Zobrazeno 1 - 10
of 72
pro vyhledávání: '"Ilana Lotan"'
Autor:
Noa Regev, Nurit Degani-Katzav, Alon Korngreen, Adi Etzioni, Sivan Siloni, Alessandro Alaimo, Dodo Chikvashvili, Alvaro Villarroel, Bernard Attali, Ilana Lotan
Publikováno v:
PLoS ONE, Vol 4, Iss 8, p e6586 (2009)
KCNQ2/KCNQ3 channels are the molecular correlates of the neuronal M-channels, which play a major role in the control of neuronal excitability. Notably, they differ from homomeric KCNQ2 channels in their distribution pattern within neurons, with uniqu
Externí odkaz:
https://doaj.org/article/8a52ffdfa7b84c1d8195262192e537be
Publikováno v:
PLoS ONE, Vol 3, Iss 1, p e1381 (2008)
K(+) efflux through voltage-gated K(+) (Kv) channels can attenuate the release of neurotransmitters, neuropeptides and hormones by hyperpolarizing the membrane potential and attenuating Ca(2+) influx. Notably, direct interaction between Kv2.1 channel
Externí odkaz:
https://doaj.org/article/47a71351f69a468982581c3dda5b17da
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 13556, p 13556 (2021)
International Journal of Molecular Sciences; Volume 22; Issue 24; Pages: 13556
International Journal of Molecular Sciences; Volume 22; Issue 24; Pages: 13556
The polybasic juxtamembrane region (5RK) of the plasma membrane neuronal SNARE, syntaxin1A (Syx), was shown by us to act as a fusion clamp in PC12 cells, making release dependent on stimulation by Ca2+. By using a Syx-based FRET probe, we demonstrate
Publikováno v:
International Journal of Molecular Sciences
The polybasic juxtamembrane region (5RK) of the plasma membrane neuronal SNARE, syntaxin1A (Syx), was previously shown by us to act as a fusion clamp in PC12 cells, as charge neutralization of 5RK promotes spontaneous and inhibits Ca2+-triggered rele
Autor:
Dafna Greitzer-Antes, Anton Sheinin, Dafna Singer-Lahat, Izhak Michaelevski, Ilana Lotan, Noa Barak-Broner
Publikováno v:
The Journal of Neuroscience. 38:220-231
The exact function of the polybasic juxtamembrane region (5RK) of the plasma membrane neuronal SNARE, syntaxin 1A (Syx), in vesicle exocytosis, although widely studied, is currently not clear. Here, we addressed the role of 5RK in Ca2+-triggered rele
Autor:
Elias Aizenman, Karen A. Hartnett, Kai He, Paul H. M. Kullmann, Ilana Lotan, John P. Horn, Meghan C. McCord
Publikováno v:
The Journal of Physiology. 592:3511-3521
Key points K+ efflux through newly membrane-inserted voltage-gated Kv2.1 K+ channels precedes neuronal apoptosis. In this study, we show that the binding site of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protei
Publikováno v:
Journal of the Neurological Sciences. 338:39-42
Objectives There is insufficient data on the efficacy of intravenous immunoglobulins (IVIg) as maintenance treatment in myasthenia gravis (MG). We therefore examined response to maintenance IVIg therapy in a cohort of MG patients. Methods We reviewed
Autor:
Dafna Greitzer-Antes, Roi Strulovich, Adi Etzioni, Joel A. Hirsch, Sivan Siloni, Dodo Chikvashvilli, Dana Sachyani, Noa Regev, Ilana Lotan
Publikováno v:
The Journal of Neuroscience. 31:14158-14171
Whereas neuronal M-type K+channels composed of KCNQ2 and KCNQ3 subunits regulate firing properties of neurons, presynaptic KCNQ2 subunits were demonstrated to regulate neurotransmitter release by directly influencing presynaptic function. Two interac
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:
Biochemistry. 47:8342-8349
Previously, we have demonstrated physical and functional interactions of the voltage-gated potassium channel Kv2.1 with the plasma membrane protein components of the exocytotic SNARE complex, syntaxin 1A, and the t-SNARE, syntaxin 1A/SNAP-25, complex