Literatura académica sobre el tema "Luciferasi"
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Artículos de revistas sobre el tema "Luciferasi"
Heise, Kerstin, Henry Oppermann, Jürgen Meixensberger, Rolf Gebhardt y Frank Gaunitz. "Dual Luciferase Assay for Secreted Luciferases Based onGaussiaand NanoLuc". ASSAY and Drug Development Technologies 11, n.º 4 (mayo de 2013): 244–52. http://dx.doi.org/10.1089/adt.2013.509.
Texto completoDelroisse, Jérôme, Esther Ullrich-Lüter, Stefanie Blaue, Olga Ortega-Martinez, Igor Eeckhaut, Patrick Flammang y Jérôme Mallefet. "A puzzling homology: a brittle star using a putative cnidarian-type luciferase for bioluminescence". Open Biology 7, n.º 4 (abril de 2017): 160300. http://dx.doi.org/10.1098/rsob.160300.
Texto completoHOSSEINKHANI, Saman, Rose SZITTNER y Edward A. MEIGHEN. "Random mutagenesis of bacterial luciferase: critical role of Glu175 in the control of luminescence decay". Biochemical Journal 385, n.º 2 (7 de enero de 2005): 575–80. http://dx.doi.org/10.1042/bj20040863.
Texto completoViviani, Vadim R., Gabriel F. Pelentir y Vanessa R. Bevilaqua. "Bioluminescence Color-Tuning Firefly Luciferases: Engineering and Prospects for Real-Time Intracellular pH Imaging and Heavy Metal Biosensing". Biosensors 12, n.º 6 (10 de junio de 2022): 400. http://dx.doi.org/10.3390/bios12060400.
Texto completoTafreshi, Narges Kh, Majid Sadeghizadeh, Rahman Emamzadeh, Bijan Ranjbar, Hossein Naderi-Manesh y Saman Hosseinkhani. "Site-directed mutagenesis of firefly luciferase: implication of conserved residue(s) in bioluminescence emission spectra among firefly luciferases". Biochemical Journal 412, n.º 1 (25 de abril de 2008): 27–33. http://dx.doi.org/10.1042/bj20070733.
Texto completoKim, Sung Bae, Ryo Nishihara, Daniel Citterio y Koji Suzuki. "Fabrication of a New Lineage of Artificial Luciferases from Natural Luciferase Pools". ACS Combinatorial Science 19, n.º 9 (9 de agosto de 2017): 594–99. http://dx.doi.org/10.1021/acscombsci.7b00081.
Texto completoKotlobay, A. A., Z. M. Kaskova y I. V. Yampolsky. "Palette of Luciferases: Natural Biotools for New Applications in Biomedicine". Acta Naturae 12, n.º 2 (7 de agosto de 2020): 15–27. http://dx.doi.org/10.32607/actanaturae.10967.
Texto completoKotlobay, A. A., Z. M. Kaskova y I. V. Yampolsky. "Palette of Luciferases: Natural Biotools for New Applications in Biomedicine". Acta Naturae 12, n.º 2 (7 de agosto de 2020): 15–27. http://dx.doi.org/10.32607/actanaturae.11152.
Texto completoSALA-NEWBY, Graciela B., Catherine M. THOMSON y Anthony K. CAMPBELL. "Sequence and biochemical similarities between the luciferases of the glow-worm Lampyris noctiluca and the firefly Photinus pyralis". Biochemical Journal 313, n.º 3 (1 de febrero de 1996): 761–67. http://dx.doi.org/10.1042/bj3130761.
Texto completoCarrasco-López, César, Juliana C. Ferreira, Nathan M. Lui, Stefan Schramm, Romain Berraud-Pache, Isabelle Navizet, Santosh Panjikar, Panče Naumov y Wael M. Rabeh. "Beetle luciferases with naturally red- and blue-shifted emission". Life Science Alliance 1, n.º 4 (agosto de 2018): e201800072. http://dx.doi.org/10.26508/lsa.201800072.
Texto completoTesis sobre el tema "Luciferasi"
Conti, Elena Eliana. "Crystal structure of firefly luciferase". Thesis, Imperial College London, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.244284.
Texto completoWalpole, C. S. J. "Active site probes for bacterial luciferase". Thesis, University of Sussex, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.356510.
Texto completoLin, Leo Yen-Cheng. "Flavin binding site in Vibrio harveyi Luciferase". Thesis, McGill University, 2004. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=85083.
Texto completoChan, Wai Shing. "Applications of the bacterial luciferin-luciferase system". HKBU Institutional Repository, 2012. https://repository.hkbu.edu.hk/etd_ra/1454.
Texto completoGupta, Rajat. "Firefly luciferase mutants as sensors of proteome stress". Diss., lmu, 2012. http://nbn-resolving.de/urn:nbn:de:bvb:19-150266.
Texto completoLasko, Daniel R. "On-line fermentation monitoring via recombinant firefly luciferase". Thesis, Massachusetts Institute of Technology, 1995. http://hdl.handle.net/1721.1/11125.
Texto completoAndrews, Thomas. "A novel dual-luciferase monitoring apparatus a thesis /". San Antonio : UTHSC, 2008. http://learningobjects.library.uthscsa.edu/cdm4/item_viewer.php?CISOROOT=/theses&CISOPTR=36&CISOBOX=1&REC=20.
Texto completoOliveira, Anderson Garbuglio de. "Estudo mecanístico da bioluminescência de fungos". Universidade de São Paulo, 2010. http://www.teses.usp.br/teses/disponiveis/46/46135/tde-08112010-093327/.
Texto completoThis thesis describes how in vitro light emission can be enzymatically obtained from the hot and cold extracts assay using different species of fungi, which also indicates a common mechanism of light emission for all these organisms. Kinetic data suggest a consecutive two-step mechanism and corroborate the 1960\'s enzymatic proposal of Airth and Foerster. Finally, using hot and cold extracts assay we were also able to purify and to determine the molecular weight of the fungal luciferin (298.1837 m/z). The isolated substance emits light enzymatically in vitro, whose light emission spectrum matches with the fungal bioluminescence one thus confirming that the substance is the fungal luciferin
Buriánková, Karolína. "Résistance ribosomique aux macrolides et leur effet sur la fidélité de traduction". Paris 11, 2003. http://www.theses.fr/2003PA112220.
Texto completoMacrolide antibiotics constitute a homogenous group of antibacterial agents produced by Streptomyces or related Actinobacteria. They inhibit protein synthesis in bacteria by binding to the 50S ribosomal subunit, preventing its assembly or inhibiting its function. In the first part of this thesis the effect of macrolides on translation accuracy was studied. We have used the reporter system based on Vibrio harveyi luciferase with a stop codon inserted in the proximal part of the luxB gene for the in vivo measurement of the nonsense codon readthrough. Erythromycin stimulated the leadthrough of the UAG stop codon and thus the decrease of the translation accuracy. This is in agreement with the hypothesis that macrolides influence the early stages of elongation process. The misreading effect of macrolides was confirmed by the study of global error frequencies using the 2-D gel electrophoresis of proteins. The second part deals with the intrinsic macrolide resistance of the Mycobacterium tuberculosis complex (MTC), generally attributed to the low permeability of the mycobacterial cell wall. However we have shown that a gene, whose product confers macrolide resistance by ribosome modification, was present in all members of the MTC. It was named ermMT (erm. 37). Part of the ermMT is deleted in some vaccinal strains of Mycobacterium bovis BCG, such as the Pasteur strain. The Pasteur strain was susceptible to macrolides, whereas MTC species were resistant to them. The expression of ermMT in the macrolide-sensitive Mycobacterium strains conferred macrolide resistance. Comparison of the resistance patterns and ribosomal affinity for erythromycin of Mycobacterium host strains expressing ermMT or other erm genes indicates that ermMT confers a type I resistance to macrolides, lincosamides and streptogramins, coiresponding to the mono-methylation of A2058 in 23S rRNA. Our results indicate that ermMT plays a major role in the intrinsic macrolide resistance of members of the MTC
Eriksson, Jonas. "Advancements in Firefly Luciferase-Based Assays and Pyrosequencing Technology". Doctoral thesis, KTH, Biotechnology, 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3708.
Texto completoPyrosequencing is a new DNA sequencing method relying on thesequencing-by-synthesis principle and bioluminometric detectionof nucleotide incorporation events. The objective of thisthesis was improvement of the Pyrosequencing method byincreasing the thermal stability of firefly luciferase, and byintroducing an alternative DNA polymerase and a new nucleotideanalog. Furthermore, the development of a new bioluminescentassay is described for the detection of inorganicpyrophosphatase activity.
The wild-type North American firefly(Photinus pyralis)luciferase is a heat-sensitiveenzyme, the catalytic activity of which is rapidly lost attemperatures over 30°C. Two strategies for increasing thethermostability of the enzyme are presented and discussed. Inthe first strategy, the solution thermodynamics of the systemis affected by osmolytes in such a way that heat-mediatedinactivation of the enzyme is prevented. In the secondstrategy, the enzyme is thermostabilized by mutagenesis. Bothstabilizing strategies can be utilized to allow bioluminometricassays to be performed at higher temperatures. For instance,both DNA polymerase and ATP sulfurylase activity could beanalyzed at 37°C.
The osmolyte strategy was successfully employed forincreasing the reaction temperature for the Pyrosequencingmethod. By increasing the reaction temperature to 37°Cunspecific signals from primer-dimers and 3-end loopswere reduced. Furthermore, sequencing of a challenging templateat 37°C, which previously yielded poor, non-interpretablesequence signals at lower temperatures was now possible.
Introduction of a new adenosine nucleotide analog,7-deaza-2-deoxyadenosine-5-triphosphate (c7dATP) reduced the inhibitory effect on apyraseobserved with the currently used analog,2-deoxyadenosine-5-O-(1-thiotriphosphate)(dATPαS).
Sequencing of homopolymeric T-regions has previously beendifficult with the exonuclease-deficient form of the DNApolymerase I large (Klenow) fragment. By using the DNApolymerase from bacteriophage T7, known as Sequenase, templateswith homopolymeric T-regions were successfully sequenced.Furthermore, it was found that the strand displacement activityfor both polymerases was strongly assisted if the displacedstrand had a 5-overhang. In contrast, the stranddisplacement activity for both polymerases was inhibitedwithout an overhang, resulting in reduced sequencingperformance in double stranded regions.
A firefly bioluminescent assay for the real-time detectionof inorganic pyrophosphatase in the hydrolytic direction wasalso developed. The assay is versatile and has a linearresponse in the range between 8 and 500 mU.
Key words:bioluminescence, osmolytes, glycine betaine,thermostability, firefly luciferase, inorganic pyrophosphatase,inorganic pyrophosphate, Pyrosequencing technology, secondaryDNA-structures, Sequenase, Klenow-polymerase, reaction rates,temperature, c7dATP, dATPαS.
Libros sobre el tema "Luciferasi"
A, DeLuca Marlene y McElroy William David 1917-, eds. Bioluminescence and chemiluminescence. Orlando: Academic Press, 1986.
Buscar texto completoM, Ziegler Miriam y Baldwin Thomas O, eds. Bioluminescence and chemiluminescence. San Diego, Calif: Academic Press, 2000.
Buscar texto completoThompson, James. Lucifer's tears. London: Avon, 2011.
Buscar texto completoRollins, L. A. Lucifer's lexicon. Port Townsend, Wash: Loompanics Unlimited, 1987.
Buscar texto completoCave, Hugh B. Lucifer's eye. New York: Tom Doherty, 1991.
Buscar texto completoLarry, Niven. Lucifer's hammer. New York: Ballantine Pub. Group, 1998.
Buscar texto completoLucifer's tears. Waterville, Me: Thorndike Press, 2011.
Buscar texto completoLucifer's crown. Waterville, Me: Five Star, 2004.
Buscar texto completoLucifer's lady. London: Hale, 1988.
Buscar texto completoLucifer's flood. Lake Mary, Fla: Realms, 2008.
Buscar texto completoCapítulos de libros sobre el tema "Luciferasi"
Deluca, Marlene. "Firefly Luciferase". En Advances in Enzymology - and Related Areas of Molecular Biology, 37–68. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122891.ch2.
Texto completoWettey, Frank R. y Antony P. Jackson. "Luciferase reporter assay". En Subcellular Biochemistry, 423–25. Dordrecht: Springer Netherlands, 2006. http://dx.doi.org/10.1007/978-1-4020-4896-8_39.
Texto completoArndt, T. "Luciferin-Luciferase-System". En Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_1977-1.
Texto completoArndt, T. "Luciferin-Luciferase-System". En Springer Reference Medizin, 1535. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_1977.
Texto completoBauer, Paul. "Luciferase Reporter Gene Assays". En Encyclopedia of Cancer, 1–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_3430-2.
Texto completoBarry, Michael A., Shannon May y Eric A. Weaver. "Imaging Luciferase-Expressing Viruses". En Methods in Molecular Biology, 79–87. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-340-0_6.
Texto completoMcClung, C. Robertson y Qiguang Xie. "Measurement of Luciferase Rhythms". En Methods in Molecular Biology, 1–11. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0700-7_1.
Texto completoBauer, Paul. "Luciferase Reporter Gene Assays". En Encyclopedia of Cancer, 2543–47. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_3430.
Texto completoBauer, Paul. "Luciferase Reporter Gene Assays". En Encyclopedia of Cancer, 2077–81. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_3430.
Texto completoSarrion-Perdigones, Alejandro, Yezabel Gonzalez, Lyra Chang, Tatiana Gallego-Flores, Damian W. Young y Koen J. T. Venken. "Multiplex Hextuple Luciferase Assaying". En Bioluminescence, 433–56. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2453-1_33.
Texto completoActas de conferencias sobre el tema "Luciferasi"
HOSSEINKHANI, SAMAN, NARGES KH TAFRESHI, MAJID SADEGHIZADEH, RAHMAN EMAMZADEH, BIJAN RANJBAR y HOSSEIN NADERI-MANESH. "SITE-DIRECTED MUTAGENESIS OF LAMPYRIS TURKESTANICUS LUCIFERASE: THE EFFECT OF CONSERVED RESIDUE(S) IN BIOLUMINESCENCE EMISSION SPECTRA AMONG FIREFLY LUCIFERASES". En Proceedings of the 15th International Symposium. WORLD SCIENTIFIC, 2008. http://dx.doi.org/10.1142/9789812839589_0004.
Texto completoFan, Z. Hugh, Qian Mei y Steve Soper. "Microfluidic Reactors for Bioluminescence Detection". En ASME 2009 International Mechanical Engineering Congress and Exposition. ASMEDC, 2009. http://dx.doi.org/10.1115/imece2009-12464.
Texto completoMEZHEVIKIN, VV, IE SUKOVATAYA y NA TYULKOVA. "KINETIC INVESTIGATION OF BACTERIAL LUCIFERASE". En Proceedings of the 13th International Symposium. WORLD SCIENTIFIC, 2005. http://dx.doi.org/10.1142/9789812702203_0018.
Texto completoSZITTNER, ROSE, LEO LIN y EDWARD MEIGHEN. "CHIMERIC BACTERIAL LUCIFERASES". En Proceedings of the 11th International Symposium. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812811158_0033.
Texto completoUGAROVA, N. N., E. I. DEMENTIEVA y I. A. LUNDOVSKIKH. "THERMOINACTIVATION AND REACTIVATION OF FIREFLY LUCIFERASE". En Proceedings of the 11th International Symposium. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812811158_0048.
Texto completoLAW, G. H., O. A. GANDELMAN, L. C. TISI, C. R. LOWE y JAH MURRAY. "ALTERING THE SURFACE HYDROPHOBICITY OF FIREFLY LUCIFERASE". En Bioluminescence and Chemiluminescence - Progress and Current Applications - 12th International Symposium on Bioluminescence (BL) and Chemiluminescence (CL). WORLD SCIENTIFIC, 2002. http://dx.doi.org/10.1142/9789812776624_0007.
Texto completoKuhn, Jonathan, Rachel Broza y Ekaterina Verkin. "Making temporal maps using bacterial luciferase: Bacteriophage". En Biomedical Optics 2004, editado por Alexander P. Savitsky, Lubov Y. Brovko, Darryl J. Bornhop, Ramesh Raghavachari y Samuel I. Achilefu. SPIE, 2004. http://dx.doi.org/10.1117/12.530706.
Texto completoHAWKINS, E. M., D. GARVIN, A. PAGUIO, P. STECHA, B. SWANSON, F. FAN y K. V. WOOD. "ADVANCING THE DEVELOPMENT OF DUAL-LUCIFERASE ASSAYS". En Chemistry, Biology and Applications. WORLD SCIENTIFIC, 2007. http://dx.doi.org/10.1142/9789812770196_0024.
Texto completoJATHOUL, A. P., O. A. GANDELMAN, G. H. E. LAW, J. A. H. MURRAY y L. C. TISI. "DESIGNING ENHANCED THERMOSTABLE LUCIFERASE FOR PROTEOLYTIC ASSAY". En Chemistry, Biology and Applications. WORLD SCIENTIFIC, 2007. http://dx.doi.org/10.1142/9789812770196_0026.
Texto completoZHUANG, YAO, AILEEN P. PAGUIO, MONIKA G. GRUBER y KEITH V. WOOD. "SYNTHETIC LUCIFERASE GENES AS BETTER REPORTER MOLECULES". En Proceedings of the 11th International Symposium. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812811158_0114.
Texto completoInformes sobre el tema "Luciferasi"
McElroy, W. D. Firefly Luciferase-Structure and Function. Fort Belvoir, VA: Defense Technical Information Center, julio de 1988. http://dx.doi.org/10.21236/ada198292.
Texto completoWu, Anna M. F-18 Labeled Diabody-Luciferase Fusion Proteins for Optical-ImmunoPET. Office of Scientific and Technical Information (OSTI), enero de 2013. http://dx.doi.org/10.2172/1060194.
Texto completoWood, Keith V. Luciferases of Luminous Beetles: Evolution, Color Variation, and Applications. Fort Belvoir, VA: Defense Technical Information Center, marzo de 1992. http://dx.doi.org/10.21236/ada251122.
Texto completoIglesia-Rodriguez, M. D., Oscar M. Schofield, Scott M. Glenn y Mark Moline. Development of a Suite of Luciferase Gene Probes for the Screening and Detection of Marine Bioluminescent Systems and Organisms. Fort Belvoir, VA: Defense Technical Information Center, enero de 2006. http://dx.doi.org/10.21236/ada523730.
Texto completoIglesia-Rodriguez, M. D., Oscar M. Schofield, Scott M. Glenn y Mark Moline. Development of a Suite of Luciferase Gene Probes for the Screening and Detection of Marine Bioluminescent Systems and Organisms. Fort Belvoir, VA: Defense Technical Information Center, septiembre de 2007. http://dx.doi.org/10.21236/ada550656.
Texto completoLocy, Robert D., Hillel Fromm, Joe H. Cherry y Narendra K. Singh. Regulation of Arabidopsis Glutamate Decarboxylase in Response to Heat Stress: Modulation of Enzyme Activity and Gene Expression. United States Department of Agriculture, enero de 2001. http://dx.doi.org/10.32747/2001.7575288.bard.
Texto completoSessa, Guido y Gregory Martin. MAP kinase cascades activated by SlMAPKKKε and their involvement in tomato resistance to bacterial pathogens. United States Department of Agriculture, enero de 2012. http://dx.doi.org/10.32747/2012.7699834.bard.
Texto completoSchwartz, Bertha, Vaclav Vetvicka, Ofer Danai y Yitzhak Hadar. Increasing the value of mushrooms as functional foods: induction of alpha and beta glucan content via novel cultivation methods. United States Department of Agriculture, enero de 2015. http://dx.doi.org/10.32747/2015.7600033.bard.
Texto completoReplenishing the malaria drug discovery pipeline: Screening and hit evaluation of the MMV Hit Generation Library 1 (HGL1) against asexual blood stage Plasmodium falciparum using a nano luciferase reporter read-out. EMBL-EBI, agosto de 2022. http://dx.doi.org/10.6019/chembl4888484.
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