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The present study analyzes possible inflammatory responses in the mouse lines Epm2a (-/-) (laforin knock-out) and Epm2b (-/-) (malin (zeige NHLRC1 Proteine) knock-out) with disease progression.
Laforin-silenced cells was able to induce autophagic flux, proteasomal activity and reduce the polyubiquitinated proteins by heat shock.
This study also suggests a malin (zeige NHLRC1 Proteine) function independent of laforin, possibly in lysosomal biogenesis and/or lysosomal glycogen (zeige GYS1 Proteine) disposal.
loss of laforin results in activation of serum/glucocorticoid-induced kinase 1 in cellular and animals models
expression of Epm2a blocks formation of Lafora bodies and restores the impairment in macroautophagy, preventing the development of Lafora bodies in Epm2a-deficient mice.
in laforin-deficient mice, stress drastically accelerates Lafora bodies accumulation and Lafora disease.
Results indicate that laforin has no effect on whole-body glucose metabolism and insulin (zeige INS Proteine) sensitivity.
malin (zeige NHLRC1 Proteine) functions to regulate laforin and that malin (zeige NHLRC1 Proteine) deficiency at least in part causes LB and LD through increased laforin binding to glycogen (zeige GYS1 Proteine).
Results show that a functional laforin-malin (zeige NHLRC1 Proteine) complex plays a critical role in disrupting Lafora bodies and relieving endoplasmic reticulum stres.
A detailed microscopic analysis of the neuropil of a Laforin-deficient (epm2a-/-) mouse model shows neurofibrillary degeneration and senile-like plaques prominent in the hippocampus and ventral pons.
rs702304 and rs2235481 within the EPM2A gene were associated with schizophrenia liability.
Laforin prevents the auto-degradation of malin (zeige NHLRC1 Proteine) by presenting itself as a substrate. Malin (zeige NHLRC1 Proteine) preferentially degrades the phosphatase-inactive laforin monomer.
Laforin-glycan interactions occur with a favourable enthalpic contribution counter-balanced by an unfavourable entropic contribution.
laforin is responsible for glycogen (zeige GYS1 Proteine) dephosphorylation during exercise and acts during the cytosolic degradation of glycogen (zeige GYS1 Proteine)
Lafora disease proteins laforin and malin (zeige NHLRC1 Proteine) negatively regulate the HIPK2 (zeige HIPK2 Proteine)-p53 (zeige TP53 Proteine) cell death pathway.
This study suggest that variations in phenotypes of EPM2A-deficient Lafora disease.
novel molecular determinants in the laforin active site that help decipher the mechanism of glucan phosphatase activity.
The crystal structure of laforin bound to phosphoglucan product, reveals its unique integrated tertiary and quaternary structure.
This study identified some Mild Lafora disease have EPM2A mutation.
Studied the role of conformational changes in human laforin structure due to existing single mutation W32G and prepared double mutation W32G/K87A related to loss of glycogen (zeige GYS1 Proteine) binding.
This gene encodes a dual-specificity phosphatase that associates with polyribosomes. The encoded protein may be involved in the regulation of glycogen metabolism. Mutations in this gene have been associated with myoclonic epilepsy of Lafora. Alternative splicing results in multiple transcript variants.
, lafora PTPase
, epilepsy, progressive myoclonic epilepsy, type 2 gene alpha
, epilepsy, progressive myoclonus type 2, Lafora disease (laforin)