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Journal articles on the topic 'Oxidative inactivation'

Author: Grafiati

Published: 7 June 2025

Last updated: 2 August 2025

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1

Gopalakrishna, R., and W. B. Anderson. "Ca2+- and phospholipid-independent activation of protein kinase C by selective oxidative modification of the regulatory domain." Proceedings of the National Academy of Sciences 86, no. 17 (1989): 6758–62. http://dx.doi.org/10.1073/pnas.86.17.6758.

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The susceptibility of purified protein kinase C to oxidative inactivation by H2O2 was found to be increased by Ca2+ either alone at a high (5 mM) concentration or at a low (approximately 50 microM) concentration along with phosphatidylserine and diacylglycerol and by tumor-promoting phorbol esters even in the absence of Ca2+. This suggested that the membrane-bound and/or catalytically active form of protein kinase C is relatively more susceptible to oxidative inactivation. Although both the regulatory and catalytic domains of protein kinase C were susceptible to oxidative inactivation, a selec

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2

Andersson, S., A. Kheiter, and T. A. Merritt. "Oxidative Inactivation of Surfactants." Lung 177, no. 3 (1999): 179–89. http://dx.doi.org/10.1007/pl00007639.

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3

Janero, D. R., and C. Yarwood. "Oxidative modulation and inactivation of rabbit cardiac adenylate deaminase." Biochemical Journal 306, no. 2 (1995): 421–27. http://dx.doi.org/10.1042/bj3060421.

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Oxidative stress and adenine nucleotide catabolism occur concomitantly in several disease states, such as cardiac ischaemia-reperfusion, and may act as synergistic determinants of tissue injury. However, the mechanisms underlying this potential interaction remain ill-defined. We examined the influence of oxidative stress on the molecular, kinetic and regulatory properties of a ubiquitous AMP-catabolizing enzyme, adenylate deaminase (AMPD) (EC 3.5.4.6). To this intent, rabbit heart AMPD and an H2O2/ascorbate/iron oxidation system were employed. Enzyme exposure to the complete oxidation system a

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4

Andersson, Sture, Ahmed Kheiter, Erlinda Manalo, John Amirkhanian, and T. Allen Merritt. "OXIDATIVE INACTIVATION OF SURFACTANT † 1929." Pediatric Research 39 (April 1996): 324. http://dx.doi.org/10.1203/00006450-199604001-01953.

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Ceccaldi, Pierre, Marta C. Marques, Vincent Fourmond, Inês Cardoso Pereira, and Christophe Léger. "Oxidative inactivation of NiFeSe hydrogenase." Chemical Communications 51, no. 75 (2015): 14223–26. http://dx.doi.org/10.1039/c5cc05930e.

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We propose a resolution to the paradox that spectroscopic studies of NiFeSe hydrogenase have not revealed any major signal attributable to Ni<sup>III</sup> states formed upon reaction with O<sub>2</sub>, despite the fact that two inactive states are formed upon either aerobic or anaerobic oxidation.

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6

Parkkinen, Jaakko, Outi Vääränen, and Elina Vahtera. "Plasma Ascorbate Protects Coagulation Factors against Photooxidation." Thrombosis and Haemostasis 75, no. 02 (1996): 292–97. http://dx.doi.org/10.1055/s-0038-1650263.

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SummaryIt has been suggested that proteins, unlike lipids, are not protected against oxidative damage by antioxidants in plasma. We have studied the effect of photodynamic virus inactivation treatment of fresh human plasma on coagulation factor activities. Photodynamic treatment generates singlet oxygen which causes inactivation of fibrinogen and factor VIII. Other coagulation factors or anticoagulant proteins are clearly less affected. We found that there is an inverse correlation between the extent of coagulation factor inactivation during the treatment and the plasma ascorbate concentration

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7

Cavarra, Eleonora, Monica Lucattelli, Federica Gambelli, et al. "Human SLPI inactivation after cigarette smoke exposure in a new in vivo model of pulmonary oxidative stress." American Journal of Physiology-Lung Cellular and Molecular Physiology 281, no. 2 (2001): L412—L417. http://dx.doi.org/10.1152/ajplung.2001.281.2.l412.

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The role of oxidative stress in inactivating antiproteases is the object of debate. To address this question, we developed an in vivo model of pulmonary oxidative stress induced by cigarette smoke (CS) in mice. The major mouse trypsin inhibitor contrapsin is not sensitive to oxidation, and the mouse secretory leukoprotease inhibitor (SLPI) does not inhibit trypsin. Instead, human recombinant (hr) SLPI inhibits trypsin and is sensitive to oxidation. Thus we determined the effect of CS in vivo on hrSLPI antiproteolytic function in the airways of mice. CS caused a significant decrease in total an

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8

Kim, Sunghwan, Dionisia P. Sideris, Carolyn S. Sevier, and Chris A. Kaiser. "Balanced Ero1 activation and inactivation establishes ER redox homeostasis." Journal of Cell Biology 196, no. 6 (2012): 713–25. http://dx.doi.org/10.1083/jcb.201110090.

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The endoplasmic reticulum (ER) provides an environment optimized for oxidative protein folding through the action of Ero1p, which generates disulfide bonds, and Pdi1p, which receives disulfide bonds from Ero1p and transfers them to substrate proteins. Feedback regulation of Ero1p through reduction and oxidation of regulatory bonds within Ero1p is essential for maintaining the proper redox balance in the ER. In this paper, we show that Pdi1p is the key regulator of Ero1p activity. Reduced Pdi1p resulted in the activation of Ero1p by direct reduction of Ero1p regulatory bonds. Conversely, upon d

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CONCONI, Mariangela, Isabelle PETROPOULOS, Istvan EMOD, Evelyne TURLIN, Francis BIVILLE, and Bertrand FRIGUET. "Protection from oxidative inactivation of the 20S proteasome byheat-shock protein 90." Biochemical Journal 333, no. 2 (1998): 407–15. http://dx.doi.org/10.1042/bj3330407.

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Heat-shock protein 90 (Hsp 90) has been implicated in both protection against oxidative inactivation and inhibition of the multicatalytic proteinase (MCP, also known as 20 S proteasome). We report here that the protective and inhibitory effects of Hsp 90 depend on the activation state of the proteasome. Hsp 90 (and also α-crystallin) inhibits the N-Cbz-Leu-Leu-Leu-MCA-hydrolysing activity (Cbz = benzyloxycarbonyl; MCA = 7-amido-4-methylcoumarin) when the rat liver MCP is in its latent form, but no inhibitory effects are observed when the MCP is in its active form. Metal-catalysed oxidation of

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10

Marcillat, O., Y. Zhang, and K. J. A. Davies. "Oxidative and non-oxidative mechanisms in the inactivation of cardiac mitochondrial electron transport chain components by doxorubicin." Biochemical Journal 259, no. 1 (1989): 181–89. http://dx.doi.org/10.1042/bj2590181.

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The quinonoid anthracycline, doxorubicin (Adriamycin) is a potent anti-neoplastic agent whose clinical use is limited by severe cardiotoxicity. Mitochondrial damage is a major component of this cardiotoxicity, and rival oxidative and non-oxidative mechanisms for inactivation of the electron transport chain have been proposed. Using bovine heart submitochondrial preparations (SMP) we have now found that both oxidative and non-oxidative mechanisms occur in vitro, depending solely on the concentration of doxorubicin employed. Redox cycling of doxorubicin by Complex I of the respiratory chain (whi

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11

Dagnell, Markus, Qing Cheng, and Elias S. J. Arnér. "Qualitative Differences in Protection of PTP1B Activity by the Reductive Trx1 or TRP14 Enzyme Systems upon Oxidative Challenges with Polysulfides or H2O2 Together with Bicarbonate." Antioxidants 10, no. 1 (2021): 111. http://dx.doi.org/10.3390/antiox10010111.

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Protein tyrosine phosphatases (PTPs) can be regulated by several redox-dependent mechanisms and control growth factor-activated receptor tyrosine kinase phosphorylation cascades. Reversible oxidation of PTPs is counteracted by reductive enzymes, including thioredoxin (Trx) and Trx-related protein of 14 kDa (TRP14), keeping PTPs in their reduced active states. Different modes of oxidative inactivation of PTPs concomitant with assessment of activating reduction have been little studied in direct comparative analyses. Determining PTP1B activities, we here compared the potency of inactivation by b

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12

Fernandes, Alexandre F., Qingning Bian, Jian-Kang Jiang, et al. "Proteasome Inactivation Promotes p38 Mitogen-activated Protein Kinase-dependent Phosphatidylinositol 3-kinase Activation and Increases Interleukin-8 Production in Retinal Pigment Epithelial Cells." Molecular Biology of the Cell 20, no. 16 (2009): 3690–99. http://dx.doi.org/10.1091/mbc.e08-10-1068.

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Oxidative stress and inflammation are implicated in the pathogenesis of many age-related diseases. We have demonstrated previously that oxidative inactivation of the proteasome is a molecular link between oxidative stress and overexpression of interleukin (IL)-8. Here, we elucidated a novel signaling cascade that leads to up-regulation of IL-8 in response to proteasome inactivation. The sequence of events in this cascade includes proteasome inactivation, activation of mitogen-activated protein kinase kinase (MKK)3/MKK6, activation of p38 mitogen-activated protein kinase (MAPK), epidermal growt

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13

Maisch, Tim. "Resistance in antimicrobial photodynamic inactivation of bacteria." Photochemical & Photobiological Sciences 14, no. 8 (2015): 1518–26. http://dx.doi.org/10.1039/c5pp00037h.

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Until now it has been questionable if bacteria can develop resistance against photodynamic antimicrobial chemotherapy (PACT). This perspective summarises the current knowledge about the susceptibility of bacteria towards oxidative stress and sheds some light on the possible development of PACT-induced oxidative stress resistance.

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14

Vissers, M. C., and C. C. Winterbourn. "Myeloperoxidase-dependent oxidative inactivation of neutrophil neutral proteinases and microbicidal enzymes." Biochemical Journal 245, no. 1 (1987): 277–80. http://dx.doi.org/10.1042/bj2450277.

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The susceptibility of a number of human neutrophil granule enzymes to oxidative inactivation was investigated. Addition of H2O2 to the cell-free medium from stimulated neutrophils resulted in inactivation of all enzymes tested. This was inhibited by azide and methionine, indicating that inactivation was due to myeloperoxidase-derived oxidants. Lysozyme was more than 50% inactivated by one addition of 100 nmol of H2O2/ml, whereas myeloperoxidase, beta-glucuronidase, gelatinase and collagenase were almost completely inactivated by three additions. Cathepsin G was slightly less susceptible, where

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15

Martin, Gottfried, and Peter Böger. "Two Ways of Hydrogen Peroxide Formation in the Oxidative Inactivation of Cyanobacterial Glutamine Synthetase." Zeitschrift für Naturforschung C 52, no. 11-12 (1997): 812–16. http://dx.doi.org/10.1515/znc-1997-11-1214.

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Abstract Using crude extracts from the cyanobacterium Anabaena variabilis glutamine synthetase (GS) activity was rapidly irreversibly reduced to about 60% during dark incubation ("spontaneous GS inactivation"). An additional decrease was observed by the addition of ammonia in the light ("ammonia-mediated inactivation"). Both effects were prevented by EDTA, MnCl2 or catalase indicative of the involvement of H202. This is a key intermediate in oxidative enzyme inactivation. In both spontaneous and am monia-mediated GS inactivation H202 is produced in different ways. Spontaneous inactivation is

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16

Joshi, Suresh G., Moogega Cooper, Adam Yost, et al. "Nonthermal Dielectric-Barrier Discharge Plasma-Induced Inactivation Involves Oxidative DNA Damage and Membrane Lipid Peroxidation inEscherichia coli." Antimicrobial Agents and Chemotherapy 55, no. 3 (2011): 1053–62. http://dx.doi.org/10.1128/aac.01002-10.

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ABSTRACTOxidative stress leads to membrane lipid peroxidation, which yields products causing variable degrees of detrimental oxidative modifications in cells. Reactive oxygen species (ROS) are the key regulators in this process and induce lipid peroxidation inEscherichia coli. Application of nonthermal (cold) plasma is increasingly used for inactivation of surface contaminants. Recently, we reported a successful application of nonthermal plasma, using a floating-electrode dielectric-barrier discharge (FE-DBD) technique for rapid inactivation of bacterial contaminants in normal atmospheric air

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17

Stadtman, E. R. "Ascorbic acid and oxidative inactivation of proteins." American Journal of Clinical Nutrition 54, no. 6 (1991): 1125S—1128S. http://dx.doi.org/10.1093/ajcn/54.6.1125s.

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18

Mangione, S., F. Kueppers, C. Puglia, and LW Greenspon. "Erythrocytes prevent inactivation of alpha 1-antitrypsin by cigarette smoke." European Respiratory Journal 4, no. 1 (1991): 26–30. http://dx.doi.org/10.1183/09031936.93.04010026.

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Red blood cells (RBC) possess strong antioxidant activity. We tested whether this activity was sufficient to prevent the oxidative inactivation of alpha 1-antitrypsin (alpha 1-AT) by cigarette smoke. We found that RBC in physiological concentrations completely prevented the inactivation of alpha 1-AT. The major erythrocytic antioxidants, catalase, superoxide dismutase and glutathione were then selectively inhibited and the RBC retested. Only the inhibition of catalase significantly impaired the protective ability of added erythrocytes. We suggest that RBC antioxidants may be an important varia

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19

Seregina, Tatiana A., Irina Yu Petrushanko, Pavel I. Zaripov, et al. "Activation of Purine Biosynthesis Suppresses the Sensitivity of E. coli gmhA Mutant to Antibiotics." International Journal of Molecular Sciences 24, no. 22 (2023): 16070. http://dx.doi.org/10.3390/ijms242216070.

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Inactivation of enzymes responsible for biosynthesis of the cell wall component of ADP-glycero-manno-heptose causes the development of oxidative stress and sensitivity of bacteria to antibiotics of a hydrophobic nature. The metabolic precursor of ADP-heptose is sedoheptulose-7-phosphate (S7P), an intermediate of the non-oxidative branch of the pentose phosphate pathway (PPP), in which ribose-5-phosphate and NADPH are generated. Inactivation of the first stage of ADP-heptose synthesis (ΔgmhA) prevents the outflow of S7P from the PPP, and this mutant is characterized by a reduced biosynthesis of

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Müller, Wolfgang, and Katrin Bittner. "Differential Oxidative Modulation of Voltage-Dependent K+ Currents in Rat Hippocampal Neurons." Journal of Neurophysiology 87, no. 6 (2002): 2990–95. http://dx.doi.org/10.1152/jn.2002.87.6.2990.

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Oxidative stress is enhanced by [Ca2+]i-dependent stimulation of phospholipases and mitochondria and has been implicated in immune defense, ischemia, and excitotoxicity. Using whole cell recording from hippocampal neurons, we show that arachidonic acid (AA) and hydrogen peroxide (H2O2) both reduce the transient K+ current I A by −54 and −68%, respectively, and shift steady-state inactivation by −10 and −15 mV, respectively. While AA was effective at an extracellular concentration of 1 μM and an intracellular concentration of 1 pM, extracellular H2O2 was equally effective only at a concentratio

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21

Tsai, C. S., J. R. P. Godin, and A. J. Wand. "Dye-sensitized photo-oxidation of enzymes." Biochemical Journal 225, no. 1 (1985): 203–8. http://dx.doi.org/10.1042/bj2250203.

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Heart lipoamide dehydrogenase, liver alcohol dehydrogenase and egg-white lysozyme are photo-oxidized in the presence of various dye sensitizers. The photodynamic process is preceded by the binding between the enzyme and the sensitizers. Among the commonly used dyes, halogenated xanthines and thiazine are effective sensitizers for the photo-inactivation of these three enzymes. Histidine residues are the primary target for the sensitized photo-oxidation that inactivates lipoamide dehydrogenase and alcohol dehydrogenase. However, the destruction of tryptophan residues is responsible for the photo

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22

Kazama, Futaba. "Viral inactivation by potassium ferrate." Water Science and Technology 31, no. 5-6 (1995): 165–68. http://dx.doi.org/10.2166/wst.1995.0591.

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The kinetics of inactivation by potassium ferrate were studied using a bacteriophage, F-specific RNA-coliphage Qβ as a viral model. The inactivation appeared to be expressed by Hom's model in phosphate buffer at pH 6, 7, and 8. The rate of inactivation depended on pH; the lower pH, the faster inactivation observed. To consider the mechanism by which ferrate caused inactivation, the efficiency of inactivation was checked after ferrate decomposition in buffer. Effective inactivation following Hom's model was also observed after the complete decomposition of ferrate ion; however, the efficiency o

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Ngkelo, Anta, Roland F. Hoffmann, Andrew L. Durham та ін. "Glycogen synthase kinase-3β modulation of glucocorticoid responsiveness in COPD". American Journal of Physiology-Lung Cellular and Molecular Physiology 309, № 10 (2015): L1112—L1123. http://dx.doi.org/10.1152/ajplung.00077.2015.

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In chronic obstructive pulmonary disease (COPD), oxidative stress regulates the inflammatory response of bronchial epithelium and monocytes/macrophages through kinase modulation and has been linked to glucocorticoid unresponsiveness. Glycogen synthase-3β (GSK3β) inactivation plays a key role in mediating signaling processes upon reactive oxygen species (ROS) exposure. We hypothesized that GSK3β is involved in oxidative stress-induced glucocorticoid insensitivity in COPD. We studied levels of phospho-GSK3β-Ser9, a marker of GSK3β inactivation, in lung sections and cultured monocytes and bronchi

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Ou, P., and S. P. Wolff. "Erythrocyte catalase inactivation (H2O2 production) by ascorbic acid and glucose in the presence of aminotriazole: role of transition metals and relevance to diabetes." Biochemical Journal 303, no. 3 (1994): 935–39. http://dx.doi.org/10.1042/bj3030935.

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Erythrocytes exposed to ascorbic acid in the presence of aminotriazole undergo a dose- and time-dependent inactivation of endogenous catalase which is proportional to environmental hydrogen peroxide (H2O2) concentrations. The production of H2O2 seems to be dependent upon the availability of transition metal chelatable by o-phenanthroline (OPT), although the kinetics of catalase inactivation and H2O2 production by externally added copper ions in the presence of OPT is complex. Furthermore, although glucose is also able to undergo a transition-metal-catalysed oxidation yielding H2O2, the product

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Temesgen, Tamirat Tefera, Kristoffer Relling Tysnes, and Lucy Jane Robertson. "Use of Oxidative Stress Responses to Determine the Efficacy of Inactivation Treatments on Cryptosporidium Oocysts." Microorganisms 9, no. 7 (2021): 1463. http://dx.doi.org/10.3390/microorganisms9071463.

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Cryptosporidium oocysts are known for being very robust, and their prolonged survival in the environment has resulted in outbreaks of cryptosporidiosis associated with the consumption of contaminated water or food. Although inactivation methods used for drinking water treatment, such as UV irradiation, can inactivate Cryptosporidium oocysts, they are not necessarily suitable for use with other environmental matrices, such as food. In order to identify alternative ways to inactivate Cryptosporidium oocysts, improved methods for viability assessment are needed. Here we describe a proof of concep

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Chang, Christina L., Giancarlo Marra, Dharam P. Chauhan, et al. "Oxidative stress inactivates the human DNA mismatch repair system." American Journal of Physiology-Cell Physiology 283, no. 1 (2002): C148—C154. http://dx.doi.org/10.1152/ajpcell.00422.2001.

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In the human DNA mismatch repair (MMR) system, hMSH2 forms the hMutSα and hMutSβ complexes with hMSH6 and hMSH3, respectively, whereas hMLH1 and hPMS2 form the hMutLα heterodimer. These complexes, together with other components in the MMR system, correct single-base mismatches and small insertion/deletion loops that occur during DNA replication. Microsatellite instability (MSI) occurs when the loops in DNA microsatellites are not corrected because of a malfunctioning MMR system. Low-frequency MSI (MSI-L) is seen in some chronically inflamed tissues in the absence of genetic inactivation of the

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Sato, Shinichi, Michihiko Tsushima, and Hiroyuki Nakamura. "Target-protein-selective inactivation and labelling using an oxidative catalyst." Organic & Biomolecular Chemistry 16, no. 34 (2018): 6168–79. http://dx.doi.org/10.1039/c8ob01484a.

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Reactive oxygen species (ROS) and radical species generated by oxidative single-electron transfer (SET) catalysts induce local environmental oxidative reactions, resulting in protein inactivation and labelling in proximity to the catalysts.

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DAVIS, David A., Fonda M. NEWCOMB, Jackob MOSKOVITZ, et al. "HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase." Biochemical Journal 346, no. 2 (2000): 305–11. http://dx.doi.org/10.1042/bj3460305.

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Human immunodeficiency viruses encode a homodimeric protease that is essential for the production of infectious virus. Previous studies have shown that HIV-1 protease is susceptible to oxidative inactivation at the dimer interface at Cys-95, a process that can be reversed both chemically and enzymically. Here we demonstrate a related yet distinct mechanism of reversible inactivation of the HIV-2 protease. Exposure of the HIV-2 protease to H2O2 resulted in conversion of the two methionine residues (Met-76 and Met-95) to methionine sulphoxide as determined by amino acid analysis and mass spectro

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Schmidt, Kurt, Ernst R. Werner, and Bernd Mayer. "Tetrahydrobiopterin protects soluble guanylate cyclase against oxidative inactivation." Pteridines 24, no. 1 (2013): 47–50. http://dx.doi.org/10.1515/pterid-2013-0015.

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AbstractTetrahydrobiopterin (BH4) is a major endogenous vasoprotective agent that improves endothelial function by increasing nitric oxide (NO) synthesis and scavenging of superoxide and peroxynitrite. Accordingly, administration of BH4 is considered as a promising therapy of cardiovascular diseases associated with endothelial dysfunction and oxidative stress. In a recent study we identified a novel function of BH4 that might contribute to the beneficial vascular effects of the pteridine. As demonstrated with cultured porcine aortic endothelial cells, oxidative inactivation of soluble guanylat

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Janero, D. R., D. Hreniuk, and H. M. Sharif. "Hydroperoxide-induced oxidative stress impairs heart muscle cell carbohydrate metabolism." American Journal of Physiology-Cell Physiology 266, no. 1 (1994): C179—C188. http://dx.doi.org/10.1152/ajpcell.1994.266.1.c179.

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Hydrogen peroxide (H2O2) may incite cardiac ischemia-reperfusion injury. We evaluate herein the influence of H2O2-induced oxidative stress on heart muscle hexose metabolism in cultured neonatal rat cardiomyocytes, which have a substrate preference for carbohydrate. Cardiomyocyte exposure to 50 microM-1.0 mM bolus H2O2 transiently activated the pentose phosphate cycle and thereafter inhibited cellular glucose oxidation and glycolysis. These metabolic derangements were nonperoxidative in nature (as assessed in alpha-tocopherol-loaded cells) and occurred without acute change in cardiomyocyte hexo

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Park, Ohkmae K., and Ronald Bauerle. "Metal-Catalyzed Oxidation of Phenylalanine-Sensitive 3-Deoxy-d-arabino-Heptulosonate-7-Phosphate Synthase from Escherichia coli: Inactivation and Destabilization by Oxidation of Active-Site Cysteines." Journal of Bacteriology 181, no. 5 (1999): 1636–42. http://dx.doi.org/10.1128/jb.181.5.1636-1642.1999.

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ABSTRACT The in vitro instability of the phenylalanine-sensitive 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase [DAHPS(Phe)] from Escherichia coli has been found to be due to a metal-catalyzed oxidation mechanism. DAHPS(Phe) is one of three differentially feedback-regulated isoforms of the enzyme which catalyzes the first step of aromatic biosynthesis, the formation of DAHP from phosphoenolpyruvate andd-erythrose-4-phosphate. The activity of the apoenzyme decayed exponentially, with a half-life of about 1 day at room temperature, and the heterotetramer slowly dissociated to the monomeric

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Lind, SE, JR McDonagh, and CJ Smith. "Oxidative inactivation of plasmin and other serine proteases by copper and ascorbate." Blood 82, no. 5 (1993): 1522–31. http://dx.doi.org/10.1182/blood.v82.5.1522.1522.

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Abstract Fibrin thrombi form at sites of injury, where leukocytes release a variety of oxidants. To determine whether oxidants might affect proteins of the fibrinolytic system, we examined the effects of various oxidants on plasmin. Plasmin was not inhibited by micromolar concentrations of hypochlorous acid, chloramine T, or H2O2. Neither Fe nor Cu affected plasmin alone or in the presence of H2O2. However, incubation of plasmin with 5 mumol/L Cu(I or II) in the presence of the reducing agent ascorbic acid resulted in a loss of its hydrolytic activity towards proteins as well as towards small

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Lind, SE, JR McDonagh, and CJ Smith. "Oxidative inactivation of plasmin and other serine proteases by copper and ascorbate." Blood 82, no. 5 (1993): 1522–31. http://dx.doi.org/10.1182/blood.v82.5.1522.bloodjournal8251522.

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Fibrin thrombi form at sites of injury, where leukocytes release a variety of oxidants. To determine whether oxidants might affect proteins of the fibrinolytic system, we examined the effects of various oxidants on plasmin. Plasmin was not inhibited by micromolar concentrations of hypochlorous acid, chloramine T, or H2O2. Neither Fe nor Cu affected plasmin alone or in the presence of H2O2. However, incubation of plasmin with 5 mumol/L Cu(I or II) in the presence of the reducing agent ascorbic acid resulted in a loss of its hydrolytic activity towards proteins as well as towards small synthetic

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Edwards, S. W., H. L. Nurcombe, and C. A. Hart. "Oxidative inactivation of myeloperoxidase released from human neutrophils." Biochemical Journal 245, no. 3 (1987): 925–28. http://dx.doi.org/10.1042/bj2450925.

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Within 1 min of stimulation of human neutrophils by the chemotactic peptide (N-formyl-L-methionyl-L-leucyl-L-phenylalanine) plus cytochalasin B, myeloperoxidase (together with other granule enzymes) was secreted and detected extracellularly. In contrast with the other granule constituents assayed (vitamin B12-binding protein and beta-glucuronidase), the activity of released myeloperoxidase rapidly decreased, so that, by 10 min after stimulation, only about 5% of the total cellular activity was detected. This inactivation was shown to be dependent on oxidant generation during the respiratory bu

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Anderson, R. F., R. Hille, and K. B. Patel. "Inactivation of Xanthine Oxidase by Oxidative Radical Attack." International Journal of Radiation Biology 68, no. 5 (1995): 535–41. http://dx.doi.org/10.1080/09553009514551521.

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Cecarini, Valentina, Qunxing Ding, and Jeffrey N. Keller. "Oxidative inactivation of the proteasome in Alzheimer's disease." Free Radical Research 41, no. 6 (2007): 673–80. http://dx.doi.org/10.1080/10715760701286159.

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Sok, Dai-Eun. "Ascorbate-Induced Oxidative Inactivation of Zn2+-Glycerophosphocholine Cholinephosphodiesterase." Journal of Neurochemistry 70, no. 3 (2002): 1167–74. http://dx.doi.org/10.1046/j.1471-4159.1998.70031167.x.

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Schmidt, Kurt, Andrea Neubauer, Bernd Kolesnik, et al. "Tetrahydrobiopterin Protects Soluble Guanylate Cyclase against Oxidative Inactivation." Molecular Pharmacology 82, no. 3 (2012): 420–27. http://dx.doi.org/10.1124/mol.112.079855.

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Wan, Lili, Elizabeth Ottinger, Sungchan Cho, and Gideon Dreyfuss. "Inactivation of the SMN Complex by Oxidative Stress." Molecular Cell 31, no. 2 (2008): 244–54. http://dx.doi.org/10.1016/j.molcel.2008.06.004.

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Bautista, Juan, Raquel Corpas, Rosa Ramos, Olga Cremades, Juan Fco Gutiérrez, and Salvador Alegre. "Brain Mitochondrial Complex I Inactivation by Oxidative Modification." Biochemical and Biophysical Research Communications 275, no. 3 (2000): 890–94. http://dx.doi.org/10.1006/bbrc.2000.3388.

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Campolo, Nicolás, Mauricio Mastrogiovanni, Michele Mariotti, Michael Davies, Silvina Bartesaghi, and Rafael Radi. "Mechanisms of Oxidative Inactivation of Human Glutamine Synthetase." Free Radical Biology and Medicine 192 (November 2022): 119. http://dx.doi.org/10.1016/j.freeradbiomed.2022.10.218.

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Demicheli, Verónica, Diego M. Moreno, and Rafael Radi. "Human Mn-superoxide dismutase inactivation by peroxynitrite: a paradigm of metal-catalyzed tyrosine nitration in vitro and in vivo." Metallomics 10, no. 5 (2018): 679–95. http://dx.doi.org/10.1039/c7mt00348j.

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Rychtowski, Piotr, Oliwia Paszkiewicz, Agata Markowska-Szczupak, Grzegorz Leniec, and Beata Tryba. "Sulphated TiO2 Reduced by Ammonia and Hydrogen as an Excellent Photocatalyst for Bacteria Inactivation." Materials 17, no. 1 (2023): 66. http://dx.doi.org/10.3390/ma17010066.

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This study presents a relatively low-cost method for modifying TiO2-based materials for photocatalytic bacterial inactivation. The photocatalytic inactivation of Gram-negative (Escherichia coli) and Gram-positive (Staphylococcus epidermidis) bacteria using modified sulphated TiO2 was studied. The modification focused on the reduction of TiO2 by ammonia agents and hydrogen at 400–450 °C. The results showed a high impact of sulphate species on the inactivation of E. coli. The presence of these species generated acid sites on TiO2, which shifted the pH of the reacted titania slurry solution to lo

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Shang, F., and A. Taylor. "Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells." Biochemical Journal 307, no. 1 (1995): 297–303. http://dx.doi.org/10.1042/bj3070297.

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Roles for ubiquitin (an 8.5 kDa polypeptide) involve its conjugation to proteins as a signal to initiate degradation and as a stress protein. We investigated ubiquitin conjugation and ubiquitin-dependent proteolytic activities in cultured bovine lens epithelial cells (BLECs) upon oxidative challenge. A 44% decrease in intracellular glutathione confirmed oxidative stress upon incubation with 1 mM H2O2. After 30 min incubation, endogenous high-molecular-mass ubiquitin conjugates decreased 73%, and intracellular proteolysis decreased about 50%. In the supernatants of the oxidatively treated BLECs

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Doeller, J. E., and B. A. Wittenberg. "Myoglobin function and energy metabolism of isolated cardiac myocytes: effect of sodium nitrite." American Journal of Physiology-Heart and Circulatory Physiology 261, no. 1 (1991): H53—H62. http://dx.doi.org/10.1152/ajpheart.1991.261.1.h53.

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Inactivation of intracellular myoglobin by sodium nitrite or by carbon monoxide in isolated cardiac myocytes diminishes steady-state respiratory rate and phosphocreatine concentration (PCr) by approximately 25% at nonlimiting oxygen pressures; oxidative phosphorylation and glycolysis together are insufficient to maintain ATP, and PCr falls. At concentrations required to convert myoglobin to high-spin ferric myoglobin, nitrite does not affect the respiration of isolated aerobic heart mitochondria. The creatine phosphokinase-catalyzed equilibrium between PCr and ATP is not affected by nitrite. M

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Méndez-García, LA, M. Martínez-Castillo, N. Villegas-Sepúlveda, L. Orozco, and EJ Córdova. "Curcumin induces p53-independent inactivation of Nrf2 during oxidative stress–induced apoptosis." Human & Experimental Toxicology 38, no. 8 (2019): 951–61. http://dx.doi.org/10.1177/0960327119845035.

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The transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2) is a master regulator of a battery of antioxidant and detoxificant genes with cytoprotective function. Since Nrf2 inactivation is necessary for the complete execution of apoptosis in the presence of extensive cellular damage caused by oxidative stress, constant activation of Nrf2 may protect tumoral cells from apoptosis. The tumor suppressor gene p53 has been suggested to participate in apoptosis-related repression of Nrf2. Thus, we studied the inactivation of Nrf2 during oxidant-induced apoptosis in a p53 dysfunctiona

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Vincent, Kylie A., Alison Parkin, Oliver Lenz, et al. "Electrochemical Definitions of O2Sensitivity and Oxidative Inactivation in Hydrogenases." Journal of the American Chemical Society 127, no. 51 (2005): 18179–89. http://dx.doi.org/10.1021/ja055160v.

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Murakami, Keiko, and Masataka Yoshino. "Inactivation of aconitase in yeast exposed to oxidative stress." IUBMB Life 41, no. 3 (1997): 481–86. http://dx.doi.org/10.1080/15216549700201501.

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Horowitz, P. M., M. Butler, and G. D. McClure. "Reducing sugars can induce the oxidative inactivation of rhodanese." Journal of Biological Chemistry 267, no. 33 (1992): 23596–600. http://dx.doi.org/10.1016/s0021-9258(18)35880-0.

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Filipe Teixeira, Pedro, Catarina Moreira Pinho, Rui M. Branca, Janne Lehtiö, Rodney L. Levine, and Elzbieta Glaser. "In vitro oxidative inactivation of human presequence protease (hPreP)." Free Radical Biology and Medicine 53, no. 11 (2012): 2188–95. http://dx.doi.org/10.1016/j.freeradbiomed.2012.09.039.

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