Literatura académica sobre el tema "Short-chain dehydrogenase/reductase (SDR)"
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Artículos de revistas sobre el tema "Short-chain dehydrogenase/reductase (SDR)"
Gallego, Oriol, Olga V. Belyaeva, Sergio Porté, F. Xavier Ruiz, Anton V. Stetsenko, Elena V. Shabrova, Natalia V. Kostereva, Jaume Farrés, Xavier Parés y Natalia Y. Kedishvili. "Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids". Biochemical Journal 399, n.º 1 (13 de septiembre de 2006): 101–9. http://dx.doi.org/10.1042/bj20051988.
Texto completoGabrielli, Franco, Marco Antinucci y Sergio Tofanelli. "Gene Structure Evolution of the Short-Chain Dehydrogenase/Reductase (SDR) Family". Genes 14, n.º 1 (30 de diciembre de 2022): 110. http://dx.doi.org/10.3390/genes14010110.
Texto completoLi, Aipeng, Lidan Ye, Xiaohong Yang, Chengcheng Yang, Jiali Gu y Hongwei Yu. "Structure-guided stereoselectivity inversion of a short-chain dehydrogenase/reductase towards halogenated acetophenones". Chemical Communications 52, n.º 37 (2016): 6284–87. http://dx.doi.org/10.1039/c6cc00051g.
Texto completoPersson, Bengt, Yvonne Kallberg, James E. Bray, Elspeth Bruford, Stephen L. Dellaporta, Angelo D. Favia, Roser Gonzalez Duarte et al. "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chemico-Biological Interactions 178, n.º 1-3 (marzo de 2009): 94–98. http://dx.doi.org/10.1016/j.cbi.2008.10.040.
Texto completoBray, James E., Brian D. Marsden y Udo Oppermann. "The human short-chain dehydrogenase/reductase (SDR) superfamily: A bioinformatics summary". Chemico-Biological Interactions 178, n.º 1-3 (marzo de 2009): 99–109. http://dx.doi.org/10.1016/j.cbi.2008.10.058.
Texto completoDavidson, Jaysón, Kyndall Nicholas, Jeremy Young, Deborah G. Conrady, Stephen Mayclin, Sandhya Subramanian, Bart L. Staker, Peter J. Myler y Oluwatoyin A. Asojo. "Crystal structure of a putative short-chain dehydrogenase/reductase from Paraburkholderia xenovorans". Acta Crystallographica Section F Structural Biology Communications 78, n.º 1 (1 de enero de 2022): 25–30. http://dx.doi.org/10.1107/s2053230x21012632.
Texto completoAlenazi, Jawaher, Stephen Mayclin, Sandhya Subramanian, Peter J. Myler y Oluwatoyin A. Asojo. "Crystal structure of a short-chain dehydrogenase/reductase from Burkholderia phymatum in complex with NAD". Acta Crystallographica Section F Structural Biology Communications 78, n.º 2 (27 de enero de 2022): 52–58. http://dx.doi.org/10.1107/s2053230x22000218.
Texto completoContreras, Ángela, Irene Merino, Enrique Álvarez, David Bolonio, José-Eugenio Ortiz, Luis Oñate-Sánchez y Luis Gómez. "A poplar short-chain dehydrogenase reductase plays a potential key role in biphenyl detoxification". Proceedings of the National Academy of Sciences 118, n.º 35 (26 de agosto de 2021): e2103378118. http://dx.doi.org/10.1073/pnas.2103378118.
Texto completoJacob, Asha I., Sirin A. I. Adham, David S. Capstick, Scott R. D. Clark, Tara Spence y Trevor C. Charles. "Mutational Analysis of the Sinorhizobium meliloti Short-Chain Dehydrogenase/Reductase Family Reveals Substantial Contribution to Symbiosis and Catabolic Diversity". Molecular Plant-Microbe Interactions® 21, n.º 7 (julio de 2008): 979–87. http://dx.doi.org/10.1094/mpmi-21-7-0979.
Texto completoBryndová, J., P. Klusoňová, M. Kučka, K. Mazancová-Vagnerová, I. Mikšík y J. Pácha. "Cloning and expression of chicken 20-hydroxysteroid dehydrogenase". Journal of Molecular Endocrinology 37, n.º 3 (diciembre de 2006): 453–62. http://dx.doi.org/10.1677/jme.1.02025.
Texto completoTesis sobre el tema "Short-chain dehydrogenase/reductase (SDR)"
Olandersson, Sandra. "Evaluation of Machine Learning Algorithms for Classification of Short-Chain Dehydrogenase/Reductase Protein Sequences". Thesis, Blekinge Tekniska Högskola, Institutionen för programvaruteknik och datavetenskap, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:bth-3828.
Texto completoKlassificeringen av proteinsekvenser är ett område inom Bioinformatik, vilket idag drar till sig ett stort intresse. Maskininlärningsalgoritmer anses här kunna förbättra utförandet av klassificeringsfasen. Denna uppsats rör tillämpandet av olika maskininlärningsalgoritmer för klassificering av ett dataset med short-chain dehydrogenases/reductases (SDR) proteiner. Klassificeringen rör både indelningen av proteinerna i två huvudklasser, Classic och Extended, och deras olika subklasser. Resultaten av de olika algoritmerna jämförs för att välja ut den mest lämpliga algoritmen för detta specifika klassificeringsproblem.
Sandra Olandersson Blåbärsvägen 27 372 38 Ronneby home: 0457-12084
ROTONDO, ROSSELLA. "New enzymatic pathway(s) in 4-hydroxynonenal metabolism". Doctoral thesis, Università di Siena, 2017. http://hdl.handle.net/11365/1007903.
Texto completoGong, Wenjie [Verfasser]. "Characterization of the LysR-type Transcriptional Regulator HsdR Gene and Its Adjacent Short-chain Dehydrogenase, Reductase SDRx Gene in Comamonas testosteroni ATCC 11996 / Wenjie Gong". Kiel : Universitätsbibliothek Kiel, 2011. http://d-nb.info/1020244666/34.
Texto completoScherbak, Nikolai, Anneli Ala-Häiväla, Mikael Brosché, Nathalie Böwer, Hilja Strid, John R. Gittins, Elin M. Grahn, Leif A. Eriksson y Åke Strid. "The pea SAD short-chain dehydrogenase/reductase : quinone reduction, tissue distribution, and heterologous expression". Örebro universitet, Akademin för naturvetenskap och teknik, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:oru:diva-15765.
Texto completoLuba, James. "Studies of Leishmania major Pteridine Reductase 1, a Novel Short Chain Dehydrogenase". eScholarship@UMMS, 1997. https://escholarship.umassmed.edu/gsbs_diss/45.
Texto completoKeller, Brigitte D. "Search for new steroid hormone metabolizing enzymes functional genomics of the short chain dehydrogenase, reductase superfamily /". [S.l.] : [s.n.], 2006. http://mediatum2.ub.tum.de/doc/603773/document.pdf.
Texto completoHoffmann, Frank [Verfasser]. "Carbonyl Reductases and Pluripotent Hydroxysteroid Dehydrogenases of the Short-Chain Dehydrogenase/Reductase Superfamily : Structural Aspects of Oligomerization in 3-Hydroxysteroid Dehydrogenase/Carbonyl Reductase from Comamonas testosteroni / Frank Hoffmann". Hamburg : Diplom.de, 2009. http://d-nb.info/1117660591/34.
Texto completoTakase, Ryuichi. "Studies on Structure-Function Relationship and Conversion of Coenzyme Requirement in Bacterial α-Keto Acid Reductases Responsible for Metabolism of Acidic Polysaccharides". Kyoto University, 2015. http://hdl.handle.net/2433/200458.
Texto completo0048
新制・課程博士
博士(農学)
甲第19195号
農博第2134号
新制||農||1034(附属図書館)
学位論文||H27||N4941(農学部図書室)
32187
京都大学大学院農学研究科食品生物科学専攻
(主査)教授 谷 史人, 教授 保川 清, 准教授 橋本 渉
学位規則第4条第1項該当
Jacob, Asha Ivy. "STUDY OF SHORT CHAIN DEHYDROGENASE / REDUCTASES (SDRs) IN SINORHIZOBIUM MELILOTI". Thesis, 2007. http://hdl.handle.net/10012/3346.
Texto completoCho, Yen-Ching y 卓燕菁. "Stereoselective production of phenylephrine by short-chain dehydrogenase/reductase from Serratia quinivorans BCRC 14811". Thesis, 2010. http://ndltd.ncl.edu.tw/handle/70482776642221323026.
Texto completo國立中興大學
生命科學院碩士在職專班
98
In order to avoid involved in the chemical synthesis method, the present study was designed to use a biotransformation approach to produce L-PE from 1-(3-hydroxyphenyl)-2-(methylamino) ethanone (HPMAE). We found that S. quinivorans BCRC 14811 could convert HPMAE to L-PE with 15% of yield. Addition of 2-phenylethanol and acetophenone in the culture medium could increase conversion yield from 15% to 88% and 83%, respectively. A genomic library of S. quinivorans BCRC 14811 was constructed for the screening of clones capable of converting HPMAE to PE using pQE30 as cloning vector and HPMAE-sensitive Escherichia coli NovaBlue as host cell. Luria-Bertani plate containing 1 to 10 mM HPMAE were used as the selection medium. However no positive clone was obtained. Short-chain dehydrogenase / reductase (SDR) was cloned from S. quinivorans BCRC 14811 by PCR. When the sdr gene was expressed in E. coli BL21(DE3), the recombinant E. coli cell can convert 10 mM HPMAE to 8.9 mM D-PE with a yield of about 89% and 60 mM HPMAE to 56.2 mM D-PE with a conversion yield of 94%. The SDR was purified by immobilized metal affinity chromatography. Enzyme activity assay demonstrated that the SDR protein could uses NADPH and NADH as cofactors, which exhibit a specific activities of 257 U/mg and 285 U/mg, respectively.
Capítulos de libros sobre el tema "Short-chain dehydrogenase/reductase (SDR)"
Furnham, Nicholas, Gemma L. Holliday y Janet M. Thornton. "The NAD Binding Domain and the Short-Chain Dehydrogenase/Reductase (SDR) Superfamily". En Protein Families, 191–206. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118743089.ch8.
Texto completoWhiteley, John M., Nguyen H. Xuong y Kottayil I. Varughese. "Is Dihydropteridine Reductase an Anomalous Dihydrofolate Reductase, a Flavin-Like Enzyme, or a Short-Chain Dehydrogenase?" En Advances in Experimental Medicine and Biology, 115–21. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2960-6_23.
Texto completoInformes sobre el tema "Short-chain dehydrogenase/reductase (SDR)"
Or, Etti, David Galbraith y 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, diciembre de 2002. http://dx.doi.org/10.32747/2002.7587232.bard.
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