Sequestration of chaperones and proteasome into Lafora bodies and proteasomal dysfunction induced by Lafora disease-associated mutations of malin

By Rao Sudheendra N.R.   Maity Ranjan   Sharma Jaiprakash   Dey Parthanarayan   Shankar Susarla Krishna   Satishchandra Parthasarathy   Jana Nihar Ranjan  

Human Molecular Genetics, Vol. 19, Iss. 23, 2010-12 ,pp. : 4726-4734

Oxford University Press

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Laforin, a dual specificity phosphatase involved in Lafora disease, regulates insulin response and whole-body energy balance in mice

By Vernia Santiago   Heredia Miguel   Criado Olga   Rodriguez de Cordoba Santiago   Garcia-Roves Pablo M.   Cansell Céline   Denis Raphael   Luquet Serge   Foufelle Fabienne   Ferre Pascal   Sanz Pascual  

Human Molecular Genetics, Vol. 20, Iss. 13, 2011-07 ,pp. : 2571-2584

Oxford University Press

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Laforin, the most common protein mutated in Lafora disease, regulates autophagy

By Aguado Carmen   Sarkar Sovan   Korolchuk Viktor I.   Criado Olga   Vernia Santiago   Boya Patricia   Sanz Pascual   de Crdoba Santiago Rodrguez   Knecht Erwin   Rubinsztein David C.  

Human Molecular Genetics, Vol. 19, Iss. 14, 2010-07 ,pp. : 2867-2876

Oxford University Press

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The Lafora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain

By Ganesh S.  

Human Molecular Genetics, Vol. 12, Iss. 18, 2003-09 ,pp. : 2359-2368

Oxford University Press

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Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation

By Fernández-Sánchez Maria Elena  

Human Molecular Genetics, Vol. 12, Iss. 23, 2003-12 ,pp. : 3161-3171

Oxford University Press

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