Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Reut Friedrich"'
Autor:
Reut Friedrich, Uri Ashery
Publikováno v:
Journal of Neuroscience Methods. 193:271-280
Amperometry is a commonly used technique for detecting the kinetics of single-vesicle exocytosis with excellent temporal and spatial resolution. However, different methods of analyzing the amperometric signals can produce conflicting conclusions. We
Autor:
Rachel Nachman, Jens Rettig, Uri Ashery, Ilana Lotan, Dodo Chikvashvili, Reut Friedrich, Lori Feinshreiber, Anton Sheinin, Ofer Yizhar, Dafna Singer-Lahat, Ulf Matti
Publikováno v:
Journal of Cell Science. 123:1940-1947
Regulation of exocytosis by voltage-gated K+ channels has classically been viewed as inhibition mediated by K+ fluxes. We recently identified a new role for Kv2.1 in facilitating vesicle release from neuroendocrine cells, which is independent of K+ f
Publikováno v:
Journal of Neurochemistry. 97:818-833
Elevation of the intracellular calcium concentration ([Ca2+]i) to levels below 1 µm alters synaptic transmission and induces short-term plasticity. To identify calcium sensors involved in this signalling, we investigated soluble C2 domain-containing
Publikováno v:
Molecular neurobiology. 41(1)
Ca(+2)-dependent exocytosis involves vesicle docking, priming, fusion, and recycling. This process is performed and regulated by a vast number of synaptic proteins and depends on proper protein-protein and protein-lipid interactions. Double C2 domain
Autor:
Emma Connell, Uri Ashery, Orit Gutman, Yoav I. Henis, Reut Friedrich, Alexander J. Groffen, J. R. T. van Weering, Bazbek Davletov
Publikováno v:
Friedrich, R, Groffen, A J A, Connell, E, van Weering, J R T, Gotman, O, Henis, Y I, Davletov, B & Ashery, U 2008, ' DOC2B acts as a calcium switch and enhances vesicle fusion ', The Journal of Neuroscience, vol. 28, pp. 6794-6806 . https://doi.org/10.1523/JNEUROSCI.0538-08.2008
Friedrich, R, Groffen, A J A, Connell, E, van Weering, J R T, Gotman, O, Henis, Y I, Davletov, B & Ashery, U 2008, ' DOC2B acts as a calcium switch and enhances vesicle fusion ', Journal of Neuroscience, vol. 28, pp. 6794-6806 . https://doi.org/10.1523/JNEUROSCI.0538-08.2008
Journal of Neuroscience, 28, 6794-6806. Society for Neuroscience
The Journal of Neuroscience, 28, 6794-6806. Society for Neuroscience
Friedrich, R, Groffen, A J A, Connell, E, van Weering, J R T, Gotman, O, Henis, Y I, Davletov, B & Ashery, U 2008, ' DOC2B acts as a calcium switch and enhances vesicle fusion ', Journal of Neuroscience, vol. 28, pp. 6794-6806 . https://doi.org/10.1523/JNEUROSCI.0538-08.2008
Journal of Neuroscience, 28, 6794-6806. Society for Neuroscience
The Journal of Neuroscience, 28, 6794-6806. Society for Neuroscience
Calcium-dependent exocytosis is regulated by a vast number of proteins. DOC2B is a synaptic protein that translocates to the plasma membrane (PM) after small elevations in intracellular calcium concentration. The aim of this study was to investigate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09733616d23d413f94b1f8692dfe5e23
https://research.vu.nl/en/publications/3418371a-fd54-4082-bd4d-73c48a8e0079
https://research.vu.nl/en/publications/3418371a-fd54-4082-bd4d-73c48a8e0079
Autor:
Uri Ashery, Ilana Lotan, Reut Friedrich, Dodo Chikvashvili, Dafna Singer-Lahat, Dafna Greitzer, Lori Feinshreiber, Anton Sheinin, Sharon Tsuk, Edwin S. Levitan, Morris Benveniste
Kv channels inhibit release indirectly by hyperpolarizing membrane potential, but the significance of Kv channel interaction with the secretory apparatus is not known. The Kv2.1 channel is commonly expressed in the soma and dendrites of neurons, wher
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db6840d044ed3fc8d0873dee503e0f0f
https://europepmc.org/articles/PMC6673747/
https://europepmc.org/articles/PMC6673747/
Publikováno v:
Journal of neurochemistry. 97(3)
Elevation of the intracellular calcium concentration ([Ca2+]i) to levels below 1 microm alters synaptic transmission and induces short-term plasticity. To identify calcium sensors involved in this signalling, we investigated soluble C2 domain-contain