| Identification of NHLRC1 as a Novel AKT Activator from a Lung Cancer Epigenome-Wide Association Study (EWAS). | Identification of NHLRC1 as a Novel AKT Activator from a Lung Cancer Epigenome-Wide Association Study (EWAS).
Faltus C, Lahnsteiner A, Barrdahl M, Assenov Y, Hüsing A, Bogatyrova O, Laplana M, Johnson T, Muley T, Meister M, Warth A, Thomas M, Plass C, Kaaks R, Risch A., Free PMC Article | 10/15/2022 |
| Compound heterozygosity for novel variations of the NHLRC1 Gene in a family with Lafora disease. | Compound heterozygosity for novel variations of the NHLRC1 Gene in a family with Lafora disease.
Tang X, Li X, Chen Y, Wu D. | 06/25/2022 |
| The rare rs769301934 variant in NHLRC1 is a common cause of Lafora disease in Turkey. | The rare rs769301934 variant in NHLRC1 is a common cause of Lafora disease in Turkey.
Haryanyan G, Ozdemir O, Tutkavul K, Dervent A, Ayta S, Ozkara C, Salman B, Yucesan E, Kesim Y, Susgun S, Ozbek U, Baykan B, Ugur Iseri SA, Bebek N. | 05/21/2022 |
| Laforin/malin complex interacts physically and co-localizes intracellularly with core components of the PI3KC3 complex (Beclin1, Vps34 and Vps15), and that this interaction is specific and results in the polyubiquitination of these proteins. | Regulation of the autophagic PI3KC3 complex by laforin/malin E3-ubiquitin ligase, two proteins involved in Lafora disease.
Sanchez-Martin P, Lahuerta M, Viana R, Knecht E, Sanz P., Free PMC Article | 04/25/2020 |
| Malin promotes its own degradation via auto-ubiquitination.Malin preferentially degrades the phosphatase-inactive laforin monomer. | Interdependence of laforin and malin proteins for their stability and functions could underlie the molecular basis of locus heterogeneity in Lafora disease.
Mittal S, Upadhyay M, Singh PK, Parihar R, Ganesh S. | 09/17/2016 |
| laforin/malin complex is able to interact with and ubiquitinate both PKM1 and PKM2 | The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.
Viana R, Lujan P, Sanz P., Free PMC Article | 01/30/2016 |
| Lafora disease proteins laforin and malin negatively regulate the HIPK2-p53 cell death pathway. | Lafora disease proteins laforin and malin negatively regulate the HIPK2-p53 cell death pathway.
Upadhyay M, Gupta S, Bhadauriya P, Ganesh S. | 10/3/2015 |
| This study demonistrated that NHLRC1 mutations were detected in some case of Mild Lafora disease patients. | Mild Lafora disease: clinical, neurophysiologic, and genetic findings.
Ferlazzo E, Canafoglia L, Michelucci R, Gambardella A, Gennaro E, Pasini E, Riguzzi P, Plasmati R, Volpi L, Labate A, Gasparini S, Villani F, Casazza M, Viri M, Zara F, Minassian BA, Turnbull J, Serratosa JM, Guerrero-López R, Franceschetti S, Aguglia U. | 03/7/2015 |
| Without functional laforin-malin complex assembled on polyglucosan bodies, polyglucosan is not degraded. | Laforin-malin complex degrades polyglucosan bodies in concert with glycogen debranching enzyme and brain isoform glycogen phosphorylase.
Liu Y, Zeng L, Ma K, Baba O, Zheng P, Liu Y, Wang Y., Free PMC Article | 11/22/2014 |
| Malin regulates the recruitment of mRNA-decapping enzyme 1A (Dcp1a) to processing bodies. | 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, Singh PK, Bhadauriya P, Ganesh S. | 09/14/2013 |
| Malin forms a functional complex with laforin. This complex promotes the ubiquitination of proteins involved in glycogen metabolism and misregulation of pathways involved in this process results in Lafora body formation. (Review) | Deciphering the role of malin in the lafora progressive myoclonus epilepsy.
Romá-Mateo C, Sanz P, Gentry MS., Free PMC Article | 02/9/2013 |
| This study identified that NHLRC1 gene mutations leading to Lafora disease in six Turkish families. | Four novel and two recurrent NHLRC1 (EPM2B) and EPM2A gene mutations leading to Lafora disease in six Turkish families.
Salar S, Yeni N, Gündüz A, Güler A, Gökçay A, Velioğlu S, Gündoğdu A, Hande Çağlayan S. | 06/2/2012 |
| Our results indicate that malin regulates Wnt signaling pathway through the degradation of dishevelled2 and suggest possible deregulation of Wnt signaling in Lafora disease. | Malin regulates Wnt signaling pathway through degradation of dishevelled2.
Sharma J, Mulherkar S, Mukherjee D, Jana NR., Free PMC Article | 04/28/2012 |
| Mutations in the NHL repeat containing 1 (NHLRC1) gene are described in association with a more benign clinical course and later age of death in an adolescent patient. | Rapidly progressive phenotype of Lafora disease associated with a novel NHLRC1 mutation.
Brackmann FA, Kiefer A, Agaimy A, Gencik M, Trollmann R. | 03/31/2012 |
| Laforin and malin are defective in Lafora disease (LD), a neurodegenerative disorder associated with epileptic seizures | Malin and laforin are essential components of a protein complex that protects cells from thermal stress.
Sengupta S, Badhwar I, Upadhyay M, Singh S, Ganesh S. | 12/24/2011 |
| malin(C46Y), malin(P69A), malin(D146N), and malin(L261P) mutants failed to downregulate the level of R5/PTG, a regulatory subunit of protein phosphatase 1 involved in glycogen synthesis. | Lafora progressive myoclonus epilepsy: NHLRC1 mutations affect glycogen metabolism.
Couarch P, Vernia S, Gourfinkel-An I, Lesca G, Gataullina S, Fedirko E, Trouillard O, Depienne C, Dulac O, Steschenko D, Leguern E, Sanz P, Baulac S., Free PMC Article | 12/10/2011 |
| malin negatively regulates neuronatin and its loss of function in Lafora disease results in increased accumulation of neuronatin | Lafora disease ubiquitin ligase malin promotes proteasomal degradation of neuronatin and regulates glycogen synthesis.
Sharma J, Rao SN, Shankar SK, Satishchandra P, Jana NR. | 12/3/2011 |
| Malin is related to TRIM32 at both the phylogenetic and functional level. | Lafora disease E3-ubiquitin ligase malin is related to TRIM32 at both the phylogenetic and functional level.
Romá-Mateo C, Moreno D, Vernia S, Rubio T, Bridges TM, Gentry MS, Sanz P., Free PMC Article | 11/26/2011 |
| study described several novel mutations of EPM2A and NHLRC1 and brought additional data to genetic epidemiology of Lafora disease (LD); emphasized the high mutation rate in patients with classical LD as well as the high negativity rate of skin biopsy | Novel mutations in EPM2A and NHLRC1 widen the spectrum of Lafora disease.
Lesca G, Boutry-Kryza N, de Toffol B, Milh M, Steschenko D, Lemesle-Martin M, Maillard L, Foletti G, Rudolf G, Nielsen JE, á Rogvi-Hansen B, Erdal J, Mancini J, Thauvin-Robinet C, M'Rrabet A, Ville D, Szepetowski P, Raffo E, Hirsch E, Ryvlin P, Calender A, Genton P. | 01/1/2011 |
| These results suggest that the modification introduced by the laforin-malin complex could affect the subcellular distribution of AMPK beta subunits. | The laforin-malin complex, involved in Lafora disease, promotes the incorporation of K63-linked ubiquitin chains into AMP-activated protein kinase beta subunits.
Moreno D, Towler MC, Hardie DG, Knecht E, Sanz P., Free PMC Article | 11/27/2010 |
| the co-chaperone carboxyl terminus of the Hsc70-interacting protein (CHIP) stabilizes malin by modulating the activity of Hsp70. | Co-chaperone CHIP stabilizes aggregate-prone malin, a ubiquitin ligase mutated in Lafora disease.
Rao SN, Sharma J, Maity R, Jana NR., Free PMC Article | 02/1/2010 |
| Results describe a novel homozygous single-nucleotide variant in the NHLRC1 gene in a Malian consanguineous family. | Novel mutation in the NHLRC1 gene in a Malian family with a severe phenotype of Lafora disease.
Traoré M, Landouré G, Motley W, Sangaré M, Meilleur K, Coulibaly S, Traoré S, Niaré B, Mochel F, La Pean A, Vortmeyer A, Mani H, Fischbeck KH., Free PMC Article | 01/21/2010 |
| laforin and malin play a role protecting cells from ER-stress, likely contributing to the elimination of unfolded proteins | Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin.
Vernia S, Rubio T, Heredia M, Rodríguez de Córdoba S, Sanz P., Free PMC Article | 01/21/2010 |
| phosphorylation of R5/PTG at Ser-8 by AMPK accelerates its laforin/malin-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity. | 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 complex.
Vernia S, Solaz-Fuster MC, Gimeno-Alcañiz JV, Rubio T, García-Haro L, Foretz M, de Córdoba SR, Sanz P., Free PMC Article | 01/21/2010 |
| Meta-analysis of gene-disease association. (HuGE Navigator) | 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, Ganesh S. | 03/25/2009 |