Статті в журналах з теми "SDR enzyme"
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Ознайомтеся з топ-50 статей у журналах для дослідження на тему "SDR enzyme".
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Ferrandi, 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 джерелаMineo, Chieko, Yun-Shu Ying, Christine Chapline, Susan Jaken та Richard G. W. Anderson. "Targeting of Protein Kinase Cα to Caveolae". Journal of Cell Biology 141, № 3 (4 травня 1998): 601–10. http://dx.doi.org/10.1083/jcb.141.3.601.
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 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 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 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 джерелаPrasad, Kailash. "Importance of Flaxseed and its Components in the Management of Hypertension." International Journal of Angiology 28, no. 03 (February 22, 2019): 153–60. http://dx.doi.org/10.1055/s-0039-1678691.
Повний текст джерелаDa Costa, Matthieu, Ophelia Gevaert, Stevie Van Overtveldt, Joanna Lange, Henk-Jan Joosten, Tom Desmet, and Koen Beerens. "Structure-function relationships in NDP-sugar active SDR enzymes: Fingerprints for functional annotation and enzyme engineering." Biotechnology Advances 48 (May 2021): 107705. http://dx.doi.org/10.1016/j.biotechadv.2021.107705.
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 джерелаvan Hylckama Vlieg, Johan E. T., Lixia Tang, Jeffrey H. Lutje Spelberg, Tim Smilda, Gerrit J. Poelarends, Tjibbe Bosma, Annet E. J. van Merode, Marco W. Fraaije, and Dick B. Janssen. "Halohydrin Dehalogenases Are Structurally and Mechanistically Related to Short-Chain Dehydrogenases/Reductases." Journal of Bacteriology 183, no. 17 (September 1, 2001): 5058–66. http://dx.doi.org/10.1128/jb.183.17.5058-5066.2001.
Повний текст джерелаYao, Juan, Zhang Zhang, Zhenghua Deng, Youqiang Wang, and Yongcan Guo. "An enzyme free electrochemical biosensor for sensitive detection of miRNA with a high discrimination factor by coupling the strand displacement reaction and catalytic hairpin assembly recycling." Analyst 142, no. 21 (2017): 4116–23. http://dx.doi.org/10.1039/c7an01224a.
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 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 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 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 джерелаKazakova, Oxana B., Natalya I. Medvedeva, Irina E. Smirnova, Tatyana V. Lopatina, and Alexander V. Veselovsky. "The Introduction of Hydrazone, Hydrazide, or Azepane Moieties to the Triterpenoid Core Enhances an Activity Against M. tuberculosis." Medicinal Chemistry 17, no. 2 (December 30, 2020): 134–45. http://dx.doi.org/10.2174/1573406416666200115161700.
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 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 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 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 джерелаOppermann, Udo C. T., Samina Salim, Lars O. Tjernberg, Lars Terenius та Hans Jörnvall. "Binding of amyloid β-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease". FEBS Letters 451, № 3 (28 травня 1999): 238–42. http://dx.doi.org/10.1016/s0014-5793(99)00586-4.
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 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 джерелаYamaguchi, Hideaki, Yoshinori Kanayama, Junichi Soejima, and Shohei Yamaki. "Changes in the Amounts of the NAD-dependent Sorbitol Dehydrogenase and Its Involvement in the Development of Apple Fruit." Journal of the American Society for Horticultural Science 121, no. 5 (September 1996): 848–52. http://dx.doi.org/10.21273/jashs.121.5.848.
Повний текст джерелаBianco, Riccardo Lo, Mark Rieger, and She-Jean S. Sung. "Sorbitol Metabolism in Growing Tissues of Peach." HortScience 32, no. 3 (June 1997): 530C—530. http://dx.doi.org/10.21273/hortsci.32.3.530c.
Повний текст джерелаSatué, Katy, Laura Miguel-Pastor, Deborah Chicharro, and Juan Carlos Gardón. "Hepatic Enzyme Profile in Horses." Animals 12, no. 7 (March 29, 2022): 861. http://dx.doi.org/10.3390/ani12070861.
Повний текст джерелаDreval, A. V., L. A. Marchenkova, O. P. Kuznetsova, G. A. Onoprienko, V. I. Shumsky, I. A. Komissarova, Y. R. Narcissov, et al. "Diagnostic value of redox leukocyte enzymes in postmenopausal osteopenia." Problems of Endocrinology 45, no. 2 (April 3, 1999): 31–35. http://dx.doi.org/10.14341/probl11745.
Повний текст джерелаMarlow, Gary C., and Wayne H. Loescher. "Sorbitol Metabolism, the Climacteric, and Watercore in Apples." Journal of the American Society for Horticultural Science 110, no. 5 (September 1985): 676–80. http://dx.doi.org/10.21273/jashs.110.5.676.
Повний текст джерелаZHU, Xiaohong, Guiliang TANG та Gad GALILI. "The catabolic function of the α-aminoadipic acid pathway in plants is associated with unidirectional activity of lysine–oxoglutarate reductase, but not saccharopine dehydrogenase". Biochemical Journal 351, № 1 (26 вересня 2000): 215–20. http://dx.doi.org/10.1042/bj3510215.
Повний текст джерелаNoone, A., Y. Lao, T. Crawford, D. Kennedy, J. Martin, A. Ferrante, D. Wabnitz, and A. Kontos. "O035 Elevated liver enzymes in paediatric sleep disordered breathing." SLEEP Advances 3, Supplement_1 (October 1, 2022): A14. http://dx.doi.org/10.1093/sleepadvances/zpac029.034.
Повний текст джерелаMuhammad Rafiq Khan, M Khan, and A Shah. "A Study of Heart Enzyme Profile in Myocardial Infarction." Scientific Inquiry and Review 2, no. 2 (April 30, 2018): 01–10. http://dx.doi.org/10.32350/sir/22/020201.
Повний текст джерелаPisoschi, Catalina, Virgil Darie, and Mihai Serban. "STUDY OF RENAL SORBITOLDEHYDROGENASE IN EXPERIMENTAL DIABETIC NEPHROPATHY." SOUTHERN BRAZILIAN JOURNAL OF CHEMISTRY 6, no. 7 (December 20, 1998): 77–82. http://dx.doi.org/10.48141/sbjchem.v6.n7.1998.76_1998_2.pdf.
Повний текст джерелаZhu, Xiaohong, Guiliang Tang, and Gad Galili. "The Activity of theArabidopsisBifunctional Lysine-ketoglutarate Reductase/Saccharopine Dehydrogenase Enzyme of Lysine Catabolism Is Regulated by Functional Interaction between Its Two Enzyme Domains." Journal of Biological Chemistry 277, no. 51 (October 21, 2002): 49655–61. http://dx.doi.org/10.1074/jbc.m205466200.
Повний текст джерелаHederstedt, L., and L. O. Hedén. "New properties of Bacillus subtilis succinate dehydrogenase altered at the active site. The apparent active site thiol of succinate oxidoreductases is dispensable for succinate oxidation." Biochemical Journal 260, no. 2 (June 1, 1989): 491–97. http://dx.doi.org/10.1042/bj2600491.
Повний текст джерелаDAI, Z., Y. YIN, and Z. WANG. "Activities of key enzymes involved in starch synthesis in grains of wheat under different irrigation patterns." Journal of Agricultural Science 147, no. 4 (April 22, 2009): 437–44. http://dx.doi.org/10.1017/s0021859609008612.
Повний текст джерелаKuppusamy, Chinnadurai, Arul Ganesh, Karthikeyeni Sambanthan, Eyini Muthukumarasamy, and Balaji Paulraj*. "Enzyme modulation studies of Fumaronitrile on fresh water fish Oreochromis mossambicus." International Journal of Bioassays 5, no. 11 (October 31, 2016): 5050. http://dx.doi.org/10.21746/ijbio.2016.11.0011.
Повний текст джерелаOppermann, Udo C. T., Charlotta Filling, and Hans Jörnvall. "Forms and functions of human SDR enzymes." Chemico-Biological Interactions 130-132 (January 2001): 699–705. http://dx.doi.org/10.1016/s0009-2797(00)00301-x.
Повний текст джерелаKim, Geun-Joong, Dong-Eun Lee, and Hak-Sung Kim. "Construction and Evaluation of a Novel Bifunctional N-Carbamylase–d-Hydantoinase Fusion Enzyme." Applied and Environmental Microbiology 66, no. 5 (May 1, 2000): 2133–38. http://dx.doi.org/10.1128/aem.66.5.2133-2138.2000.
Повний текст джерелаFrye, Stephen V. "Inhibitors of Sa-Reductase." Current Pharmaceutical Design 2, no. 1 (February 1996): 59–84. http://dx.doi.org/10.2174/1381612802666220920215559.
Повний текст джерелаDunn, S. E., and R. N. Michel. "Coordinated expression of myosin heavy chain isoforms and metabolic enzymes within overloaded rat muscle fibers." American Journal of Physiology-Cell Physiology 273, no. 2 (August 1, 1997): C371—C383. http://dx.doi.org/10.1152/ajpcell.1997.273.2.c371.
Повний текст джерелаBianco, Riccardo Lo, Mark Rieger, and She-Jean S. Sung. "Activities of Sucrose and Sorbitol Metabolizing Enzymes in Vegetative Sinks of Peach and Correlation with Sink Growth Rate." Journal of the American Society for Horticultural Science 124, no. 4 (July 1999): 381–88. http://dx.doi.org/10.21273/jashs.124.4.381.
Повний текст джерелаHOSHI, Ayumu, Motoko TAKAHASHI, Junichi FUJII, Theingi MYINT, Hideaki KANETO, Keiichiro SUZUKI, Yoshimitsu YAMASAKI, Takenobu KAMADA, and Naoyuki TANIGUCHI. "Glycation and inactivation of sorbitol dehydrogenase in normal and diabetic rats." Biochemical Journal 318, no. 1 (August 15, 1996): 119–23. http://dx.doi.org/10.1042/bj3180119.
Повний текст джерелаBianco, Riccardo Lo, Mark Rieger, and Shi-Jean S. Sung. "Carbohydrate Metabolism of Vegetative and Reproductive Sinks in the Late-maturing Cultivar Encore." HortScience 33, no. 3 (June 1998): 541c—541. http://dx.doi.org/10.21273/hortsci.33.3.541c.
Повний текст джерелаZhao, Zhongwei, Richard A. Rothery, and Joel H. Weiner. "Effects of site-directed mutations in Escherichia coli succinate dehydrogenase on the enzyme activity and production of superoxide radicalsThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB — Membrane Proteins in Health and Disease." Biochemistry and Cell Biology 84, no. 6 (December 2006): 1013–21. http://dx.doi.org/10.1139/o06-188.
Повний текст джерелаDavis, David A., Kathleen E. Singer, Maria De La Luz Sierra, Masashi Narazaki, Fuquan Yang, Henry M. Fales, Robert Yarchoan та Giovanna Tosato. "Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1α in the circulation". Blood 105, № 12 (15 червня 2005): 4561–68. http://dx.doi.org/10.1182/blood-2004-12-4618.
Повний текст джерелаHöppner, Astrid, Dietmar Schomburg, and Karsten Niefind. "Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination." Biological Chemistry 394, no. 11 (November 1, 2013): 1505–16. http://dx.doi.org/10.1515/hsz-2013-0170.
Повний текст джерелаVladutiu, Georgirene D., and Reid R. Heffner. "Succinate Dehydrogenase Deficiency." Archives of Pathology & Laboratory Medicine 124, no. 12 (December 1, 2000): 1755–58. http://dx.doi.org/10.5858/2000-124-1755-sdd.
Повний текст джерелаKarboski, James A., Paul J. Godley, Paul A. Frohna, Michael W. Horton, and William J. Reitmeyer. "Marked Digoxin-Likeimmunoreactive Factor Interference with an Enzyme Immunoassay." Drug Intelligence & Clinical Pharmacy 22, no. 9 (September 1988): 703–5. http://dx.doi.org/10.1177/106002808802200913.
Повний текст джерелаDube, Praveen, A. Shwetha, and B. B. Hosetti. "Impact of copper cyanide on the key metabolic enzymes of freshwater fish Catla catla (Hamilton)." Biotehnologija u stocarstvu 30, no. 3 (2014): 499–508. http://dx.doi.org/10.2298/bah1403499d.
Повний текст джерелаLomax, R. B., and W. R. Robertson. "The effects of hypo- and hyperthyroidism on fibre composition and mitochondrial enzyme activities in rat skeletal muscle." Journal of Endocrinology 133, no. 3 (June 1992): 375—NP. http://dx.doi.org/10.1677/joe.0.1330375.
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