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NOX2/gp91phox is a critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. It also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc. Defects in CYBB are a cause of X-linke

This gene encodes a member of the Ced-4 family of apoptosis proteins. Ced-family members contain a caspase recruitment domain (CARD) and are known to be key mediators of programmed cell death. The encoded protein contains a distinct N-terminal pyrin-like motif, which is possibly involved in protein-protein interactions. This protein interacts strongly with caspase 2 and weakly with caspase 9. Overexpression of this gene was demonstrated to induce apoptosis in cells. Multiple alternatively spl

Myosin heavy chains are ubiquitous Actin-based motor proteins that convert the chemical energy derived from ATP hydrolysis into the mechanical energy that drives diverse motile processes in eukaryotic cells, including cytokinesis, vesicular transport and cellular locomotion. Muscle myosin is a heterohexamer consisting of two myosin heavy chains and two associated nonidentical pairs of myosin light chains. The seven myosin heavy chain isoforms that predominate in mammalian skeletal muscles inc

Varicella Zoster Virus (VZV), a member of the human herpes virus family, causes two distinct clinical manifestations: childhood chickenpox(Varicella) and shingles (zoster). Varicella is the outcome of the primary infection with VZV, whereas, zoster is the result of VZV reactivation from latently infected sensory ganglia which occurs predominantly in aging and immunosuppressed individuals.$nVZV virons are spherical and 150-200 nm in diameter. Its lipid envelope encloses the nucleocapsid of 16

The protein encoded by this gene is a member of the regulator of G protein signaling (RGS) family. RGS family members share similarity with S. cerevisiae SST2 and C. elegans egl-10 proteins, which contain a characteristic conserved RGS domain. RGS proteins accelerate GTPase activity of G protein alpha-subunits, thereby driving G protein into their inactive GDP-bound form, thus negatively regulating G protein signaling. RGS proteins have been implicated in the fine tuning of a variety of cellul

This gene encodes a member of the calcium dependent lectin superfamily of type II transmembrane receptors. Expression of the encoded protein is induced upon activation of T lymphocytes, and may play a role in proliferation. Furthermore, the protein may act to transmit signals in natural killer cells and platelets. [provided by RefSeq, Aug 2011]