Relevant bibliographies by topics / 3-dioxygenase

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic '3-dioxygenase'

Author: Grafiati
Published: 4 June 2021
Last updated: 7 July 2024

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Journal articles on the topic "3-dioxygenase"

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Mars, Astrid E., Jaap Kingma, Stefan R. Kaschabek, Walter Reineke, and Dick B. Janssen. "Conversion of 3-Chlorocatechol by Various Catechol 2,3-Dioxygenases and Sequence Analysis of the Chlorocatechol Dioxygenase Region of Pseudomonas putida GJ31." Journal of Bacteriology 181, no. 4 (1999): 1309–18. http://dx.doi.org/10.1128/jb.181.4.1309-1318.1999.

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ABSTRACT Pseudomonas putida GJ31 contains an unusual catechol 2,3-dioxygenase that converts 3-chlorocatechol and 3-methylcatechol, which enables the organism to use both chloroaromatics and methylaromatics for growth. A 3.1-kb region of genomic DNA of strain GJ31 containing the gene for this chlorocatechol 2,3-dioxygenase (cbzE) was cloned and sequenced. The cbzE gene appeared to be plasmid localized and was found in a region that also harbors genes encoding a transposase, a ferredoxin that was homologous to XylT, an open reading frame with similarity to a protein of ameta-cleavage pathway wit
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Khan, Ashraf A., Rong-Fu Wang, Wei-Wen Cao, Daniel R. Doerge, David Wennerstrom, and Carl E. Cerniglia. "Molecular Cloning, Nucleotide Sequence, and Expression of Genes Encoding a Polycyclic Aromatic Ring Dioxygenase from Mycobacterium sp. Strain PYR-1." Applied and Environmental Microbiology 67, no. 8 (2001): 3577–85. http://dx.doi.org/10.1128/aem.67.8.3577-3585.2001.

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ABSTRACT Mycobacterium sp. strain PYR-1 degrades high-molecular-weight polycyclic hydrocarbons (PAHs) primarily through the introduction of both atoms of molecular oxygen by a dioxygenase. To clone the dioxygenase genes involved in PAH degradation, two-dimensional (2D) gel electrophoresis of PAH-induced proteins from cultures of Mycobacterium sp. strain PYR-1 was used to detect proteins that increased after phenanthrene, dibenzothiophene, and pyrene exposure. Comparison of proteins from induced and uninduced cultures on 2D gels indicated that at least six major proteins were expressed (105, 81
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Kaschabek, Stefan R., Thomas Kasberg, Dagmar Müller, Astrid E. Mars, Dick B. Janssen, and Walter Reineke. "Degradation of Chloroaromatics: Purification and Characterization of a Novel Type of Chlorocatechol 2,3-Dioxygenase of Pseudomonas putida GJ31." Journal of Bacteriology 180, no. 2 (1998): 296–302. http://dx.doi.org/10.1128/jb.180.2.296-302.1998.

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ABSTRACT A purification procedure for a new kind of extradiol dioxygenase, termed chlorocatechol 2,3-dioxygenase, that converts 3-chlorocatechol productively was developed. Structural and kinetic properties of the enzyme, which is part of the degradative pathway used for growth ofPseudomonas putida GJ31 with chlorobenzene, were investigated. The enzyme has a subunit molecular mass of 33.4 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Estimation of the native M r value under nondenaturating conditions by gel filtration gave a molecular mass of 135 ± 10 kDa, indicating a homo
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Liu, Hong, Shu-Jun Wang, Jun-Jie Zhang, Hui Dai, Huiru Tang, and Ning-Yi Zhou. "Patchwork Assembly ofnag-Like Nitroarene Dioxygenase Genes and the 3-Chlorocatechol Degradation Cluster for Evolution of the 2-Chloronitrobenzene Catabolism Pathway in Pseudomonas stutzeri ZWLR2-1." Applied and Environmental Microbiology 77, no. 13 (2011): 4547–52. http://dx.doi.org/10.1128/aem.02543-10.

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ABSTRACTPseudomonas stutzeriZWLR2-1 utilizes 2-chloronitrobenzene (2CNB) as a sole source of carbon, nitrogen, and energy. To identify genes involved in this pathway, a 16.2-kb DNA fragment containing putative 2CNB dioxygenase genes was cloned and sequenced. Of the products from the 19 open reading frames that resulted from this fragment, CnbAc and CnbAd exhibited striking identities to the respective α and β subunits of the Nag-like ring-hydroxylating dioxygenases involved in the metabolism of nitrotoluene, nitrobenzene, and naphthalene. The encoding genes were also flanked by two copies of i
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Mahan, Kristina M., Joseph T. Penrod, Kou-San Ju, et al. "Selection for Growth on 3-Nitrotoluene by 2-Nitrotoluene-Utilizing Acidovorax sp. Strain JS42 Identifies Nitroarene Dioxygenases with Altered Specificities." Applied and Environmental Microbiology 81, no. 1 (2014): 309–19. http://dx.doi.org/10.1128/aem.02772-14.

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ABSTRACTAcidovoraxsp. strain JS42 uses 2-nitrotoluene as a sole source of carbon and energy. The first enzyme of the degradation pathway, 2-nitrotoluene 2,3-dioxygenase, adds both atoms of molecular oxygen to 2-nitrotoluene, forming nitrite and 3-methylcatechol. All three mononitrotoluene isomers serve as substrates for 2-nitrotoluene dioxygenase, but strain JS42 is unable to grow on 3- or 4-nitrotoluene. Using both long- and short-term selections, we obtained spontaneous mutants of strain JS42 that grew on 3-nitrotoluene. All of the strains obtained by short-term selection had mutations in th
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Boyd, Derek R., Narain D. Sharma, Ludmila V. Modyanova, et al. "Dioxygenase-catalyzed cis-dihydroxylation of pyridine-ring systems." Canadian Journal of Chemistry 80, no. 6 (2002): 589–600. http://dx.doi.org/10.1139/v02-062.

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Toluene dioxygenase-catalyzed dihydroxylation, in the carbocyclic rings of quinoline, 2-chloroquinoline, 2-methoxyquinoline, and 3-bromoquinoline, was found to yield the corresponding enantiopure cis-5,6- and -7,8-dihy dro diol metabolites using whole cells of Pseudomonas putida UV4. cis-Dihydroxylation at the 3,4-bond of 2-chloroquino line, 2-methoxyquinoline, and 2-quinolone was also found to yield the heterocyclic cis-dihydrodiol metabolite, (+)-cis-(3S,4S)-3,4-dihydroxy-3,4-dihydro-2-quinolone. Heterocyclic cis-dihydrodiol metabolites, resulting from dihydroxylation at the 5,6- and 3,4-bon
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Haddad, Sandra, D. Matthew Eby, and Ellen L. Neidle. "Cloning and Expression of the Benzoate Dioxygenase Genes from Rhodococcus sp. Strain 19070." Applied and Environmental Microbiology 67, no. 6 (2001): 2507–14. http://dx.doi.org/10.1128/aem.67.6.2507-2514.2001.

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ABSTRACT The bopXYZ genes from the gram-positive bacteriumRhodococcus sp. strain 19070 encode a broad-substrate-specific benzoate dioxygenase. Expression of the BopXY terminal oxygenase enabled Escherichia coli to convert benzoate or anthranilate (2-aminobenzoate) to a nonaromaticcis-diol or catechol, respectively. This expression system also rapidly transformed m-toluate (3-methylbenzoate) to an unidentified product. In contrast, 2-chlorobenzoate was not a good substrate. The BopXYZ dioxygenase was homologous to the chromosomally encoded benzoate dioxygenase (BenABC) and the plasmid-encoded t
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Tchesnokov, Egor P., Matthias Fellner, Eleni Siakkou, et al. "The Cysteine Dioxygenase Homologue fromPseudomonas aeruginosaIs a 3-Mercaptopropionate Dioxygenase." Journal of Biological Chemistry 290, no. 40 (2015): 24424–37. http://dx.doi.org/10.1074/jbc.m114.635672.

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Wallis, M. G., and S. K. Chapman. "3-Methylcatechol 2,3-dioxygenase - a comparison with other non-heme iron dioxygenases." Journal of Inorganic Biochemistry 43, no. 2-3 (1991): 563. http://dx.doi.org/10.1016/0162-0134(91)84538-k.

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Riegert, Ulrich, Gesche Heiss, Andrea Elisabeth Kuhm, et al. "Catalytic Properties of the 3-Chlorocatechol-Oxidizing 2,3-Dihydroxybiphenyl 1,2-Dioxygenase from Sphingomonas sp. Strain BN6." Journal of Bacteriology 181, no. 16 (1999): 4812–17. http://dx.doi.org/10.1128/jb.181.16.4812-4817.1999.

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ABSTRACT The 2,3-dihydroxybiphenyl dioxygenase from Sphingomonassp. strain BN6 (BphC1-BN6) differs from most other extradiol dioxygenases by its ability to oxidize 3-chlorocatechol to 3-chloro-2-hydroxymuconic semialdehyde by a distal cleavage mechanism. The turnover of different substrates and the effects of various inhibitors on BphC1-BN6 were compared with those of another 2,3-dihydroxybiphenyl dioxygenase from the same strain (BphC2-BN6) as well as with those of the archetypical catechol 2,3-dioxygenase (C23O-mt2) encoded by the TOL plasmid. Cell extracts containing C23O-mt2 or BphC2-BN6 c
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Dissertations / Theses on the topic "3-dioxygenase"

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Alameer, Fouad Elrafaie Ali. "Synthesis of mechanism probes and potential inhibitors for tryptophan 2, 3-dioxygenase and indoleamine 2, 3-dioxygenase enzymes." Thesis, University of Leicester, 2017. http://hdl.handle.net/2381/39876.

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In biological terms, the kynurenine pathway is considered as a one of the major degradation pathway of tryptophan (L-Trp) in which the first and rate-limiting step in this pathway is the oxidation of L-Trp to N-formylkynurenin (NFK). In spite of the fact that many mechanism have been proposed to explain how the transformation occurs, the mechanism of this oxygen-dependent reaction has not yet been determined. Nonetheless, this type of unique reaction is catalysed by two heme-containing dioxygenase enzymes:- tryptophan 2,3-dioxygenase (TDO), and indoleamine 2,3-dioxygenase (IDO), and due to the
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Habibi, Darya. "Mechanisms of selective immunosuppressive effects of indoleamine 2, 3-dioxygenase and borrelidin." Thesis, University of British Columbia, 2011. http://hdl.handle.net/2429/36674.

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Indoleamine 2, 3-dioxygenase (IDO), a tryptophan degrading enzyme, is a potent immunomodulatory factor that has been considered as a promising candidate in down-regulating alloimmune responses. IDO expression generates a tryptophan-deficient environment that selectively induces apoptosis in immune cells but not in primary skin cells. However, the mechanism(s) underlying these selective effects of IDO is not elucidated. In this doctoral research project, we hypothesize that different sensitivity of immune cells versus skin cells to IDO-induced tryptophan-deficient environment is due to the diff
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Fu, Rong. "Biochemical and Spectroscopic Characterization of Tryptophan Oxygenation: Tryptophan 2, 3-Dioxygenase and Maug." Digital Archive @ GSU, 2009. http://digitalarchive.gsu.edu/chemistry_diss/44.

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TDO utilizes b-type heme as a cofactor to activate dioxygen and insert two oxygen atoms into free L-tryptophan. We revealed two unidentified enzymatic activities of ferric TDO from Ralstonia metallidurans, which are peroxide driven oxygenation and catalase-like activity. The stoichiometric titration suggests that two moles of H2O2 were required for the production of one mole of N-formylkynurenine. We have also observed monooxygenated-L-tryptophan. Three enzyme-based intermediates were sequentially detected in the peroxide oxidation of ferric TDO in the absence of L-Trp including compound I-typ
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Galik, Ryan. "Inhibition of Cytokine Induced Indoleamine 2, 3-Dioxygenase Expression in a Human Monocytic Cancer Cell Line." Ohio University / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1535036948694968.

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Arefayene, Million. "Identification and functional characterization of genetic variants in the human indoleamine 2, 3-dioxygenase (INDO) gene." Thesis, Connect to resource online, 2008. http://hdl.handle.net/1805/1704.

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Thesis (Ph.D.)--Indiana University, 2008.<br>Title from screen (viewed on June 4, 2009). Department of Pharmacology and Toxicology, Indiana University-Purdue University Indianapolis (IUPUI). Advisor(s): David A. Flockhart. Includes vita. Includes bibliographical references (leaves 124-139).
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Karvelis, Laimonas. "Investigation of the Degradation of Carboxypyridines in Bacteria." Doctoral thesis, Lithuanian Academic Libraries Network (LABT), 2012. http://vddb.laba.lt/obj/LT-eLABa-0001:E.02~2012~D_20121001_092919-52075.

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The main aim of this work was the study of bacteria capable to degrade the pyridine monocarboxylic acids. Achromobacter sp. strain JS18 capable to utilize 3-hydroxypyridine- 2-carboxylic acid was selected by screening of microorganisms hydroxylating the pyridine ring at unusual positions or transforming pyridine derivatives . The strain 5HP consuming 5- hydroxypyridine-2-carboxylic acid as a sole carbon and energy source was isolated from soil. The 16S rRNA-based phylogenetic analysis showed that the isolate belongs to Pusillimonas genus. It was found that picolinic, nicotinic and dipicolinic
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Pelletier, Matthew K. "Molecular and Biochemical Genetics of 2-Oxoglutarate-Dependent Dioxygenases Required for Flavonoid Biosynthesis in Arabidopsis thaliana." Diss., Virginia Tech, 1997. http://hdl.handle.net/10919/30599.

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Three 2-oxoglutarate-dependent dioxygenases required for flavonoid biosynthesis were characterized in Arabidopsis thaliana. Genes encoding flavanone 3-hydroxylase (F3H), flavonol synthase (FLS), and leucoanthocyanidin dioxygenase (LDOX) were cloned and sequenced. The predicted proteins encoded by each of these Arabidopsis genes shared high homology with all F3H, FLS, or LDOX sequences available in Genbank. Low-stringency DNA blot analysis indicated that F3H and LDOX are encoded by a single gene in Arabidopsis, while FLS may be encoded by two or three genes. RNA blot analysis was performed
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Baradar, Jalili Reza. "Development and application of a non-rejectable composite pancreatic islet allograft using indoleamine 2, 3 dioxygenase in a diabetic mouse model." Thesis, University of British Columbia, 2009. http://hdl.handle.net/2429/24154.

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Success of transplantation of pancreatic islets as a promising therapeutic method for restoring efficient regulated insulin secretion in type 1 diabetes depends on lifelong use of immunosuppressive drugs. With the goal of eliminating the necessity of systemic immunosuppressive agents after islet transplantation, in this doctoral research project we hypothesized that a novel non-rejectable islet graft through employing a local immunosuppressive factor, indoleamine 2, 3 dioxygenase (IDO) can be developed and applied. IDO is a tryptophan degrading enzyme and functions as a potent immunomodulatory
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Schmid, Manuela. "Eimeria falciformis infection of mouse cells identifies host determinants of parasite development." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2014. http://dx.doi.org/10.18452/17001.

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Eimeria falciformis ist ein Apicomplexa-Parasit, welcher das Blinddarmepithel der Maus befällt. Aufgrund des monoxenen Lebenszyklus in einem exzellent-erforschten Wirt, bietet sich E. falciformis als Modellorganismus an, um Wirts-Parasit-Interaktionen zu untersuchen. Im Rahmen dieser Arbeit wurden mit Hilfe von Genexpressionsanalysen bei E. falciformis-infizierten Zellen und Mäusen Wirtsfaktoren identifiziert, welche für die in vitro bzw. in vivo Entwicklung des Parasiten vonnöten sind. Der Transkriptionsfaktor c-FOS (FBJ osteosarcoma oncogene) zeigte eine erhöhte Expression bei der Infektion
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Francis, Kevin. "On the Biochemistry, Mechanism and Physiological Role of Fungal Nitronate Monooxygenase." Digital Archive @ GSU, 2011. http://digitalarchive.gsu.edu/chemistry_diss/51.

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Nitronate monooxygenase (E.C. 1.13.11.16), formerly known as 2-nitropropane dioxygenase (EC 1.13.11.32), is a flavin dependent enzyme that catalyzes the oxidation of nitronates to their corresponding carbonyl compounds and nitrite. Despite the fact that the enzyme was first isolated from Neurospora crassa 60 years ago, the biochemical and physiological properties of nitronate monooxygenase have remained largely elusive. This dissertation will present the work that established both the catalytic mechanism and physiological role of the fungal enzyme. The biological and biochemical properties of
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Book chapters on the topic "3-dioxygenase"

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Schomburg, Dietmar, and Dörte Stephan. "Naringenîn 3-dioxygenase." In Enzyme Handbook. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_63.

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Schomburg, Dietmar, and Dörte Stephan. "3-Carboxyethylcatechol 2,3-dioxygenase." In Enzyme Handbook. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_15.

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Schomburg, Dietmar, and Dörte Stephan. "3-Hydroxyanthranilate 3,4-dioxygenase." In Enzyme Handbook. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_6.

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Schomburg, Dietmar, and Dörte Stephan. "Procollagen-proline 3-dioxygenase." In Enzyme Handbook. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_61.

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Schomburg, Dietmar, and Dörte Stephan. "3-Hydroxy-2-methylpyridine carboxylate dioxygenase." In Enzyme Handbook. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_73.

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Ji, X. D., M. Nishimura, and M. P. Heyes. "Non-Competitive Inhibition of 3-Hydroxyanthranilate-3, 4-Dioxygenase by 4-Chloro-3-Hydroxyanthranilic Acid in Whole Brain of Rat." In Advances in Experimental Medicine and Biology. Springer New York, 1991. http://dx.doi.org/10.1007/978-1-4684-5952-4_67.

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Schomburg, Dietmar, and Dörte Stephan. "Sulfur dioxygenase." In Enzyme Handbook. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_17.

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Schomburg, Dietmar, and Dörte Stephan. "Cysteamine dioxygenase." In Enzyme Handbook. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_18.

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Schomburg, Dietmar, and Dörte Stephan. "Cysteine dioxygenase." In Enzyme Handbook. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_19.

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Schomburg, Dietmar, and Dörte Stephan. "Thymine dioxygenase." In Enzyme Handbook. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_60.

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Conference papers on the topic "3-dioxygenase"

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Lynch, Kevin, Sarah Gradeki, Min Kwak, Alejandro Gru, Nolan Wages, and Craig Slingluff. "Abstract 5083: Indoleamine 2-3 dioxygenase expression by metastatic melanoma cells correlates with increased overall survival." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-5083.

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KUAN, YU-DIAO, and Che-Hsin Lee. "Abstract 1019: Salmonella break tumor immune tolerance by downregulation tumor indoleamine 2, 3-dioxygenase 1 expression." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-1019.

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Ahmad, Jamil, Javaria Ashraf, Kashif Asghar, and Umar Khan Niazi. "Qualitative modelling and analysis of the regulatory network of indoleamine 2, 3-dioxygenase in tumour immune escape." In 2011 International Conference on Computer Networks and Information Technology (ICCNIT). IEEE, 2011. http://dx.doi.org/10.1109/iccnit.2011.6020905.

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Ogura, Takashi, Sachiko Yanagisawa, Norihiro Okada, et al. "Resonance Raman Identification Of A Fe[sup IV] = O Type Reaction Intermediate During Indoleamine 2, 3-Dioxygenase Reaction." In XXII INTERNATIONAL CONFERENCE ON RAMAN SPECTROSCOPY. AIP, 2010. http://dx.doi.org/10.1063/1.3482874.

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Nakamura, Takafumi. "Abstract 4638: The p53 suppression on tumor cells may recruit macrophages and modulate their expression of the indoleamine 2, 3-dioxygenase." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-4638.

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Zakharia, Yousef, Joseph Drabick, Samir Khleif, et al. "Abstract CT087: Phase II trial of theiIndoleamine 2, 3-dioxygenase pathway (IDO) inhibitor indoximod plus immune checkpoint inhibitors for the treatment of unresectable stage 3 or 4 melanoma." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-ct087.

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Gu, F., SK Noonepalle, E.-J. Lee, et al. "Abstract P6-02-08: Modulation of indoleamine 2, 3-dioxygenase (IDO1) expression in breast cancer cells by activated CD8+ T cells is controlled by DNA promoter methylation." In Abstracts: 2016 San Antonio Breast Cancer Symposium; December 6-10, 2016; San Antonio, Texas. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.sabcs16-p6-02-08.

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Nakamura, Takafumi. "Abstract 4713: A Kampo (Japanese herbal) medicine Juzentaihoto may suppress the expression of indoleamine 2, 3-dioxygenase on macrophages and prolong the survival of transgenic mice bearing lens-epithelial cell carcinoma." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4713.

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Papadopoulos, Kyriakos, Paul Eder, Sarina A. Piha-Paul, et al. "Abstract CT011: First-in-human Phase I study of M4112, the first dual inhibitor of indoleamine 2,3-dioxygenase-1 and tryptophan 2,3-dioxygenase 2, in patients with advanced solid malignancies." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-ct011.

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Papadopoulos, Kyriakos, Paul Eder, Sarina A. Piha-Paul, et al. "Abstract CT011: First-in-human Phase I study of M4112, the first dual inhibitor of indoleamine 2,3-dioxygenase-1 and tryptophan 2,3-dioxygenase 2, in patients with advanced solid malignancies." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-ct011.

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