Protein Tyrosine Phosphatases as Mediators of Redox Signaling

Hertog, Jeroen den

doi:10.1002/9783527627585.ch8

Cited by 2 publications

(1 citation statement)

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“…Because of the properties, redox modification on cysteine residues could influence function of proteins reversibly and consume ROS by generating cysteine sulfenic acide (R-SOH) and cysteine sulfinic acid (R-SO 2 H) 61 . Otherwise, cysteine residues modification could cause allosteric interaction in proteins and alter or eliminate protein function permanently as well 62 . Redox modification on protein cysteine thiol has been shown to regulate protein activity involved in transcription, translation and function performing 63 .…”

Section: The Relation Between Oxidative Stress and Crcmentioning

confidence: 99%

Redox Imbalance in the Development of Colorectal Cancer

et al. 2017

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Redox imbalance is resulted from the destruction of balance between oxidants and antioxidants. The dominant oxidants are reactive oxygen species (ROS), which are involved in multiple cellular processes by physiologically transporting signal as a second messenger or pathologically oxidizing DNA, lipids, and proteins. Generally speaking, low concentration of ROS is indispensable for cell survival and proliferation. However, high concentration of ROS is cytotoxic. Additionally, ROS are now known to induce the oxidative modification of macromolecules especially proteins. The redox modification of proteins is involved in numerous biological processes related to diseases including CRC. Herein, we attempt to afford an overview that highlights the crosstalk between redox imbalance and CRC.

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Section: The Relation Between Oxidative Stress and Crcmentioning

confidence: 99%