Статті в журналах з теми "Short-chain dehydrogenase/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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 джерелаBuysschaert, Geraldine, Kenneth Verstraete, Savvas N. Savvides, and Bjorn Vergauwen. "Crystallization of an atypical short-chain dehydrogenase fromVibrio vulnificuslacking the conserved catalytic tetrad." Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, no. 7 (June 27, 2012): 771–74. http://dx.doi.org/10.1107/s1744309112018672.
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 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 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 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 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 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.
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 джерелаLukacik, Petra, Brigitte Keller, Gabor Bunkoczi, Kathryn Kavanagh, Wen Hwa Lee, Jerzy Adamski, and Udo Oppermann. "Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity." Biochemical Journal 402, no. 3 (February 26, 2007): 419–27. http://dx.doi.org/10.1042/bj20061319.
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 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 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 джерелаAbd Hamid, Nur Athirah, Zamri Zainal, and Ismanizan Ismail. "Two members of unassigned type of short-chain dehydrogenase/reductase superfamily (SDR) isolated from Persicaria minor show response towards ABA and drought stress." Journal of Plant Biochemistry and Biotechnology 27, no. 3 (November 21, 2017): 260–71. http://dx.doi.org/10.1007/s13562-017-0436-4.
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 джерелаGuidugli, Karina R., Christine Hepperle, and Klaus Hartfelder. "A member of the short-chain dehydrogenase/reductase (SDR) superfamily is a target of the ecdysone response in honey bee (Apis mellifera) caste development." Apidologie 35, no. 1 (January 2004): 37–47. http://dx.doi.org/10.1051/apido:2003068.
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 джерелаBEROIS, M., J. ROMERO-SEVERSON, and D. W. SEVERSON. "RNAi knock-downs support roles for the mucin-like (AeIMUC1) gene and short-chain dehydrogenase/reductase (SDR) gene in Aedes aegypti susceptibility to Plasmodium gallinaceum." Medical and Veterinary Entomology 26, no. 1 (May 25, 2011): 112–15. http://dx.doi.org/10.1111/j.1365-2915.2011.00965.x.
Повний текст джерелаTheriault, Jean-Francois, Dao-Wei Zhu та Sheng-Xiang Lin. "The trans-membrane 17βHSD7: Kinetic study and preliminary crystallization data". Acta Crystallographica Section A Foundations and Advances 70, a1 (5 серпня 2014): C1503. http://dx.doi.org/10.1107/s2053273314084964.
Повний текст джерелаManning, Jonathan R., Matthew A. Bailey, Dinesh C. Soares, Donald R. Dunbar, and John J. Mullins. "In silico structure-function analysis of pathological variation in the HSD11B2 gene sequence." Physiological Genomics 42, no. 3 (August 2010): 319–30. http://dx.doi.org/10.1152/physiolgenomics.00053.2010.
Повний текст джерелаDeisenroth, Chad, Aaron R. Thorner, Takeharu Enomoto, Charles M. Perou, and Yanping Zhang. "Mitochondrial HEP27 Is a c-Myb Target Gene That Inhibits Mdm2 and Stabilizes p53." Molecular and Cellular Biology 30, no. 16 (June 14, 2010): 3981–93. http://dx.doi.org/10.1128/mcb.01284-09.
Повний текст джерелаJörnvall, Hans, Bengt Persson, Maria Krook, Silvia Atrian, Roser Gonzalez-Duarte, Jonathan Jeffery, and Debashis Ghosh. "Short-chain dehydrogenases/reductases (SDR)." Biochemistry 34, no. 18 (May 1995): 6003–13. http://dx.doi.org/10.1021/bi00018a001.
Повний текст джерелаMarmont, Lindsey S., Gregory B. Whitfield, Roland Pfoh, Rohan J. Williams, Trevor E. Randall, Alexandra Ostaszewski, Erum Razvi, et al. "PelX is a UDP-N-acetylglucosamine C4-epimerase involved in Pel polysaccharide–dependent biofilm formation." Journal of Biological Chemistry 295, no. 34 (June 29, 2020): 11949–62. http://dx.doi.org/10.1074/jbc.ra120.014555.
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