Artículos de revistas sobre el tema "Short-chain dehydrogenase/reductase (SDR)"
Crea una cita precisa en los estilos APA, MLA, Chicago, Harvard y otros
Consulte los 50 mejores artículos de revistas para su investigación sobre el tema "Short-chain dehydrogenase/reductase (SDR)".
Junto a cada fuente en la lista de referencias hay un botón "Agregar a la bibliografía". Pulsa este botón, y generaremos automáticamente la referencia bibliográfica para la obra elegida en el estilo de cita que necesites: APA, MLA, Harvard, Vancouver, Chicago, etc.
También puede descargar el texto completo de la publicación académica en formato pdf y leer en línea su resumen siempre que esté disponible en los metadatos.
Explore artículos de revistas sobre una amplia variedad de disciplinas y organice su bibliografía correctamente.
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 completoBhinija, Kisana, Pattana Srifah Huehne, Skorn Mongkolsuk, Somkid Sitthimonchai y 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 (enero de 2022): 295–304. http://dx.doi.org/10.1016/j.sajb.2021.08.034.
Texto completoYu, Shuhan, Qiguo Sun, Jiaxuan Wu, Pengcheng Zhao, Yanmei Sun y Zhenfei Guo. "Genome-Wide Identification and Characterization of Short-Chain Dehydrogenase/Reductase (SDR) Gene Family in Medicago truncatula". International Journal of Molecular Sciences 22, n.º 17 (31 de agosto de 2021): 9498. http://dx.doi.org/10.3390/ijms22179498.
Texto completoShah, Bhumika S., Sasha G. Tetu, Stephen J. Harrop, Ian T. Paulsen y 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, n.º 10 (25 de septiembre de 2014): 1318–23. http://dx.doi.org/10.1107/s2053230x14019785.
Texto completoTANAKA, Nobutada. "Structure and Function of the enzymes belonging to the SDR(Short-chain Dehydrogenase/Reductase) Family." Nihon Kessho Gakkaishi 38, n.º 3 (1996): 235–43. http://dx.doi.org/10.5940/jcrsj.38.235.
Texto completoNguyen, Giang Thu, Shinae Kim, Hyeonseok Jin, Dong-Hyung Cho, Hang-Suk Chun, Woo-Keun Kim y Jeong Ho Chang. "Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from Candida Albicans". Crystals 9, n.º 9 (10 de septiembre de 2019): 471. http://dx.doi.org/10.3390/cryst9090471.
Texto completoFerrandi, Erica Elisa, Ivan Bassanini, Susanna Bertuletti, Sergio Riva, Chiara Tognoli, Marta Vanoni y 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, n.º 20 (12 de octubre de 2022): 12153. http://dx.doi.org/10.3390/ijms232012153.
Texto completoKowalik, Dorota, Ferdinand Haller, Jerzy Adamski y 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, n.º 4-5 (noviembre de 2009): 117–24. http://dx.doi.org/10.1016/j.jsbmb.2009.08.001.
Texto completoChen, Weiguo, Min-Sun Song y Joseph L. Napoli. "SDR-O : an orphan short-chain dehydrogenase/reductase localized at mouse chromosome 10/human chromosome 12". Gene 294, n.º 1-2 (julio de 2002): 141–46. http://dx.doi.org/10.1016/s0378-1119(02)00757-6.
Texto completoSałuda-Gorgul, Anna, Karolina Seta, Magdalena Nowakowska y Andrzej K. Bednarek. "WWOX Oxidoreductase – Substrate and Enzymatic Characterization". Zeitschrift für Naturforschung C 66, n.º 1-2 (1 de febrero de 2011): 73–82. http://dx.doi.org/10.1515/znc-2011-1-210.
Texto completoSameeullah, Muhammad, Muhammet Yildirim, Noreen Aslam, Mehmet Cengiz Baloğlu, Buhara Yucesan, Andreas G. Lössl, Kiran Saba, Mohammad Tahir Waheed y 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, n.º 21 (29 de octubre de 2021): 11736. http://dx.doi.org/10.3390/ijms222111736.
Texto completoGao, Miaomiao, Kaili Nie, Meng Qin, Haijun Xu, Fang Wang y Luo Liu. "Molecular Mechanism Study on Stereo-Selectivity of α or β Hydroxysteroid Dehydrogenases". Crystals 11, n.º 3 (25 de febrero de 2021): 224. http://dx.doi.org/10.3390/cryst11030224.
Texto completoCheng, Zhong, Yao Li, Chun Sui, Xiaobo Sun y 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, n.º 7 (27 de junio de 2015): 901–5. http://dx.doi.org/10.1107/s2053230x15008559.
Texto completoBüsing, Imke, H. Wolfgang Höffken, Michael Breuer, Lars Wöhlbrand, Bernhard Hauer y 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, n.º 5 (2015): 327–39. http://dx.doi.org/10.1159/000439113.
Texto completoSirko, A., A. Wegleńska, M. Hryniewicz y 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, n.º 1 (31 de marzo de 1997): 153–57. http://dx.doi.org/10.18388/abp.1997_4453.
Texto completoPennacchio, Angela, Biagio Pucci, Francesco Secundo, Francesco La Cara, Mosè Rossi y 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, n.º 13 (2 de mayo de 2008): 3949–58. http://dx.doi.org/10.1128/aem.00217-08.
Texto completoRodarte, Justas V., Jan Abendroth, Thomas E. Edwards, Donald D. Lorimer, Bart L. Staker, Sunny Zhang, Peter J. Myler y Krystle J. McLaughlin. "Crystal structure of acetoacetyl-CoA reductase from Rickettsia felis". Acta Crystallographica Section F Structural Biology Communications 77, n.º 2 (1 de febrero de 2021): 54–60. http://dx.doi.org/10.1107/s2053230x21001497.
Texto completoBuysschaert, Geraldine, Kenneth Verstraete, Savvas N. Savvides y 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, n.º 7 (27 de junio de 2012): 771–74. http://dx.doi.org/10.1107/s1744309112018672.
Texto completoKallberg, Yvonne, Udo Oppermann, Hans Jörnvall y Bengt Persson. "Short-chain dehydrogenase/reductase (SDR) relationships: A large family with eight clusters common to human, animal, and plant genomes". Protein Science 11, n.º 3 (13 de abril de 2009): 636–41. http://dx.doi.org/10.1110/ps.26902.
Texto completoZhou, Yan, Yifeng Wei, Lianyun Lin, Tong Xu, Ee Lui Ang, Huimin Zhao, Zhiguang Yuchi y Yan Zhang. "Biochemical and structural investigation of sulfoacetaldehyde reductase from Klebsiella oxytoca". Biochemical Journal 476, n.º 4 (28 de febrero de 2019): 733–46. http://dx.doi.org/10.1042/bcj20190005.
Texto completoFRANSEN, Marc, Paul P. VAN VELDHOVEN y 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, n.º 2 (25 de mayo de 1999): 561–68. http://dx.doi.org/10.1042/bj3400561.
Texto completoJanssen, D. B., M. Majerić-Elenkov, G. Hasnaoui, B. Hauer y J. H. Lutje Spelberg. "Enantioselective formation and ring-opening of epoxides catalysed by halohydrin dehalogenases". Biochemical Society Transactions 34, n.º 2 (20 de marzo de 2006): 291–95. http://dx.doi.org/10.1042/bst0340291.
Texto completoCassetta, Alberto, Ivet Krastanova, Katja Kristan, Mojca Brunskole Švegelj, Doriano Lamba, Tea Lanišnik Rižner y 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, n.º 1 (14 de diciembre de 2011): 151–60. http://dx.doi.org/10.1042/bj20110567.
Texto completoZhang, Hui, Bei Wang, Shengli Yang, Hongwei Yu y Lidan Ye. "Enhancing Acetophenone Tolerance of Anti-Prelog Short-Chain Dehydrogenase/Reductase EbSDR8 Using a Whole-Cell Catalyst by Directed Evolution". Catalysts 12, n.º 9 (19 de septiembre de 2022): 1071. http://dx.doi.org/10.3390/catal12091071.
Texto completoIsotani, Kentaro, Junji Kurokawa, Fumiko Suzuki, Syunsuke Nomoto, Takashi Negishi, Michiko Matsuda y Nobuya Itoh. "Gene Cloning and Characterization of Two NADH-Dependent 3-Quinuclidinone Reductases from Microbacterium luteolum JCM 9174". Applied and Environmental Microbiology 79, n.º 4 (21 de diciembre de 2012): 1378–84. http://dx.doi.org/10.1128/aem.03099-12.
Texto completoLukacik, Petra, Brigitte Keller, Gabor Bunkoczi, Kathryn Kavanagh, Wen Hwa Lee, Jerzy Adamski y Udo Oppermann. "Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity". Biochemical Journal 402, n.º 3 (26 de febrero de 2007): 419–27. http://dx.doi.org/10.1042/bj20061319.
Texto completoShafqat, Naeem, Joao R. C. Muniz, Ewa S. Pilka, Evangelos Papagrigoriou, Frank von Delft, Udo Oppermann y Wyatt W. Yue. "Insight into S-adenosylmethionine biosynthesis from the crystal structures of the human methionine adenosyltransferase catalytic and regulatory subunits". Biochemical Journal 452, n.º 1 (25 de abril de 2013): 27–36. http://dx.doi.org/10.1042/bj20121580.
Texto completoPampa, Kudigana J., Neratur K. Lokanath, Naoki Kunishima y 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, n.º 4 (19 de marzo de 2014): 994–1004. http://dx.doi.org/10.1107/s1399004713034925.
Texto completoSzeliga, Magdalena, Joanna Ciura y Mirosław Tyrka. "Representational Difference Analysis of Transcripts Involved in Jervine Biosynthesis". Life 10, n.º 6 (19 de junio de 2020): 88. http://dx.doi.org/10.3390/life10060088.
Texto completoAbd Hamid, Nur Athirah, Zamri Zainal y 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, n.º 3 (21 de noviembre de 2017): 260–71. http://dx.doi.org/10.1007/s13562-017-0436-4.
Texto completoPeng, Junbo, Janith V. S. Aluthmuhandiram, K. W. Thilini Chethana, Qi Zhang, Qikai Xing, Hui Wang, Mei Liu, Wei Zhang, Xinghong Li y Jiye Yan. "An NmrA-Like Protein, Lws1, Is Important for Pathogenesis in the Woody Plant Pathogen Lasiodiplodia theobromae". Plants 11, n.º 17 (24 de agosto de 2022): 2197. http://dx.doi.org/10.3390/plants11172197.
Texto completoOrduña, Patricia, Antonia I. Castillo-Rodal, Martha E. Mercado, Samuel Ponce de León y 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.
Texto completoLee, Jung-Kul, Bong-Seong Koo, Sang-Yong Kim y Hyung-Hwan Hyun. "Purification and Characterization of a Novel Mannitol Dehydrogenase from a Newly Isolated Strain of Candida magnoliae". Applied and Environmental Microbiology 69, n.º 8 (agosto de 2003): 4438–47. http://dx.doi.org/10.1128/aem.69.8.4438-4447.2003.
Texto completoGuidugli, Karina R., Christine Hepperle y 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, n.º 1 (enero de 2004): 37–47. http://dx.doi.org/10.1051/apido:2003068.
Texto completoVögeli, Bastian, Raoul G. Rosenthal, Gabriele M. M. Stoffel, Tristan Wagner, Patrick Kiefer, Niña Socorro Cortina, Seigo Shima y Tobias J. Erb. "InhA, the enoyl-thioester reductase from Mycobacterium tuberculosis forms a covalent adduct during catalysis". Journal of Biological Chemistry 293, n.º 44 (14 de septiembre de 2018): 17200–17207. http://dx.doi.org/10.1074/jbc.ra118.005405.
Texto completoBEROIS, M., J. ROMERO-SEVERSON y 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, n.º 1 (25 de mayo de 2011): 112–15. http://dx.doi.org/10.1111/j.1365-2915.2011.00965.x.
Texto completoTheriault, Jean-Francois, Dao-Wei Zhu y Sheng-Xiang Lin. "The trans-membrane 17βHSD7: Kinetic study and preliminary crystallization data". Acta Crystallographica Section A Foundations and Advances 70, a1 (5 de agosto de 2014): C1503. http://dx.doi.org/10.1107/s2053273314084964.
Texto completoManning, Jonathan R., Matthew A. Bailey, Dinesh C. Soares, Donald R. Dunbar y John J. Mullins. "In silico structure-function analysis of pathological variation in the HSD11B2 gene sequence". Physiological Genomics 42, n.º 3 (agosto de 2010): 319–30. http://dx.doi.org/10.1152/physiolgenomics.00053.2010.
Texto completoDeisenroth, Chad, Aaron R. Thorner, Takeharu Enomoto, Charles M. Perou y Yanping Zhang. "Mitochondrial HEP27 Is a c-Myb Target Gene That Inhibits Mdm2 and Stabilizes p53". Molecular and Cellular Biology 30, n.º 16 (14 de junio de 2010): 3981–93. http://dx.doi.org/10.1128/mcb.01284-09.
Texto completoJörnvall, Hans, Bengt Persson, Maria Krook, Silvia Atrian, Roser Gonzalez-Duarte, Jonathan Jeffery y Debashis Ghosh. "Short-chain dehydrogenases/reductases (SDR)". Biochemistry 34, n.º 18 (mayo de 1995): 6003–13. http://dx.doi.org/10.1021/bi00018a001.
Texto completoMarmont, 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, n.º 34 (29 de junio de 2020): 11949–62. http://dx.doi.org/10.1074/jbc.ra120.014555.
Texto completo