J
Junjie Wang
Researcher at University of Miami
Publications - 20
Citations - 1635
Junjie Wang is an academic researcher from University of Miami. The author has contributed to research in topics: Pannexin & Membrane channel. The author has an hindex of 14, co-authored 17 publications receiving 1486 citations.
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Journal ArticleDOI
Activation of pannexin 1 channels by ATP through P2Y receptors and by cytoplasmic calcium
TL;DR: It is shown that pannexin 1 channels can be activated by extracellular ATP acting through purinergic receptors of the P2Y group as well as by cytoplasmic calcium.
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Modulation of membrane channel currents by gap junction protein mimetic peptides: size matters
TL;DR: The channel inhibition by peptides shares commonalities with channel effects of polyethylene glycol (PEG), suggesting a steric block as a mechanism and a functional relatedness of innexin and pannexin channels.
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Pannexin1 and Pannexin2 Channels Show Quaternary Similarities to Connexons and Different Oligomerization Numbers from Each Other
Cinzia Ambrosi,Oliver Gassmann,Jennifer Pranskevich,Daniela Boassa,Amy Smock,Junjie Wang,Gerhard Dahl,Claudia Steinem,Gina E. Sosinsky +8 more
TL;DR: This work expressed and purified Panx1 and Panx2 using a baculovirus Sf9 expression system and obtained doughnut-like structures similar to those seen previously in purified connexin hemichannels (connexons) and mammalian membranes, finding that they were unstable over time.
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ATP signaling is deficient in cultured Pannexin1-null mouse astrocytes.
TL;DR: The electrophysiological and fluorescence imaging analyses performed on these cells fully support the previous pharmacological and Panx1 knockdown studies that showed profoundly lower dye uptake and ATP release than wild‐type untreated astrocytes and propose thatPanx1 channels serve as K+ sensors for changes in the extracellular milieu such as those occurring under pathological conditions.
Journal ArticleDOI
The bizarre pharmacology of the ATP release channel pannexin1
TL;DR: Observations indicate that Panx1 may play an extended role in a wider spectrum of physiological functions, and may share structural domains with other proteins, not readily revealed by sequence alignments.