Marie-Louise Bang

Senior Researcher

Area of interest:

Marie-Louise Bang was born in Denmark and earned her Master’s degree in Chemical Engineering with specialization in Biotechnology from the Technical University of Denmark in 1997. She did her PhD studies at the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany supported by a Marie Curie training grant (1997-2001) and subsequently her postdoctoral studies at the University of California San Diego (UCSD) supported by a fellowship from the American Heart Association. In 2007 she moved to Milan where she was awarded Assistant Telethon Scientist at the Dulbecco Telethon Institute and started up her independent research group at the Institute of Biomedical Technologies of the National Research Council (ITB-CNR) in collaboration with Multimedica Hospital. In 2010 she obtained a permanent position at CNR and in 2012 her laboratory moved to the Institute of Genetic and Biomedical Research (IRGB-CNR), UOS Milan at Humanitas Research Hospital. Her research is focused on studying the role of sarcomeric proteins in striated muscle structure, function, and disease to provide insights into the mechanisms underlying cardiac and skeletal muscle diseases, which is the requisite for the identification of novel therapeutic targets. Her research is currently funded by an ERAPerMed grant and she has previously obtained funding from the Telethon Foundation, Italian Ministry of Education, Universities and Research (MIUR), Ministry of Health, the Cariplo Foundation, and others.


Most significant publications:


Filomena, M C; Yamamoto, D L; Caremani, M; Kadarla, V K; Mastrototaro, G; Serio, S; Vydyanath, A; Mutarelli, M; Garofalo, A; Pertici, I; Knöll, R; Nigro, V; Luther, P K; Lieber, R L; Beck, M R; Linari, M; Bang, M L

Myopalladin promotes muscle growth through modulation of the serum response factor pathway Journal Article

In: J Cachexia Sarcopenia Muscle, 11 (1), pp. 169–194, 2020.



Bang, Marie-Louise

Animal Models of Congenital Cardiomyopathies Associated With Mutations in Z-Line Proteins Journal Article

In: Journal of Cellular Physiology, 232 (1), pp. 38–52, 2017, ISSN: 1097-4652.

Abstract | Links | BibTeX


Mastrototaro, Giuseppina; Liang, Xingqun; Li, Xiaodong; Carullo, Pierluigi; Piroddi, Nicoletta; Tesi, Chiara; Gu, Yusu; Dalton, Nancy D; Peterson, Kirk L; Poggesi, Corrado; Sheikh, Farah; Chen, Ju; Bang, Marie-Louise

Nebulette knockout mice have normal cardiac function, but show Z-line widening and up-regulation of cardiac stress markers Journal Article

In: Cardiovascular Research, 107 (2), pp. 216–225, 2015, ISSN: 1755-3245.

Abstract | Links | BibTeX

Bang, M L; Chen, J

Roles of Nebulin Family Members in the Ħeart Journal Article

In: Circ J, 79 (10), pp. 2081–2087, 2015.



Bang, Marie-Louise; Gu, Yusu; Dalton, Nancy D; Peterson, Kirk L; Chien, Kenneth R; Chen, Ju

The muscle ankyrin repeat proteins CARP, Ankrd2, and DARP are not essential for normal cardiac development and function at basal conditions and in response to pressure overload Journal Article

In: PloS One, 9 (4), pp. e93638, 2014, ISSN: 1932-6203.

Abstract | Links | BibTeX


Yamamoto, Daniel L; Vitiello, Carmen; Zhang, Jianlin; Gokhin, David S; Castaldi, Alessandra; Coulis, Gerald; Piaser, Fabio; Filomena, Maria Carmela; Eggenhuizen, Peter J; Kunderfranco, Paolo; Camerini, Serena; Takano, Kazunori; Endo, Takeshi; Crescenzi, Marco; Luther, Pradeep K L; Lieber, Richard L; Chen, Ju; Bang, Marie-Louise

The nebulin SH3 domain is dispensable for normal skeletal muscle structure but is required for effective active load bearing in mouse Journal Article

In: Journal of Cell Science, 126 (Pt 23), pp. 5477–5489, 2013, ISSN: 1477-9137.

Abstract | Links | BibTeX


Bang, M L; Caremani, M; Brunello, E; Littlefield, R; Lieber, R L; Chen, J; Lombardi, V; Linari, M

Nebulin plays a direct role in promoting strong actin-myosin interactions Journal Article

In: FASEB J, 23 (12), pp. 4117–4125, 2009.



Bang, M L; Li, X; Littlefield, R; Bremner, S; Thor, A; Knowlton, K U; Lieber, R L; Chen, J

Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle Journal Article

In: J Cell Biol, 173 (6), pp. 905–916, 2006.