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Ole Thastrup

Researcher at Novo Nordisk

Publications -  47
Citations -  7540

Ole Thastrup is an academic researcher from Novo Nordisk. The author has contributed to research in topics: Thapsigargin & Calcium. The author has an hindex of 30, co-authored 44 publications receiving 7438 citations. Previous affiliations of Ole Thastrup include National Institutes of Health & University College London.

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Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase.

TL;DR: The results suggest that thapsigargin increases the concentration of cytosolic free Ca2+ in sensitive cells by an acute and highly specific arrest of the endoplasmic reticulum Ca 2+ pump, followed by a rapid Ca2+.
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Activation of calcium entry by the tumor promoter thapsigargin in parotid acinar cells. Evidence that an intracellular calcium pool and not an inositol phosphate regulates calcium fluxes at the plasma membrane.

TL;DR: The mechanisms for activation of Ca2+ entry by thapsigargin and methacholine are the same and are consistent with the idea that entry is initiated by the depletion of the intracellular inositol 1,4,5-trisphosphate-sensitive Ca2+, according to previously proposed models.
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Thapsigargin, a novel molecular probe for studying intracellular calcium release and storage.

TL;DR: This work aims to demonstrate the efforts towards in-situ applicability of EMMARM, which aims to provide real-time information about concrete mechanical properties of EMTs.
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[Leu31, Pro34]neuropeptide Y: a specific Y1 receptor agonist

TL;DR: It is concluded that [Leu31, Pro34]NPY is a specific Y1 receptor agonist and that the analog or variants of it can be useful in delineating the physiological importance of Y1 receptors.
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A novel tumour promoter, thapsigargin, transiently increases cytoplasmic free Ca2+ without generation of inositol phosphates in NG115-401L neuronal cells.

TL;DR: The data suggest that thapsigargin releases Ca2+ from an intracellular store by a novel mechanism, independent of the hydrolysis of phosphoinositides and concomitant activation of protein kinase C, which may provide a valuable tool for the analysis of intrACEllular signalling mechanisms.