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Общее количество найденных документов : 23
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1.
| Atomic resolution structure of obelin: soaking with calcium enhances electron density of the second oxygen atom substituted at the C2-position of coelenterazine/Z. J. Liu [et al.] // BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS:ACADEMIC PRESS INC ELSEVIER SCIENCE, 2003. т.Vol. 311,N Is. 2.-С.433-439
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| Bacterial Luciferases from Vibrio harveyi and Photobacterium leiognathi Demonstrate Different Conformational Stability as Detected by Time-Resolved Fluorescence Spectroscopy/E. V. Nemtseva, D. V. Gulnov, M. A. Gerasimova [et al.] // INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES:MDPI, 2021. т.Vol. 22,N Is. 19.- Ст.10449
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| Bioluminescent and spectroscopic properties of His-Trp-Tyr triad mutants of obelin and aequorin/E. V. Eremeeva [et al.] // PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES:ROYAL SOC CHEMISTRY, 2013. т.Vol. 12,N Is. 6.-С.1016-1024
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| Bioluminescent properties of obelin and aequorin with novel coelenterazine analogues/R. .. Gealageas [et al.] // ANALYTICAL AND BIOANALYTICAL CHEMISTRY:SPRINGER HEIDELBERG, 2014. т.Vol. 406,N Is. 11.-С.2695-2707
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| Ca2+-regulated photoproteins: structure, bioluminescent reaction mechanism, engineering, and application/E. S. Vysotski [et al.] // LUMINESCENCE:WILEY-BLACKWELL, 2010. т.Vol. 25,N Is. 2.-С.212-212
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| Calcium-regulated photoproteins of marine coelenterates/E. S. Vysotski, S. V. Markova, L. A. Frank // MOLECULAR BIOLOGY:MAIK NAUKA/INTERPERIODICA/SPRINGER, 2006. т.Vol. 40,N Is. 3.-С.355-367
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| Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase/M. S. Titushin [et al.] // PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES:ROYAL SOC CHEMISTRY, 2008. т.Vol. 7,N Is. 2.-С.189-196
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| Expression, purification and characterization of the secreted luciferase of the copepod Metridia longa from Sf9 insect cells/G. A. Stepanyuk [et al.] // PROTEIN EXPRESSION AND PURIFICATION:ACADEMIC PRESS INC ELSEVIER SCIENCE, 2008. т.Vol. 61,N Is. 2.-С.142-148
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| Functional divergence between evolutionary-related LuxG and Fre oxidoreductases of luminous bacteria/A. A. Deeva [et al.] // PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS:WILEY, 2019. т.Vol. 87,N Is. 9.-С.723-729
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| Green-fluorescent protein from the bioluminescent jellyfish Clytia gregaria: cDNA cloning, expression, and characterization of novel recombinant protein/S. V. Markova [et al.] // PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES:ROYAL SOC CHEMISTRY, 2010. т.Vol. 9,N Is. 6.-С.757-765
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| Interchange of aequorin and obelin bioluminescence color is determined by substitution of one active site residue of each photoprotein/G. A. Stepanyuk [et al.] // FEBS LETTERS:ELSEVIER SCIENCE BV, 2005. т.Vol. 579,N Is. 5.-С.1008-1014
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| Interchange of aequorin and obelin bioluminescence color is determined by substitution of one active site residue of each photoprotein/G. A. Stepanyuk [et al.] // FEBS LETTERS:ELSEVIER SCIENCE BV, 2005. т.Vol. 579,N Is. 5.-С.1008-1014
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| Ligand binding and conformational states of the photoprotein obelin/E. V. Eremeeva [et al.] // FEBS LETTERS:ELSEVIER SCIENCE BV, 2012. т.Vol. 586,N Is. 23.-С.4173-4179
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14.
| NMR-derived Topology of a GFP-photoprotein Energy Transfer Complex/M. S. Titushin [et al.] // JOURNAL OF BIOLOGICAL CHEMISTRY:AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2010. т.Vol. 285,N Is. 52.-С.40891-40900
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| Oxygen Activation of Apo-obelin-Coelenterazine Complex/E. V. Eremeeva [et al.] // CHEMBIOCHEM:WILEY-V C H VERLAG GMBH, 2013. т.Vol. 14,N Is. 6.-С.739-745
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| Picosecond Fluorescence Relaxation Spectroscopy of the Calcium-Discharged Photoproteins Aequorin and Obelin/B. .. van Oort [et al.] // BIOCHEMISTRY:AMER CHEMICAL SOC, 2009. т.Vol. 48,N Is. 44.-С.10486-10491
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| Protein-protein complexation in bioluminescence/M. S. Titushin [et al.] // PROTEIN & CELL:HIGHER EDUCATION PRESS, 2011. т.Vol. 2,N Is. 12.-С.957-972
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| Role of key residues of obelin in coelenterazine binding and conversion into 2-hydroperoxy adduct/E. V. Eremeeva [et al.] // JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY:ELSEVIER SCIENCE SA, 2013. т.Vol. 127.-С.133-139
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| Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca2+-loaded apoprotein conformation state/G. A. Stepanyuk [et al.] // BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS:ELSEVIER SCIENCE BV, 2013. т.Vol. 1834,N Is. 10.-С.2139-2146
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20.
| Structures of the Ca2+-regulated photoprotein obelin Y138F mutant before and after bioluminescence support the catalytic function of a water molecule in the reaction/P. V. Natashin [et al.] // ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY:WILEY-BLACKWELL, 2014. т.Vol. 70.-С.720-732
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