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Общее количество найденных документов : 19
Показаны документы с 1 по 19
1.

All Ca2+-binding loops of light-sensitive ctenophore photoprotein berovin bind magnesium ions: The spatial structure of Mg2 +-loaded apo-berovin/L. P. Burakova [et al.] // Journal of Photochemistry and Photobiology B: Biology, 2016. т.Vol. 154.-С.57-66
2.

Bioluminescent and biochemical properties of Cys-free Ca2+-regulated photoproteins obelin and aequorin/E. V. Eremeeva, E. S. Vysotski // Journal of Photochemistry and Photobiology B: Biology:Elsevier B.V., 2017. т.Vol. 174.-С.97-105
3.

Bioluminescent and biochemical properties of Cys-free Ca2+-regulated photoproteins obelin and aequorin/E. V. Eremeeva, E. S. Vysotski // JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY:ELSEVIER SCIENCE SA, 2017. т.Vol. 174.-С.97-105
4.

Bioluminescent properties of hydromedusan Ca2+ - regulated photoproteins and their semi-synthetic derivatives/N. .. Malikova, E. .. Vysotski // LUMINESCENCE:WILEY-BLACKWELL, 2014. т.Vol. 29.-С.28-29
5.

Characterization of hydromedusan Ca2+-regulated photoproteins as a tool for measurement of Ca(2+)concentration/N. P. Malikova [et al.] // ANALYTICAL AND BIOANALYTICAL CHEMISTRY:SPRINGER HEIDELBERG, 2014. т.Vol. 406,N Is. 23.-С.5715-5726
6.

Characterization of hydromedusan Ca2+-regulated photoproteins as a tool for measurement of Ca2+concentration/N. P. Malikova [et al.] // , 2014
7.

Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins/P. V. Natashin [et al.] // FEBS Journal, 2014. т.Vol. 281,N Is. 5.-С.1432-1445
8.

Exploring Bioluminescence Function of the Ca2+-regulated Photoproteins with Site-directed Mutagenesis/E. V. Eremeeva, E. S. Vysotski // PHOTOCHEMISTRY AND PHOTOBIOLOGY:WILEY, 2019. т.Vol. 95,N Is. 1.-С.8-23
9.

Hydrogen bond network near OH group of 6-(p-hydroxyphenyl) substituent of coelenterazine determines the bioluminescence spectra differences among hydromedusan calcium-regulated photoproteins/E. Vysotski [et al.] // FEBS OPEN BIO:WILEY, 2018. т.Vol. 8.-С.435-436
10.

Mitrocomin from the jellyfish Mitrocoma cellularia with deleted C-terminal tyrosine reveals a higher bioluminescence activity compared to wild type photoprotein/L. P. Burakova [et al.] // Journal of Photochemistry and Photobiology B: Biology, 2016. т.Vol. 162.-С.286-297
11.

Recombinant Ca2+-regulated photoproteins of ctenophores: current knowledge and application prospects/L. P. Burakova, E. S. Vysotski // Applied Microbiology and Biotechnology:Springer Verlag, 2019. т.Vol. 103,N Is. 15.-С.5929-5946
12.

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
13.

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
14.

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
15.

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
16.

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
17.

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
18.

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
19.

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
 

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