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^a314.27.19^2VINITI
В 93

Высоцкий, Е. С.
Зависимая от NADPN и ATP люминесценция экстрактов светящихся бактерий [Текст] : научное издание / Е. С. Высоцкий, В. В. Заворуев, В. В. Межевикин // Биохимия. - 1982. - Т. 47, N 12. - С. 1983-1987 . - ISSN 0320-9725

ГРНТИ

31.27.19

РУБ 314.27.19
Рубрики:
БАКТЕРИИ
   СВЕТЯЩИЕСЯ ЛЮМИНЕСЦЕНЦИЯ
   НАДФН
   ВЛИЯНИЕ
   АТФ
   ВЛИЯНИЕ
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Заворуев, В.В.; Межевикин, В.В.

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CONFORMATIONAL-ANALYSIS OF CYCLIC FORM OF ATP [Текст] / P. I. BELOBROV, T. P. SANDALOVA // Bioorg. Khim. - 1980. - Vol. 6, Is. 11. - С. 1714-1721. - Cited References: 19 . - 8. - ISSN 0132-3423

РУБ Biochemistry & Molecular Biology + Chemistry, Organic

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
BELOBROV, P.I.; SANDALOVA, T.P.

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NADPH-DEPENDENT AND ATP-DEPENDENT LUMINESCENCE OF EXTRACTS OF LUMINESCENT BACTERIA [Text] / E. S. VYSOTSKII, V. V. ZAVORUEV, V. V. MEZHEVIKIN // Biochem.-Moscow. - 1982. - Vol. 47, Is. 12. - P1682-1686. - Cited References: 10 . - 5. - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
VYSOTSKII, E.S.; ZAVORUEV, V.V.; MEZHEVIKIN, V.V.

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NADPH- and ATP-dependent luminescence of extracts from luminous bacteria / E. S. Vysotsky, V. V. Zavoruev, V. V. Mezhevikin // Biokhimiya. - 1982. - Vol. 47, Is. 12. - С. 1983-1987 . - ISSN 0320-9725
Кл.слова (ненормированные):
adenosine triphosphate -- reduced nicotinamide adenine dinucleotide phosphate -- bacterium -- bioluminescence -- nonhuman

Scopus
Держатели документа:
Inst. Biophys., Sib. Branch USSR Acad. Sci., Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotsky, E.S.; Zavoruev, V.V.; Mezhevikin, V.V.

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PROSPECTS FOR APPLICATION OF BIOLUMINESCENCE METHOD IN MEDICINE [Текст] / I. I. GITELZON, T. P. SANDALOVA // VESTNIK AKADEMII MEDITSINSKIKH NAUK SSSR. - 1990. - Is. 9. - С. 31-35. - Cited References: 41 . - ISSN 0002-3027

РУБ Medicine, General & Internal
Рубрики:
AMINO-ACID SEQUENCE
   NUCLEOTIDE-SEQUENCE
   VIBRIO-HARVEYI
   BACTERIAL LUCIFERASE
   FIREFLY LUCIFERASE
   SUBUNIT
   CELLS
   GENE
   PHOTOPROTEINS
   EXPRESSION
Аннотация: Major advances in the development and application of the bioluminescent analysis to detect certain biologically active substances are discussed. The main merit of the method lies in its high sensitivity and specificity along with its simplicity and rapid performance. The available methodologies allow for detection of substances of varying nature: Ca2+, ATP, FMN, NAD(P), long-chain aldehydes, ATP- and NAD(P)-dependent enzymes and their substrates, many xenobiotics and antibiotics, and mutagens. The bioluminescence methodologies may be widely applied in clinical laboratory diagnosis.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
GITELZON, I.I.; SANDALOVA, T.P.

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Purification and partial spectral characterization of a novel luciferin from the luminous enchytraeid Fridericia heliota / V. N. Petushkov, N. S. Rodionova // Journal of Photochemistry and Photobiology B: Biology. - 2007. - Vol. 87, Is. 2. - P130-136, DOI 10.1016/j.jphotobiol.2007.03.006 . - ISSN 1011-1344
Кл.слова (ненормированные):
ATP -- Bioluminescence -- Earthworms -- Enchytraeid -- Luciferase -- Luciferin -- adenosine triphosphate -- luciferase -- luciferin -- animal cell -- anion exchange chromatography -- annelid worm -- article -- controlled study -- earthworm -- firefly -- luminance -- luminescence -- nonhuman -- priority journal -- protein analysis -- protein purification -- radiation absorption -- reversed phase liquid chromatography -- ultraviolet radiation -- Adenosine Triphosphate -- Animals -- Luciferases -- Luminescent Agents -- Oligochaeta -- Spectrum Analysis -- Enchytraeidae -- Fridericia heliota
Аннотация: A homogeneous luciferin preparation has been obtained from the luminous soil enchytraeid Fridericia heliota, which has an ATP-dependent luminescent system. A procedure for luciferin purification without losing fractions of active luciferase has been developed. The luciferin specific activity is 4000 times increased; its UV absorption spectrum maximum is 294 nm with a local minimum at 262 nm. The luciferin of the enchytraeid F. heliota is significantly different from firefly luciferin, whose luminescent reaction also requires ATP, and it also appears to have no similarities to other known luciferins. В© 2007 Elsevier B.V. All rights reserved.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Rodionova, N.S.

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Effect of different salts and detergents on luciferin-luciferase luminescence of the enchytraeid Fridericia heliota / N. S. Rodionova, V. N. Petushkov // Journal of Photochemistry and Photobiology B: Biology. - 2006. - Vol. 83, Is. 2. - P123-128, DOI 10.1016/j.jphotobiol.2005.12.014 . - ISSN 1011-1344
Кл.слова (ненормированные):
ATP -- Bioluminescence -- Earthworms -- Ions -- Luciferin-luciferase systems -- Triton X-100 -- adenosine triphosphate -- anion -- bromine -- calcium ion -- carbonic acid -- cation -- chloride -- chromium derivative -- detergent -- dodecyl sulfate sodium -- inorganic salt -- iodine -- iron derivative -- luciferase -- luciferin -- magnesium ion -- manganese -- nitrate -- phosphate -- sulfate -- sulfite -- triton x 100 -- annelid worm -- article -- bioluminescence -- concentration (parameters) -- controlled study -- enzyme activation -- enzyme activity -- enzyme inhibition -- enzyme mechanism -- in vitro study -- nonhuman -- priority journal -- qualitative analysis -- quantitative analysis -- Adenosine Triphosphate -- Animals -- Cations, Divalent -- Cations, Monovalent -- Detergents -- Firefly Luciferin -- Kinetics -- Luciferases -- Luminescence -- Metals -- Oligochaeta -- Photobiology -- Salts -- Annelida -- Clitellata -- earthworms (sp.) -- Enchytraeidae -- Fridericia heliota -- Oligochaeta (Metazoa) -- Pheretima sieboldi
Аннотация: The study addresses the effect produced by different inorganic salts and detergents (SDS, Triton X-100, the Tween series) on the ATP-dependent bioluminescent reaction catalyzed by the luciferase of the new earthworm species Fridericia heliota (Annelida: Clitellata: Oligochaeta: Enchytraeidae). It has been shown that the effect of divalent metal salts on luminescence is determined by the action of cations. Three of them - Mg2+, Mn2+ and Ca2+ - can stimulate luciferase activity at concentrations varying within a wide range, and Mn2+ can act as a 100%-effective substitute for Mg2+ in F. heliota luminescence reaction in vitro. The inhibitory effect of monovalent metal salts on luminescence is largely determined by the action of the anion part of the molecule. The effectiveness of the inhibitory effect of anions increases in the following order: {Mathematical expression}. Of the sodium salts, dodecyl sulfate, which is an anionic detergent, produces the strongest inhibitory effect on luciferase. On the contrary, nonionic detergents produce a stimulatory effect on the F. heliota luciferase. The action of the most effective of them - Triton X-100 - is determined by its ability to reduce the actual concentration of lipid inhibitors in the reaction mixture. В© 2006 Elsevier B.V. All rights reserved.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Rodionova, N.S.; Petushkov, V.N.

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ATP is a cosubstrate of the luciferase of the earthworm Fridericia heliota (Annelida: Clitellata: Oligochaeta: Enchytraeidae) / N. S. Rodionova, V. S. Bondar', V. N. Petushkov // Doklady Biochemistry and Biophysics. - 2003. - Vol. 392, Is. 1-6. - P253-255, DOI 10.1023/A:1026134628735 . - ISSN 1607-6729
Кл.слова (ненормированные):
adenosine diphosphate -- adenosine phosphate -- adenosine triphosphate -- luciferase -- luciferin -- magnesium -- animal cell -- article -- controlled study -- earthworm -- hydrolysis -- luminescence -- nonhuman -- Adenosine Diphosphate -- Adenosine Triphosphate -- Animals -- Firefly Luciferin -- Kinetics -- Luciferases -- Luminescent Measurements -- Magnesium -- Oligochaeta -- Substrate Specificity -- Animalia -- Annelida -- Clitellata -- Enchytraeidae -- Pheretima sieboldi

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Rodionova, N.S.; Bondar', V.S.; Petushkov, V.N.

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Characterization of hydromedusan Ca2+-regulated photoproteins as a tool for measurement of Ca2+concentration / N. P. Malikova [et al.] // . - 2014, DOI 10.1007/s00216-014-7986-2 . - ISSN 1618-2642
Кл.слова (ненормированные):
Aequorin -- Calcium -- Clytin -- Coelenterazine -- Mitrocomin -- Obelin
Аннотация: Calcium ion is a ubiquitous intracellular messenger, performing this function in many eukaryotic cells. To understand calcium regulation mechanisms and how disturbances of these mechanisms are associated with disease states, it is necessary to measure calcium inside cells. Ca2+-regulated photoproteins have been successfully used for this purpose for many years. Here we report the results of comparative studies on the properties of recombinant aequorin from Aequorea victoria, recombinant obelins from Obelia geniculata and Obelia longissima, recombinant mitrocomin from Mitrocoma cellularia, and recombinant clytin from Clytia gregaria as intracellular calcium indicators in a set of identical in vitro and in vivo experiments. Although photoproteins reveal a high degree of identity of amino acid sequences and spatial structures, and, apparently, have a common mechanism for the bioluminescence reaction, they were found to differ in the Ca2+ concentration detection limit, the sensitivity of bioluminescence to Mg2+, and the rates of the rise of the luminescence signal with a sudden change of Ca2+ concentration. In addition, the bioluminescence activities of Chinese hamster ovary cells expressing wild-type photoproteins also differed. The light signals of cells expressing mitrocomin, for example, slightly exceeded the background, suggesting that mitrocomin may be hardly used to detect intracellular Ca2+ without modifications improving its properties. On the basis of experiments on the activation of endogenous P2Y2 receptor in Chinese hamster ovary cells by ATP, we suggest that wild-type aequorin and obelin from O. longissima are more suitable for calcium detection in cytoplasm, whereas clytin and obelin from O. geniculata can be used for calcium measurement in cell compartments with high Ca2+ concentration. [Figure not available: see fulltext.] © 2014 Springer-Verlag Berlin Heidelberg.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, 660036, Russian Federation
Laboratory of Bioluminescent Biotechnologies, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Malikova, N.P.; Burakova, L.P.; Markova, S.V.; Vysotski, E.S.

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10.

A novel ATP-dependent bioluminescent system from the Siberian earthworm Fridericia heliota: structure elucidation of luciferin and its analogs [Text] / V. . Petushkov [et al.] // Luminescence. - 2014. - Vol. 29. - P54-55. - Cited References: 3 . - ISSN 1522-7235. - ISSN 1522-7243

WOS
Держатели документа:
[Dubinnyi, Maxim
Tsarkova, Aleksandra
Baranov, Mikhail
Yampolsky, Ilia] Russian Acad Sci, Inst Bioorgan Chem, Moscow, Russia
[Petushkov, Valentin
Rodionova, Natalja
Shimomura, Osamu] Russian Acad Sci, Inst Biophys, Lab Photobiol, Siberian Branch, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V...; Dubinnyi, M...; Tsarkova, A...; Rodionova, N...; Baranov, M...; Shimomura, O...; Yampolsky, I...

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11.

A Novel Type of Luciferin from the Siberian Luminous Earthworm Fridericia heliota: Structure Elucidation by Spectral Studies and Total Synthesis [Text] / V. N. Petushkov [et al.] // Angew. Chem.-Int. Edit. - 2014. - Vol. 53, Is. 22. - P5566-5568, DOI 10.1002/anie.201400529. - Cited References: 13. - We thank Dr. Alexander O. Chizhov for recording mass spectra and Dr. K. S. Mineev for NMR analysis of synthetic intermediates. We acknowledge support from the Program of the Government of the Russian Federation "Measures to attract leading scientists to Russian educational institutions" (grant no. 11. G34.31.0058), the programs MCB RAS, President of the Russian Federation "Leading science school" (grant 3951.2012.4) and the Russian Foundation for Basic Research (grant 14-03-01015). B. M. S. was supported by a stipend from the Program of the President of the Russian Federation. . - ISSN 1433-7851. - ISSN 1521-3773

РУБ Chemistry, Multidisciplinary
Рубрики:
BIOLUMINESCENT EARTHWORM
Кл.слова (ненормированные):
bioluminescence -- luciferin -- natural products -- NMR spectroscopy -- total synthesis
Аннотация: The structure elucidation and synthesis of the luciferin from the recently discovered luminous earthworm Fridericia heliota is reported. This luciferin is a key component of a novel ATP-dependent bioluminescence system. UV, fluorescence, NMR, and HRMS spectroscopy studies were performed on 0.005 mg of the isolated substance and revealed four isomeric structures that conform to spectral data. These isomers were chemically synthesized and one of them was found to produce light when reacted with a protein extract from F. heliota. The novel luciferin was found to have an unusual extensively modified peptidic nature, thus implying an unprecedented mechanism of action.

WOS
Держатели документа:
[Petushkov, Valentin N.
Rodionova, Natalja S.
Shimomura, Osamu] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
[Petushkov, Valentin N.
Rodionova, Natalja S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Lab Photobiol, Krasnoyarsk 660036, Russia
[Dubinnyi, Maxim A.
Tsarkova, Aleksandra S.
Baranov, Mikhail S.
Kublitski, Vadim S.
Yampolsky, Ilia V.] Russian Acad Sci, Inst Bioorgan Chem, Moscow 117997, Russia
[Shimomura, Osamu] Marine Biol Lab, Woods Hole, MA 02543 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Dubinnyi, M.A.; Tsarkova, A.S.; Rodionova, N.S.; Baranov, M.S.; Kublitski, V.S.; Shimomura, O...; Yampolsky, I.V.; Government of the Russian Federation "Measures to attract leading scientists to Russian educational institutions" [11. G34.31.0058]; programs MCB RAS; Russian Federation "Leading science school" [3951.2012.4]; Russian Foundation for Basic Research [14-03-01015]; Russian Federation

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12.

Characterization of hydromedusan Ca2+-regulated photoproteins as a tool for measurement of Ca(2+)concentration [Text] / N. P. Malikova [et al.] // Anal. Bioanal. Chem. - 2014. - Vol. 406, Is. 23. - P5715-5726, DOI 10.1007/s00216-014-7986-2. - Cited References: 67. - This work was supported by RFBR grant 12-04-00131, by the programs of the Government of the Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058) and "Molecular and Cellular Biology" of the Russian Academy of Sciences, and the grant from the President of the Russian Federation "Leading Science School" (3951.2012.4). . - ISSN 1618-2642. - ISSN 1618-2650

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
LIGHT-SENSITIVE PHOTOPROTEIN
   CTENOPHORE BEROE ABYSSICOLA
   GREEN-FLUORESCENT PROTEIN
   INTRACELLULAR CALCIUM
   SEQUENCE-ANALYSIS
   CA-2+-ACTIVATED PHOTOPROTEIN
   CA2+-BINDING PHOTOPROTEIN
   SEMISYNTHETIC AEQUORINS
   LUMINESCENT PROTEIN
   RECOMBINANT OBELIN
Кл.слова (ненормированные):
Calcium -- Coelenterazine -- Aequorin -- Obelin -- Clytin -- Mitrocomin
Аннотация: Calcium ion is a ubiquitous intracellular messenger, performing this function in many eukaryotic cells. To understand calcium regulation mechanisms and how disturbances of these mechanisms are associated with disease states, it is necessary to measure calcium inside cells. Ca2+-regulated photoproteins have been successfully used for this purpose for many years. Here we report the results of comparative studies on the properties of recombinant aequorin from Aequorea victoria, recombinant obelins from Obelia geniculata and Obelia longissima, recombinant mitrocomin from Mitrocoma cellularia, and recombinant clytin from Clytia gregaria as intracellular calcium indicators in a set of identical in vitro and in vivo experiments. Although photoproteins reveal a high degree of identity of amino acid sequences and spatial structures, and, apparently, have a common mechanism for the bioluminescence reaction, they were found to differ in the Ca2+ concentration detection limit, the sensitivity of bioluminescence to Mg2+, and the rates of the rise of the luminescence signal with a sudden change of Ca2+ concentration. In addition, the bioluminescence activities of Chinese hamster ovary cells expressing wild-type photoproteins also differed. The light signals of cells expressing mitrocomin, for example, slightly exceeded the background, suggesting that mitrocomin may be hardly used to detect intracellular Ca2+ without modifications improving its properties. On the basis of experiments on the activation of endogenous P2Y(2) receptor in Chinese hamster ovary cells by ATP, we suggest that wild-type aequorin and obelin from O. longissima are more suitable for calcium detection in cytoplasm, whereas clytin and obelin from O. geniculata can be used for calcium measurement in cell compartments with high Ca2+ concentration.

WOS
Держатели документа:
[Malikova, Natalia P.
Burakova, Ludmila P.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Malikova, Natalia P.
Burakova, Ludmila P.
Markova, Svetlana V.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Malikova, N.P.; Burakova, L.P.; Markova, S.V.; Vysotski, E.S.; RFBR [12-04-00131]; Government of the Russian Federation [11.G34.31.0058]; Russian Academy of Sciences; Russian Federation "Leading Science School" [3951.2012.4]

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13.

CONFORMATIONAL-ANALYSIS OF CYCLIC FORM OF ATP [Текст] / P. I. BELOBROV, T. P. SANDALOVA // Bioorg. Khim. - 1980. - Vol. 6, Is. 11. - P. 1714-1721. - Cited References: 19 . - ISSN 0132-3423

РУБ Biochemistry & Molecular Biology + Chemistry, Organic

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
BELOBROV, P.I.; SANDALOVA, T.P.

Найти похожие

14.

NADPH-DEPENDENT AND ATP-DEPENDENT LUMINESCENCE OF EXTRACTS OF LUMINESCENT BACTERIA [Text] / E. S. VYSOTSKII, V. V. ZAVORUEV, V. V. MEZHEVIKIN // Biochem.-Moscow. - 1982. - Vol. 47, Is. 12. - P. 1682-1686. - Cited References: 10 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
VYSOTSKII, E.S.; ZAVORUEV, V.V.; MEZHEVIKIN, V.V.

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15.

Model of the active site of firefly luciferase [Text] / T. P. Sandalova, N. N. Ugarova // Biochem.-Moscow. - 1999. - Vol. 64, Is. 8. - P. 962-967. - Cited References: 20 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
ESCHERICHIA-COLI
   SEQUENCE
   CLONING
   ENZYME
   CDNA
   SUPERFAMILY
Кл.слова (ненормированные):
bioluminescence -- firefly luciferase -- ATP -- luciferin -- spatial structure -- active site -- enzyme-substrate complex
Аннотация: A model for the spatial structure of firefly luciferase-ATP-luciferin complex is suggested using the coordinates of unliganded luciferase and the enzyme-substrate complex of the adenylating subunit of gramicidin S synthetase known from the literature. Conformational changes in luciferase can occur during substrate binding resulting in a relative orientation of two luciferase domains similar to that in case of the AMP-phenylalanine-synthetase complex. The model is consistent with data on the physicochemical properties of firefly luciferase and its complexes with the substrates.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Karolinska Inst, S-17177 Stockholm, Sweden
Moscow MV Lomonosov State Univ, Sch Chem, Moscow 119899, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sandalova, T.P.; Ugarova, N.N.

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16.

Characteristics of oxygen transport through the surface of the isolated perfused rat liver / K. V. Shadrin [et al.] // Doklad. Biochem. Biophys. - 2015. - Vol. 464, Is. 1. - P298-300, DOI 10.1134/S1607672915050075 . - ISSN 1607-6729
Аннотация: It is shown that the transport of oxygen through the surface of the isolated perfused rat liver is an energy-dependent process that requires the energy of ATP hydrolysis. © 2015, Pleiades Publishing, Ltd.

Scopus,
WOS
Держатели документа:
Krasnoyarsk Research Center, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodnyi pr. 79, Krasnoyarsk, Russian Federation
Voino-Yasenetskii State Medical University, Ministry of Health of the Russian Federation, ul. Partizana Zheleznyaka 1, Krasnoyarsk, Krasnoyarsk Krai, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Shadrin, K. V.; Morgulis, I. I.; Pahomova, V. G.; Rupenko, A. P.; Khlebopros, R. G.

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17.

Salinity modulates thermotolerance, energy metabolism and stress response in amphipods Gammarus lacustris / K. P. Vereshchagina [et al.] // PeerJ. - 2016. - Vol. 2016, Is. 11, DOI 10.7717/peerj.2657 . - ISSN 2167-8359
Кл.слова (ненормированные):
Adaptation -- Amphipoda -- Gammarus lacustris -- Salinity -- Thermal tolerance
Аннотация: Temperature and salinity are important abiotic factors for aquatic invertebrates. We investigated the influence of different salinity regimes on thermotolerance, energy metabolism and cellular stress defense mechanisms in amphipods Gammarus lacustris Sars from two populations. We exposed amphipods to different thermal scenarios and determined their survival as well as activity of major antioxidant enzymes (peroxidase, catalase, glutathione S-transferase) and parameters of energy metabolism (content of glucose, glycogen, ATP, ADP, AMP and lactate). Amphipods from a freshwater population were more sensitive to the thermal challenge, showing higher mortality during acute and gradual temperature change compared to their counterparts from a saline lake. A more thermotolerant population from a saline lake had high activity of antioxidant enzymes. The energy limitations of the freshwater population (indicated by low baseline glucose levels, downward shift of the critical temperature of aerobic metabolism and inability to maintain steady-state ATP levels during warming) was ob- served, possibly reflecting a trade-off between the energy demands for osmoregulation under the hypo-osmotic condition of a freshwater environment and protection against temperature stress. © 2016 Vereshchagina et al.

Scopus,
Смотреть статью
Держатели документа:
Institute of Biology, Irkutsk State University, Irkutsk, Russian Federation
Baikal Research Centre, Irkutsk, Russian Federation
Institute of Biophysics SB RAS, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation
Institute for Biological Sciences, University of Rostock, Rostock, Germany

Доп.точки доступа:
Vereshchagina, K. P.; Lubyaga, Y. A.; Shatilina, Z.; Bedulina, D.; Gurkov, A.; Axenov-Gribanov, D. V.; Baduev, B.; Kondrateva, E. S.; Gubanov, M.; Zadereev, E.; Sokolova, I.; Timofeyev, M.

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18.

Progress in the Study of Bioluminescent Earthworms / N. S. Rodionova [et al.] // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P416-428, DOI 10.1111/php.12709 . - ISSN 0031-8655
Аннотация: Even though bioluminescent oligochaetes rarely catch people's eyes due to their secretive lifestyle, glowing earthworms sighting reports have come from different areas on all continents except Antarctica. A major breakthrough in the research of earthworm bioluminescence occurred in the 1960s with the studies of the North American Diplocardia longa. Comparative studies conducted on 13 earthworm species belonging to six genera showed that N-isovaleryl-3-aminopropanal (Diplocardia luciferin) is the common substrate for bioluminescence in all examined species, while luciferases appeared to be responsible for the color of bioluminescence. The second momentous change in the situation has occurred with the discovery in Siberia (Russia) of two unknown luminous enchytraeids. The two bioluminescent systems belong to different types, have different spectral characteristics and localization, and different temperature and pH optima. They are unique, and this fact is confirmed by the negative results of all possible cross-reactions. The bioluminescent system of Henlea sp. comprises four essential components: luciferase, luciferin, oxygen and calcium ion. For Friderica heliota, the luminescent reaction requires five components: luciferase, luciferin, ATP, magnesium ion and oxygen. Along with luciferin, more than a dozen analogues were isolated from worm biomass. These novel peptide-like natural compounds represent an unprecedented chemistry found in terrestrial organisms. © 2017 The American Society of Photobiology

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Держатели документа:
Laboratory of Photobiology, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Department of Physics, Earth and Environmental Sciences, University of Siena, Siena, Italy
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russian Federation
Pirogov Russian National Research Medical University, Moscow, Russian Federation

Доп.точки доступа:
Rodionova, N. S.; Rota, E.; Tsarkova, A. S.; Petushkov, V. N.

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19.

Role of Hsp90 and ATP in modulating apyrase activity and firefly luciferase kinetics / M. A. Kirillova [et al.] // Int. J. Biol. Macromol. - 2019. - Vol. 131. - P691-696, DOI 10.1016/j.ijbiomac.2019.03.110 . - ISSN 0141-8130
Кл.слова (ненормированные):
Bioluminescence -- Heat shock protein 90 -- High-throughput screening -- adenosine triphosphate -- apyrase -- bovine serum albumin -- firefly luciferase -- heat shock protein 90 -- stabilizing agent -- Article -- bioluminescence -- clinical study -- conformation -- controlled study -- denaturation -- enzyme activity -- enzyme kinetics -- high throughput screening -- incubation time -- nonhuman -- protein protein interaction -- protein refolding -- temperature -- thermal denaturation -- time
Аннотация: The present manuscript describes a novel bioassay consisting of apyrase and heat shock protein 90 (Hsp90) without additional co-chaperone supplementation; intended for high-throughput screening of anti-cancer drugs and prognosis of stress. In this regard, Hsp90 and adenosine 5?-triphosphate (ATP) mediated firefly luciferase (FLuc) kinetics was investigated using apyrase and FLuc as client proteins. Bioluminescent assay containing Hsp90, ATP, and apyrase led to complete loss of luminescence at 50 °C which indicates the protective role of Hsp90 against thermal denaturation. Similarly, the assay sample comprising Hsp90, ATP, and FLuc showed 2 fold increments in luminescence than their counterparts. Introduction of bovine serum albumin (BSA) to the pre-incubated assay mixture led to an initial rise in the luminescence (28%) in comparison to the sample containing Hsp90, ATP and FLuc. Therefore, FLuc based HTS assays are not suitable for clinical samples which may contain stabilizing agents. However, thermally denatured FLuc and apyrase could not regain their active conformation even when Hsp90 and ATP were introduced in the assay system. This observation justifies the role of Hsp90 to be protective rather than a reparation agent when acts without co-chaperones. © 2019

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Держатели документа:
Laboratory of Bioluminescent Biotechnologies, Department of Biophysics, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, 79 Svobodny Prospect, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Kirillova, M. A.; Ranjan, R.; Esimbekova, E. N.; Kratasyuk, V. A.

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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.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 21. - Ст. 7846. - P1-22, DOI 10.3390/ijms21217846 . - ISSN 1661-6596
Кл.слова (ненормированные):
Aequorin -- Bioluminescence -- BRET -- Calcium sensor -- GPCR assay -- Mutagenesis -- Neuronal network imaging
Аннотация: Considerable efforts have been focused on shifting the wavelength of aequorin Ca2+? dependent blue bioluminescence through fusion with fluorescent proteins. This approach has notably yielded the widely used GFP?aequorin (GA) Ca2+ sensor emitting green light, and tdTomato-aequorin (Redquorin), whose bioluminescence is completely shifted to red, but whose Ca2+ sensitivity is low. In the present study, the screening of aequorin mutants generated at twenty?four amino acid positions in and around EF?hand Ca2+?binding domains resulted in the isolation of six aequorin single or double mutants (AequorinXS) in EF2, EF3, and C?terminal tail, which exhibited markedly higher Ca2+ sensitivity than wild?type aequorin in vitro. The corresponding Redquorin mutants all showed higher Ca2+ sensitivity than wild?type Redquorin, and four of them (RedquorinXS) matched the Ca2+ sensitivity of GA in vitro. RedquorinXS mutants exhibited unaltered thermostability and peak emission wavelengths. Upon stable expression in mammalian cell line, all RedquorinXS mutants reported the activation of the P2Y2 receptor by ATP with higher sensitivity and assay robustness than wt?Redquorin, and one, RedquorinXS?Q159T, outperformed GA. Finally, wide?field bioluminescence imaging in mouse neocortical slices showed that RedquorinXS?Q159T and GA similarly reported neuronal network activities elicited by the removal of extracellular Mg2+. Our results indicate that RedquorinXS?Q159T is a red light?emitting Ca2+ sensor suitable for the monitoring of intracellular signaling in a variety of applications in cells and tissues, and is a promising candidate for the transcranial monitoring of brain activities in living mice. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

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Держатели документа:
Institut de Neurobiologie Alfred Fessard, UPR 3294, Centre National de la Recherche Scientifique (CNRS), Avenue de la Terrasse, Gif?sur?Yvette, 91198, France
BioEmergences Unit, CNRS USR 3695, Universite Paris?Saclay, Avenue de la Terrasse, Gif?sur?Yvette, 91198, France
Neuroscience Paris Seine ? Institut de Biologie Paris Seine (NPS ? IBPS), CNRS, UMR8246, INSERM U1130, Sorbonne Universite UM119, Paris, 75005, France
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Bakayan, A.; Picaud, S.; Malikova, N. P.; Tricoire, L.; Lambolez, B.; Vysotski, E. S.; Peyrieras, N.

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