Статті в журналах з теми "Luciferasi"
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Heise, Kerstin, Henry Oppermann, Jürgen Meixensberger, Rolf Gebhardt, and Frank Gaunitz. "Dual Luciferase Assay for Secreted Luciferases Based onGaussiaand NanoLuc." ASSAY and Drug Development Technologies 11, no. 4 (May 2013): 244–52. http://dx.doi.org/10.1089/adt.2013.509.
Повний текст джерелаDelroisse, Jérôme, Esther Ullrich-Lüter, Stefanie Blaue, Olga Ortega-Martinez, Igor Eeckhaut, Patrick Flammang, and Jérôme Mallefet. "A puzzling homology: a brittle star using a putative cnidarian-type luciferase for bioluminescence." Open Biology 7, no. 4 (April 2017): 160300. http://dx.doi.org/10.1098/rsob.160300.
Повний текст джерелаHOSSEINKHANI, Saman, Rose SZITTNER, and Edward A. MEIGHEN. "Random mutagenesis of bacterial luciferase: critical role of Glu175 in the control of luminescence decay." Biochemical Journal 385, no. 2 (January 7, 2005): 575–80. http://dx.doi.org/10.1042/bj20040863.
Повний текст джерелаViviani, Vadim R., Gabriel F. Pelentir, and Vanessa R. Bevilaqua. "Bioluminescence Color-Tuning Firefly Luciferases: Engineering and Prospects for Real-Time Intracellular pH Imaging and Heavy Metal Biosensing." Biosensors 12, no. 6 (June 10, 2022): 400. http://dx.doi.org/10.3390/bios12060400.
Повний текст джерелаTafreshi, Narges Kh, Majid Sadeghizadeh, Rahman Emamzadeh, Bijan Ranjbar, Hossein Naderi-Manesh, and Saman Hosseinkhani. "Site-directed mutagenesis of firefly luciferase: implication of conserved residue(s) in bioluminescence emission spectra among firefly luciferases." Biochemical Journal 412, no. 1 (April 25, 2008): 27–33. http://dx.doi.org/10.1042/bj20070733.
Повний текст джерелаKim, Sung Bae, Ryo Nishihara, Daniel Citterio, and Koji Suzuki. "Fabrication of a New Lineage of Artificial Luciferases from Natural Luciferase Pools." ACS Combinatorial Science 19, no. 9 (August 9, 2017): 594–99. http://dx.doi.org/10.1021/acscombsci.7b00081.
Повний текст джерелаKotlobay, A. A., Z. M. Kaskova, and I. V. Yampolsky. "Palette of Luciferases: Natural Biotools for New Applications in Biomedicine." Acta Naturae 12, no. 2 (August 7, 2020): 15–27. http://dx.doi.org/10.32607/actanaturae.10967.
Повний текст джерелаKotlobay, A. A., Z. M. Kaskova, and I. V. Yampolsky. "Palette of Luciferases: Natural Biotools for New Applications in Biomedicine." Acta Naturae 12, no. 2 (August 7, 2020): 15–27. http://dx.doi.org/10.32607/actanaturae.11152.
Повний текст джерелаSALA-NEWBY, Graciela B., Catherine M. THOMSON, and Anthony K. CAMPBELL. "Sequence and biochemical similarities between the luciferases of the glow-worm Lampyris noctiluca and the firefly Photinus pyralis." Biochemical Journal 313, no. 3 (February 1, 1996): 761–67. http://dx.doi.org/10.1042/bj3130761.
Повний текст джерелаCarrasco-López, César, Juliana C. Ferreira, Nathan M. Lui, Stefan Schramm, Romain Berraud-Pache, Isabelle Navizet, Santosh Panjikar, Panče Naumov, and Wael M. Rabeh. "Beetle luciferases with naturally red- and blue-shifted emission." Life Science Alliance 1, no. 4 (August 2018): e201800072. http://dx.doi.org/10.26508/lsa.201800072.
Повний текст джерелаKamiya, Genta, Nobuo Kitada, Tadaomi Furuta, Takashi Hirano, Shojiro Maki, and Sung Bae Kim. "C-Series Coelenterazine-Driven Bioluminescence Signature Imaging." International Journal of Molecular Sciences 23, no. 21 (October 27, 2022): 13047. http://dx.doi.org/10.3390/ijms232113047.
Повний текст джерелаAmaral, Danilo T., Gabriela Oliveira, Jaqueline R. Silva, and Vadim R. Viviani. "A new orange emitting luciferase from the Southern-Amazon Pyrophorus angustus (Coleoptera: Elateridae) click-beetle: structure and bioluminescence color relationship, evolutional and ecological considerations." Photochemical & Photobiological Sciences 15, no. 9 (2016): 1148–54. http://dx.doi.org/10.1039/c6pp00165c.
Повний текст джерелаChini, A., S. Murray, J. Grant, C. Thomson, and G. Loake. "Characterisation of a PR-1: Luciferase transgenic line deployed to uncover novel defence-related Arabidopsis mutants by luciferase imaging." Plant Protection Science 38, SI 2 - 6th Conf EFPP 2002 (December 31, 2017): 615–16. http://dx.doi.org/10.17221/10570-pps.
Повний текст джерелаBraeuning, Albert, та Silvia Vetter. "The nuclear factor κB inhibitor (E)-2-fluoro-4′-methoxystilbene inhibits firefly luciferase". Bioscience Reports 32, № 6 (14 вересня 2012): 531–37. http://dx.doi.org/10.1042/bsr20120043.
Повний текст джерелаKenda, Maša, Jan Vegelj, Barbara Herlah, Andrej Perdih, Přemysl Mladěnka, and Marija Sollner Dolenc. "Evaluation of Firefly and Renilla Luciferase Inhibition in Reporter-Gene Assays: A Case of Isoflavonoids." International Journal of Molecular Sciences 22, no. 13 (June 28, 2021): 6927. http://dx.doi.org/10.3390/ijms22136927.
Повний текст джерелаKargar, Farzane, Mojtaba Mortazavi, Masoud Torkzadeh-Mahani, Safa Lotfi, and Shahryar Shakeri. "Evaluation of Luciferase Thermal Stability by Arginine Saturation in the Flexible Loops." Current Proteomics 17, no. 1 (January 6, 2020): 30–39. http://dx.doi.org/10.2174/1570164616666190320151005.
Повний текст джерелаViviani, Vadim R., Vanessa R. Bevilaqua, Daniel R. de Souza, Gabriel F. Pelentir, Michio Kakiuchi, and Takashi Hirano. "A Very Bright Far-Red Bioluminescence Emitting Combination Based on Engineered Railroad Worm Luciferase and 6′-Amino-Analogs for Bioimaging Purposes." International Journal of Molecular Sciences 22, no. 1 (December 30, 2020): 303. http://dx.doi.org/10.3390/ijms22010303.
Повний текст джерелаNemtseva, Elena V., Dmitry V. Gulnov, Marina A. Gerasimova, Lev A. Sukovatyi, Ludmila P. Burakova, Natalya E. Karuzina, Bogdan S. Melnik, and Valentina A. Kratasyuk. "Bacterial Luciferases from Vibrio harveyi and Photobacterium leiognathi Demonstrate Different Conformational Stability as Detected by Time-Resolved Fluorescence Spectroscopy." International Journal of Molecular Sciences 22, no. 19 (September 28, 2021): 10449. http://dx.doi.org/10.3390/ijms221910449.
Повний текст джерелаAMIDON, Wendy J., Joanne E. PFEIL, and Susannah GAL. "Modification of luciferase to be a substrate for plant aspartic proteinase." Biochemical Journal 343, no. 2 (October 8, 1999): 425–33. http://dx.doi.org/10.1042/bj3430425.
Повний текст джерелаDoi, Motomichi, Megumi Sato, and Yoshihiro Ohmiya. "In Vivo Simultaneous Analysis of Gene Expression by Dual-Color Luciferases in Caenorhabditis elegans." International Journal of Molecular Sciences 22, no. 1 (December 24, 2020): 119. http://dx.doi.org/10.3390/ijms22010119.
Повний текст джерелаNakajima, Yoshihiro, and Yoshihiro Ohmiya. "Bioluminescence assays: multicolor luciferase assay, secreted luciferase assay and imaging luciferase assay." Expert Opinion on Drug Discovery 5, no. 9 (July 21, 2010): 835–49. http://dx.doi.org/10.1517/17460441.2010.506213.
Повний текст джерелаDeeva, Anna A., Albert E. Lisitsa, Lev A. Sukovatyi, Tatiana N. Melnik, Valentina A. Kratasyuk, and Elena V. Nemtseva. "Structure-Function Relationships in Temperature Effects on Bacterial Luciferases: Nothing Is Perfect." International Journal of Molecular Sciences 23, no. 15 (July 23, 2022): 8119. http://dx.doi.org/10.3390/ijms23158119.
Повний текст джерелаMazo-Vargas, Anyimilehidi, Heungwon Park, Mert Aydin, and Nicolas E. Buchler. "Measuring fast gene dynamics in single cells with time-lapse luminescence microscopy." Molecular Biology of the Cell 25, no. 22 (November 5, 2014): 3699–708. http://dx.doi.org/10.1091/mbc.e14-07-1187.
Повний текст джерелаViviani, Vadim R., T. L. Oehlmeyer, F. G. C. Arnoldi, and M. R. Brochetto-Braga. "A New Firefly Luciferase with Bimodal Spectrum: Identification of Structural Determinants of Spectral pH-Sensitivity in Firefly Luciferases¶." Photochemistry and Photobiology 81, no. 4 (2005): 843. http://dx.doi.org/10.1562/2004-12-09-ra-398r.1.
Повний текст джерелаViviani, Vadim R., T. L. Oehlmeyer, F. G. C. Arnoldi, and M. R. Brochetto-Braga. "A New Firefly Luciferase with Bimodal Spectrum: Identification of Structural Determinants of Spectral pH-Sensitivity in Firefly Luciferases¶." Photochemistry and Photobiology 81, no. 4 (April 30, 2007): 843–48. http://dx.doi.org/10.1111/j.1751-1097.2005.tb01452.x.
Повний текст джерелаDaniel, Catherine, Sabine Poiret, Véronique Dennin, Denise Boutillier, and Bruno Pot. "Bioluminescence Imaging Study of Spatial and Temporal Persistence of Lactobacillus plantarum and Lactococcus lactis in Living Mice." Applied and Environmental Microbiology 79, no. 4 (November 30, 2012): 1086–94. http://dx.doi.org/10.1128/aem.03221-12.
Повний текст джерелаKarimi, Elham, Maryam Nikkhah, and Saman Hosseinkhani. "Label-Free and Bioluminescence-Based Nano-Biosensor for ATP Detection." Biosensors 12, no. 11 (October 24, 2022): 918. http://dx.doi.org/10.3390/bios12110918.
Повний текст джерелаDeane, Caitlin. "Luciferase matchmaker." Nature Chemical Biology 13, no. 4 (March 22, 2017): 343. http://dx.doi.org/10.1038/nchembio.2352.
Повний текст джерелаSmale, S. T. "Luciferase Assay." Cold Spring Harbor Protocols 2010, no. 5 (May 1, 2010): pdb.prot5421. http://dx.doi.org/10.1101/pdb.prot5421.
Повний текст джерелаTsuji, Frederick I., E. Melvin Gindler, and David L. Davis. "LUCIFERASE-ANTILUCIFEFUSE*,†." Annals of the New York Academy of Sciences 103, no. 2 (December 15, 2006): 715–23. http://dx.doi.org/10.1111/j.1749-6632.1963.tb53728.x.
Повний текст джерелаBieleski, Lara, and Simon J. Talbot. "Kaposi's Sarcoma-Associated Herpesvirus vCyclin Open Reading Frame Contains an Internal Ribosome Entry Site." Journal of Virology 75, no. 4 (February 15, 2001): 1864–69. http://dx.doi.org/10.1128/jvi.75.4.1864-1869.2001.
Повний текст джерелаSilva Neto, A. J., V. Scorsato, F. G. C. Arnoldi, and V. R. Viviani. "Pyrearinus termitilluminans larval click beetle luciferase: active site properties, structure and function relationships and comparison with other beetle luciferases." Photochemical & Photobiological Sciences 8, no. 12 (2009): 1748. http://dx.doi.org/10.1039/b9pp00053d.
Повний текст джерелаKrasitskaya, Vasilisa V., Eugenia E. Bashmakova, and Ludmila A. Frank. "Coelenterazine-Dependent Luciferases as a Powerful Analytical Tool for Research and Biomedical Applications." International Journal of Molecular Sciences 21, no. 20 (October 10, 2020): 7465. http://dx.doi.org/10.3390/ijms21207465.
Повний текст джерелаLeach, Franklin R. "A View on the Active Site of Firefly Luciferase." Natural Product Communications 3, no. 9 (September 2008): 1934578X0800300. http://dx.doi.org/10.1177/1934578x0800300908.
Повний текст джерелаZambito, Giorgia, Natasa Gaspar, Yanto Ridwan, Mary P. Hall, Ce Shi, Thomas A. Kirkland, Lance P. Encell, Clemens Löwik, and Laura Mezzanotte. "Evaluating Brightness and Spectral Properties of Click Beetle and Firefly Luciferases Using Luciferin Analogues: Identification of Preferred Pairings of Luciferase and Substrate for In Vivo Bioluminescence Imaging." Molecular Imaging and Biology 22, no. 6 (September 14, 2020): 1523–31. http://dx.doi.org/10.1007/s11307-020-01523-7.
Повний текст джерелаManukhov, I. V., and G. B. Zavilgelsky. "Biosensors for the Determination of Promoters and Chaperones Activity in Bacillus subtilis Cells." Biotekhnologiya 36, no. 6 (2020): 68–77. http://dx.doi.org/10.21519/0234-2758-2020-36-6-68-77.
Повний текст джерелаLeitão, João M. M., and Joaquim C. G. Esteves da Silva. "Firefly luciferase inhibition." Journal of Photochemistry and Photobiology B: Biology 101, no. 1 (October 2010): 1–8. http://dx.doi.org/10.1016/j.jphotobiol.2010.06.015.
Повний текст джерелаHardy, Ralph W. F. "Let Out Luciferase." Nature Biotechnology 7, no. 9 (September 1989): 967. http://dx.doi.org/10.1038/nbt0989-967b.
Повний текст джерелаBhaumik, S., X. Z. Lewis, and S. S. Gambhir. "Optical imaging of Renilla luciferase, synthetic Renilla luciferase, and firefly luciferase reporter gene expression in living mice." Journal of Biomedical Optics 9, no. 3 (2004): 578. http://dx.doi.org/10.1117/1.1647546.
Повний текст джерелаOmokoko, Tana A., Uli Luxemburger, Shaheer Bardissi, Petra Simon, Magdalena Utsch, Andrea Breitkreuz, Özlem Türeci, and Ugur Sahin. "Luciferase mRNA Transfection of Antigen Presenting Cells Permits Sensitive Nonradioactive Measurement of Cellular and Humoral Cytotoxicity." Journal of Immunology Research 2016 (2016): 1–13. http://dx.doi.org/10.1155/2016/9540975.
Повний текст джерелаViviani, Vadim R., and Etelvino J. H. Bechara. "BIOLUMINESCENCE OF BRAZILIAN FIREFLIES (COLEOPTERA: LAMPYRIDAE): SPECTRAL DISTRIBUTION and pH EFFECT ON LUCIFERASE-ELICITED COLORS. COMPARISON WITH ELATERID and PHENGODID LUCIFERASES." Photochemistry and Photobiology 62, no. 3 (September 1995): 490–95. http://dx.doi.org/10.1111/j.1751-1097.1995.tb02373.x.
Повний текст джерелаInoue, Yusuke, Fugeng Sheng, Shigeru Kiryu, Makoto Watanabe, Harnprasopwat Ratanakanit, Kiyoko Izawa, Arinobu Tojo, and Kuni Ohtomo. "Gaussia Luciferase for Bioluminescence Tumor Monitoring in Comparison with Firefly Luciferase." Molecular Imaging 10, no. 5 (September 2011): 7290.2010.00057. http://dx.doi.org/10.2310/7290.2010.00057.
Повний текст джерелаFoucault, M. L., L. Thomas, S. Goussard, B. R. Branchini, and C. Grillot-Courvalin. "In Vivo Bioluminescence Imaging for the Study of Intestinal Colonization by Escherichia coli in Mice." Applied and Environmental Microbiology 76, no. 1 (October 30, 2009): 264–74. http://dx.doi.org/10.1128/aem.01686-09.
Повний текст джерелаCarvalho, M. C., A. Tomazini, D. T. Amaral, M. T. Murakami, and V. R. Viviani. "Luciferase isozymes from the Brazilian Aspisoma lineatum (Lampyridae) firefly: origin of efficient pH-sensitive lantern luciferases from fat body pH-insensitive ancestors." Photochemical & Photobiological Sciences 19, no. 12 (2020): 1750–64. http://dx.doi.org/10.1039/d0pp00272k.
Повний текст джерелаChang, Dalu, Suihan Feng, Vladimir Girik, Howard Riezman, and Nicolas Winssinger. "Luciferase Controlled Protein Interactions." Journal of the American Chemical Society 143, no. 10 (March 8, 2021): 3665–70. http://dx.doi.org/10.1021/jacs.0c11016.
Повний текст джерелаBakhtiarova, Adel, Paul Taslimi, Stephen J. Elliman, Penelope A. Kosinski, Brian Hubbard, Michael Kavana, and Daniel M. Kemp. "Resveratrol inhibits firefly luciferase." Biochemical and Biophysical Research Communications 351, no. 2 (December 2006): 481–84. http://dx.doi.org/10.1016/j.bbrc.2006.10.057.
Повний текст джерелаBaldwin, Thomas O., Jon A. Christopher, Frank M. Raushel, James F. Sinclair, Miriam M. Ziegler, Andrew J. Fisher, and Ivan Rayment. "Structure of bacterial luciferase." Current Opinion in Structural Biology 5, no. 6 (December 1995): 798–809. http://dx.doi.org/10.1016/0959-440x(95)80014-x.
Повний текст джерелаChang, Dalu, Eric Lindberg, Suihan Feng, Simona Angerani, Howard Riezman, and Nicolas Winssinger. "Luciferase‐Induced Photouncaging: Bioluminolysis." Angewandte Chemie International Edition 58, no. 45 (September 20, 2019): 16033–37. http://dx.doi.org/10.1002/anie.201907734.
Повний текст джерелаChang, Dalu, Eric Lindberg, Suihan Feng, Simona Angerani, Howard Riezman, and Nicolas Winssinger. "Luciferase‐Induced Photouncaging: Bioluminolysis." Angewandte Chemie 131, no. 45 (September 20, 2019): 16179–83. http://dx.doi.org/10.1002/ange.201907734.
Повний текст джерелаAbramenko, N. A., P. I. Vnukova, E. S. Golovina, I. E. Makarenko, A. A. Mosikian, A. G. Nikiforova, P. A. Gremyakova, and V. I. Kazey. "Development and Validation of Approach for the Detection of Neutralizing Antibodies Against Insulin (Glargine) in Human Blood Plasma." Drug development & registration 8, no. 3 (September 5, 2019): 70–78. http://dx.doi.org/10.33380/2305-2066-2019-8-3-70-78.
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