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Sergey Zelenin

Researcher at Royal Institute of Technology

Publications -  37
Citations -  2187

Sergey Zelenin is an academic researcher from Royal Institute of Technology. The author has contributed to research in topics: Aquaporin 4 & Water transport. The author has an hindex of 22, co-authored 37 publications receiving 2036 citations. Previous affiliations of Sergey Zelenin include Karolinska Institutet & Aarhus University.

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Journal ArticleDOI

Water permeability of aquaporin-4 is decreased by protein kinase C and dopamine

TL;DR: It is concluded that PKC and dopamine decrease AQP4 water permeability via phosphorylation at Ser180 and that the effect is likely mediated by gating of the channel.
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Cell signaling microdomain with Na,K-ATPase and inositol 1,4,5-trisphosphate receptor generates calcium oscillations.

TL;DR: It is reported that Na,K-ATPase and inositol 1,4,5-trisphosphate ( InsP3) receptor (InsP3R) form a cell signaling microdomain that, in the presence of ouabain, generates slow Ca2+ oscillations in renal cells.
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Adenylate cyclase-coupled vasopressin receptor activates AQP2 promoter via a dual effect on CRE and AP1 elements.

TL;DR: The role of vasopressin is established as a regulator of transcription and the first example of how a message from a highly specific receptor is transduced to the transcription of a final target protein with known biological effects is established.
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Identification of a molecular target for glutamate regulation of astrocyte water permeability.

TL;DR: It is reported that glutamate increases astrocyte water permeability and that the molecular target for this effect is the aquaporin‐4 (AQP4) serine 111 residue, which is in a strategic position for control of the water channel gating.
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Low Doses of Ouabain Protect from Serum Deprivation–Triggered Apoptosis and Stimulate Kidney Cell Proliferation via Activation of NF-κB

TL;DR: It was shown that the NH2 terminal tail of the Na,K-ATPase alpha subunit plays a key role in ouabain-triggered calcium oscillations and did not protect from apoptosis in serum-deprived cells that expressed a mutant Na, kappaB subunit with deletion of the NH1 terminal tail.