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Tullio Pozzan

Researcher at University of Padua

Publications -  32
Citations -  19543

Tullio Pozzan is an academic researcher from University of Padua. The author has contributed to research in topics: Mitochondrion & Intracellular. The author has an hindex of 28, co-authored 32 publications receiving 18821 citations. Previous affiliations of Tullio Pozzan include University of Massachusetts Amherst & National Research Council.

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Calcium homeostasis in intact lymphocytes: cytoplasmic free calcium monitored with a new, intracellularly trapped fluorescent indicator.

TL;DR: Quin2 is a tetracarboxylic acid which binds Ca2+ with 1:1 stoichiometry and an effective dissociation constant of 115 nM in a cationic background mimicking cytoplasm.
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Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca2+ Responses

TL;DR: The spatial relation between mitochondria and endoplasmic reticulum in living HeLa cells was analyzed at high resolution in three dimensions with two differently colored, specifically targeted green fluorescent proteins to emphasize the importance of cell architecture and the distribution of organelles in regulation of Ca2+ signaling.
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Neuron-to-astrocyte signaling is central to the dynamic control of brain microcirculation

TL;DR: In vivo blockade of glutamate-mediated [Ca2+]i elevations in astrocytes reduced the blood flow increase in the somatosensory cortex during contralateral forepaw stimulation and showed that neuron-to-astrocyte signaling is a key mechanism in functional hyperemia.
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BAX and BAK Regulation of Endoplasmic Reticulum Ca2+: A Control Point for Apoptosis

TL;DR: BAX and BAK operate in both the ER and mitochondria as an essential gateway for selected apoptotic signals, and targeting of BAX to mitochondria selectively restored apoptosis to “BH3-only” signals.
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Microdomains with high Ca2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria

TL;DR: It is concluded that in vivo, domains of high [Ca2+]i are transiently generated close to IP3-gated channels and sensed by nearby mitochondria; this may provide an efficient mechanism for optimizing mitochondrial activity upon cell stimulation.