Статті в журналах з теми "Reductase (SDR)"
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Gallego, Oriol, Olga V. Belyaeva, Sergio Porté, F. Xavier Ruiz, Anton V. Stetsenko, Elena V. Shabrova, Natalia V. Kostereva, Jaume Farrés, Xavier Parés, and Natalia Y. Kedishvili. "Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids." Biochemical Journal 399, no. 1 (September 13, 2006): 101–9. http://dx.doi.org/10.1042/bj20051988.
Повний текст джерелаGabrielli, Franco, Marco Antinucci, and Sergio Tofanelli. "Gene Structure Evolution of the Short-Chain Dehydrogenase/Reductase (SDR) Family." Genes 14, no. 1 (December 30, 2022): 110. http://dx.doi.org/10.3390/genes14010110.
Повний текст джерелаLi, Aipeng, Lidan Ye, Xiaohong Yang, Chengcheng Yang, Jiali Gu, and Hongwei Yu. "Structure-guided stereoselectivity inversion of a short-chain dehydrogenase/reductase towards halogenated acetophenones." Chemical Communications 52, no. 37 (2016): 6284–87. http://dx.doi.org/10.1039/c6cc00051g.
Повний текст джерелаJoles, Jaap, Nel Willekes-Koolschijn, Hein Koomans, Arie van Tol, Tini Geelhoed-Mieras, Daan Crommelin, Louis van Bloois, et al. "Subcutaneous administration of HMG-CoA reductase inhibitors in hyperlipidaemic and normal rats." Laboratory Animals 26, no. 4 (October 1, 1992): 269–80. http://dx.doi.org/10.1258/002367792780745689.
Повний текст джерелаDavidson, Jaysón, Kyndall Nicholas, Jeremy Young, Deborah G. Conrady, Stephen Mayclin, Sandhya Subramanian, Bart L. Staker, Peter J. Myler, and Oluwatoyin A. Asojo. "Crystal structure of a putative short-chain dehydrogenase/reductase from Paraburkholderia xenovorans." Acta Crystallographica Section F Structural Biology Communications 78, no. 1 (January 1, 2022): 25–30. http://dx.doi.org/10.1107/s2053230x21012632.
Повний текст джерелаNguyen, Giang Thu, Shinae Kim, Hyeonseok Jin, Dong-Hyung Cho, Hang-Suk Chun, Woo-Keun Kim, and Jeong Ho Chang. "Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from Candida Albicans." Crystals 9, no. 9 (September 10, 2019): 471. http://dx.doi.org/10.3390/cryst9090471.
Повний текст джерелаSameeullah, Muhammad, Muhammet Yildirim, Noreen Aslam, Mehmet Cengiz Baloğlu, Buhara Yucesan, Andreas G. Lössl, Kiran Saba, Mohammad Tahir Waheed та Ekrem Gurel. "Plastidial Expression of 3β-Hydroxysteroid Dehydrogenase and Progesterone 5β-Reductase Genes Confer Enhanced Salt Tolerance in Tobacco". International Journal of Molecular Sciences 22, № 21 (29 жовтня 2021): 11736. http://dx.doi.org/10.3390/ijms222111736.
Повний текст джерелаJacob, Asha I., Sirin A. I. Adham, David S. Capstick, Scott R. D. Clark, Tara Spence, and 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, no. 7 (July 2008): 979–87. http://dx.doi.org/10.1094/mpmi-21-7-0979.
Повний текст джерелаStambergova, Hana, Lucie Skarydova, James E. Dunford, and Vladimir Wsol. "Biochemical properties of human dehydrogenase/reductase (SDR family) member 7." Chemico-Biological Interactions 207 (January 2014): 52–57. http://dx.doi.org/10.1016/j.cbi.2013.11.003.
Повний текст джерелаBryndová, J., P. Klusoňová, M. Kučka, K. Mazancová-Vagnerová, I. Mikšík, and J. Pácha. "Cloning and expression of chicken 20-hydroxysteroid dehydrogenase." Journal of Molecular Endocrinology 37, no. 3 (December 2006): 453–62. http://dx.doi.org/10.1677/jme.1.02025.
Повний текст джерелаFRANSEN, Marc, Paul P. VAN VELDHOVEN, and Suresh SUBRAMANI. "Identification of peroxisomal proteins by using M13 phage protein VI phage display: molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase." Biochemical Journal 340, no. 2 (May 25, 1999): 561–68. http://dx.doi.org/10.1042/bj3400561.
Повний текст джерелаFerrandi, Erica Elisa, Ivan Bassanini, Susanna Bertuletti, Sergio Riva, Chiara Tognoli, Marta Vanoni, and Daniela Monti. "Functional Characterization and Synthetic Application of Is2-SDR, a Novel Thermostable and Promiscuous Ketoreductase from a Hot Spring Metagenome." International Journal of Molecular Sciences 23, no. 20 (October 12, 2022): 12153. http://dx.doi.org/10.3390/ijms232012153.
Повний текст джерелаPersson, 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, no. 1-3 (March 2009): 94–98. http://dx.doi.org/10.1016/j.cbi.2008.10.040.
Повний текст джерелаBray, James E., Brian D. Marsden, and Udo Oppermann. "The human short-chain dehydrogenase/reductase (SDR) superfamily: A bioinformatics summary." Chemico-Biological Interactions 178, no. 1-3 (March 2009): 99–109. http://dx.doi.org/10.1016/j.cbi.2008.10.058.
Повний текст джерелаShah, Bhumika S., Sasha G. Tetu, Stephen J. Harrop, Ian T. Paulsen, and Bridget C. Mabbutt. "Structure of a short-chain dehydrogenase/reductase (SDR) within a genomic island from a clinical strain ofAcinetobacter baumannii." Acta Crystallographica Section F Structural Biology Communications 70, no. 10 (September 25, 2014): 1318–23. http://dx.doi.org/10.1107/s2053230x14019785.
Повний текст джерелаContreras, Ángela, Irene Merino, Enrique Álvarez, David Bolonio, José-Eugenio Ortiz, Luis Oñate-Sánchez, and Luis Gómez. "A poplar short-chain dehydrogenase reductase plays a potential key role in biphenyl detoxification." Proceedings of the National Academy of Sciences 118, no. 35 (August 26, 2021): e2103378118. http://dx.doi.org/10.1073/pnas.2103378118.
Повний текст джерелаBhinija, Kisana, Pattana Srifah Huehne, Skorn Mongkolsuk, Somkid Sitthimonchai, and Jutamaad Satayavivad. "A short-chain dehydrogenase/reductase (SDR) detection for the isoflavone reductase gene in Bulbophyllum and other orchids." South African Journal of Botany 144 (January 2022): 295–304. http://dx.doi.org/10.1016/j.sajb.2021.08.034.
Повний текст джерелаPang, Yu, Wen-Qiang Song, Fang-Yuan Chen, and Yong-Mei Qin. "A new cotton SDR family gene encodes a polypeptide possessing aldehyde reductase and 3-ketoacyl-CoA reductase activities." Biochemistry (Moscow) 75, no. 3 (March 2010): 320–26. http://dx.doi.org/10.1134/s0006297910030089.
Повний текст джерелаRodarte, Justas V., Jan Abendroth, Thomas E. Edwards, Donald D. Lorimer, Bart L. Staker, Sunny Zhang, Peter J. Myler, and Krystle J. McLaughlin. "Crystal structure of acetoacetyl-CoA reductase from Rickettsia felis." Acta Crystallographica Section F Structural Biology Communications 77, no. 2 (February 1, 2021): 54–60. http://dx.doi.org/10.1107/s2053230x21001497.
Повний текст джерелаYu, Shuhan, Qiguo Sun, Jiaxuan Wu, Pengcheng Zhao, Yanmei Sun, and Zhenfei Guo. "Genome-Wide Identification and Characterization of Short-Chain Dehydrogenase/Reductase (SDR) Gene Family in Medicago truncatula." International Journal of Molecular Sciences 22, no. 17 (August 31, 2021): 9498. http://dx.doi.org/10.3390/ijms22179498.
Повний текст джерелаHeibel, Sandra, Celine Chen, Joseph Urban, and Harry Dawson. "Effect of 1,25-dihydroxyvitamin D on all-trans retinoic acid metabolism and interleukin-4 signaling in porcine alternatively activated lung macrophages. (IRM7P.493)." Journal of Immunology 192, no. 1_Supplement (May 1, 2014): 126.18. http://dx.doi.org/10.4049/jimmunol.192.supp.126.18.
Повний текст джерелаSałuda-Gorgul, Anna, Karolina Seta, Magdalena Nowakowska, and Andrzej K. Bednarek. "WWOX Oxidoreductase – Substrate and Enzymatic Characterization." Zeitschrift für Naturforschung C 66, no. 1-2 (February 1, 2011): 73–82. http://dx.doi.org/10.1515/znc-2011-1-210.
Повний текст джерелаBüsing, Imke, H. Wolfgang Höffken, Michael Breuer, Lars Wöhlbrand, Bernhard Hauer, and Ralf Rabus. "Molecular Genetic and Crystal Structural Analysis of 1-(4-Hydroxyphenyl)-Ethanol Dehydrogenase from ‘Aromatoleum aromaticum' EbN1." Journal of Molecular Microbiology and Biotechnology 25, no. 5 (2015): 327–39. http://dx.doi.org/10.1159/000439113.
Повний текст джерелаSzeliga, Magdalena, Joanna Ciura, and Mirosław Tyrka. "Representational Difference Analysis of Transcripts Involved in Jervine Biosynthesis." Life 10, no. 6 (June 19, 2020): 88. http://dx.doi.org/10.3390/life10060088.
Повний текст джерелаKowalik, Dorota, Ferdinand Haller, Jerzy Adamski, and Gabriele Moeller. "In search for function of two human orphan SDR enzymes: Hydroxysteroid dehydrogenase like 2 (HSDL2) and short-chain dehydrogenase/reductase-orphan (SDR-O)." Journal of Steroid Biochemistry and Molecular Biology 117, no. 4-5 (November 2009): 117–24. http://dx.doi.org/10.1016/j.jsbmb.2009.08.001.
Повний текст джерелаShafqat, Naeem, Joao R. C. Muniz, Ewa S. Pilka, Evangelos Papagrigoriou, Frank von Delft, Udo Oppermann, and Wyatt W. Yue. "Insight into S-adenosylmethionine biosynthesis from the crystal structures of the human methionine adenosyltransferase catalytic and regulatory subunits." Biochemical Journal 452, no. 1 (April 25, 2013): 27–36. http://dx.doi.org/10.1042/bj20121580.
Повний текст джерелаTANAKA, Nobutada. "Structure and Function of the enzymes belonging to the SDR(Short-chain Dehydrogenase/Reductase) Family." Nihon Kessho Gakkaishi 38, no. 3 (1996): 235–43. http://dx.doi.org/10.5940/jcrsj.38.235.
Повний текст джерелаFujimoto, Kengo, Masayuki Hara, Hirotaka Yamada, Masato Sakurai, Akemi Inaba, Akito Tomomura, and Setsuko Katoh. "Role of the conserved Ser–Tyr–Lys triad of the SDR family in sepiapterin reductase." Chemico-Biological Interactions 130-132 (January 2001): 825–32. http://dx.doi.org/10.1016/s0009-2797(00)00238-6.
Повний текст джерелаEndo, Satoshi, Namiki Miyagi, Toshiyuki Matsunaga, Akira Hara та Akira Ikari. "Human dehydrogenase/reductase (SDR family) member 11 is a novel type of 17β-hydroxysteroid dehydrogenase". Biochemical and Biophysical Research Communications 472, № 1 (березень 2016): 231–36. http://dx.doi.org/10.1016/j.bbrc.2016.01.190.
Повний текст джерелаAlenazi, Jawaher, Stephen Mayclin, Sandhya Subramanian, Peter J. Myler, and 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, no. 2 (January 27, 2022): 52–58. http://dx.doi.org/10.1107/s2053230x22000218.
Повний текст джерелаChen, Weiguo, Min-Sun Song, and Joseph L. Napoli. "SDR-O : an orphan short-chain dehydrogenase/reductase localized at mouse chromosome 10/human chromosome 12." Gene 294, no. 1-2 (July 2002): 141–46. http://dx.doi.org/10.1016/s0378-1119(02)00757-6.
Повний текст джерелаLundová, Tereza, Hana Štambergová, Lucie Zemanová, Markéta Svobodová, Jana Havránková, Miroslav Šafr, and Vladimír Wsól. "Human dehydrogenase/reductase (SDR family) member 8 (DHRS8): a description and evaluation of its biochemical properties." Molecular and Cellular Biochemistry 411, no. 1-2 (October 16, 2015): 35–42. http://dx.doi.org/10.1007/s11010-015-2566-0.
Повний текст джерелаCheng, Zhong, Yao Li, Chun Sui, Xiaobo Sun, and Yong Xie. "Synthesis, purification and crystallographic studies of the C-terminal sterol carrier protein type 2 (SCP-2) domain of human hydroxysteroid dehydrogenase-like protein 2." Acta Crystallographica Section F Structural Biology Communications 71, no. 7 (June 27, 2015): 901–5. http://dx.doi.org/10.1107/s2053230x15008559.
Повний текст джерелаZhou, Yan, Yifeng Wei, Lianyun Lin, Tong Xu, Ee Lui Ang, Huimin Zhao, Zhiguang Yuchi, and Yan Zhang. "Biochemical and structural investigation of sulfoacetaldehyde reductase from Klebsiella oxytoca." Biochemical Journal 476, no. 4 (February 28, 2019): 733–46. http://dx.doi.org/10.1042/bcj20190005.
Повний текст джерелаEndo, Satoshi, Namiki Miyagi, Toshiyuki Matsunaga, and Akira Ikari. "Rabbit dehydrogenase/reductase SDR family member 11 (DHRS11): Its identity with acetohexamide reductase with broad substrate specificity and inhibitor sensitivity, different from human DHRS11." Chemico-Biological Interactions 305 (May 2019): 12–20. http://dx.doi.org/10.1016/j.cbi.2019.03.026.
Повний текст джерелаCassetta, Alberto, Ivet Krastanova, Katja Kristan, Mojca Brunskole Švegelj, Doriano Lamba, Tea Lanišnik Rižner та Jure Stojan. "Insights into subtle conformational differences in the substrate-binding loop of fungal 17β-hydroxysteroid dehydrogenase: a combined structural and kinetic approach". Biochemical Journal 441, № 1 (14 грудня 2011): 151–60. http://dx.doi.org/10.1042/bj20110567.
Повний текст джерелаJanssen, D. B., M. Majerić-Elenkov, G. Hasnaoui, B. Hauer, and J. H. Lutje Spelberg. "Enantioselective formation and ring-opening of epoxides catalysed by halohydrin dehalogenases." Biochemical Society Transactions 34, no. 2 (March 20, 2006): 291–95. http://dx.doi.org/10.1042/bst0340291.
Повний текст джерелаSirko, A., A. Wegleńska, M. Hryniewicz, and D. M. Hulanicka. "Characterization of the Escherichia coli gene encoding a new member of the short-chain dehydrogenase/reductase (SDR) family." Acta Biochimica Polonica 44, no. 1 (March 31, 1997): 153–57. http://dx.doi.org/10.18388/abp.1997_4453.
Повний текст джерелаPennacchio, Angela, Biagio Pucci, Francesco Secundo, Francesco La Cara, Mosè Rossi, and Carlo A. Raia. "Purification and Characterization of a Novel Recombinant Highly Enantioselective Short-Chain NAD(H)-Dependent Alcohol Dehydrogenase from Thermus thermophilus." Applied and Environmental Microbiology 74, no. 13 (May 2, 2008): 3949–58. http://dx.doi.org/10.1128/aem.00217-08.
Повний текст джерелаKisiela, Michael, Annette Faust, Bettina Ebert, Edmund Maser, and Axel J. Scheidig. "Crystal structure and catalytic characterization of the dehydrogenase/reductase SDR family member 4 ( DHRS 4) from Caenorhabditis elegans." FEBS Journal 285, no. 2 (November 28, 2017): 275–93. http://dx.doi.org/10.1111/febs.14337.
Повний текст джерелаIsotani, Kentaro, Junji Kurokawa, Fumiko Suzuki, Syunsuke Nomoto, Takashi Negishi, Michiko Matsuda, and Nobuya Itoh. "Gene Cloning and Characterization of Two NADH-Dependent 3-Quinuclidinone Reductases from Microbacterium luteolum JCM 9174." Applied and Environmental Microbiology 79, no. 4 (December 21, 2012): 1378–84. http://dx.doi.org/10.1128/aem.03099-12.
Повний текст джерелаGao, Miaomiao, Kaili Nie, Meng Qin, Haijun Xu, Fang Wang та Luo Liu. "Molecular Mechanism Study on Stereo-Selectivity of α or β Hydroxysteroid Dehydrogenases". Crystals 11, № 3 (25 лютого 2021): 224. http://dx.doi.org/10.3390/cryst11030224.
Повний текст джерелаPampa, Kudigana J., Neratur K. Lokanath, Naoki Kunishima, and Ravishankar Vittal Rai. "The first crystal structure of NAD-dependent 3-dehydro-2-deoxy-D-gluconate dehydrogenase fromThermus thermophilusHB8." Acta Crystallographica Section D Biological Crystallography 70, no. 4 (March 19, 2014): 994–1004. http://dx.doi.org/10.1107/s1399004713034925.
Повний текст джерелаVögeli, Bastian, Raoul G. Rosenthal, Gabriele M. M. Stoffel, Tristan Wagner, Patrick Kiefer, Niña Socorro Cortina, Seigo Shima, and Tobias J. Erb. "InhA, the enoyl-thioester reductase from Mycobacterium tuberculosis forms a covalent adduct during catalysis." Journal of Biological Chemistry 293, no. 44 (September 14, 2018): 17200–17207. http://dx.doi.org/10.1074/jbc.ra118.005405.
Повний текст джерелаKallberg, Yvonne, Udo Oppermann, Hans Jörnvall, and Bengt Persson. "Short-chain dehydrogenase/reductase (SDR) relationships: A large family with eight clusters common to human, animal, and plant genomes." Protein Science 11, no. 3 (April 13, 2009): 636–41. http://dx.doi.org/10.1110/ps.26902.
Повний текст джерелаEndo, Satoshi, Yoshifumi Morikawa, Yudai Kudo, Koichi Suenami, Toshiyuki Matsunaga, Akira Ikari, and Akira Hara. "Human dehydrogenase/reductase SDR family member 11 (DHRS11) and aldo-keto reductase 1C isoforms in comparison: Substrate and reaction specificity in the reduction of 11-keto-C19-steroids." Journal of Steroid Biochemistry and Molecular Biology 199 (May 2020): 105586. http://dx.doi.org/10.1016/j.jsbmb.2020.105586.
Повний текст джерелаPeng, Junbo, Janith V. S. Aluthmuhandiram, K. W. Thilini Chethana, Qi Zhang, Qikai Xing, Hui Wang, Mei Liu, Wei Zhang, Xinghong Li, and Jiye Yan. "An NmrA-Like Protein, Lws1, Is Important for Pathogenesis in the Woody Plant Pathogen Lasiodiplodia theobromae." Plants 11, no. 17 (August 24, 2022): 2197. http://dx.doi.org/10.3390/plants11172197.
Повний текст джерелаOrduña, Patricia, Antonia I. Castillo-Rodal, Martha E. Mercado, Samuel Ponce de León, and Yolanda López-Vidal. "Specific Proteins in Nontuberculous Mycobacteria: New Potential Tools." BioMed Research International 2015 (2015): 1–10. http://dx.doi.org/10.1155/2015/964178.
Повний текст джерелаLee, Jung-Kul, Bong-Seong Koo, Sang-Yong Kim, and Hyung-Hwan Hyun. "Purification and Characterization of a Novel Mannitol Dehydrogenase from a Newly Isolated Strain of Candida magnoliae." Applied and Environmental Microbiology 69, no. 8 (August 2003): 4438–47. http://dx.doi.org/10.1128/aem.69.8.4438-4447.2003.
Повний текст джерелаZhang, Hui, Bei Wang, Shengli Yang, Hongwei Yu, and Lidan Ye. "Enhancing Acetophenone Tolerance of Anti-Prelog Short-Chain Dehydrogenase/Reductase EbSDR8 Using a Whole-Cell Catalyst by Directed Evolution." Catalysts 12, no. 9 (September 19, 2022): 1071. http://dx.doi.org/10.3390/catal12091071.
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