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1.

Влияние температуры на активность и стабильность обелина/В. С. Бондарь [и др.] // Биохимия, 1992. т.Т. 57,N N 7.-С.1039-1048
2.

Violet bioluminescence and fast kinetics from W92F obelin: Structure-based proposals for the bioluminescence triggering and the identification of the emitting species/E. S. Vysotski [et al.] // BIOCHEMISTRY:AMER CHEMICAL SOC, 2003. т.Vol. 42,N Is. 20.-С.6013-6024
3.

Variation of Spectral Characteristics of Coelenteramide-Containing Fluorescent Protein from Obelia Longissima Exposed to Dimethyl Sulfoxide/A. S. Petrova [et al.] // RUSSIAN PHYSICS JOURNAL:SPRINGER, 2016. т.Vol. 59,N Is. 4.-С.562-567
4.

Unusual shift in the visible absorption spectrum of an active ctenophore photoprotein elucidated by time-dependent density functional theory/F. N. Tomilin, A. V. Rogova, L. P. Burakova [et al.] // Photochemical and Photobiological Sciences:Springer Nature, 2021. т.Vol. 20,N Is. 4.-С.559-570
5.

Unusual shift in the visible absorption spectrum of an active ctenophore photoprotein elucidated by time-dependent density functional theory/F. N. Tomilin, A. V. Rogova, L. P. Burakova [et al.] // PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES:SPRINGERNATURE, 2021. т.Vol. 20,N Is. 4.-С.559-570
6.

Unexpected Coelenterazine Degradation Products of Beroe abyssicola Photoprotein Photoinactivation/L. P. Burakova, M. S. Lyakhovich, K. S. Mineev [et al.] // ORGANIC LETTERS:AMER CHEMICAL SOC, 2021. т.Vol. 23,N Is. 17.-С.6846-6849
7.

Unanimous Model for Describing the Fast Bioluminescence Kinetics of Ca2+-regulated Photoproteins of Different Organisms/E. V. Eremeeva [et al.] // PHOTOCHEMISTRY AND PHOTOBIOLOGY:WILEY, 2017. т.Vol. 93,N Is. 2.-С.495-502
8.

Ultraviolet fluorescence of coelenteramide and coelenteramide-containing fluorescent proteins. Experimental and theoretical study/R. R. Alieva [et al.] // Journal of Photochemistry and Photobiology B: Biology, 2016. т.Vol. 162.-С.318-323
9.

The light-sensitive photoprotein berovin from the bioluminescent ctenophore Beroe abyssicola: a novel type of Ca2+-regulated photoprotein/S. V. Markova [et al.] // FEBS JOURNAL:WILEY-BLACKWELL, 2012. т.Vol. 279,N Is. 5.-С.856-870
10.

The intrinsic fluorescence of apo-obelin and apo-aequorin and use of its quenching to characterize coelenterazine binding/E. V. Eremeeva [et al.] // FEBS LETTERS:ELSEVIER SCIENCE BV, 2009. т.Vol. 583,N Is. 12.-С.1939-1944
11.

The interaction of C-terminal Tyr208 and Tyr13 of the first α-helix ensures a closed conformation of ctenophore photoprotein berovin/L. P. Burakova, E. V. Eremeeva, E. S. Vysotski // Photochemical and Photobiological Sciences, 2020. т.Vol. 19,N Is. 3.-С.313-323
12.

The interaction of C-terminal Tyr208 and Tyr13 of the first alpha-helix ensures a closed conformation of ctenophore photoprotein berovin/L. P. Burakova, E. V. Eremeeva, E. S. Vysotski // PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES:ROYAL SOC CHEMISTRY, 2020. т.Vol. 19,N Is. 3.-С.313-323
13.

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
14.

Specific Activities of Hydromedusan Ca2+-Regulated Photoproteins/N. P. Malikova, E. V. Eremeeva, D. V. Gulnov [et al.] // Photochemistry and Photobiology:John Wiley and Sons Inc, 2021
15.

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
16.

Semisynthetic photoprotein reporters for tracking fast Ca2+ transients/N. P. Malikova, A. J. Borgdorff, E. S. Vysotski // Photochemical and Photobiological Sciences, 2015. т.Vol. 14,N Is. 12.-С.2213-2224
17.

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
18.

Role of conservative residue Cys158 in the formation of an active photoprotein complex of obelin/V. S. Bondar [et al.] // BIOCHEMISTRY-MOSCOW:MAIK NAUKA/INTERPERIODICA, 2001. т.Vol. 66,N Is. 9.-С.1014-1018
19.

Role of certain amino acid residues of the coelenterazine-binding cavity in bioluminescence of light-sensitive Ca2+-regulated photoprotein berovin/L. P. Burakova [et al.] // Photochemical and Photobiological Sciences, 2016. т.Vol. 15,N Is. 5.-С.691-704
20.

RedquorinXS Mutants with Enhanced Calcium Sensitivity and Bioluminescence Output Efficiently Report Cellular and Neuronal Network Activities/A. Bakayan, S. Picaud, N. P. Malikova [et al.] // INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES:MDPI, 2020. т.Vol. 21,N Is. 21.- Ст.7846
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