Cysteine Oxidative Posttranslational Modifications
نویسندگان
چکیده
منابع مشابه
Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system.
In the cardiovascular system, changes in oxidative balance can affect many aspects of cellular physiology through redox-signaling. Depending on the magnitude, fluctuations in the cell's production of reactive oxygen and nitrogen species can regulate normal metabolic processes, activate protective mechanisms, or be cytotoxic. Reactive oxygen and nitrogen species can have many effects including t...
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Antioxidant enzymatic pathways form a critical network that detoxifies ROS in response to myocardial stress or injury. Genetic alteration of the expression levels of individual enzymes has yielded mixed results with regard to attenuating in vivo myocardial ischemia-reperfusion injury, an extreme oxidative stress. We hypothesized that overexpression of an antioxidant network (AON) composed of SO...
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P ho sp ho ry la ti o n N-Terminal: S6, S9, S15, T18, S20 ATM, DNAPK, • CK1 ERKs, ATR, p38 • kinase, mTOR, Chk1/Chk2, JNK, MAPKAP2, Hipk4 Activated by DNA damage, UV light, ionizing radiation, replicative senes• cence, or phosphatidylcholines. N-terminal phosphorylation causes p53 stabilization by inhibiting the p53• MDM2 interaction. Knockin mice carrying separate analogs to human Ser18/ • Ser...
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Reactive protein cysteine thiolates are instrumental in redox regulation. Oxidants, such as hydrogen peroxide (H2O2), react with thiolates to form oxidative post-translational modifications, enabling physiological redox signaling. Cardiac disease and aging are associated with oxidative stress which can impair redox signaling by altering essential cysteine thiolates. We previously found that car...
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Tissue factor (TF), a membrane protein, is an initiator of blood coagulation in vivo. In this review we discuss how posttranslational modifications affect activity and other properties of TF. Glycosylation of the extracellular domain and the composition of carbohydrates at three glycosylation sites have an influence on TF activity in the extrinsic FXase by increasing the rate of FX proteolysis....
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ژورنال
عنوان ژورنال: Circulation Research
سال: 2013
ISSN: 0009-7330,1524-4571
DOI: 10.1161/circresaha.112.268680