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MeSH Review


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Disease relevance of Oxidation-Reduction


Psychiatry related information on Oxidation-Reduction


High impact information on Oxidation-Reduction

  • Cellular redox status is maintained by intracellular redox-regulating molecules, including thioredoxin (TRX) [11].
  • Molybdenum-cofactor-containing enzymes catalyze the transfer of an oxygen atom, ultimately derived from or incorporated into water, to or from a substrate in a two-electron redox reaction [12].
  • Moreover, redox chemistry appears to play a critical role both in the trans-activation of oxygen-responsive genes in unicellular organisms as well as in the activation of HIF-1 [13].
  • The catalytic mechanism of FGly generation was elucidated by six high-resolution structures of FGE in different redox environments [14].
  • The oxidation state of the heme iron also determines whether E75 can interact with its heterodimer partner DHR3, suggesting an additional role as a redox sensor [15].

Chemical compound and disease context of Oxidation-Reduction


Biological context of Oxidation-Reduction

  • Dueling activities of AIF in cell death versus survival: DNA binding and redox activity [21].
  • These studies thus link the H2B transcriptional machinery to cell cycle regulators, and possibly to cellular metabolic state (redox status), and set the stage for studies of the underlying mechanisms and the basis for coordinated histone gene expression and coupling to DNA replication [22].
  • The resulting structure transports calcium ions across the bilayer of a liposome to develop both a calcium ion concentration gradient and a membrane potential, expanding Mitchell's concept of a redox loop mechanism for protons to include divalent cations [23].
  • In contrast, the neuroprotective effects of NO result from downregulation of NMDA-receptor activity by reaction with thiol group(s) of the receptor's redox modulatory site [24].
  • A previously unknown redox cofactor has been identified in the active site of lysyl oxidase from the bovine aorta [25].

Anatomical context of Oxidation-Reduction


Associations of Oxidation-Reduction with chemical compounds

  • Irradiation with blue light relieves this repression, presumably through an intra- or intermolecular redox reaction mediated through the flavin bound to the N-terminal photolyase-like domain [30].
  • Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form [31].
  • Here we report that PO2 dynamically controls the redox state of 6-8 out of 50 thiols in each RyR1 subunit and thereby tunes the response to NO [32].
  • The catalytic activity of Ltk in the ER may be regulated via changes in the cellular redox potential, a novel mechanism for regulating protein tyrosine kinases [33].
  • A pleiotropic-negative mutant in mttA prevents the periplasmic localization of twin arginine redox enzymes, including nitrate reductase (NapA) and trimethylamine N-oxide reductase (TorA) [34].

Gene context of Oxidation-Reduction

  • Txnip encodes a cytoplasmic protein that binds and inhibits thioredoxin, a major regulator of cellular redox state [35].
  • We propose that UCP-2 is an inducible protein that is neuroprotective by activating cellular redox signaling or by inducing mild mitochondrial uncoupling that prevents the release of apoptogenic proteins [36].
  • Human HAP1 (REF1) encodes the major AP endonuclease which, in addition to its role in DNA repair, functions as a redox regulatory protein [37].
  • Thus, antigen receptor signaling induces generation of discrete species of oxidants that selectively regulate two distinct redox sensitive pathways, a proapoptotic (FasL) and a proliferative pathway (ERK) [38].
  • Together, we here present evidence showing that cellular glucocorticoid responsiveness is coordinately modulated by redox state and TRX level and propose that cross talk between neuroendocrine control of stress responses and cellular antioxidant systems may be essential for mammalian adaptation processes [39].

Analytical, diagnostic and therapeutic context of Oxidation-Reduction

  • Such interactions may be prevented by altering the intracellular redox potential or by site-directed mutagenesis of the relevant cysteine residue(s) [40].
  • Isosbestic fluorometry provides appropriate correction for these vascular phenomena and permits simultaneous evaluation of mitochondrial nicotinamide adenine dinucleotide redox state, microcirculatory volume, and hemoglobin oxygenation [41].
  • To determine effects of the increased sympathetic vasoconstrictor drive on muscle oxygenation, we measured changes in tissue oxygen stores and mitochondrial cytochrome a,a3 redox state in rhythmically contracting human forearm muscles with near infrared spectroscopy while simultaneously measuring muscle SNA with microelectrodes [42].
  • Evidence for control of this activity by a redox site in cell cultures, brain tissues and in recombinant NMDA receptors are discussed by Henri Gozlan and Yehezkel Ben-Ari [43].
  • The redox potentials that were obtained from analysis of the cyclic "voltammograms," 365 mV for cytochrome f and 250 and 380 mV for cytochrome c oxidase (vs. normal hydrogen electrode), compare quite well with the values reported by using conventional titration methods [44].


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