Junxia Lu
Assistant Professor, PI
Life Science and Technology
Shanghai Tech University
China
Biography
Dr. Junxia Lu obtained her bachelor and master degrees from Department of Chemistry of Fudan University. She received her doctor degree from Miami University in Ohio in 2007. After graduation, she joined National Institute of Health (NIH, USA) as a visiting fellow till 2011. Since then, she spent one year at Pacific Northwest National Laboratory as a research associate and worked at NIH during 2013-2014. Dr. Junxia joinede School of Life Science and Technology of ShanghaiTech University as an assistant professor, PI since 2015.
Research Interest
Dr. Lu’s research interest is focused on the structural study of protein assemblies involved in human diseases, such as Alzheimer’s disease and AIDS. The protein assemblies, such as amyloid-β fibrils formed in the brain plague of Alzheimer’s disease patients, are not soluble and in non-crystalline form, present a unique challenge for us to study. Solid-state NMR, as an idea technique to study these kinds of proteins, is applied in her research to understand the structural implication of these protein macrostructures to human disease.
Publications
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Lu, J.X., Sharpe S., Yau, W.Y. and Tycko R. Oligomerization State and Supramolecular Structure of the HIV-1 Vpu Protein Transmembrane Segment in Phospholipid Bilayers Protein Science (2010) 19, 1877-1896
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Lu, J.X., Xu, Y.M., Shaw, W.J. Phosphorylation and Ionic Strength Alter the LRAP-HAP interface in the N-terminus Biochemistry (2013) 52, 2196-2205
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Lu, J.X., Xu, Y.M., Shaw, W.J. Mineral Association Changes the Secondary Structure and Dynamics of Amelogenin Journal of Dental Research (2013) 92, 1000-1004
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Lu, J.X., Qiang, W, Yau W.M., Schwieters, C. D., Meredith, S.C. and Tycko R. Molecular structure of β-amyloid fibrils in Alzheimer’s disease brain tissue Cell (2013) 154,1257-1268 (with video paperflick)
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Lu, J.X., Burton, S.D. Xu, Y.M., Buchko G.W. and Shaw, W.J. The flexible structure of the K24S28 region of Leucine-Rich Amelogenin Protein (LRAP) bound to apatites as a function of surface type, calcium, mutation, and ionic strength Frontiers Physiology (2014), 5, 254, 1-8
