Dissertations / Theses on the topic 'Thioredoxin'
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Paunescu, Karina. "DNA-Stabilität und Thioredoxin-Thioredoxin-Reduktase im Zellkern." [S.l.] : [s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=969680333.
Full textOsborne, Leisa Jane. "Characterisation of Thioredoxin Dimers: A Biochemical Study." Thesis, Griffith University, 2011. http://hdl.handle.net/10072/365531.
Full textThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Physical Science
Science, Environment, Engineering and Technology
Full Text
Missirlis, Fanis. "Functional characterization of novel thioredoxin reductase and thioredoxin peroxidase in Drosophila." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2002. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/NQ65830.pdf.
Full textShah, Fenil. "Thioredoxin and its Target Proteins: Thioredoxin Expression under Different Oxygen Conditions." Thesis, Griffith University, 2011. http://hdl.handle.net/10072/367670.
Full textThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Physical Sciences
Science, Environment, Engineering and Technology
Full Text
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.
Full textGregory, Mary Sarah-Jane. "Thioredoxin and Oxidative Stress." Thesis, Griffith University, 2004. http://hdl.handle.net/10072/367183.
Full textThesis (Masters)
Master of Philosophy (MPhil)
School of Health Sciences
Full Text
Björkhem, Bergman Linda. "Thioredoxin reductase and selenium in carcinogenesis and multidrug resistance /." Stockholm, 2004. http://diss.kib.ki.se/2004/91-7349-954-4/.
Full textZhong, Liangwei. "Selenium in mammalian thioredoxin reductase /." Stockholm, 2000. http://diss.kib.ki.se/2000/91-628-4243-9/.
Full textCallister, Matthew Eric James. "Thioredoxin and the inflammatory response." Thesis, Imperial College London, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.414905.
Full textRozell, Björn. "Immunohistochemical studies of the thioredoxin system." Göteborg : Dept. of Histology, University of Göteborg, 1987. http://catalog.hathitrust.org/api/volumes/oclc/17242526.html.
Full textSze, Jun Hui. "Targeting Thioredoxin Reductase in Multiple Myeloma." Thesis, Griffith University, 2020. http://hdl.handle.net/10072/392857.
Full textThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Environment and Sc
Science, Environment, Engineering and Technology
Full Text
James, Paul Brian Charles. "Investigation into peroxiredoxin and interactions in the peroxiredoxin peroxide scavenging system." Thesis, University of Exeter, 2010. http://hdl.handle.net/10036/3162.
Full textNalvarte, Ivan. "Functional characterization of cytosolic and mitochondrial thioredoxin reductases /." Stockholm, 2006. http://diss.kib.ki.se/2006/91-7140-919-X/.
Full textJauregui, Jose. "Auranofin Targets Thioredoxin Reductases in Trichomonas vaginalis." Scholarly Commons, 2017. https://scholarlycommons.pacific.edu/uop_etds/2976.
Full textDamdimopoulos, Anastasios E. "Identification and functional characterization of novel thioredoxin systems /." Stockholm,, 2003. http://diss.kib.ki.se/2003/91-7349-661-8/.
Full text蕭嘉慧 and Ka-wai Siu. "Identification of biological inhibitors of the mammalian thioredoxin system." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1999. http://hub.hku.hk/bib/B31221634.
Full textEckenroth, Brian E. "The Mechanism of High MR Thioredoxin Reductase Investigated by Semisynthesis and Crystallography." ScholarWorks @ UVM, 2007. http://scholarworks.uvm.edu/graddis/73.
Full textLoganathan, Usha R. "Characterization of the thioredoxin system in Methanosarcina mazei." Thesis, Virginia Tech, 2014. http://hdl.handle.net/10919/71334.
Full textMaster of Science
Matsuo, Yoshiyuki. "Identification of a Novel Thioredoxin-related Transmembrane Protein." Kyoto University, 2001. http://hdl.handle.net/2433/150552.
Full textUeno, Masaya. "Thioredoxin-dependent redox regulation of p53 mediated-p21activation." Kyoto University, 2000. http://hdl.handle.net/2433/180842.
Full textNishiyama, Akira. "Identification of thioredoxin-binding protein-2/vitamin D_3 up-regulated protein 1 as a nagative regulator of thioredoxin function and expression." Kyoto University, 1999. http://hdl.handle.net/2433/181259.
Full textClapper, Erin M. "Investigating Intrinsic and Extrinsic Mechanisms of Tyrosine Kinase Inhibitor Resistance in Chronic Myeloid Leukaemia." Thesis, Griffith University, 2021. http://hdl.handle.net/10072/409643.
Full textThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Environment and Sc
Science, Environment, Engineering and Technology
Full Text
McKown, Richard Dwayne. "Localization and partial immunological characterization of Fasciola hepatica Thioredoxin." Texas A&M University, 2004. http://hdl.handle.net/1969.1/1401.
Full textChiu, Joyce Biotechnology & Biomolecular Sciences Faculty of Science UNSW. "Protein engineering of DNA polymerase I: thioredoxin dependent processivity." Awarded by:University of New South Wales. School of Biotechnology and Biomolecular Sciences, 2005. http://handle.unsw.edu.au/1959.4/23077.
Full textRen, Bin. "Crystallographic studies on redox enzymes containing the thioredoxin fold /." Stockholm, 1999. http://diss.kib.ki.se/1999/91-628-3302-2/.
Full textLee, Chi-wai. "Impact of gestational diabetes mellitus on placental thioredoxin system." Click to view the E-thesis via HKUTO, 2007. http://sunzi.lib.hku.hk/HKUTO/record/B39558897.
Full textLeaver, Susannah. "Intracellular and extracellular thioredoxin implications for the inflammatory response." Thesis, Imperial College London, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.537565.
Full textLee, Chi-wai, and 李志慧. "Impact of gestational diabetes mellitus on placental thioredoxin system." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2007. http://hub.hku.hk/bib/B39558897.
Full textTakashima, Yuichiro. "Differential expression of glutaredoxin and thioredoxin during monocytic differentiation." Kyoto University, 2000. http://hdl.handle.net/2433/151447.
Full textEftekharpour, Eftekhar. "Glutathione dependent and thioredoxin dependent peroxidase systems in neural cells." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/NQ63863.pdf.
Full textHo, Ian-ian. "Does Ras/MEK signaling stimulate the expression of thioredoxin reductase? /." View the Table of Contents & Abstract, 2007. http://sunzi.lib.hku.hk/hkuto/record/B38348123.
Full textHall, Gareth A. F. "Structural and functional analysis of thioredoxin and associated inhibitor complexes." Thesis, University of Nottingham, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.495589.
Full textHo, Ian-ian, and 何欣欣. "Does Ras/MEK signaling stimulate the expression of thioredoxin reductase?" Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2007. http://hub.hku.hk/bib/B45011217.
Full textFloen, Miranda J. "Thioredoxin-1| Identification of redox substrates and response to hyperoxia." Thesis, University of South Dakota, 2016. http://pqdtopen.proquest.com/#viewpdf?dispub=10132866.
Full textBronchopulmonary dysplasia (BPD) is a serious respiratory complication for the preterm newborn characterized clinically by prolonged respiratory distress and histologically by alveolar simplification and decreased pulmonary vasculature. The development of BPD is well linked to oxidative stress suffered by the newborn as a result of a preterm fetal-neonatal transition, supplemental oxygen, infection, increased inflammation, and mechanical ventilation. Damage suffered by oxidative stress may be through direct mechanisms or through alteration of redox¬sensitive pathways involved in cell death, cell survival, differentiation, and proliferation. Redox¬sensitive modifications regulating protein function and redox-sensitive pathways have mainly been ascribed to oxidative modification of cysteine thiols. As their modification is critical for protein function, maintenance of the thiol redox status is crucial. Thioredoxin-1 (Trx1) functions in maintenance of thiol redox homeostasis, and its redox activity is intimately linked to antioxidant, cytoprotection, proliferation responses, and cytoprotection. While Trx1 targets of redox regulation have been identified, we hypothesize that additional protein may be redox regulated and that Trx1 target profiles may change during oxidative stress. Therefore a novel immunoprecipitation approach, identified as the substrate trap approach, was developed to identify Trx1 targets. The following demonstrates the use of the substrate trap approach for identification of Trx1 redox targets and further application of the approach to identify alterations in target profiles in response to oxidative stress. Use of nuclear targeted substrate trap was successfully employed to enrich from nuclear Trx1 targets. As a final component the characterization of the Trx1 system in mouse from late embryonic development through the first week of life animals were exposed to room air or hyperoxia (model of BPD). Characterization indicates impairment of the Trx1 system in response to hyperoxic injury. As Trx1 is known to regulate proliferation, cell death, survival, differentiation pathways, impairment of the Trx1 system during early neonatal development may potentiate hyperoxic injury and alterations in lung development. Better understanding of Trx1 interactions occur through the substrate trap in a physiological model of BPD will help elucidate redox-signaling pathways involved in BPD pathogenesis.
Tan, Aiguo. "Thioredoxin-1 attenuates indomethacin-induced gastric mucosal injury in mice." Kyoto University, 2008. http://hdl.handle.net/2433/135862.
Full textHanschmann, Eva-Maria [Verfasser]. "Thioredoxin family proteins in physiology and disease / Eva-Maria Hanschmann." Marburg : Universitätsbibliothek Marburg, 2011. http://d-nb.info/1016617615/34.
Full textZurek, Mark [Verfasser]. "Regulation der kardialen Myofibroblastendifferenzierung – Rolle von Thioredoxin-1 / Mark Zurek." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2020. http://d-nb.info/1212238664/34.
Full textDai, Shaodong. "Structural and functional studies of NADPH and ferredoxin dependent thioredoxin reductases /." Uppsala : Swedish Univ. of Agricultural Sciences (Sveriges lantbruksuniv.), 1998. http://epsilon.slu.se/avh/1998/91-576-5480-8.gif.
Full textAttarian, Rodgoun. "Detoxification of glutathione and nitrosoglutathione by thioredoxin system of Mycobacterium tuberculosis." Thesis, University of British Columbia, 2009. http://hdl.handle.net/2429/11175.
Full textPetry, Sebastian Friedrich [Verfasser]. "Thioredoxin family proteins in the db/db mouse / Sebastian Friedrich Petry." Gießen : Universitätsbibliothek, 2015. http://d-nb.info/1077438826/34.
Full textFindlay, 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.
Full textSusanti, Dwi. "Sulfite reductase and thioredoxin in oxidative stress responses of methanogenic archaea." Diss., Virginia Tech, 2013. http://hdl.handle.net/10919/51423.
Full textOur 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.
Kawasaki, Kimio. "Helicobacter felis-induced gastritis was suppressed in mice overexpressing thioredoxin-1." Kyoto University, 2005. http://hdl.handle.net/2433/144494.
Full textOkubo, Kenichi. "Amelioration of ischemia-reperfusion injury by human thioredoxin in rabbit lung." Kyoto University, 1997. http://hdl.handle.net/2433/202158.
Full textAndres, Allen Mariano. "Metabolic role of thioredoxin-interacting protein in facilitating the fasting response." Diss., [La Jolla] : [San Diego] : University of California, San Diego ; San Diego State University, 2009. http://wwwlib.umi.com/cr/ucsd/fullcit?p3369671.
Full textTitle from first page of PDF file (viewed September 15, 2009). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (p. 99-119).
Karlenius, Therese Christina. "Regulation of the Thioredoxin System under Hypoxia and Different Oxygen Conditions." Thesis, Griffith University, 2011. http://hdl.handle.net/10072/365526.
Full textThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Physical Sciences
Science, Environment, Engineering and Technology
Full Text
Bhatia, Maneet. "Inhibition of the Thioredoxin System: Regulation by the Cancer Cell Environment." Thesis, Griffith University, 2016. http://hdl.handle.net/10072/367262.
Full textThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Natural Sciences
Science, Environment, Engineering and Technology
Full Text
Wang, Sicong. "Investigating cellular responses after inhibition of the thioredoxin system in lymphoma." Thesis, Griffith University, 2022. http://hdl.handle.net/10072/417233.
Full textThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Environment and Sc
Science, Environment, Engineering and Technology
Full Text
Nonn, Larisa. "The role of the mitochondrial thioredoxin-2 system in cell function." Diss., The University of Arizona, 2003. http://hdl.handle.net/10150/289903.
Full textSABELLI, RENATO. "Organ sulfur compounds and interactions with the detoxification and redox system enzymes." Doctoral thesis, Università degli Studi di Roma "Tor Vergata", 2010. http://hdl.handle.net/2108/1194.
Full textMany Organ Sulfur Compounds (OSCs), founded in garlic, are able to induce apoptosis in various tumoral cell lines [80]. Recently, in the aqueous phase of boiled garlic has been found the 2-propenyl thiosulfate (2-PTS), and it can induce apoptosis in several tumor cell lines, through the intracellular ROS production [16, 75]. Besides, recent works [38, 39, 75] highlight that the enzymes thioalkenylation can be one of the causes of cytotoxic effect of this type of compounds. Since to this observations, has been valuated the cytotoxic effect of 2-PTS on a human lymphoblastoma cell line (HuT 78), monitoring the activity and expression of some enzymes involved in the OSCs metabolism, such as Rhodanese (TST), Glutathione-Stransferase (GST), Thioredoxin (Trx), Thioredoxin reductase (Trd). All these enzyme are very important for the cell vitality, and their dysfunction causes severe diseases [7] and is related to the apoptotic induction [2, 54, 76]. In our experiments we have observed the ability of 2-PTS to oxidase all the proteins examined trough a thioalkenylation mechanism of cysteine residues, except Trx, essential for their enzymatic activity. Has been also observed the reaction between the 2-PTS and another important molecule, the glutathione (GSH). The 2-PTS can react with the GSH at physiological condition, producing S-allyl-mercaptoglutathione (GSSP), which is used, after its characterization, for molecular and cellular studies. Molecular studies indicates that GSSP is a competitive inhibitor of GSTM1-1, with a Ki of about 0,1 mM. Cellular studies on HuT 78 cell line, shows an inhibition of cell proliferation, with a G1/S phase blockage of the cell cycle, and an activation of p38 MAPKinase. It has been also observed the ability of GSSP to increment the intracellular concentration of Doxorubicin, incrementing its cytotoxic effect, in the case of combinate treatment of GSSP and Dox, respect to the only treatment with a non-toxic concentration of Doxo. The increase of the effect of Doxo is attended with an increment of expression of CDKN1A, p21. All these results gives prominence to the discovery of the role of the Trx-Trd-TST system as detoxifying system of the OSCs, because a dysregulation of expression or activity of one o more components of the system, as the case of some pathology [8, 9, 88, 91], could compromise the detoxification skill of the cell, explaining the major sensibility of some tumor cells to the OSCs treatment, or causing the develop of pathology correlated to the incorrect OSCs metabolism [88, 91]. Moreover, the inhibition of GST from 2-PTS and GSSP gives further indications on the intracellular mechanism of action of this type of compounds. In the end, the discover of the GSSP effect give indications on the possibility to use the co-treatment with chemoterapic (Doxo) and OSCs as possible methodological approach to reduce the used chemoterapic dose.