Structure, regulation and evolution of Nox‐family NADPH oxidases that produce reactive oxygen species
By H. Sumimoto. The FEBS Journal, 2008
693 citations recorded by the source corpus.
Subfields: Environmental Chemistry, Immunology, Physiology
View Paper: https://www.semanticscholar.org/paper/d8ce69a01499ddb69cddf57cb455ce4a00d86ebf
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Citations in the corpus
- Nox proteins in signal transduction (2009, background): “In contrast to the cytosolic localization of p47phox in resting cells, NoxO1 is constitutively associated with Nox1, and lacks the autoinhibitory region found on p47phox, which may be responsible for some constitutive activity [104].”
- NADPH Oxidase-4 Mediates Myofibroblast Activation and Fibrogenic Responses to Lung Injury (2009, background): “In support of this notion, NOX4 is almost exclusively expressed in chordate”
- Biochemistry, Physiology and Pathophysiology of NADPH Oxidases in the Cardiovascular System (2012, background): “Phosphatidylinositol (4,5)-bisphosphate modulates nox5 localization via an n-terminal polybasic region.”
- NADPH oxidase 4 (Nox4) is a major source of oxidative stress in the failing heart (2010, background): “Noxs are major enzymes responsible for production of superoxide (O2 ) by transferring electrons across the membrane from NAD(P)H to molecular oxygen (8, 9).”
- Respiratory burst oxidases: the engines of ROS signaling. (2011, background): “Plant RBOH proteins are homologues of the gp91 protein from mammalian phagocytes, which can induce oxidative burst in the absence of cytosolic components ([20,32,36]; Figure 1).”
- Oxygen Toxicity and Reactive Oxygen Species: The Devil Is in the Details (2009, background): “However, other cellular components, such as endoplasmic reticulum-bound enzymes, cytoplasmic enzyme systems, and the surface of the plasma membrane, also contribute (5,6).”