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Jerry P. Eu

Researcher at Duke University

Publications -  26
Citations -  4524

Jerry P. Eu is an academic researcher from Duke University. The author has contributed to research in topics: Ryanodine receptor & RYR1. The author has an hindex of 21, co-authored 26 publications receiving 4381 citations. Previous affiliations of Jerry P. Eu include Howard Hughes Medical Institute.

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Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient

TL;DR: By sensing the physiological oxygen gradient in tissues, hemoglobin exploits conformation-associated changes in the position of cysteinebeta93 SNO to bring local blood flow into line with oxygen requirements.
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Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation.

TL;DR: Results reveal that ion channels can differentiate nitrosative from oxidative signals and indicate that the cardiac calcium release channel (ryanodine receptor) in canines is regulated by posttranslational chemical modification(s) of sulfurs.
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The skeletal muscle calcium release channel: Coupled O2 sensor and NO signaling functions

TL;DR: The demonstration that channel cysteine residues subserve coupled O2 sensor and NO regulatory functions and that these operate through the prototypic allosteric effector calmodulin may have general implications for the regulation of redox-related systems.
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STIM1 signalling controls store-operated calcium entry required for development and contractile function in skeletal muscle

TL;DR: It is shown that stromal interaction molecule 1 is expressed in both myotubes and adult skeletal muscle, and it is suggested that STIM1 has a universal role as an ER/SR calcium sensor in both excitable and non-excitable cells.
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Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO

TL;DR: The results reveal that different cysteines within the channel have been adapted to serve in nitrosative and oxidative responses, and that S-nitrosylation of the cysteine-containing CaM-binding domain underlies the mechanism of CaM -dependent regulation of RyR1 by NO.