Artykuły w czasopismach na temat „Enzyme activation”
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Wollenberger, Ulla, and Frieder W. Scheller. "Enzyme activation for activator and enzyme activity measurement☆." Biosensors and Bioelectronics 8, no. 6 (1993): 291–97. http://dx.doi.org/10.1016/0956-5663(93)85009-d.
Pełny tekst źródłaWang, Fang, Yuchen Liu, Chang Du, and Renjun Gao. "Current Strategies for Real-Time Enzyme Activation." Biomolecules 12, no. 5 (2022): 599. http://dx.doi.org/10.3390/biom12050599.
Pełny tekst źródłaHamilton-Miller, J. M. T., and Q. Li. "Enzyme-Catalyzed Antimicrobial Activation." Antimicrobial Agents and Chemotherapy 46, no. 11 (2002): 3692. http://dx.doi.org/10.1128/aac.46.11.3692.2002.
Pełny tekst źródłaHadfield, Andrea T. "Electron-Induced Enzyme Activation." Structure 14, no. 1 (2006): 1–2. http://dx.doi.org/10.1016/j.str.2005.12.002.
Pełny tekst źródłaBott, R., G. Ganshaw, M. Soltis, P. Kuhn, and M. Knapp. "Snapshots of Enzyme Activation." Acta Crystallographica Section A Foundations of Crystallography 56, s1 (2000): s247. http://dx.doi.org/10.1107/s0108767300025319.
Pełny tekst źródłaCassels, R., R. Fears, and R. A. Smith. "The interaction of streptokinase.plasminogen activator complex, tissue-type plasminogen activator, urokinase and their acylated derivatives with fibrin and cyanogen bromide digest of fibrinogen. Relationship to fibrinolytic potency in vitro." Biochemical Journal 247, no. 2 (1987): 395–400. http://dx.doi.org/10.1042/bj2470395.
Pełny tekst źródłaArcus, Vickery L., and Adrian J. Mulholland. "Temperature, Dynamics, and Enzyme-Catalyzed Reaction Rates." Annual Review of Biophysics 49, no. 1 (2020): 163–80. http://dx.doi.org/10.1146/annurev-biophys-121219-081520.
Pełny tekst źródłaKHOLODENKO, Boris N., and Guy C. BROWN. "Paradoxical control properties of enzymes within pathways: can activation cause an enzyme to have increased control?" Biochemical Journal 314, no. 3 (1996): 753–60. http://dx.doi.org/10.1042/bj3140753.
Pełny tekst źródłaVater, C. A., H. Nagase, and E. D. Harris. "Proactivator-dependent activation of procollagenase induced by treatment with EGTA." Biochemical Journal 237, no. 3 (1986): 853–58. http://dx.doi.org/10.1042/bj2370853.
Pełny tekst źródłaShisler, Krista A., Rachel U. Hutcheson, Masaki Horitani, et al. "Monovalent Cation Activation of the Radical SAM Enzyme Pyruvate Formate-Lyase Activating Enzyme." Journal of the American Chemical Society 139, no. 34 (2017): 11803–13. http://dx.doi.org/10.1021/jacs.7b04883.
Pełny tekst źródłaPark, Yong-Doo, Yi Yang, Qing-Xi Chen, Hai-Ning Lin, Qiang Liu, and Hai-Meng Zhou. "Kinetics of complexing activation by the magnesium ion on green crab (Scylla serrata) alkaline phosphatase." Biochemistry and Cell Biology 79, no. 6 (2001): 765–72. http://dx.doi.org/10.1139/o01-152.
Pełny tekst źródłaHung, Hui-Chih, Meng-Wei Kuo, Gu-Gang Chang, and Guang-Yaw Liu. "Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human mitochondrial NAD(P)+-dependent malate dehydrogenase (malic enzyme)." Biochemical Journal 392, no. 1 (2005): 39–45. http://dx.doi.org/10.1042/bj20050641.
Pełny tekst źródłaLee, Moo-Yeal, and Jonathan S. Dordick. "Enzyme activation for nonaqueous media." Current Opinion in Biotechnology 13, no. 4 (2002): 376–84. http://dx.doi.org/10.1016/s0958-1669(02)00337-3.
Pełny tekst źródłaTakegawa, Mai, Tsubasa Tagawa, Ayumi Ogata, Shigeru Shimamoto, and Yuji Hidaka. "Enzyme Activation Mechanism of Cocoonase." Biophysical Journal 118, no. 3 (2020): 532a. http://dx.doi.org/10.1016/j.bpj.2019.11.2919.
Pełny tekst źródłaBOATRIGHT, Kelly M., Cristina DEIS, Jean-Bernard DENAULT, Daniel P. SUTHERLIN, and Guy S. SALVESEN. "Activation of caspases-8 and -10 by FLIPL." Biochemical Journal 382, no. 2 (2004): 651–57. http://dx.doi.org/10.1042/bj20040809.
Pełny tekst źródłaGhosh, S. K., S. Majumder, N. K. Mukhopadhyay, and S. K. Bose. "Functional characterization of constituent enzyme fractions of mycobacillin synthetase." Biochemical Journal 230, no. 3 (1985): 785–89. http://dx.doi.org/10.1042/bj2300785.
Pełny tekst źródłaGRIGG, Michael E., Kleoniki GOUNARIS, and Murray E. SELKIRK. "Characterization of a platelet-activating factor acetylhydrolase secreted by the nematode parasite Nippostrongylus brasiliensis." Biochemical Journal 317, no. 2 (1996): 541–47. http://dx.doi.org/10.1042/bj3170541.
Pełny tekst źródłaDušeková, Eva, Martin Berta, Dagmar Sedláková, et al. "Specific anion effect on properties of HRV 3C protease." Biophysical chemistry 287 (May 11, 2022): 106825. https://doi.org/10.1016/j.bpc.2022.106825.
Pełny tekst źródłaChau, Helen S., and Stephen K. Ng. "Activation of phosphoenolpyruvate carboxykinase isolated from Veillonella parvula." Biochemistry and Cell Biology 64, no. 9 (1986): 898–905. http://dx.doi.org/10.1139/o86-120.
Pełny tekst źródłaKomatsu, Masayuki, Madhu Biyani, Sunita Ghimire Gautam, and Koichi Nishigaki. "Peptide-Modulated Activity Enhancement of Acidic Protease Cathepsin E at Neutral pH." International Journal of Peptides 2012 (December 17, 2012): 1–7. http://dx.doi.org/10.1155/2012/316432.
Pełny tekst źródłaZhang, Wei-Wei, Kent Redman, Sharon Churchill та Perry Churchill. "Comparison of D-β-hydroxybutyrate dehydrogenase from rat liver and brain mitochondria". Biochemistry and Cell Biology 68, № 10 (1990): 1225–30. http://dx.doi.org/10.1139/o90-182.
Pełny tekst źródłaMarkovic, Milica, Shimon Ben-Shabat, and Arik Dahan. "Computational Simulations to Guide Enzyme-Mediated Prodrug Activation." International Journal of Molecular Sciences 21, no. 10 (2020): 3621. http://dx.doi.org/10.3390/ijms21103621.
Pełny tekst źródłaLEE, Sang Hyoung, J. David JOHNSON, Michael P. WALSH, et al. "Differential regulation of Ca2+/calmodulin-dependent enzymes by plant calmodulin isoforms and free Ca2+ concentration." Biochemical Journal 350, no. 1 (2000): 299–306. http://dx.doi.org/10.1042/bj3500299.
Pełny tekst źródłaCárdenas, M. L., and A. Cornish-Bowden. "Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector." Biochemical Journal 257, no. 2 (1989): 339–45. http://dx.doi.org/10.1042/bj2570339.
Pełny tekst źródłaSharrock, Abigail V., Jeff S. Mumm, Elsie M. Williams, et al. "Structural Evaluation of a Nitroreductase Engineered for Improved Activation of the 5-Nitroimidazole PET Probe SN33623." International Journal of Molecular Sciences 25, no. 12 (2024): 6593. http://dx.doi.org/10.3390/ijms25126593.
Pełny tekst źródłaPederick, Jordan L., Andrew P. Thompson, Stephen G. Bell, and John B. Bruning. "d-Alanine–d-alanine ligase as a model for the activation of ATP-grasp enzymes by monovalent cations." Journal of Biological Chemistry 295, no. 23 (2020): 7894–904. http://dx.doi.org/10.1074/jbc.ra120.012936.
Pełny tekst źródłaEDWARDS, Robert A., Michael P. WALSH, Cindy SUTHERLAND, and Hans J. VOGEL. "Activation of calcineurin and smooth muscle myosin light chain kinase by Met-to-Leu mutants of calmodulin." Biochemical Journal 331, no. 1 (1998): 149–52. http://dx.doi.org/10.1042/bj3310149.
Pełny tekst źródłaPlafker, Scott M., Kendra S. Plafker, Allan M. Weissman, and Ian G. Macara. "Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import." Journal of Cell Biology 167, no. 4 (2004): 649–59. http://dx.doi.org/10.1083/jcb.200406001.
Pełny tekst źródłaAnderson, Louise, and Per Gardeström. "Reductive light activation of enzyme activity." Physiologia Plantarum 110, no. 3 (2008): 295. http://dx.doi.org/10.1111/j.1399-3054.2000.1100301.x.
Pełny tekst źródłaRana, S., N. Pozzi, L. A. Pelc, and E. Di Cera. "Redesigning allosteric activation in an enzyme." Proceedings of the National Academy of Sciences 108, no. 13 (2011): 5221–25. http://dx.doi.org/10.1073/pnas.1018860108.
Pełny tekst źródłaRooseboom, Martijn, Jan N. M. Commandeur, and Nico P. E. Vermeulen. "Enzyme-Catalyzed Activation of Anticancer Prodrugs." Pharmacological Reviews 56, no. 1 (2004): 53–102. http://dx.doi.org/10.1124/pr.56.1.3.
Pełny tekst źródłaAnderson, Louise, and Per Gardestrom. "Reductive light activation of enzyme activity." Physiologia Plantarum 110, no. 3 (2000): 295. http://dx.doi.org/10.1034/j.1399-3054.2000.1100301.x.
Pełny tekst źródłaYang, Yan-hui, Herve Aloysius, Daigo Inoyama, Yu Chen, and Long-qin Hu. "Enzyme-mediated hydrolytic activation of prodrugs." Acta Pharmaceutica Sinica B 1, no. 3 (2011): 143–59. http://dx.doi.org/10.1016/j.apsb.2011.08.001.
Pełny tekst źródłaChakrabarty, Arindam, Debajyoti Dutta, Mithu Baidya, Anirudha Dutta, Amit Kumar Das, and Sudip K. Ghosh. "Metronidazole Activation by a Deeply Entangled Dimeric Malic Enzyme in Entamoeba histolytica." Pathogens 14, no. 3 (2025): 277. https://doi.org/10.3390/pathogens14030277.
Pełny tekst źródłaPyatakova, N. V., and I. S. Severina. "Soluble guanylate cyclase in the molecular mechanism underlying the therapeutic action of drugs." Biomeditsinskaya Khimiya 58, no. 1 (2012): 32–42. http://dx.doi.org/10.18097/pbmc20125801032.
Pełny tekst źródłaBerger, Stefanie, Cornelia Welte, and Uwe Deppenmeier. "Acetate Activation inMethanosaeta thermophila: Characterization of the Key Enzymes Pyrophosphatase and Acetyl-CoA Synthetase." Archaea 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/315153.
Pełny tekst źródłaTrusek, Anna. "Graphene oxide flake activation via divinylsulfone – a procedure for efficient β-galactosidase immobilization". Polish Journal of Chemical Technology 21, № 1 (2019): 27–32. http://dx.doi.org/10.2478/pjct-2019-0006.
Pełny tekst źródłaMarshall, Andrew C., and John B. Bruning. "Engineering potassium activation into biosynthetic thiolase." Biochemical Journal 478, no. 15 (2021): 3047–62. http://dx.doi.org/10.1042/bcj20210455.
Pełny tekst źródłaTran, Giang Thi Linh, and Oanh Ngoc Huynh. "Preparation and immobilization Glucoamylase and Pectinase by CLEA method." Science and Technology Development Journal 17, no. 2 (2014): 45–51. http://dx.doi.org/10.32508/stdj.v17i2.1358.
Pełny tekst źródłaDemirkan, Elif, Tuba Avci, and Yakup Aykut. "Protease immobilization on cellulose monoacetate/chitosan-blended nanofibers." Journal of Industrial Textiles 47, no. 8 (2017): 2092–111. http://dx.doi.org/10.1177/1528083717720205.
Pełny tekst źródłaAkram, Muhammad, Urooj Rehman, Misbah Ahmed, and Isaac John Umaru. "Exploring the Dynamics of Enzyme Activity: Environmental and Biological Influences." African Journal of Biochemistry and Molecular Biology Research 2, no. 2 (2025): 125–34. https://doi.org/10.58578/ajbmbr.v2i2.5268.
Pełny tekst źródłaPage, Michael J., and Enrico Di Cera. "Role of Na+and K+in Enzyme Function." Physiological Reviews 86, no. 4 (2006): 1049–92. http://dx.doi.org/10.1152/physrev.00008.2006.
Pełny tekst źródłaEdmund, Aaron B., Timothy F. Walseth, Nicholas M. Levinson, and Lincoln R. Potter. "The pseudokinase domains of guanylyl cyclase–A and –B allosterically increase the affinity of their catalytic domains for substrate." Science Signaling 12, no. 566 (2019): eaau5378. http://dx.doi.org/10.1126/scisignal.aau5378.
Pełny tekst źródłaSaito, T., L. Small, and UW Goodenough. "Activation of adenylyl cyclase in Chlamydomonas reinhardtii by adhesion and by heat." Journal of Cell Biology 122, no. 1 (1993): 137–47. http://dx.doi.org/10.1083/jcb.122.1.137.
Pełny tekst źródłaIwase, Katsumi, Brian C. W. Hummel, and Paul G. Walfish. "Cytosol components from human placenta and rat liver in iodothyronine 5- and 5′-deiodination." Biochemistry and Cell Biology 67, no. 1 (1989): 58–63. http://dx.doi.org/10.1139/o89-009.
Pełny tekst źródłaChosa, Naoyuki, Takashi Fukumitsu, Kengo Fujimoto, and Eiji Ohnishi. "Activation of prophenoloxidase A1 by an activating enzyme in Drosophila melanogaster." Insect Biochemistry and Molecular Biology 27, no. 1 (1997): 61–68. http://dx.doi.org/10.1016/s0965-1748(96)00070-7.
Pełny tekst źródłaKazemi, Masoud, Fahmi Himo, and Johan Åqvist. "Enzyme catalysis by entropy without Circe effect." Proceedings of the National Academy of Sciences 113, no. 9 (2016): 2406–11. http://dx.doi.org/10.1073/pnas.1521020113.
Pełny tekst źródłaTiganescu, Ana, Melanie Hupe, Yoshikazu Uchida, Theodora Mauro, Peter M. Elias, and Walter M. Holleran. "Increased glucocorticoid activation during mouse skin wound healing." Journal of Endocrinology 221, no. 1 (2014): 51–61. http://dx.doi.org/10.1530/joe-13-0420.
Pełny tekst źródłaFillat, M. F., D. E. Edmondson, and C. Gomez-Moreno. "Light-dependent de-activation/re-activation of Anabaena variabilis ferredoxin: NADP+ reductase." Biochemical Journal 274, no. 3 (1991): 781–86. http://dx.doi.org/10.1042/bj2740781.
Pełny tekst źródłaArnold, Laurence H., Simone Kunzelmann, Martin R. Webb, and Ian A. Taylor. "A Continuous Enzyme-Coupled Assay for Triphosphohydrolase Activity of HIV-1 Restriction Factor SAMHD1." Antimicrobial Agents and Chemotherapy 59, no. 1 (2014): 186–92. http://dx.doi.org/10.1128/aac.03903-14.
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