Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Donovan Ventimiglia"'
Publikováno v:
eLife, Vol 6 (2017)
Synaptic vesicle release properties vary between neuronal cell types, but in most cases the molecular basis of this heterogeneity is unknown. Here, we compare in vivo synaptic properties of two neuronal classes in the C. elegans central nervous syste
Externí odkaz:
https://doaj.org/article/c27ca233a5984ba8872e18390fab11d3
Autor:
Donovan Ventimiglia, Mia Krout, Jie Liu, Brett M. Collins, Haowen Liu, Jing Tang, Lei Li, Zhitao Hu, Jihong Bai, Janet E. Richmond, Yu Wang, Saroja Weeratunga, Yi Yu, Jingyao Xia
Publikováno v:
The Journal of cell biology. 220(4)
Ca2+-dependent neurotransmitter release requires synaptotagmins as Ca2+ sensors to trigger synaptic vesicle (SV) exocytosis via binding of their tandem C2 domains—C2A and C2B—to Ca2+. We have previously demonstrated that SNT-1, a mouse synaptotag
Autor:
Mary Ann Jordan, Leslie Wilson, Stuart C. Feinstein, Donovan Ventimiglia, Kenneth Rose, Alphan Altinok, M.E. Sargin, Erkan Kiris, B.S. Manjunath, Michelle R. Gaylord
Publikováno v:
Journal of Biological Chemistry. 286:14257-14270
Tau is a multiply phosphorylated protein that is essential for the development and maintenance of the nervous system. Errors in Tau action are associated with Alzheimer disease and related dementias. A huge literature has led to the widely held notio
Significance Most behaviors and neuronal responses are variable across individual animals and repeated presentation of the same stimulus. Current neuronal recording techniques examine one animal at a time, whereas hundreds to thousands of trials may
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3ed165f9fc532bf7c8568dbac1d759e
https://europepmc.org/articles/PMC3831453/
https://europepmc.org/articles/PMC3831453/
Autor:
Erkan, Kiris, Donovan, Ventimiglia, Mehmet E, Sargin, Michelle R, Gaylord, Alphan, Altinok, Kenneth, Rose, B S, Manjunath, Mary Ann, Jordan, Leslie, Wilson, Stuart C, Feinstein
Publikováno v:
The Journal of biological chemistry. 286(16)
Tau is a multiply phosphorylated protein that is essential for the development and maintenance of the nervous system. Errors in Tau action are associated with Alzheimer disease and related dementias. A huge literature has led to the widely held notio
Publikováno v:
Methods in cell biology. 95
The regulation of microtubule growing and shortening dynamics is essential for proper cell function and viability, and microtubule-associated proteins (MAPs) such as the neural protein tau are critical regulators of these dynamic processes. Further,
The regulation of microtubule growing and shortening dynamics is essential for proper cell function and viability, and microtubule-associated proteins (MAPs) such as the neural protein tau are critical regulators of these dynamic processes. Further,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::727275c2866e2d653070a45fab41a01a
https://doi.org/10.1016/s0091-679x(10)95024-3
https://doi.org/10.1016/s0091-679x(10)95024-3
Autor:
Daniel J. Needleman, Donovan Ventimiglia, Cyrus R. Safinya, Mahn Won Kim, Uri Raviv, Myung Chul Choi, Erkan Kiris, Michelle R. Gaylord, Leslie Wilson, Herbert P. Miller, Stuart C. Feinstein
Publikováno v:
Biophysical Journal. 96(3):504a-505a
Neuronal microtubules (MTs) are 25 nm protein nanotubes used as tracks for intracellular trafficking of biomolecules, for example, those involved in transmitting signals between neurons. Distinct members of MAP tau isoforms regulate microtubule assem
Autor:
Daniel J. Needleman, Cyrus R. Safinya, Myung Chul Choi, Donovan Ventimiglia, Michelle R. Gaylord, Stuart C. Feinstein, Nichole E. LaPointe, Leslie Wilson, Mahn Won Kim, Erkan Kiris, Herb P. Miller, Joanna Deek, Uri Raviv, Peter J. Chung
Publikováno v:
Biophysical Journal. (3):363a
Microtubules (MTs), a major component of the eukaryotic cytoskeleton, are 25 nm protein nanotubes with walls comprised of assembled protofilaments built from αβ heterodimeric tubulin. In neural cells, different isoforms of the microtubule-associate