-A662-B62015D01493Q36127081-34BBDAFD-F07F-4F16-A080-BBF5D20CD0C8Q36153880-1CE8D15D-6C6D-4BFB-8BC2-81245E0D144BQ36281719-AB8A4297-DBBA-48C0-BAA4-B0D2C673F7EAQ36379394-DEF92A36-81A4-4E9E-A56D-F909950E94BDQ36499661-AF11B791-4A8A-497A-984E-CA915D54FBBFQ37043068-338DE459-E3E0-4B8A-B551-476C602A353AQ37095413-711B1617-9C42-4B1E-AC9C-23E2AA448D52
P2860
A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen.
description
2001 nî lūn-bûn
@nan
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen.
@ast
A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen.
@en
type
label
A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen.
@ast
A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen.
@en
prefLabel
A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen.
@ast
A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen.
@en
P2093
P2860
P356
P1476
A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen.
@en
P2093
Jack E Dixon
Jeanne A Stuckey
Jianyong Wang
Matthew J Wishart
P2860
P304
P356
10.1074/JBC.C100686200
P407
P577
2001-12-05T00:00:00Z