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Sign in to add traineeJana Hartmann | grad student | 1992-1995 | Max Planck Institute for Medical Research, Heidelberg, Germany |
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Publications
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Sharma S, Lindau M. (2016) The mystery of the fusion pore. Nature Structural & Molecular Biology. 23: 5-6 |
Jayant K, Singhai A, Cao Y, et al. (2015) Non-Faradaic Electrochemical Detection of Exocytosis from Mast and Chromaffin Cells Using Floating-Gate MOS Transistors. Scientific Reports. 5: 18477 |
Sharma S, Kim BN, Stansfeld PJ, et al. (2015) A Coarse Grained Model for a Lipid Membrane with Physiological Composition and Leaflet Asymmetry. Plos One. 10: e0144814 |
Fang Q, Zhao Y, Herbst AD, et al. (2015) Positively charged amino acids at the SNAP-25 C terminus determine fusion rates, fusion pore properties, and energetics of tight SNARE complex zippering. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 35: 3230-9 |
Fang Q, Lindau M. (2014) How could SNARE proteins open a fusion pore? Physiology (Bethesda, Md.). 29: 278-85 |
Zhao Y, Fang Q, Herbst AD, et al. (2013) Rapid structural change in synaptosomal-associated protein 25 (SNAP25) precedes the fusion of single vesicles with the plasma membrane in live chromaffin cells. Proceedings of the National Academy of Sciences of the United States of America. 110: 14249-54 |
Stavrinidou E, Leleux P, Rajaona H, et al. (2013) Direct measurement of ion mobility in a conducting polymer. Advanced Materials (Deerfield Beach, Fla.). 25: 4488-93 |
Fang Q, Zhao Y, Lindau M. (2013) Juxtamembrane tryptophans of synaptobrevin 2 control the process of membrane fusion. Febs Letters. 587: 67-72 |
Kim BN, Herbst AD, Kim SJ, et al. (2013) Parallel recording of neurotransmitters release from chromaffin cells using a 10×10 CMOS IC potentiostat array with on-chip working electrodes. Biosensors & Bioelectronics. 41: 736-44 |
Lindau M, Hall BA, Chetwynd A, et al. (2012) Coarse-grain simulations reveal movement of the synaptobrevin C-terminus in response to piconewton forces. Biophysical Journal. 103: 959-69 |