redox   75

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Customize your Keyboard | FalbaTech
This looks like kind of a neat shop for custom-made Redox keyboards and the like.
keyboards  ergodox  redox  2020 
10 weeks ago by handcoding
Spatial and temporal alterations in protein structure by EGF regulate cryptic cysteine oxidation | Science Signaling
Stimulation of plasma membrane receptor tyrosine kinases (RTKs), such as the epidermal growth factor receptor (EGFR), locally increases the abundance of reactive oxygen species (ROS). These ROS then oxidize cysteine residues in proteins to potentiate downstream signaling. Spatial confinement of ROS is an important regulatory mechanism of redox signaling that enables the stimulation of different RTKs to oxidize distinct sets of downstream proteins. To uncover additional mechanisms that specify cysteines that are redox regulated by EGF stimulation, we performed time-resolved quantification of the EGF-dependent oxidation of 4200 cysteine sites in A431 cells. Fifty-one percent of cysteines were statistically significantly oxidized by EGF stimulation. Furthermore, EGF induced three distinct spatiotemporal patterns of cysteine oxidation in functionally organized protein networks, consistent with the spatial confinement model. Unexpectedly, protein crystal structure analysis and molecular dynamics simulations indicated widespread redox regulation of cryptic cysteine residues that are solvent exposed only upon changes in protein conformation. Phosphorylation and increased flux of nucleotide substrates served as two distinct modes by which EGF specified the cryptic cysteine residues that became solvent exposed and redox regulated. Because proteins that are structurally regulated by different RTKs or cellular perturbations are largely unique, these findings suggest that solvent exposure and redox regulation of cryptic cysteine residues contextually delineate redox signaling networks.
redox  oxidative_stress  EGF  ROS 
10 weeks ago by Segalllab
APE1 Upregulates MMP-14 via Redox-Sensitive ARF6-Mediated Recycling to Promote Cell Invasion of Esophageal Adenocarcinoma | Cancer Research
Esophageal adenocarcinoma (EAC) is an aggressive malignancy with poor clinical outcome. The incidence of EAC has been rising rapidly in the past three decades. Here, we showed that apurinic/apyrimidinic endonuclease (APE1) is overexpressed in EAC cell lines, and patients' samples of dysplasia and EAC. Downregulation of APE1 or inhibition of its redox function significantly repressed invasion. Overexpression of a redox-defective mutant, C65A, abrogated the proinvasive phenotype of APE1. APE1 regulated invasion via upregulation of matrix metalloproteinase 14 (MMP-14), which subsequently activated MMP-2, leading to degradation of the extracellular matrix in a redox-dependent manner. Downregulation of APE1 or inhibition of its redox function decreased the rate of endocytosis and recycling of MMP-14 protein. APE1 interacted with ARF6, a key regulator of MMP-14 recycling, which maintained ARF6 activity in an APE1-redox–dependent manner, promoting its ability to regulate MMP-14 recycling to the cell surface. In summary, these findings identify a novel redox-sensitive APE1–ARF6–MMP-14 signaling axis that mediates cellular invasion in esophageal carcinogenesis.

Significance: This study demonstrates the association between oxidative stress and the development and metastatic behavior of esophageal adenocarcinoma.
MMP14  arf6  recycling  membrane_targeting  MMP2  redox 
december 2019 by Segalllab
我也来个系列 #河马叔消磨时间,分享一些很耗时间但于己没什么用的东西。

第 1 期 —— 体验 Redox 操作系统

是一个专注于安全(可靠)的微内核操作系统,目标兼容 Linux|POSIX 程序。

Redox  from twitter_favs
august 2019 by robbinhan
Mahjong Chem
play mahjong to practice oxidation numbers, polyatomic ions, whether a compound is a strong or weak electrolyte, electron configurations, weak and strong acids and bases, whether pairs of compounds form precipitates, metric prefixes, and elemental symbols
science  chemistry  practice  atoms  molecules  matter  acid_base  measurement  redox  applet  AP_chem  games  nomenclature  electrons 
june 2019 by MsHsi
Redox State Controls Phase Separation of the Yeast Ataxin-2 Protein via Reversible Oxidation of Its Methionine-Rich Low-Complexity Domain - ScienceDirect
Interesting way for redox levels to regulate phase separations

Yeast ataxin-2, also known as Pbp1, senses the activity state of mitochondria in order to regulate TORC1. A domain of Pbp1 required to adapt cells to mitochondrial activity is of low sequence complexity. The low-complexity (LC) domain of Pbp1 forms labile, cross-β polymers that facilitate phase transition of the protein into liquid-like or gel-like states. Phase transition for other LC domains is reliant upon widely distributed aromatic amino acids. In place of tyrosine or phenylalanine residues prototypically used for phase separation, Pbp1 contains 24 similarly disposed methionine residues. Here, we show that the Pbp1 methionine residues are sensitive to hydrogen peroxide (H2O2)-mediated oxidation in vitro and in living cells. Methionine oxidation melts Pbp1 liquid-like droplets in a manner reversed by methionine sulfoxide reductase enzymes. These observations explain how reversible formation of labile polymers by the Pbp1 LC domain enables the protein to function as a sensor of cellular redox state.
redox  oxidative_stress  phase_separation 
may 2019 by Segalllab

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