Laforin, a dual-specificity phosphatase involved in Lafora disease, is phosphorylated at Ser25by AMP-activated protein kinase

Glycogen hyperphosphorylation underlies lafora body formation

(2010) Julie Turnbull et al.   ANNALS OF NEUROLOGY

Genetic Depletion of the Malin E3 Ubiquitin Ligase in Mice Leads to Lafora Bodies and the Accumulation of Insoluble Laforin

(2010) Anna A. DePaoli-Roach et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Lafora progressive myoclonus epilepsy: A meta-analysis of reported mutations in the first decade following the discovery of theEPM2AandNHLRC1genes

(2009) Shweta Singh et al.   HUMAN MUTATION

Lafora disease: insights into neurodegeneration from plant metabolism

(2009) Matthew S. Gentry et al.   TRENDS IN BIOCHEMICAL SCIENCES

Abnormal Metabolism of Glycogen Phosphate as a Cause for Lafora Disease

(2008) Vincent S. Tagliabracci et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Laforin Negatively Regulates Cell Cycle Progression through Glycogen Synthase Kinase 3 -Dependent Mechanisms

(2008) R. Liu et al.   MOLECULAR AND CELLULAR BIOLOGY

AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint

(2008) Dana M. Gwinn et al.   MOLECULAR CELL

PROMALS3D web server for accurate multiple protein sequence and structure alignments

(2008) J. Pei et al.   NUCLEIC ACIDS RESEARCH