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Eitan Reuveny
Researcher at Weizmann Institute of Science
Publications - 67
Citations - 4171
Eitan Reuveny is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: G protein-coupled inwardly-rectifying potassium channel & Potassium channel. The author has an hindex of 31, co-authored 61 publications receiving 3951 citations. Previous affiliations of Eitan Reuveny include Northwestern University & University of California, San Francisco.
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Journal ArticleDOI
Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel
TL;DR: A complementary DNA for a G-protein-coupled inwardly rectifying K+ channel (GIRK1) from rat heart is isolated and probably corresponds to the muscarinic K channel because its functional properties resemble those of the a trial muscaric K channel.
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Activation of the cloned muscarinic potassium channel by G protein βγ subunits
Eitan Reuveny,Paul A. Slesinger,James Inglese,Janine Morales,Jorge A. Iñiguez-Lluhi,Robert J. Lefkowitz,Henry R. Bourne,Yuh Nung Jan,Lily Yeh Jan +8 more
TL;DR: It is reported here that coexpression of GIRK1 with G βγ but not Gαβγ in Xenopus oocytes results in channel activity that persists in the absence of cytoplasmic GTP, and Gβγ appears to be sufficient for the activation of G IRK1 muscarinic potassium channels.
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Molecular Basis for Interactions of G Protein βγ Subunits with Effectors
Carolyn E. Ford,Nikolai P. Skiba,Hyunsu Bae,Yehia Daaka,Eitan Reuveny,Lee R. Shekter,Ramon Rosal,Gezhi Weng,Chii-Shen Yang,Ravi Iyengar,Richard J. Miller,Lily Yeh Jan,Robert J. Lefkowitz,Heidi E. Hamm +13 more
TL;DR: Analysis of the ability of mutants to regulate the activity of calcium and potassium channels, adenylyl cyclase 2, phospholipase C-β2, and β-adrenergic receptor kinase revealed the Gβ residues required for activation of each effector and provides evidence for partially overlapping domains on Gβ for regulation of these effectors.
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SARAF Inactivates the Store Operated Calcium Entry Machinery to Prevent Excess Calcium Refilling
TL;DR: SARAF is an endoplasmic reticulum membrane resident protein that associates with STIM to facilitate slow Ca(2+)-dependent inactivation of SOCE, a role that is likely to be important in protecting cells from Ca( 2+) overfilling.
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Regulation of sgk by aldosterone and its effects on the epithelial Na(+) channel.
TL;DR: regulation of sgk by aldosterone in native mammalian epithelia and its effect on ENaC are characterized to suggest that the response is mediated, at least in part, by occupancy of the mineralocorticoid receptor.