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Статті в журналах з теми "Thioredoxin; oxidative stress"
Berndt, Carsten, Christopher Horst Lillig, and Arne Holmgren. "Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system." American Journal of Physiology-Heart and Circulatory Physiology 292, no. 3 (March 2007): H1227—H1236. http://dx.doi.org/10.1152/ajpheart.01162.2006.
Повний текст джерелаTrotter, Eleanor W., and Chris M. Grant. "Overlapping Roles of the Cytoplasmic and Mitochondrial Redox Regulatory Systems in the Yeast Saccharomyces cerevisiae." Eukaryotic Cell 4, no. 2 (February 2005): 392–400. http://dx.doi.org/10.1128/ec.4.2.392-400.2005.
Повний текст джерелаSmits, Wiep Klaas, Jean-Yves F. Dubois, Sierd Bron, Jan Maarten van Dijl, and Oscar P. Kuipers. "Tricksy Business: Transcriptome Analysis Reveals the Involvement of Thioredoxin A in Redox Homeostasis, Oxidative Stress, Sulfur Metabolism, and Cellular Differentiation in Bacillus subtilis." Journal of Bacteriology 187, no. 12 (June 15, 2005): 3921–30. http://dx.doi.org/10.1128/jb.187.12.3921-3930.2005.
Повний текст джерелаRohrbach, Susanne, Stefanie Gruenler, Mirja Teschner, and Juergen Holtz. "The thioredoxin system in aging muscle: key role of mitochondrial thioredoxin reductase in the protective effects of caloric restriction?" American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 291, no. 4 (October 2006): R927—R935. http://dx.doi.org/10.1152/ajpregu.00890.2005.
Повний текст джерелаWatson, Walter H., and Dean P. Jones. "Oxidation of nuclear thioredoxin during oxidative stress." FEBS Letters 543, no. 1-3 (April 29, 2003): 144–47. http://dx.doi.org/10.1016/s0014-5793(03)00430-7.
Повний текст джерелаMasutani, Hiroshi, Yoshimi Yamaguchi, Ryoko Otsuki, Nobue Kanoh, Yuji Kunimoto, Kazuo Murata, and Junji Yodoi. "Important Role of Antioxidants in Oxidative Stress Thioredoxin and Thioredoxin Inducers against Oxidative Stress." Journal of Clinical Biochemistry and Nutrition 37, no. 2 (2005): 45–53. http://dx.doi.org/10.3164/jcbn.37.45.
Повний текст джерелаAchard, Maud E. S., Amanda J. Hamilton, Tarek Dankowski, Begoña Heras, Mark S. Schembri, Jennifer L. Edwards, Michael P. Jennings, and Alastair G. McEwan. "A Periplasmic Thioredoxin-Like Protein Plays a Role in Defense against Oxidative Stress in Neisseria gonorrhoeae." Infection and Immunity 77, no. 11 (August 17, 2009): 4934–39. http://dx.doi.org/10.1128/iai.00714-09.
Повний текст джерелаFlores, Lisa C., Melanie Ortiz, Sara Dube, Gene B. Hubbard, Shuko Lee, Adam Salmon, Yiqiang Zhang, and Yuji Ikeno. "Thioredoxin, oxidative stress, cancer and aging." Longevity & Healthspan 1, no. 1 (2012): 4. http://dx.doi.org/10.1186/2046-2395-1-4.
Повний текст джерелаSilva-Adaya, Daniela, María E. Gonsebatt, and Jorge Guevara. "Thioredoxin System Regulation in the Central Nervous System: Experimental Models and Clinical Evidence." Oxidative Medicine and Cellular Longevity 2014 (2014): 1–13. http://dx.doi.org/10.1155/2014/590808.
Повний текст джерелаBjur, Eva, Sofia Eriksson-Ygberg, Fredrik Åslund, and Mikael Rhen. "Thioredoxin 1 Promotes Intracellular Replication and Virulence of Salmonella enterica Serovar Typhimurium." Infection and Immunity 74, no. 9 (September 2006): 5140–51. http://dx.doi.org/10.1128/iai.00449-06.
Повний текст джерелаДисертації з теми "Thioredoxin; oxidative stress"
Gregory, Mary Sarah-Jane, and n/a. "Thioredoxin and Oxidative Stress." Griffith University. School of Health Science, 2004. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20040301.082639.
Повний текст джерелаFindlay, Victoria Jane. "The role of thioredoxin peroxidases in the yeast oxidative stress response." Thesis, University of Newcastle Upon Tyne, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.391954.
Повний текст джерелаSusanti, Dwi. "Sulfite reductase and thioredoxin in oxidative stress responses of methanogenic archaea." Diss., Virginia Tech, 2013. http://hdl.handle.net/10919/51423.
Повний текст джерелаOur laboratory is interested in studying the mechanism underlying the oxygen tolerance and oxidative stress responses in methanogenic archaea, which are obligate anaerobe. Our research concerns two aspects of oxidative stress. (i) Responses toward extracellular toxic species such as SO32-, that forms as a result of reactions of O2 with reduced compounds in the environment. These species are mostly seen in anaerobic environments upon O2 exposure due to the abundance of reduced components therein. (ii) Responses toward intracellular toxic species such as superoxide and hydrogen peroxide that are generated upon entry of O2 and subsequent reaction of O2 with reduced component inside the cell. Aerobic microorganisms experience the second problem. Since a large number of microorganisms of Earth are anaerobes and the oxidative defense mechanisms of anaerobes are relatively less studied, the research in our laboratory has focused on this area. My thesis research covers two studies that fall in the above-mentioned two focus areas.
In 2005-2007 our laboratory discovered that certain methanogens use an unusual sulfite reductase, named F420-dependent sulfite reductase (Fsr), for the detoxification of SO32- that is produced outside the cell from a reaction between oxygen and sulfide. This reaction occurred during early oxygenation of Earth and continues to occur in deep-sea hydrothermal vents. Fsr, a flavoprotein, carries out a 6-electron reduction of SO32- to S2-. It is a chimeric protein where N- and C-terminal halves (Fsr-N and Fsr-C) are homologs of F420H2 dehydrogenase and dissimilatory sulfite reductase (Dsr), respectively. We hypothesized that Fsr was developed in a methanogen from pre-existing parts. To begin testing this hypothesis we have carried out bioinformatics analyses of methanogen genomes and found that both Fsr-N homologs and Fsr-C homologs are abundant in methanogens. We called the Fsr-C homolog dissimilatory sulfite reductase-like protein (Dsr-LP). Thus, Fsr was likely assembled from freestanding Fsr-N homologs and Dsr-like proteins (Dsr-LP) in methanogens. During the course of this study, we also identified two new putative F420H2-dependent enzymes, namely F420H2-dependent glutamate synthase and assimilatory sulfite reductase.
Another aspect of my research concerns the reactivation of proteins that are deactivated by the entry of oxygen inside the cell. Here I focused specifically on the role of thioredoxin (Trx) in methanogens. Trx, a small redox regulatory protein, is ubiquitous in all living cells. In bacteria and eukarya, Trx regulates a wide variety of cellular processes including cell divison, biosynthesis and oxidative stress response. Though some Trxs of methanogens have been structurally and biochemically characterized, their physiological roles in these organisms are unknown. Our bioinformatics analysis suggested that Trx is ubiquitous in methanogens and the pattern of its distribution in various phylogenetic classes paralleled the respective evolutionary histories and metabolic versatilities. Using a proteomics approach, we have identified 155 Trx targets in a hyperthermophilic phylogenetically deeply-rooted methanogen, Methanocaldococcus jannaschii. Our analysis of two of these targets employing biochemical assays suggested that Trx is needed for reactivation of oxidatively deactivated enzymes in M. jannaschii. To our knowledge, this is the first report on the role of Trx in an organism from the archaeal domain.
During the course of our work on methanogen Trxs, we investigated the evolutionary histories of different Trx systems that are composed of Trxs and cognate Trx reductases. In collaboration with other laboratories, we conducted bioinformatics analysis for the distribution of one of such systems, ferredoxin-dependent thioredoxin reductase (FTR), in all organisms. We found that FTR was most likely originated in the phylogenetically deeply-rooted microaerophilic bacteria where it regulates CO2 fixation via the reverse citric acid cycle.
Ph. D.
Walther, Ashley Elizabeth. "Role of the Schizosaccharomyces pombe Enzyme Thioredoxin Peroxidase in Oxidative Stress Resistance." Thesis, Boston College, 2006. http://hdl.handle.net/2345/420.
Повний текст джерелаWithin cells, reactive oxygen species (ROS) are synthesized naturally and in response to environmental stimuli. However, ROS have deleterious effects on a wide range of cellular molecules. Oxidative stress, caused by the ROS generated by the partial reduction of oxygen, is a major cause of cell damage linked to the initiation and progression of numerous diseases. Thioredoxin peroxidase (Tpx1) plays important roles in cellular defense against ROS. Although homologous genes and their functions have been identified in other eukaryotes, the level of activity as well as the necessity of this protective enzyme in S. pombe exposed to oxidative stress has yet to be fully elucidated. To explore the role of the Tpx1 protein in oxidative stress resistance, novel strains were constructed in which the tpx1 gene was overexpressed. The polymerase chain reaction was used to amplify txp1, and the amplified sequence was cloned into the yeast overexpression plasmid, pNMT41, which allows overexpression under the control of the powerful promoter. DNA sequencing was used to determine that the sequences had been properly inserted into the vector. The plasmids were transformed into two leu- yeast strains: FWP6 and TP108-3C. Production of the Tpx1 protein was ensured using Western Blot techniques. Experimentation to test the responses of the tpx1 strain to oxidative stress will employ a variety of reactive oxygen generators, including hydrogen n peroxide, menadione, tert-butyl hydroperoxide, and paraquat. The results generally supported the proposed role of Tpx1 to confer additional resistance against the oxidative stress. In a complementary line of investigation, knockout strains are being constructed to reduce the levels of the Tpx1 in S. pombe. Gene deletion cassettes were constructed for tpx1. Currently, the strains are being analyzed for the successful replacement of the endogenous tpx1 gene by homologous recombination. If the absence of the protein results in decreased cell viability, the role of Tpx1 indicated by the overexpression experiments could be supported
Thesis (BS) — Boston College, 2006
Submitted to: Boston College. College of Arts and Sciences
Discipline: Biology
Discipline: College Honors Program
Kobayashi(Miura), Mikiko. "Thioredoxin,an anti-oxidant protein,protects mouse embryos from oxidative stress-induced developmental anomalies." Kyoto University, 2002. http://hdl.handle.net/2433/149333.
Повний текст джерелаDutta, Khokon Kumar. "Two distinct mechanisms for loss of thioredoxin-binding protein-2 in oxidative stress-induced renal carcinogenesis." Kyoto University, 2007. http://hdl.handle.net/2433/135665.
Повний текст джерелаDomènech, Guil Alba 1985. "Oxidative stress in toxicity and signaling : Control of cysteine oxidation and reduction by the redoxin systems of fission yeast." Doctoral thesis, Universitat Pompeu Fabra, 2018. http://hdl.handle.net/10803/664636.
Повний текст джерелаSchizosaccharomyces pombe, as all aerobic organisms, needs oxygen to live and have to deal with the side effects of the toxicity associated to oxygen by-products. To maintain intracellular environment, S. pombe has antioxidant systems that are activated fast and in a reversible manner. Depending on the severity of the oxidative stress suffered, S. pombe has two main antioxidant response pathways, Pap1 and Sty1 pathways, for sub-toxic and toxic hydrogen peroxide (H2O2) levels, respectively. These cascades involve sensor proteins that contain cysteine residues called thiol switches, which can switch on and off their activities. Therefore, all the components involved in the antioxidant signaling cascades have to be recycled in order to be ready to act again. For these reason, the reduction systems, thioredoxin and glutathione/glutaredoxin systems, have an essential role as backup systems of the components of the H2O2 signaling redox relays in fission yeast. Along this thesis I have studied the importance of a proper activity of both reduction systems in the recycling of redox proteins to avoid cell toxicity and to assure a normal cell cycle progression. On the other hand, we characterized how thresholds of oxidative stress tolerance are important to trigger signaling or toxicity responses in S. pombe.
Loganathan, Usha R. "Characterization of the thioredoxin system in Methanosarcina mazei." Thesis, Virginia Tech, 2014. http://hdl.handle.net/10919/71334.
Повний текст джерелаMaster of Science
Singh, Komudi. "Oxidant-Induced Cell Death Mediated By A Rho Gtpase In Saccharomyces cerevisiae." Columbus, Ohio : Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view.cgi?acc%5Fnum=osu1227716169.
Повний текст джерелаTan, Shixiong Biotechnology & Biomolecular Sciences Faculty of Science UNSW. "Cellular mechanisms affecting redox homeostasis in response to stress in Saccharomyces cerevisiae." Awarded by:University of New South Wales. Biotechnology & Biomolecular Sciences, 2009. http://handle.unsw.edu.au/1959.4/44627.
Повний текст джерелаЧастини книг з теми "Thioredoxin; oxidative stress"
Nagarajan, Narayani, and Junichi Sadoshima. "Regulation of Protein Nitrosylation by Thioredoxin 1." In Biochemistry of Oxidative Stress, 163–75. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-45865-6_11.
Повний текст джерелаD’Annunzio, Veronica, Virginia Perez, Tamara Mazo, and Ricardo Jorge Gelpi. "Thioredoxin Attenuates Post-ischemic Damage in Ventricular and Mitochondrial Function." In Biochemistry of Oxidative Stress, 177–91. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-45865-6_12.
Повний текст джерелаYu, Yezhou, Giovanna Di Trapani, and Kathryn F. Tonissen. "Thioredoxin and Glutathione Systems." In Handbook of Oxidative Stress in Cancer: Mechanistic Aspects, 1–14. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-15-4501-6_143-1.
Повний текст джерелаYu, Yezhou, Giovanna Di Trapani, and Kathryn F. Tonissen. "Thioredoxin and Glutathione Systems." In Handbook of Oxidative Stress in Cancer: Mechanistic Aspects, 2407–20. Singapore: Springer Singapore, 2022. http://dx.doi.org/10.1007/978-981-15-9411-3_143.
Повний текст джерелаMunemasa, Yasunari, Jacky M. K. Kwong, Seok H. Kim, Jae H. Ahn, Joseph Caprioli, and Natik Piri. "Thioredoxins 1 and 2 Protect Retinal Ganglion Cells from Pharmacologically Induced Oxidative Stress, Optic Nerve Transection and Ocular Hypertension." In Retinal Degenerative Diseases, 355–63. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1399-9_41.
Повний текст джерелаNishinaka, Yumiko, Hiroshi Masutani, Junji Yodoi, and Yong-Chul Kim. "The Gene Regulatory Mechanism of Thioredoxin and Thioredoxin Binding Protein-2/VDUP1 in Cancer Prevention." In Oxidative Stress and Disease, 25–35. CRC Press, 2005. http://dx.doi.org/10.1201/9781420027174.ch3.
Повний текст джерелаNakamura, Hajime, Norihiko Kondo, Kiichi Hirota, Hiroshi Masutani, and Junji Yodoi. "Thiols and Thioredoxin in Cellular Redox Control." In Oxidative Stress and Disease. CRC Press, 2003. http://dx.doi.org/10.1201/9780203912874.ch4.
Повний текст джерелаUeda, Shugo, Takayuki Nakamura, Hajime Nakamura, and Junji Yodoi. "Redox Regulation of Inflammatory Tissue Damage by Thioredoxin." In Oxidative Stress and Disease, 41–60. CRC Press, 2005. http://dx.doi.org/10.1201/9781420028256.ch3.
Повний текст джерелаSu, Dan, and Vadim Gladyshev. "The Roles of Thioredoxin Reductases in Cell Signaling." In Oxidative Stress and Disease. CRC Press, 2005. http://dx.doi.org/10.1201/9781420028362.ch8.
Повний текст джерела"Redox Regulation of Inflammatory Tissue Damage by Thioredoxin." In Oxidative Stress, Inflammation, and Health, 73–92. CRC Press, 2005. http://dx.doi.org/10.1201/9781420028256-7.
Повний текст джерелаЗвіти організацій з теми "Thioredoxin; oxidative stress"
Or, Etti, David Galbraith, and Anne Fennell. Exploring mechanisms involved in grape bud dormancy: Large-scale analysis of expression reprogramming following controlled dormancy induction and dormancy release. United States Department of Agriculture, December 2002. http://dx.doi.org/10.32747/2002.7587232.bard.
Повний текст джерела