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Transgenic Rescue of the LARGEmyd Mouse: A LARGE Therapeutic Window? (2016)
Journal Article
Hildyard, J. C. W., Lacey, E., Booler, H., Hopkinson, M., Wells, D. J., & Brown, S. C. (2016). Transgenic Rescue of the LARGEmyd Mouse: A LARGE Therapeutic Window?. PLoS ONE, 11(7), e0159853. https://doi.org/10.1371/journal.pone.0159853

LARGE is a glycosyltransferase involved in glycosylation of α-dystroglycan (α-DG). Absence of this protein in the LARGEmyd mouse results in α-DG hypoglycosylation, and is associated with central nervous system abnormalities and progressive muscular d... Read More about Transgenic Rescue of the LARGEmyd Mouse: A LARGE Therapeutic Window?.

Degree of Cajal-Retzius cell mislocalisation correlates with the severity of structural brain defects in mouse models of dystroglycanopathy (2016)
Journal Article
Booler, H., Williams, J., Hopkinson, M., & Brown, S. C. (2016). Degree of Cajal-Retzius cell mislocalisation correlates with the severity of structural brain defects in mouse models of dystroglycanopathy. Brain Pathology, 26(4), 465-478. https://doi.org/10.1111/bpa.12306

The secondary dystroglycanopathies are characterized by the hypoglycosylation of alpha dystroglycan, and are associated with mutations in at least 18 genes that act on the glycosylation of this cell surface receptor rather than the Dag1 gene itself.... Read More about Degree of Cajal-Retzius cell mislocalisation correlates with the severity of structural brain defects in mouse models of dystroglycanopathy.

Prenatal muscle development in a mouse model for the secondary dystroglycanopathies (2016)
Journal Article
Kim, J., Hopkinson, M., Kavishwar, M., Fernandez-Fuente, M., & Brown, S. C. (2016). Prenatal muscle development in a mouse model for the secondary dystroglycanopathies. Skeletal Muscle, 6(3), https://doi.org/10.1186/s13395-016-0073-y

The defective glycosylation of ?-dystroglycan is associated with a group of muscular dystrophies that are collectively referred to as the secondary dystroglycanopathies. Mutations in the gene encoding fukutin-related protein (FKRP) are one of the mos... Read More about Prenatal muscle development in a mouse model for the secondary dystroglycanopathies.

Calcium Homeostasis in Myogenic Differentiation Factor 1 (MyoD)-Transformed, Virally-Transduced, Skin-Derived Equine Myotubes (2014)
Journal Article
Fernandez-Fuente, M., Terracciano, C. M., Martin-Duque, P., Brown, S. C., Vassaux, G., & Piercy, R. J. (2014). Calcium Homeostasis in Myogenic Differentiation Factor 1 (MyoD)-Transformed, Virally-Transduced, Skin-Derived Equine Myotubes. PLoS ONE, 9(8), e105971. https://doi.org/10.1371/journal.pone.0105971

Dysfunctional skeletal muscle calcium homeostasis plays a central role in the pathophysiology of several human and animal skeletal muscle disorders, in particular, genetic disorders associated with ryanodine receptor 1 (RYR1) mutations, such as malig... Read More about Calcium Homeostasis in Myogenic Differentiation Factor 1 (MyoD)-Transformed, Virally-Transduced, Skin-Derived Equine Myotubes.

Adenovirus-mediated expression of Myogenic Differentiation Factor 1 (MyoD) in equine and human dermal fibroblasts enables their conversion to caffeine-sensitive myotubes (2014)
Journal Article
Fernandez-Fuente, M., Martin-Duque, P., Vassaux, G., Brown, S. C., Muntoni, F., Terracciano, C. M., & Piercy, R. J. (2014). Adenovirus-mediated expression of Myogenic Differentiation Factor 1 (MyoD) in equine and human dermal fibroblasts enables their conversion to caffeine-sensitive myotubes. Neuromuscular Disorders, 24(3), 250-258. https://doi.org/10.1016/j.nmd.2013.11.009

Several human and animal myopathies, such as malignant hyperthermia (MH), central core disease and equine recurrent exertional rhabdomyolysis (RER) are confirmed or thought to be associated with dysfunction of skeletal muscle calcium regulation. For... Read More about Adenovirus-mediated expression of Myogenic Differentiation Factor 1 (MyoD) in equine and human dermal fibroblasts enables their conversion to caffeine-sensitive myotubes.

Assessment of the transformation of equine skin-derived fibroblasts to multinucleated skeletal myotubes following lentiviral-induced expression of equine myogenic differentiation 1
Journal Article
Fernandez-Fuente, M., Ames, E. G., Wagner, M. L., Zhou, H., Strom, M., Zammit, P. S., …Piercy, R. J. Assessment of the transformation of equine skin-derived fibroblasts to multinucleated skeletal myotubes following lentiviral-induced expression of equine myogenic differentiation 1. American Journal of Veterinary Research, 69(12), 1637-1645. https://doi.org/10.2460/ajvr.69.12.1637

Objective - To develop a reliable method for converting cultured equine skin-derived fibroblasts into muscle cells. Sample Population - Equine skin-derived fibroblasts. Procedures - The equine myogenic differentiation 1 (eqMyoD) genomic sequence was... Read More about Assessment of the transformation of equine skin-derived fibroblasts to multinucleated skeletal myotubes following lentiviral-induced expression of equine myogenic differentiation 1.

Investigating the pathology of Emery-Dreifuss muscular dystrophy
Journal Article
Brown, S. C., Piercy, R. J., Muntoni, F., & Sewry, C. A. Investigating the pathology of Emery-Dreifuss muscular dystrophy. Biochemical Society Transactions, 36(Pt 6), 1335-1338. https://doi.org/10.1042/bst0361335

EDMD (Emery-Dreifuss muscular dystrophy) is caused by mutations in either the gene encoding for lamin A/C (LMNA) located at 1q21.2-q21.3 of emerin (EMD) located at Xq28. Autosomal dominant EDMD caused by LMNA mutations is more common than the X-linke... Read More about Investigating the pathology of Emery-Dreifuss muscular dystrophy.

A comparative study of alpha-dystroglycan glycosylation in dystroglycanopathies suggests that the hypoglycosylation of alpha-dystroglycan does not consistently correlate with clinical severity.
Journal Article
Jimenez-Mallebrera, C., Torelli, S., Feng, L., Kim, J., Godfrey, C., Clement, E., …Muntoni, F. A comparative study of alpha-dystroglycan glycosylation in dystroglycanopathies suggests that the hypoglycosylation of alpha-dystroglycan does not consistently correlate with clinical severity. Brain Pathology, 19(4), 596-611. https://doi.org/10.1111/j.1750-3639.2008.00198.x