Associated Papers
Frequency enrichment of coding variants in a French-Canadian founder population and its implication for inflammatory bowel diseases.
Bhérer C et al.
Medrxiv : the Preprint Server for Health Sciences, 2025
Lafora progressive myoclonus epilepsy: Disease mechanism and therapeutic attempts.
Parihar R et al.
Journal of Biosciences, 2024
Prognostic value of pathogenic variants in Lafora Disease: systematic review and meta-analysis of patient-level data.
Pondrelli F et al.
Orphanet Journal of Rare Diseases, 2023
TRIM32 and Malin in Neurological and Neuromuscular Rare Diseases.
Kumarasinghe L et al.
Cells, 2021
Nuclear Glycogenolysis Modulates Histone Acetylation in Human Non-Small Cell Lung Cancers.
Sun RC et al.
Cell Metabolism, 2019
Correction to: Interdependence of laforin and malin proteins for their stability and functions could underlie the molecular basis of locus heterogeneity in Lafora disease.
Mittal S et al.
Journal of Biosciences, 2018
Lafora disease: from genotype to phenotype.
Parihar R et al.
Journal of Genetics, 2018
A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders.
George AJ et al.
Frontiers in Genetics, 2018
A recurrent homozygous NHLRC1 variant in siblings with Lafora disease.
Araya N et al.
Human Genome Variation, 2018
Loss of laforin or malin results in increased Drp1 level and concomitant mitochondrial fragmentation in Lafora disease mouse models.
Upadhyay M et al.
Neurobiology of Disease, 2017
Lafora disease.
Turnbull J et al.
Epileptic Disorders : International Epilepsy Journal With Videotape, 2016
Interdependence of laforin and malin proteins for their stability and functions could underlie the molecular basis of locus heterogeneity in Lafora disease.
Mittal S et al.
Journal of Biosciences, 2015
Neuronatin-mediated aberrant calcium signaling and endoplasmic reticulum stress underlie neuropathology in Lafora disease.
Sharma J et al.
The Journal of Biological Chemistry, 2013
Lafora disease E3 ubiquitin ligase malin is recruited to the processing bodies and regulates the microRNA-mediated gene silencing process via the decapping enzyme Dcp1a.
Singh S et al.
Rna Biology, 2012
Laforin is required for the functional activation of malin in endoplasmic reticulum stress resistance in neuronal cells.
Zeng L et al.
The Febs Journal, 2012
Identification and characterization of novel splice variants of the human EPM2A gene mutated in Lafora progressive myoclonus epilepsy.
Dubey D et al.
Genomics, 2012
Malin and laforin are essential components of a protein complex that protects cells from thermal stress.
Sengupta S et al.
Journal of Cell Science, 2011
Sequestration of chaperones and proteasome into Lafora bodies and proteasomal dysfunction induced by Lafora disease-associated mutations of malin.
Rao SN et al.
Human Molecular Genetics, 2010
Novel mutations in EPM2A and NHLRC1 widen the spectrum of Lafora disease.
Lesca G et al.
Epilepsia, 2010
Co-chaperone CHIP stabilizes aggregate-prone malin, a ubiquitin ligase mutated in Lafora disease.
Rao SN et al.
The Journal of Biological Chemistry, 2010
Novel mutation in the NHLRC1 gene in a Malian family with a severe phenotype of Lafora disease.
Traoré M et al.
Neurogenetics, 2009
Lafora progressive myoclonus epilepsy: a meta-analysis of reported mutations in the first decade following the discovery of the EPM2A and NHLRC1 genes.
Singh S et al.
Human Mutation, 2009
The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system.
Garyali P et al.
Human Molecular Genetics, 2009
Modulation of functional properties of laforin phosphatase by alternative splicing reveals a novel mechanism for the EPM2A gene in Lafora progressive myoclonus epilepsy.
Dubey D et al.
Human Molecular Genetics, 2008
Lafora disease in the Indian population: EPM2A and NHLRC1 gene mutations and their impact on subcellular localization of laforin and malin.
Singh S et al.
Human Mutation, 2008
Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway.
Solaz-Fuster MC et al.
Human Molecular Genetics, 2008
A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease.
Cheng A et al.
Genes & Development, 2007
Lafora disease proteins malin and laforin are recruited to aggresomes in response to proteasomal impairment.
Mittal S et al.
Human Molecular Genetics, 2007
Novel NHLRC1 mutations and genotype-phenotype correlations in patients with Lafora's progressive myoclonic epilepsy.
Singh S et al.
Journal of Medical Genetics, 2006
Recent advances in the molecular basis of Lafora's progressive myoclonus epilepsy.
Ganesh S et al.
Journal of Human Genetics, 2006
Novel glycogen synthase kinase 3 and ubiquitination pathways in progressive myoclonus epilepsy.
Lohi H et al.
Human Molecular Genetics, 2005
Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin.
Gentry MS et al.
Proceedings of the National Academy of Sciences of the United States of America, 2005
Mutations in NHLRC1 cause progressive myoclonus epilepsy.
Chan EM et al.
Nature Genetics, 2003