Laforin

[1]. Rajeshwer S Sankhala, et al. Dimeric quaternary structure of human laforin. J Biol Chem. 2015 Feb 20;290(8):4552-4559. [Content Brief]

[2]. Carmen Aguado, et al. Laforin, the most common protein mutated in Lafora disease, regulates autophagy. Hum Mol Genet. 2010 Jul 15;19(14):2867-76. [Content Brief]

[3]. B A Minassian, et al. Laforin is a cell membrane and endoplasmic reticulum-associated protein tyrosine phosphatase. Ann Neurol. 2001 Feb;49(2):271-5. [Content Brief]

[4]. Carolyn A Worby, et al. Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates. J Biol Chem. 2006 Oct 13;281(41):30412-8. [Content Brief]

[5]. David A Meekins, et al. Mechanistic Insights into Glucan Phosphatase Activity against Polyglucan Substrates. J Biol Chem. 2015 Sep 18;290(38):23361-70. [Content Brief]

[6]. Jianyong Wang, et al. A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen. J Biol Chem. 2002 Jan 25;277(4):2377-80. [Content Brief]

[7]. Madushi Raththagala, et al. Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease. Mol Cell. 2015 Jan 22;57(2):261-72. [Content Brief]

[8]. Pablo Sánchez-Martín, et al. Dimerization of the glucan phosphatase laforin requires the participation of cysteine 329. PLoS One. 2013 Jul 26;8(7):e69523. [Content Brief]

[9]. Carolyn A Worby, et al. Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG). J Biol Chem. 2008 Feb 15;283(7):4069-76. [Content Brief]

[10]. Leonarda Ianzano, et al. Loss of function of the cytoplasmic isoform of the protein laforin (EPM2A) causes Lafora progressive myoclonus epilepsy. Hum Mutat. 2004 Feb;23(2):170-176. [Content Brief]

[11]. Deepti Dubey, et al. Identification and characterization of novel splice variants of the human EPM2A gene mutated in Lafora progressive myoclonus epilepsy. Genomics. 2012 Jan;99(1):36-43. [Content Brief]

[12]. Carla Rubio-Villena, et al. Glycogenic activity of R6, a protein phosphatase 1 regulatory subunit, is modulated by the laforin-malin complex. Int J Biochem Cell Biol. 2013 Jul;45(7):1479-88. [Content Brief]

[13]. Yan Liu, et al. Dimerization of Laforin is required for its optimal phosphatase activity, regulation of GSK3beta phosphorylation, and Wnt signaling. J Biol Chem. 2006 Nov 17;281(46):34768-74. [Content Brief]

[14]. S Ganesh, et al. Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes. Hum Mol Genet. 2000 Sep 22;9(15):2251-61. [Content Brief]

[15]. Punitee Garyali, et al. The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system. Hum Mol Genet. 2009 Feb 15;18(4):688-700. [Content Brief]

[16]. Deepti Dubey, et al. Modulation of functional properties of laforin phosphatase by alternative splicing reveals a novel mechanism for the EPM2A gene in Lafora progressive myoclonus epilepsy. Hum Mol Genet. 2008 Oct 1;17(19):3010-20. [Content Brief]

[17]. Maria Elena Fernández-Sánchez, et al. Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. Hum Mol Genet. 2003 Dec 1;12(23):3161-71. [Content Brief]