alexa Kerensa Broersen | University of Twente
ISSN: 2161-0398

Journal of Physical Chemistry & Biophysics
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Kerensa Broersen

Kerensa Broersen Kerensa Broersen
Department of Nanobiophysics
University of Twente

Kerensa Broersen (1975) completed her PhD degree in protein folding and aggregation at Wageningen University, The Netherlands. She then worked as a postdoctoral research fellow at the MRC Laboratory for Molecular Biology in Cambridge (UK) for two years on fatty-acid induced α-synuclein aggregation in relation to Parkinson’s disease. During a second postdoc position at the Free University of Brussels (VUB) in Belgium she investigated the role of Aβ peptide length on oligomer toxicity in Alzheimer’s disease. Upon receiving an FWO Odysseus award she was contracted by the VUB as assistant professor and, together with her group she focused on risk factors related to Alzheimer’s disease progress. To tackle life science questions using advanced technological applications she joined a tenure track scheme at the University of Twente (The Netherlands). Here, she works together with her current team to answer questions in the field of Alzheimer’s disease since March 2011.

Research Interest

My current research interest involve the study of protein aggregation processes as disease triggering factor in neurodegenerative diseases using a high-end technology. Techniques I am interested in include fluorescence, single molecule techniques, microscopy, cell biology, and biochemical techniques. I am particularly interested in crossing disciplinary boundaries from clinical, chemical, physical to biological, to improve my understanding of disease processes. Obtaining mechanistic insight into the specific contribution of clinically identified risk factors in neurodegenerative disease progress have my keen attention, such as neuroinflammatory pathways, oxidative stress and the role of genetic variation.


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Technical Proteins: A Multitude of Applications to Discover
Kerensa Broersen
Editorial: J Phys Chem Biophys 2015, 5: e123
DOI: 10.4172/2161-0398.1000e123
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