Karl's research looks at proteins associated with the dystrophin complex and is also interested in growth and regeneration of muscle tissue.
Researcher in
Proteins associated with the dystrophin protein complex
Cell signalling and regulation of skeletal muscle fibre types
Growth and regeneration of muscle
2008-present
Senior Postdoctoral researcher
REMEDI, National University of Ireland, Galway
Cardiovascular gene therapy
2003-2007
Career Development fellow
Medical Research Council, Functional Genetics Unit, University of Oxford
Dystrophin complex-linked intermediate filament protein syncoilin: function in muscle and nerve
2000-2003
EMBO Post-doctoral researcher
University of Padova, Italy.
Transcription factor NFAT as a nerve activity sensor in skeletal muscle fibre types
1997-2000
Post-doctoral researcher
Massachusetts General Hospital and Harvard Medical School Role of calcineurin isoforms in cardiac and skeletal muscle remodelling
1994-1997
PhD
Trinity College Dublin Lactate transport and transporters in muscle
2000-2002
European Molecular Biology Organization Post-doctoral Long-term fellowship
2000-2003
Marie Curie Post-doctoral fellowship
W. Thomas Clarke, Ben Edwards, Karl J. A. McCullagh, Matthew W. Kemp, Catherine Moorwood, Diane L. Sherman, Matthew Burgess, and Kay E. Davies.
J Cell Sci 2010 123 (15): 2543-2552. August 1, 2010.
Analysis of skeletal muscle function in the C57BL6/SV129 syncoilin knockout mouse
A naturally occurring calcineurin variant inhibits FoxO activity and enhances skeletal muscle regeneration
Intermediate filament-like protein syncoilin in normal and myopathic striated muscle
Utrophin upregulation in Duchenne muscular dystrophy
Muscular dystrophies related to the cytoskeleton/nuclear envelope
NFAT is a nerve activity sensor in skeletal muscle and controls activity-dependent myosin switching
Localized IGF-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle
Revisiting calcineurin and human heart failure.
IGF-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NF-ATc1