Researcher Portfolio
Fasshauer, D.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society
Researcher Profile
Position: Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society
Position: Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons15051
Publications
(1 - 25 of 51)
: Demircioglu, F. E., Burkhardt, P., & Fasshauer, D. (2014). The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex. Proceedings of the National Academy of Sciences of the United States of America, 111(38), 13828-13833. doi:10.1073/pnas.1408254111. [PubMan] : Colbert, K. N., Hattendorf, D. A., Weiss, T. M., Burkhardt, P., Fasshauer, D., & Weis, W. I. (2013). Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation. Proceedings of the National Academy of Sciences of the United States of America, 110(31), 12637-12642. doi:10.1073/pnas.1303753110. [PubMan] : Honigmann, A., van den Bogaart, G., Iraheta, E., Risselada, H. J., Milovanovic, D., Müller, V., Müller, S., Diederichsen, U., Fasshauer, D., Grubmüller, H., Hell, S. W., Eggeling, C., Kühnel, K., & Jahn, R. (2013). Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment. Nature Structural and Molecular Biology, 20, 679-686. doi:10.1038/nsmb.2570. [PubMan] : Jahn, R., & Fasshauer, D. (2012). Molecular machines governing exocytosis of synaptic vesicles. Nature, 490(7419), 201-207. doi:10.1038/nature11320. [PubMan] : Meijer, M., Burkhardt, P., de Wit, H., Toonen, R. F., Fasshauer, D., & Verhage, M. (2012). Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission. The EMBO Journal, 31(9), 2156-2168. doi:10.1038/emboj.2012.72. [PubMan] : Burkhardt, P., Stegmann, C. M., Cooper, B., Kloepper, T. H., Imig, C., Varoqueaux, F., Wahl, M. C., & Fasshauer, D. (2011). Primordial neurosecretory apparatus identified in the choanoflagellate Monosiga brevicollis. Proceedings of the National Academy of Sciences of the United States of America, 108(37), 15264-15269. doi:10.1073/pnas.110618910. [PubMan] : Wiederhold, K., Klöpper, T. H., Walter, A. M., Stein, A., Kienle, N., Sörensen, J. B., & Fasshauer, D. (2010). A coiled coil trigger site is essential for rapid binding of synaptobrevin to the SNARE acceptor complex. Journal of Biological Chemistry, 285(28), 21549-21559. doi:10.1074/jbc.M110.105148. [PubMan] : Walter, A. M., Wiederhold, K., Bruns, D., Fasshauer, D., & Soerensen, J. B. (2010). Synaptobrevin N-terminally bound to syntaxin–SNAP-25 defines the primed vesicle state in regulated exocytosis. The Journal of Cell Biology, 188(3), 401-413. doi:10.1083/jcb.200907018. [PubMan] : Domanska, M. K., Kiessling, V., Stein, A., Fasshauer, D., & Tamm, L. K. (2009). Single vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNARE-mediated membrane fusion. Journal of Biological Chemistry, 284(46), 32158-32166. Retrieved from http://www.jbc.org/content/284/46/32158.full.pdf+html?sid=1770b896-d743-4dee-b522-8c0eee7e8f9b. [PubMan] : Winter, U., Chen, X., & Fasshauer, D. (2009). A Conserved Membrane Attachment Site in alpha-SNAP Facilitates N-Ethylmaleimide-sensitive Factor (NSF)-driven SNARE Complex Disassembly. Journal of Biological Chemistry, 284(46), 31817-31826. doi:10.1074/jbc.M109.045286. [PubMan] : Kienle, N., Kloepper, T. H., & Fasshauer, D. (2009). Differences in the SNARE evolution of fungi and metazoa. Biochemical Society Transactions, 37, 787-791. doi:10.1042/BST0370787. [PubMan] : Wiederhold, K., & Fasshauer, D. (2009). Is assembly of the SNARE complex enough to fuel membrane fusion? Journal of Biological Chemistry, 284(19), 13143-13152. doi:10.1074/jbc.M900703200. [PubMan] : Kienle, N., Kloepper, T., & Fasshauer, D. (2009). Phylogeny of the SNARE vesicle fusion machinery yields insights into the conservation of the secretory pathway in fungi. BMC Evolutionary Biology, 9: 19. [PubMan] : Radhakrishnan, A., Stein, A., Jahn, R., & Fasshauer, D. (2009). The Ca2+ affinity of synaptotagmin 1 is markedly increased by a specific interaction of its C2B domain with phosphatidylinositol 4,5-bisphosphate. Journal of Biological Chemistry, 284, 25749-25760. Retrieved from http://www.jbc.org/content/284/38/25749.full.pdf+html. [PubMan] : Bar-On, D., Winter, U., Nachliel, E., Gutman, M., Fasshauer, D., Lang, T., & Ashery, U. (2008). Imaging the assembly and disassembly kinetics of cis-SNARE complexes on native plasma membranes. FEBS Letters, 582(23-24), 3563-3568. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T36-4THJ4J9-7-B&_cdi=4938&_user=38661&_orig=browse&_coverDate=10%2F15%2F2008&_sk=994179976&view=c&wchp=dGLbVtz-zSkzS&md5=9bed8ef1395b60f5ac34c173d9ab6112&ie=/sdarticle.pdf. [PubMan] : Kloepper, T. H., Kienle, N., & Fasshauer, D. (2008). SNAREing the basis of multicellularity: consequences of protein family expansion during evolution. Molecular Biology and Evolution, 25(9), 2055-2068. Retrieved from http://mbe.oxfordjournals.org/cgi/content/full/25/9/2055. [PubMan] : Barszczewski, M., Chua, J., Stein, A., Winter, U., Heintzmann, R., Zilly, F. E., Fasshauer, D., Lang, T., & Jahn, R. (2008). A novel site of action for α -SNAP in the SNARE conformational cycle controlling membrane fusion. Molecular Biology of the Cell, 19(3), 776-784. Retrieved from http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=2262999&blobtype=pdf. [PubMan] : Burkhardt, P., Hattendorf, D. A., Weis, W. I., & Fasshauer, D. (2008). Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide. The EMBO Journal, 27(7), 923-933. Retrieved from http://www.nature.com/emboj/journal/v27/n7/pdf/emboj200837a.pdf. [PubMan] : Stein, A., Radhakrishnan, A., Riedel, D., Fasshauer, D., & Jahn, R. (2007). Synaptotagmin activates membrane fusion through a Ca2+-dependent trans interaction with phospholipids. Nature Structure & Molecular Biology, 14(10), 904-911. Retrieved from http://www.nature.com/nsmb/journal/v14/n10/full/nsmb1305.html. [PubMan] : Kloepper, T. H., Kienle, N., & Fasshauer, D. (2007). An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system. Molecular Biology of the Cell, 18(9), 3463-3471. Retrieved from http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1951749. [PubMan] : Fasshauer, D., & Wiederhold, K. (2007). Thermodynamic studies on SNARE complex assembly. FEBS Journal, 274(Suppl. 1), 111-111. [PubMan] : Winter, U., & Fasshauer, D. (2007). Disrupting SNARE complexity - biophysical investigations of NSF/SNAP-mediated SNARE complex disassembly. FEBS Journal, 274(Suppl. 1), 112-112. [PubMan] : Burghardt, P., & Fasshauer, D. (2007). A common binding mode for Sec1/munc18 proteins. FEBS Journal, 274(Suppl. 1), 112-112. [PubMan] : Stein, A., Radhakrishnan, A., & Fasshauer, D. (2007). Studies on the molecular mechanism of the acceleration of SNARE-mediated membrane fusion by synaptotagmin 1. FEBS Journal, 274(Suppl. 1), 112-112. [PubMan] : Siddiqui, T. J., Vites, O., Stein, A., Heintzmann, R., Jahn, R., & Fasshauer, D. (2007). Determinants of synaptobrevin regulation in membranes. Molecular Biology of the Cell, 18(6), 2037-2046. Retrieved from http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1877092. [PubMan]