Zeitschriftenartikel zum Thema „Enzyme activation“
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Wollenberger, Ulla, und Frieder W. Scheller. „Enzyme activation for activator and enzyme activity measurement☆“. Biosensors and Bioelectronics 8, Nr. 6 (1993): 291–97. http://dx.doi.org/10.1016/0956-5663(93)85009-d.
Wang, Fang, Yuchen Liu, Chang Du und Renjun Gao. „Current Strategies for Real-Time Enzyme Activation“. Biomolecules 12, Nr. 5 (19.04.2022): 599. http://dx.doi.org/10.3390/biom12050599.
Hamilton-Miller, J. M. T., und Q. Li. „Enzyme-Catalyzed Antimicrobial Activation“. Antimicrobial Agents and Chemotherapy 46, Nr. 11 (01.11.2002): 3692. http://dx.doi.org/10.1128/aac.46.11.3692.2002.
Hadfield, Andrea T. „Electron-Induced Enzyme Activation“. Structure 14, Nr. 1 (Januar 2006): 1–2. http://dx.doi.org/10.1016/j.str.2005.12.002.
Bott, R., G. Ganshaw, M. Soltis, P. Kuhn und M. Knapp. „Snapshots of Enzyme Activation“. Acta Crystallographica Section A Foundations of Crystallography 56, s1 (25.08.2000): s247. http://dx.doi.org/10.1107/s0108767300025319.
Shisler, Krista A., Rachel U. Hutcheson, Masaki Horitani, Kaitlin S. Duschene, Adam V. Crain, Amanda S. Byer, Eric M. Shepard et al. „Monovalent Cation Activation of the Radical SAM Enzyme Pyruvate Formate-Lyase Activating Enzyme“. Journal of the American Chemical Society 139, Nr. 34 (22.08.2017): 11803–13. http://dx.doi.org/10.1021/jacs.7b04883.
Arcus, Vickery L., und Adrian J. Mulholland. „Temperature, Dynamics, and Enzyme-Catalyzed Reaction Rates“. Annual Review of Biophysics 49, Nr. 1 (06.05.2020): 163–80. http://dx.doi.org/10.1146/annurev-biophys-121219-081520.
Lee, Moo-Yeal, und Jonathan S. Dordick. „Enzyme activation for nonaqueous media“. Current Opinion in Biotechnology 13, Nr. 4 (August 2002): 376–84. http://dx.doi.org/10.1016/s0958-1669(02)00337-3.
Takegawa, Mai, Tsubasa Tagawa, Ayumi Ogata, Shigeru Shimamoto und Yuji Hidaka. „Enzyme Activation Mechanism of Cocoonase“. Biophysical Journal 118, Nr. 3 (Februar 2020): 532a. http://dx.doi.org/10.1016/j.bpj.2019.11.2919.
Cassels, R., R. Fears und 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, Nr. 2 (15.10.1987): 395–400. http://dx.doi.org/10.1042/bj2470395.
KHOLODENKO, Boris N., und Guy C. BROWN. „Paradoxical control properties of enzymes within pathways: can activation cause an enzyme to have increased control?“ Biochemical Journal 314, Nr. 3 (15.03.1996): 753–60. http://dx.doi.org/10.1042/bj3140753.
Vater, C. A., H. Nagase und E. D. Harris. „Proactivator-dependent activation of procollagenase induced by treatment with EGTA“. Biochemical Journal 237, Nr. 3 (01.08.1986): 853–58. http://dx.doi.org/10.1042/bj2370853.
Markovic, Milica, Shimon Ben-Shabat und Arik Dahan. „Computational Simulations to Guide Enzyme-Mediated Prodrug Activation“. International Journal of Molecular Sciences 21, Nr. 10 (20.05.2020): 3621. http://dx.doi.org/10.3390/ijms21103621.
BOATRIGHT, Kelly M., Cristina DEIS, Jean-Bernard DENAULT, Daniel P. SUTHERLIN und Guy S. SALVESEN. „Activation of caspases-8 and -10 by FLIPL“. Biochemical Journal 382, Nr. 2 (24.08.2004): 651–57. http://dx.doi.org/10.1042/bj20040809.
Chau, Helen S., und Stephen K. Ng. „Activation of phosphoenolpyruvate carboxykinase isolated from Veillonella parvula“. Biochemistry and Cell Biology 64, Nr. 9 (01.09.1986): 898–905. http://dx.doi.org/10.1139/o86-120.
Hung, Hui-Chih, Meng-Wei Kuo, Gu-Gang Chang und 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, Nr. 1 (08.11.2005): 39–45. http://dx.doi.org/10.1042/bj20050641.
Park, Yong-Doo, Yi Yang, Qing-Xi Chen, Hai-Ning Lin, Qiang Liu und Hai-Meng Zhou. „Kinetics of complexing activation by the magnesium ion on green crab (Scylla serrata) alkaline phosphatase“. Biochemistry and Cell Biology 79, Nr. 6 (01.12.2001): 765–72. http://dx.doi.org/10.1139/o01-152.
Anderson, Louise, und Per Gardeström. „Reductive light activation of enzyme activity“. Physiologia Plantarum 110, Nr. 3 (18.07.2008): 295. http://dx.doi.org/10.1111/j.1399-3054.2000.1100301.x.
Rana, S., N. Pozzi, L. A. Pelc und E. Di Cera. „Redesigning allosteric activation in an enzyme“. Proceedings of the National Academy of Sciences 108, Nr. 13 (22.02.2011): 5221–25. http://dx.doi.org/10.1073/pnas.1018860108.
Rooseboom, Martijn, Jan N. M. Commandeur und Nico P. E. Vermeulen. „Enzyme-Catalyzed Activation of Anticancer Prodrugs“. Pharmacological Reviews 56, Nr. 1 (März 2004): 53–102. http://dx.doi.org/10.1124/pr.56.1.3.
Anderson, Louise, und Per Gardestrom. „Reductive light activation of enzyme activity“. Physiologia Plantarum 110, Nr. 3 (November 2000): 295. http://dx.doi.org/10.1034/j.1399-3054.2000.1100301.x.
Yang, Yan-hui, Herve Aloysius, Daigo Inoyama, Yu Chen und Long-qin Hu. „Enzyme-mediated hydrolytic activation of prodrugs“. Acta Pharmaceutica Sinica B 1, Nr. 3 (Oktober 2011): 143–59. http://dx.doi.org/10.1016/j.apsb.2011.08.001.
Ghosh, S. K., S. Majumder, N. K. Mukhopadhyay und S. K. Bose. „Functional characterization of constituent enzyme fractions of mycobacillin synthetase“. Biochemical Journal 230, Nr. 3 (15.09.1985): 785–89. http://dx.doi.org/10.1042/bj2300785.
GRIGG, Michael E., Kleoniki GOUNARIS und Murray E. SELKIRK. „Characterization of a platelet-activating factor acetylhydrolase secreted by the nematode parasite Nippostrongylus brasiliensis“. Biochemical Journal 317, Nr. 2 (15.07.1996): 541–47. http://dx.doi.org/10.1042/bj3170541.
Zhang, Wei-Wei, Kent Redman, Sharon Churchill und Perry Churchill. „Comparison of D-β-hydroxybutyrate dehydrogenase from rat liver and brain mitochondria“. Biochemistry and Cell Biology 68, Nr. 10 (01.10.1990): 1225–30. http://dx.doi.org/10.1139/o90-182.
Komatsu, Masayuki, Madhu Biyani, Sunita Ghimire Gautam und Koichi Nishigaki. „Peptide-Modulated Activity Enhancement of Acidic Protease Cathepsin E at Neutral pH“. International Journal of Peptides 2012 (17.12.2012): 1–7. http://dx.doi.org/10.1155/2012/316432.
Chosa, Naoyuki, Takashi Fukumitsu, Kengo Fujimoto und Eiji Ohnishi. „Activation of prophenoloxidase A1 by an activating enzyme in Drosophila melanogaster“. Insect Biochemistry and Molecular Biology 27, Nr. 1 (Januar 1997): 61–68. http://dx.doi.org/10.1016/s0965-1748(96)00070-7.
Marshall, Andrew C., und John B. Bruning. „Engineering potassium activation into biosynthetic thiolase“. Biochemical Journal 478, Nr. 15 (13.08.2021): 3047–62. http://dx.doi.org/10.1042/bcj20210455.
Cárdenas, M. L., und A. Cornish-Bowden. „Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector“. Biochemical Journal 257, Nr. 2 (15.01.1989): 339–45. http://dx.doi.org/10.1042/bj2570339.
LEE, Sang Hyoung, J. David JOHNSON, Michael P. WALSH, Jacquelyn E. VAN LIEROP, Cindy SUTHERLAND, Ande XU, Wayne A. SNEDDEN et al. „Differential regulation of Ca2+/calmodulin-dependent enzymes by plant calmodulin isoforms and free Ca2+ concentration“. Biochemical Journal 350, Nr. 1 (09.08.2000): 299–306. http://dx.doi.org/10.1042/bj3500299.
Trusek, Anna. „Graphene oxide flake activation via divinylsulfone – a procedure for efficient β-galactosidase immobilization“. Polish Journal of Chemical Technology 21, Nr. 1 (01.03.2019): 27–32. http://dx.doi.org/10.2478/pjct-2019-0006.
Pederick, Jordan L., Andrew P. Thompson, Stephen G. Bell und 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, Nr. 23 (25.04.2020): 7894–904. http://dx.doi.org/10.1074/jbc.ra120.012936.
EDWARDS, Robert A., Michael P. WALSH, Cindy SUTHERLAND und Hans J. VOGEL. „Activation of calcineurin and smooth muscle myosin light chain kinase by Met-to-Leu mutants of calmodulin“. Biochemical Journal 331, Nr. 1 (01.04.1998): 149–52. http://dx.doi.org/10.1042/bj3310149.
Plafker, Scott M., Kendra S. Plafker, Allan M. Weissman und Ian G. Macara. „Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import“. Journal of Cell Biology 167, Nr. 4 (15.11.2004): 649–59. http://dx.doi.org/10.1083/jcb.200406001.
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Hua, Jia-Dong, Lu Liu und Yi-Ming Qiu. „Activation of Polymer-Metal Complexes on Enzyme“. Journal of Macromolecular Science: Part A - Chemistry 26, Nr. 2-3 (Februar 1989): 495–504. http://dx.doi.org/10.1080/00222338908051989.
Molski, Andrzej. „A Model of Diffusion-Influenced Enzyme Activation“. Journal of Physical Chemistry B 104, Nr. 18 (Mai 2000): 4532–36. http://dx.doi.org/10.1021/jp9935844.
Serdakowski, Anne L., und Jonathan S. Dordick. „Enzyme activation for organic solvents made easy“. Trends in Biotechnology 26, Nr. 1 (Januar 2008): 48–54. http://dx.doi.org/10.1016/j.tibtech.2007.10.007.
Meyerson, Matthew. „Telomerase enzyme activation and human cell immortalization“. Toxicology Letters 102-103 (Dezember 1998): 41–45. http://dx.doi.org/10.1016/s0378-4274(98)00278-1.
Meyerson, M., C. Counter, E. N. Eaton, P. Steiner, R. Beijersbergen, S. D. Caddle, W. Hahn et al. „Telomerase enzyme activation and human cell immortalization“. Toxicology Letters 95 (Juli 1998): 3. http://dx.doi.org/10.1016/s0378-4274(98)80014-3.
Anderson, Vernon E., Mark W. Ruszczycky und Michael E. Harris. „Activation of Oxygen Nucleophiles in Enzyme Catalysis“. Chemical Reviews 106, Nr. 8 (August 2006): 3236–51. http://dx.doi.org/10.1021/cr050281z.
Saboury, A. A. „Enzyme inhibition and activation: A general theory“. Journal of the Iranian Chemical Society 6, Nr. 2 (Juni 2009): 219–29. http://dx.doi.org/10.1007/bf03245829.
Song, Eun-Suk, Maria Aparecida Juliano, Luiz Juliano und Louis B. Hersh. „Substrate Activation of Insulin-degrading Enzyme (Insulysin)“. Journal of Biological Chemistry 278, Nr. 50 (02.10.2003): 49789–94. http://dx.doi.org/10.1074/jbc.m308983200.
Hammerstad, Marta, Ingvild Gudim, Marie Lofstad, Åsmund Kjendseth Røhr und Hans-Petter Hersleth. „Enzyme activation by a flavoprotein redox network“. Acta Crystallographica Section A Foundations and Advances 75, a2 (18.08.2019): e128-e128. http://dx.doi.org/10.1107/s2053273319094282.
Noinaj, Nicholas, Eun Suk Song, Sonia Bhasin, Benjamin J. Alper, Walter K. Schmidt, Louis B. Hersh und David W. Rodgers. „Anion Activation Site of Insulin-degrading Enzyme“. Journal of Biological Chemistry 287, Nr. 1 (02.11.2011): 48–57. http://dx.doi.org/10.1074/jbc.m111.264614.
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de Beer, Roseri J. A. C., Berry Bögels, Gijs Schaftenaar, Barbara Zarzycka, Peter J. L. M. Quaedflieg, Floris L. van Delft, Sander B. Nabuurs und Floris P. J. T. Rutjes. „Enzyme-Specific Activation versus Leaving Group Ability“. ChemBioChem 13, Nr. 12 (23.07.2012): 1785–90. http://dx.doi.org/10.1002/cbic.201200227.
Page, Michael J., und Enrico Di Cera. „Role of Na+and K+in Enzyme Function“. Physiological Reviews 86, Nr. 4 (Oktober 2006): 1049–92. http://dx.doi.org/10.1152/physrev.00008.2006.
Fillat, M. F., D. E. Edmondson und C. Gomez-Moreno. „Light-dependent de-activation/re-activation of Anabaena variabilis ferredoxin: NADP+ reductase“. Biochemical Journal 274, Nr. 3 (15.03.1991): 781–86. http://dx.doi.org/10.1042/bj2740781.
Tiganescu, Ana, Melanie Hupe, Yoshikazu Uchida, Theodora Mauro, Peter M. Elias und Walter M. Holleran. „Increased glucocorticoid activation during mouse skin wound healing“. Journal of Endocrinology 221, Nr. 1 (24.01.2014): 51–61. http://dx.doi.org/10.1530/joe-13-0420.