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Péter Várnai

Researcher at Semmelweis University

Publications -  156
Citations -  14102

Péter Várnai is an academic researcher from Semmelweis University. The author has contributed to research in topics: Receptor & Endoplasmic reticulum. The author has an hindex of 53, co-authored 145 publications receiving 12835 citations. Previous affiliations of Péter Várnai include Centre national de la recherche scientifique & University of Sussex.

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Structural and functional features and significance of the physical linkage between ER and mitochondria

TL;DR: An unexpected dependence of cell function and survival is revealed on the maintenance of proper spacing between the ER and mitochondria, which makes mitochondria prone to Ca2+ overloading and ensuing permeability transition.
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Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels.

TL;DR: It is demonstrated that VDAC1 is physically linked to the endoplasmic reticulum Ca2+-release channel inositol 1,4,5-trisphosphate receptor (IP3R) through the molecular chaperone glucose-regulated protein 75 (grp75) and functional interaction between the channels was shown by the recombinant expression of the ligand-binding domain of the IP3R on the ER or mitochondrial surface.
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Identification of renox, an NAD(P)H oxidase in kidney.

TL;DR: The data suggest that Renox, as a renal source of reactive oxygen species, is a likely candidate for the oxygen sensor function regulating oxygen-dependent gene expression and may also have a role in the development of inflammatory processes in the kidney.
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Visualization of Phosphoinositides That Bind Pleckstrin Homology Domains: Calcium- and Agonist-induced Dynamic Changes and Relationship to Myo-[3H]inositol-labeled Phosphoinositide Pools

TL;DR: In this paper, the PLC(4,5)P2 pools that bind pleckstrin homology (PH) domains were visualized by cellular expression of a PLCδ PH domain and analysis of confocal images in living cells.

Visualization of phosphoinositides that bind pleckstrin homology domains

TL;DR: Identification and dynamic imaging of phosphoinositides that interact with PH domains will further the understanding of the regulation of such proteins by inositol phospholipids.