Dr James McNamara
Dr James McNamara
Details
Role
Team Leader / Senior Research Officer
Research area
Stem cell biology
Group
Heart Disease
Dr. James McNamara is a researcher in the Heart Disease and Regeneration Group at The Murdoch Children’s Research Institute. His research has focused on molecular mechanisms of hypertrophic cardiomyopathy, a common form of genetic heart disease. This research led to the discovery that mutations linked to hypertrophic cardiomyopathy increased the number of active myosin motors in mouse and human hearts, providing a mechanism for how these mutations impair contraction, relaxation, and energy utilisation. He received his PhD in Medicine from the University of Sydney in 2017. He then undertook undertake postdoctoral training at the University of Cincinnati, supported by an American Heart Association Postdoctoral Fellowship for this period and continued to focus on the function of MYBPC3, establishing a mechanism for its role in adrenergic signaling in the heart. In 2020 he joined Prof. Enzo Porrello and A/Prof David Elliott’s groups at MCRI. Here, he continues to study molecular mechanisms of genetic heart diseases, now utilising human pluripotent stem cells as a human model of disease. James’ research is currently supported by multiple early career fellowships.
Dr. James McNamara is a researcher in the Heart Disease and Regeneration Group at The Murdoch Children’s Research Institute. His research has focused on molecular mechanisms of hypertrophic cardiomyopathy, a common form of genetic heart disease....
Dr. James McNamara is a researcher in the Heart Disease and Regeneration Group at The Murdoch Children’s Research Institute. His research has focused on molecular mechanisms of hypertrophic cardiomyopathy, a common form of genetic heart disease. This research led to the discovery that mutations linked to hypertrophic cardiomyopathy increased the number of active myosin motors in mouse and human hearts, providing a mechanism for how these mutations impair contraction, relaxation, and energy utilisation. He received his PhD in Medicine from the University of Sydney in 2017. He then undertook undertake postdoctoral training at the University of Cincinnati, supported by an American Heart Association Postdoctoral Fellowship for this period and continued to focus on the function of MYBPC3, establishing a mechanism for its role in adrenergic signaling in the heart. In 2020 he joined Prof. Enzo Porrello and A/Prof David Elliott’s groups at MCRI. Here, he continues to study molecular mechanisms of genetic heart diseases, now utilising human pluripotent stem cells as a human model of disease. James’ research is currently supported by multiple early career fellowships.
Top Publications
- McNamara, JW, Parker, BL, Voges, HK, Mehdiabadi, NR, Bolk, F, Ahmad, F, Chung, JD, Charitakis, N, Molendijk, J, Zech, ATL, et al. Alpha kinase 3 signaling at the M-band maintains sarcomere integrity and proteostasis in striated muscle. Nature Cardiovascular Research 2(2) : 159 -173 2023 view publication
- McNamara, JW, Parker, BL, Voges, HK, Mehdiabadi, NR, Bolk, F, Chung, JD, Charitakis, N, Molendijk, J, Lal, S, Ramialison, M, et al. Alpha kinase 3 signaling at the M-band maintains sarcomere integrity and proteostasis in striated muscle. 2022 view publication
- Blazev, R, Carl, CS, Ng, Y-K, Molendijk, J, Voldstedlund, CT, Zhao, Y, Xiao, D, Kueh, AJ, Miotto, PM, Haynes, VR, et al. Phosphoproteomics of three exercise modalities identifies canonical signaling and C18ORF25 as an AMPK substrate regulating skeletal muscle function. Cell Metabolism 34(10) : 1561 -1577.e9 2022 view publication
- Lipps, C, Yogeswaran, A, McNamara, J, Wilhelm, J, Truschel, T, Aslam, M, Reischauer, S, Voss, S, Keller, T, Doerr, O, et al. C0-C1f region of cardiac myosin binding protein-C induces pro-inflammatory responses in fibroblasts. European Heart Journal 42(Supplement_1) : 2021 view publication
- Singh, RR, McNamara, JW, Sadayappan, S. Mutations in myosin S2 alter cardiac myosin-binding protein-C interaction in hypertrophic cardiomyopathy in a phosphorylation-dependent manner. Journal of Biological Chemistry 297(1) : 100836 2021 view publication
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