Jeremy Samuel Dittman

Affiliations: 
Weill Cornell Medical College, New York, NY, United States 
Area:
Molecules of Synaptic Transmission
Website:
http://sites.google.com/site/dittmanlabhomepage/
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"Jeremy Dittman"
Mean distance: 13.69 (cluster 11)
 
SNBCP

Parents

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Wade G. Regehr grad student 2000 Harvard
 (Presynaptic modulation of transmitter release in the central nervous system.)
Joshua M. Kaplan post-doc 2003-2007 Harvard Medical School/ Massachusetts General Hospital
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Publications

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Guiberson NGL, Pineda A, Abramov D, et al. (2018) Mechanism-based rescue of Munc18-1 dysfunction in varied encephalopathies by chemical chaperones. Nature Communications. 9: 3986
Wragg RT, Parisotto DA, Li Z, et al. (2017) Evolutionary Divergence of the C-terminal Domain of Complexin Accounts for Functional Disparities between Vertebrate and Invertebrate Complexins. Frontiers in Molecular Neuroscience. 10: 146
Snead D, Lai AL, Wragg RT, et al. (2017) Unique Structural Features of Membrane-Bound C-Terminal Domain Motifs Modulate Complexin Inhibitory Function. Frontiers in Molecular Neuroscience. 10: 154
Lipstein N, Verhoeven-Duif NM, Michelassi FE, et al. (2017) Synaptic UNC13A protein variant causes increased neurotransmission and dyskinetic movement disorder. The Journal of Clinical Investigation
Wragg RT, Gouzer G, Bai J, et al. (2015) Synaptic activity regulates the abundance and binding of complexin. Biophysical Journal. 108: 1318-29
Radoff DT, Dong Y, Snead D, et al. (2014) The accessory helix of complexin functions by stabilizing central helix secondary structure. Elife. 3
Goren MA, Morizumi T, Menon I, et al. (2014) Constitutive phospholipid scramblase activity of a G protein-coupled receptor. Nature Communications. 5: 5115
Snead D, Wragg RT, Dittman JS, et al. (2014) Membrane curvature sensing by the C-terminal domain of complexin. Nature Communications. 5: 4955
Wragg RT, Snead D, Dong Y, et al. (2013) Synaptic vesicles position complexin to block spontaneous fusion. Neuron. 77: 323-34
Georgiev AG, Sullivan DP, Kersting MC, et al. (2011) Osh proteins regulate membrane sterol organization but are not required for sterol movement between the ER and PM. Traffic (Copenhagen, Denmark). 12: 1341-55
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