Academic literature on the topic 'Epoxide hydrolase'

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Journal articles on the topic "Epoxide hydrolase"

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van Loo, Bert, Jaap Kingma, Michael Arand, Marcel G. Wubbolts, and Dick B. Janssen. "Diversity and Biocatalytic Potential of Epoxide Hydrolases Identified by Genome Analysis." Applied and Environmental Microbiology 72, no. 4 (2006): 2905–17. http://dx.doi.org/10.1128/aem.72.4.2905-2917.2006.

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ABSTRACT Epoxide hydrolases play an important role in the biodegradation of organic compounds and are potentially useful in enantioselective biocatalysis. An analysis of various genomic databases revealed that about 20% of sequenced organisms contain one or more putative epoxide hydrolase genes. They were found in all domains of life, and many fungi and actinobacteria contain several putative epoxide hydrolase-encoding genes. Multiple sequence alignments of epoxide hydrolases with other known and putative α/β-hydrolase fold enzymes that possess a nucleophilic aspartate revealed that these enzy
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Edqvist, J., and I. Farbos. "Characterization of a Euphorbia lagascae epoxide hydrolase gene that is induced early during germination." Biochemical Society Transactions 28, no. 6 (2000): 855–56. http://dx.doi.org/10.1042/bst0280855.

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In Euphorbia lagascae the major fatty acid in triacylglycerol is the epoxidated fatty acid vernolic acid (cis- 12-epoxyoctadeca-cis-9-enoic acid). The enzymic reactions occurring during the catabolism of epoxidated fatty acids during germination are not known, but it seems likely that the degradation requires the activity of an epoxide hydrolase. Epoxide hydrolases are a group of functionally related enzymes that catalyse the cofactor-independent hydrolysis of epoxides to their corresponding vicinal diols by the addition of a water molecule. Here we report the cloning and characterization of a
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van der Werf, Mariët J., Karin M. Overkamp, and Jan A. M. de Bont. "Limonene-1,2-Epoxide Hydrolase fromRhodococcus erythropolis DCL14 Belongs to a Novel Class of Epoxide Hydrolases." Journal of Bacteriology 180, no. 19 (1998): 5052–57. http://dx.doi.org/10.1128/jb.180.19.5052-5057.1998.

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ABSTRACT An epoxide hydrolase from Rhodococcus erythropolisDCL14 catalyzes the hydrolysis of limonene-1,2-epoxide to limonene-1,2-diol. The enzyme is induced when R. erythropolis is grown on monoterpenes, reflecting its role in the limonene degradation pathway of this microorganism. Limonene-1,2-epoxide hydrolase was purified to homogeneity. It is a monomeric cytoplasmic enzyme of 17 kDa, and its N-terminal amino acid sequence was determined. No cofactor was required for activity of this colorless enzyme. Maximal enzyme activity was measured at pH 7 and 50°C. None of the tested inhibitors or m
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McKay, J. A., R. J. Weaver, G. I. Murray, S. W. Ewen, W. T. Melvin, and M. D. Burke. "Localization of microsomal epoxide hydrolase in normal and neoplastic human kidney." Journal of Histochemistry & Cytochemistry 43, no. 6 (1995): 615–20. http://dx.doi.org/10.1177/43.6.7769232.

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Microsomal epoxide hydrolase is a xenobiotic metabolizing enzyme that catalyzes the conversion of toxic and carcinogenic epoxides to less toxic dihydrodiols. The cellular localization and distribution of microsomal epoxide hydrolase were investigated for the first time in normal and neoplastic human kidney. Light microscopic immunohistochemical studies using an alkaline phosphatase-anti-alkaline phosphatase technique showed that in normal kidney there was a wide distribution of epoxide hydrolase immunoreactivity. The main localization of epoxide hydrolase immunoreactivity was to the proximal a
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Serrano-Hervás, Eila, Marc Garcia-Borràs, and Sílvia Osuna. "Exploring the origins of selectivity in soluble epoxide hydrolase from Bacillus megaterium." Organic & Biomolecular Chemistry 15, no. 41 (2017): 8827–35. http://dx.doi.org/10.1039/c7ob01847a.

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Epoxide hydrolase (EH) enzymes catalyze the hydration of racemic epoxides to yield their corresponding vicinal diols. In this work, the Bacillus megaterium epoxide hydrolase (BmEH)-mediated hydrolysis of racemic styrene oxide (rac-SO) and its para-nitro styrene oxide (rac-p-NSO) derivative are computationally investigated using density functional theory (DFT).
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Wijekoon, C. P., P. H. Goodwin, and T. Hsiang. "The involvement of two epoxide hydrolase genes, NbEH1.1 and NbEH1.2, of Nicotiana benthamiana in the interaction with Colletotrichum destructivum, Colletotrichum orbiculare or Pseudomonas syringae pv. tabaci." Functional Plant Biology 35, no. 11 (2008): 1112. http://dx.doi.org/10.1071/fp08160.

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Epoxide hydrolase hydrates epoxides to vicinal diols in the phyto-oxylipin peroxygenase pathway resulting in the production of epoxy alcohols, dihydrodiols, triols and epoxides, including many lipid epoxides associated with resistance. Two epoxide hydrolase genes from Nicotiana benthamiana L., NbEH1.1 and NbEH1.2, were amplified from coding DNA of leaves during a susceptible response to the hemibiotrophic pathogens, Colletotrichum destructivum O’Gara, Colletotrichum orbiculare Berk. and Mont. von Arx. or Pseudomonas syringae pv. tabaci Wolf and Foster, or the hypersensitive resistance response
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Tormet-González, Gabriela D., Carolina Wilson, Gabriel Stephani de Oliveira, Jademilson Celestino dos Santos, Luciana G. de Oliveira, and Marcio Vinicius Bertacine Dias. "An epoxide hydrolase from endophytic Streptomyces shows unique structural features and wide biocatalytic activity." Acta Crystallographica Section D Structural Biology 76, no. 9 (2020): 868–75. http://dx.doi.org/10.1107/s2059798320010402.

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The genus Streptomyces is characterized by the production of a wide variety of secondary metabolites with remarkable biological activities and broad antibiotic capabilities. The presence of an unprecedented number of genes encoding hydrolytic enzymes with industrial appeal such as epoxide hydrolases (EHs) reveals its resourceful microscopic machinery. The whole-genome sequence of Streptomyces sp. CBMAI 2042, an endophytic actinobacterium isolated from Citrus sinensis branches, was explored by genome mining, and a putative α/β-epoxide hydrolase named B1EPH2 and encoded by 344 amino acids was se
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Madacki, Jan, Martin Kopál, Mary Jackson, and Jana Korduláková. "Mycobacterial Epoxide Hydrolase EphD Is Inhibited by Urea and Thiourea Derivatives." International Journal of Molecular Sciences 22, no. 6 (2021): 2884. http://dx.doi.org/10.3390/ijms22062884.

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The genome of the human intracellular pathogen Mycobacterium tuberculosis encodes an unusually large number of epoxide hydrolases, which are thought to be involved in lipid metabolism and detoxification reactions needed to endure the hostile environment of host macrophages. These enzymes therefore represent suitable targets for compounds such as urea derivatives, which are known inhibitors of soluble epoxide hydrolases. In this work, we studied in vitro the effect of the thiourea drug isoxyl on six epoxide hydrolases of M. tuberculosis using a fatty acid substrate. We show that one of the prot
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Yu, Zhigang, Benjamin B. Davis, Christophe Morisseau, et al. "Vascular localization of soluble epoxide hydrolase in the human kidney." American Journal of Physiology-Renal Physiology 286, no. 4 (2004): F720—F726. http://dx.doi.org/10.1152/ajprenal.00165.2003.

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Epoxyeicosatrienoic acids are cytochrome P-450 metabolites of arachidonic acid with multiple biological functions, including the regulation of vascular tone, renal tubular transport, cellular proliferation, and inflammation. Epoxyeicosatrienoic acids are converted by soluble epoxide hydrolase into the corresponding dihydroxyeicosatrienoic acids, and epoxyeicosatrienoic acid hydration is regarded as one mechanism whereby their biological effects are eliminated. Previous animal studies indicate that soluble epoxide hydrolase plays an important role in the regulation of renal eicosanoid levels an
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Otake, Shinya, Norihiro Ogawa, Yoshikazu Kitano, Keiji Hasumi, and Eriko Suzuki. "Isoprene Side-chain of SMTP is Essential for Soluble Epoxide Hydrolase Inhibition and Cellular Localization." Natural Product Communications 11, no. 2 (2016): 1934578X1601100. http://dx.doi.org/10.1177/1934578x1601100223.

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SMTPs, a family of natural small molecules that effectively treat ischemic stroke, are subject to clinical development. SMTPs enhance plasminogen activation and inhibit soluble epoxide hydrolase (sEH), leading to promotion of endogenous thrombolysis and anti-inflammation. The SMTP molecule consists of a tricyclic γ-lactam moiety, an isoprene side-chain, and an N-linked side-chain. Here, we investigate the yet-to-be-characterized function of the isoprene side-chain of SMTPs in sEH inhibition and cellular distribution. The results demonstrated that oxidative modification as well as truncation of
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Dissertations / Theses on the topic "Epoxide hydrolase"

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Kroetz, Deanna L. "Inhibition of human liver microsomal epoxide hydrolase /." Thesis, Connect to this title online; UW restricted, 1990. http://hdl.handle.net/1773/7958.

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Wang, Li-Wen. "Directed evolution of the Aspergillus niger epoxide hydrolase." [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=981104282.

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Maritz, Jana. "The stabilisation of epoxide hydrolase activity / Jana Maritz." Thesis, Potchefstroom University for Christian Higher Education, 2002. http://hdl.handle.net/10394/1478.

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Sellers, Kathleen Walworth. "Role of brain soluble epoxide hydrolase in cardiovascular function." [Gainesville, Fla.] : University of Florida, 2004. http://purl.fcla.edu/fcla/etd/UFE0008356.

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Thesis (Ph.D.)--University of Florida, 2004.<br>Typescript. Title from title page of source document. Document formatted into pages; contains 156 pages. Includes Vita. Includes bibliographical references.
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Hattori, Nao. "Epoxide hydrolase affects estrogen production in the human ovary." Kyoto University, 2001. http://hdl.handle.net/2433/150184.

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Davis, Benjamin Boyce. "Novel treatments for atherosclerosis with inhibitors of soluble epoxide hydrolase /." For electronic version search Digital dissertations database. Restricted to UC campuses. Access is free to UC campus dissertations, 2005. http://uclibs.org/PID/11984.

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Sandberg, Martin. "Mammalian soluble epoxide hydrolase : studies on gene structure and expression /." Uppsala : Swedish Univ. of Agricultural Sciences (Sveriges lantbruksuniv.), 2000. http://epsilon.slu.se/avh/2000/91-576-5747-5.pdf.

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Janfalk, Carlsson Åsa. "Towards Understanding of Selectivity & Enantioconvergence of an Epoxide Hydrolase." Doctoral thesis, Uppsala universitet, Institutionen för kemi - BMC, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-286557.

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Epoxide hydrolase I from Solanum tuberosum (StEH1) and isolated variants thereof has been studied for mapping structure-function relationships with the ultimate goal of being able to in silico predict modifications needed for a certain activity or selectivity. To solve this, directed evoultion using CASTing and an ISM approach was applied to improve selectivity towards either of the enantiomeric product diols from (2,3-epoxypropyl)benzene (1). A set of variants showing a range of activites and selectivities was isolated and characterized to show that both enantio- and regioselectivity was chan
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Lindberg, Diana. "Exploring Selectivity and Hysteresis : Kinetic Studies on a Potato Epoxide Hydrolase." Doctoral thesis, Uppsala universitet, Institutionen för biokemi och organisk kemi, 2010. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-112285.

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The kinetic mechanism of an α/β hydrolase fold epoxide hydrolase from potato, StEH1, has been studied with the aims of explaining the underlying causes for enantio- and regioselectivity, both being important for product purity. Further effort has been laid upon understanding the causes of a hysteretic behavior discovered in the measurements leading to Paper I. The enantioselectivity was investigated with substrates differing only in substituent size at one carbon of the oxirane ring structure. In catalysis with trans-stilbene oxide and styrene oxide, enantioselectivity is the result of differe
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Ali, Ahmed Said. "Investigation of epoxide hydrolase activity in Saccharomyces cerevisiae ORF YNR064c protein." Thesis, Uppsala universitet, Institutionen för kemi - BMC, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-203473.

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Books on the topic "Epoxide hydrolase"

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Maguire, Marcia Lynn. The role of epoxide hydrolase in aromatic anticonvulsant-induced birth defects. National Library of Canada, 1993.

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Imig, John D., and Christophe Morisseau, eds. Clinical Paths for Soluble Epoxide Hydrolase Inhibitors. Frontiers Media SA, 2020. http://dx.doi.org/10.3389/978-2-88966-161-9.

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Book chapters on the topic "Epoxide hydrolase"

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Schomburg, Dietmar, and Dörte Stephan. "Hepoxilin-epoxide hydrolase." In Enzyme Handbook 15. Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_87.

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Singh, Nalin, and Bruce D. Hammock. "Soluble Epoxide Hydrolase." In Encyclopedia of Molecular Pharmacology. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-21573-6_10020-1.

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Singh, Nalin, and Bruce D. Hammock. "Soluble Epoxide Hydrolase." In Encyclopedia of Molecular Pharmacology. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-57401-7_10020.

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Oesch, Franz, Ludwig Schladt, Renate Hartmann, Christopher Timms, and Walter Wörner. "Rat Cytosolic Epoxide Hydrolase." In Biological Reactive Intermediates III. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5134-4_16.

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Costa, Lucio G., Toby B. Cole, Gary K. Geiss, and Clement E. Furlong. "Paraoxonase, Butyrylcholinesterase, and Epoxide Hydrolase." In Gene-Environment Interactions. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/0471758043.ch9.

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Nelson, Jonathan W., and Nabil J. Alkayed. "Soluble Epoxide Hydrolase as a Stroke Target." In Translational Stroke Research. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-9530-8_13.

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Saini, Priya, and Dipti Sareen. "Epoxide Hydrolase for the Synthesis of Chiral Drugs." In Nanoscience and Biotechnology for Environmental Applications. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-97922-9_6.

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Arnoldi, A., D. Cova, and L. Rossini. "Epoxide Metabolites of Opiates and Their Interaction with the Hepatic Microsomal Epoxide Hydrolase." In Archives of Toxicology. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73113-6_65.

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Friedberg, T., C. Timms, W. Kissel, and F. Oesch. "Evidence for Several Hepatic Proteins Related to Microsomal Epoxide Hydrolase." In Archives of Toxicology. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-74117-3_20.

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Cova, D., A. Arnoldi, R. Colombo, and L. Rossini. "Stereochemical Considerations on the Inhibition of Hepatic Epoxide Hydrolase by Some Pesticides and Their Epoxides." In Archives of Toxicology. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71248-7_69.

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Conference papers on the topic "Epoxide hydrolase"

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Lazaar, Aili, Lucy Yang, Jon Robertson, et al. "Safety and pharmacology of a soluble epoxide hydrolase inhibitor." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa2120.

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Van Winkle, LS, PC Edwards, JK Chan, et al. "Microsomal Epoxide Hydrolase and Airway Sensitivity to the Air Pollutant Naphthalene." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3178.

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Tumurbaatar, Ariuntungalag, Ichinnorov Dashtseren, Sarantuya Jav, and Chimedlkhamsuren Ganbold. "Polymorphisms for epoxide hydrolase, glutathione transferase and genetic susceptibility to COPD." In ERS International Congress 2020 abstracts. European Respiratory Society, 2020. http://dx.doi.org/10.1183/13993003.congress-2020.3325.

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Yang, Jun, Jennifer Bratt, Lisa Franzi, et al. "Soluble Epoxide Hydrolase Inhibitor Attenuates The Ovalbumin-Induced Murine Asthmatic Symptoms." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1425.

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Achanta, S., A. Marcus, A. Caceres, and S. E. Jordt. "Soluble Epoxide Hydrolase Inhibitors and ACE Inhibitors Ameliorate Phosgene Inhalation Injuries." In American Thoracic Society 2023 International Conference, May 19-24, 2023 - Washington, DC. American Thoracic Society, 2023. http://dx.doi.org/10.1164/ajrccm-conference.2023.207.1_meetingabstracts.a1171.

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Kandasamy, Ram, Tiffany Chacon, Christopher Chin, and Stevan Pecic. "Simultaneous Inhibition of Soluble Epoxide Hydrolase and Fatty Acid Amide Hydrolase Prevents Nitroglycerin-induced Hypersensitivity in Female Rats." In ASPET 2024 Annual Meeting Abstract. American Society for Pharmacology and Experimental Therapeutics, 2024. http://dx.doi.org/10.1124/jpet.476.907640.

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Pecic, Stevan, Ram Kandasamy, and Jeannes Angelia. "Multitarget-Directed Ligands with Soluble Epoxide Hydrolase and Fatty Acid Amide Hydrolase Inhibitory Activities for Treatment of Chronic Pain." In ASPET 2024 Annual Meeting Abstract. American Society for Pharmacology and Experimental Therapeutics, 2024. http://dx.doi.org/10.1124/jpet.474.878670.

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Davis, Benjamin B., Jun-Yan Liu, Daniel J. Tancredi, Scott I. Simon, Bruce D. Hammock, and Kent E. Pinkerton. "Anti-inflammatory Effects Of Soluble Epoxide Hydrolase Inhibition Are Independent Of Leukocyte Recruitment." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a5751.

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Lee, Eun Yeol, and Sung Hee Choi. "Nano-formulation of Marine Recombinant Epoxide Hydrolase for the Synthesis of Enantiopure Chemicals." In 14th Asia Pacific Confederation of Chemical Engineering Congress. Research Publishing Services, 2012. http://dx.doi.org/10.3850/978-981-07-1445-1_625.

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Liu, Jun-Yan, Ai-Zhi Lin, Xian Fu, Jiang Qing, and Bruce Hammock. "Inhibition of soluble epoxide hydrolase attenuates high-sucrose diet-mediated gut barrier dysfunction." In ASPET 2024 Annual Meeting Abstract. American Society for Pharmacology and Experimental Therapeutics, 2024. http://dx.doi.org/10.1124/jpet.556.979490.

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