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An in situ method for the investigation of vertical distributions of zooplankton in lakes: test of a two-compartment enclosure [Text] / A. P. Tolomeyev, Y. S. Zadereev // Aquat. Ecol. - 2005. - Vol. 39, Is. 2. - P. 181-188, DOI 10.1007/s10452-004-5732-0. - Cited References: 21 . - ISSN 1386-2588

РУБ Ecology + Limnology + Marine & Freshwater Biology
Рубрики:
MIGRATION
   DAPHNIA
   RADIATION
   COPEPODS
   EXPOSURE
   PATTERNS
   LIGHT
Кл.слова (ненормированные):
anoxic hypolimnion -- solar radiation -- stratified lake -- vertical migration -- zooplankton
Аннотация: Two-section enclosures were designed for the investigation of the effect of various physicochemical and biological factors on vertical distribution of zooplankton in situ. The framework of the enclosure was a cylindrical polyethylene column without any partitions inside, in which the isolation of animals in different sections after in situ exposure was achieved by pinching the flexible central part of the column. Enclosures were tested at the brackish stratified meromictic Lake Shira (Russia, Khakasia). The absence of fish and carnivorous zooplankton in the lake suggests that the vertical distribution of zooplankton is mainly determined by physicochemical gradients in the water column. Experiments and field observations demonstrated that all age and size groups of Arctodiaptomus salinus and Brachionus plicatilis strongly avoided surface layers during the daylight. The escape of zooplankton from the anoxic hypolimnion was less active. Statistically significant avoidance was observed only for copepodites C4-C5 and females of A. salinus. The relatively simple construction of the columns and easy handling during the experiment were the factors that favoured the use of this device to perform in situ basic tests of the effect of different factors on the vertical distribution of zooplankton.

WOS
Держатели документа:
SB RAS, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Tolomeyev, A.P.; Zadereev, Y.S.

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Green flavoprotein from P. leiognathi: purification, characterization and identification as the product of the lux G(N) gene / A. A. Raibekas // Journal of bioluminescence and chemiluminescence. - 1991. - Vol. 6, Is. 3. - P. 169-176 . - ISSN 0884-3996
Кл.слова (ненормированные):
bacterial protein -- flavoprotein -- amino acid sequence -- article -- bacterial gene -- chemistry -- genetics -- isolation and purification -- luminescence -- molecular genetics -- molecular weight -- Photobacterium -- Amino Acid Sequence -- Bacterial Proteins -- Flavoproteins -- Genes, Bacterial -- Luminescence -- Molecular Sequence Data -- Molecular Weight -- Photobacterium -- Support, U.S. Gov't, P.H.S.
Аннотация: A green flavoprotein (GFP) was isolated and purified to homogeneity from Photobacterium leiognathi, strain 208. GFP is a homodimer of molecular weight 54,000 and contains two molecules of an unusual flavin per molecule of protein. Various biochemical characteristics including isoelectric point, trypsin and chymotrypsin degradation, SDS and temperature influence on subunit dissociation and the dissociation of the flavin chromophore, were investigated. The sequence of 23 N-terminal amino acids was determined and found to be concurrent with the N-terminal amino acid sequence encoded by the lux G(N) gene of P. leiognathi. This fact suggests that GFP is a structural component of the Photobacterium luminescence system.

Scopus
Держатели документа:
Institute of Biophysics, USSR Academy of Sciences, Krasnoyarsk. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Raibekas, A.A.

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The use of glowing wood as a source of luminescent culture of fungus mycelium [Text] / A. P. Puzyr, S. E. Medvedeva, V. S. Bondar // Mycosphere. - 2016. - Vol. 7, Is. 1. - P1-17, DOI 10.5943/mycosphere/7/1/1. - Cited References:22. - The authors are grateful to Prof. A. Frank, Director of North Borneo Biostation, for the opportunity to carry out studies of glowing wood; to Nadezhda N. Kudashova, a senior researcher at the Institute of Biology and Biophysics at the Tomsk University, for identifying the species of nonluminous fungi. This study was supported by grant no. 11.G34.31.0058 (RF Government) and Projects no. 71 (SB RAS). . - ISSN 2077-7000

РУБ Mycology
Рубрики:
BIOLUMINESCENCE CHARACTERISTICS
NEONOTHOPANUS-NAMBI
LIGHT-EMISSION
Кл.слова (ненормированные):
Bioluminescence -- culture of luminous mycelia -- kinetics of luminescent -- reaction -- light emitting wood -- luminous fungus
Аннотация: In studies of fungal bioluminescence, not only fruiting bodies and spores of the fungus, but also samples of luminescent wood, leaf litter or soil may need to be used to derive pure mycelial culture. This study describes an approach to isolating the culture of luminescent fungal mycelium from samples of light-emitting wood found on Borneo Island in November-December 2013. A GelDoc XR Imaging System (Bio-Rad Laboratories, Inc., U.S.) was used for the first time to monitor luminescence and select luminous samples. This study shows that for successful isolation of the culture of luminescent mycelium out of the luminescent wood found in the forest, it is imperative to keep the samples moist (mycelium alive until there is water), while immediate and aseptic delivery of the samples to the laboratory is not a crucial condition (inner layers of wood is "sterile"). Investigation of the growth features of the isolated mycelium in various growing conditions revealed some peculiar properties of its luminescence in comparison with the known luminescent cultures of basidiomycetes. When grown on solid nutrient media, mycelium exhibits low growth rates, long-lasting luminescence (140 days or longer), and emergence and disappearance of local zones with high levels of light emission. Mycelium produced in submerged culture does not emit light, and this effect must be caused by the absence or a very low level of the luminescent reaction substrate in the biomass. The luminescence system isolated from mycelial biomass did not induce luminescent reaction in vitro upon the addition of NADPH (recording intensity is 60 100 URL/sec). We found that enzymes of the luminescence systems isolated from mycelium pellets retained their activity and catalyzed luminescent reaction when a hot extract of the luminous fungus Armillaria sp. (IBSO 2360) was added (near 1900 URL/sec). The same effect was obtained after addition of hot extracts from the fruiting bodies of nonluminous higher fungi Pholiota squarrosa, Cortinarius sp., Hypholoma capnoides and Chroogomphus rutilus (near 3500 URL/sec). The pure culture of luminescent mycelium has been registered in the Culture Collection of IBP SB RAS as IBSO 2371; now it can be used for various in vivo and in vitro studies, including identification of the fungus.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Puzyr, A. P.; Medvedeva, S. E.; Bondar, V. S.; RF Government [11.G34.31.0058]; SB RAS [71]

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Novel Peptide Chemistry in Terrestrial Animals: Natural Luciferin Analogues from the Bioluminescent Earthworm Fridericia heliota [Text] / M. A. Dubinnyi [et al.] // Chem.-Eur. J. - 2015. - Vol. 21, Is. 10. - P3942-3947, DOI 10.1002/chem.201406498. - Cited References:17. - We thank Dr. K. V. Antonov for registration of LC-HRMS spectra. This work was supported by the Russian Science Foundation grant 14-50-00131. . - ISSN 0947-6539. - ISSN 1521-3765

РУБ Chemistry, Multidisciplinary
Рубрики:
STRUCTURE ELUCIDATION
DERIVATIVES
IDENTIFICATION
Кл.слова (ненормированные):
bioluminescence -- Fridericia heliota -- luciferin -- peptides -- structure -- elucidation
Аннотация: We report isolation and structure elucidation of AsLn5, AsLn7, AsLn11 and AsLn12: novel luciferin analogs from the bioluminescent earthworm Fridericia heliota. They were found to be highly unusual modified peptides, comprising either of the two tyrosine-derived chromophores, CompX or CompY and a set of amino acids, including threonine, gamma-aminobutyric acid, homoarginine, and unsymmetrical N,N-dimethylarginine. These natural compounds represent a unique peptide chemistry found in terrestrial animals and rise novel questions concerning their biosynthetic origin.

WOS,
Scopus
Держатели документа:
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow, Russian Federation
Pirogov Russian National Research Medical University, Ostrovitianov 1, Moscow, Russian Federation
Laboratory of Photobiology, Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Dubinnyi, Maxim A.; Tsarkova, Aleksandra S.; Petushkov, Valentin N.; Kaskova, Zinaida M.; Rodionova, Natalja S.; Kovalchuk, Sergey I.; Ziganshin, Rustam H.; Baranov, Mikhail S.; Mineev, Konstantin S.; Yampolsky, Ilia V.; Russian Science Foundation [14-50-00131]

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Isolation of luminescence system from the luminescent fungus Neonothopanus nambi [Text] / V. S. Bondar [et al.] // Dokl. Biochem. Biophys. - 2014. - Vol. 455, Is. 1. - P56-58, DOI 10.1134/S1607672914020045. - Cited References: 10. - This study was supported by the Program of the Government of the Russian Federation "On Measures to Attract the Leading Scientists to the Educational Institutions of Russia" (project no. 11, G34.31.0058) and the Siberian Branch of the Russian Academy of Sciences (project no. 71). . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics

WOS
Держатели документа:
[Bondar, V. S.
Puzyr', A. P.
Purtov, K. V.
Petunin, A. I.
Rodicheva, E. K.
Medvedeva, S. E.
Gitel'zon, I. I.] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
[Bondar, V. S.
Puzyr', A. P.
Purtov, K. V.
Burov, A. E.
Rodicheva, E. K.
Medvedeva, S. E.
Shpak, B. A.
Tyaglik, A. B.
Shimomura, O.
Gitel'zon, I. I.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Burov, A. E.] Russian Acad Sci, Nauka Special Design & Technol Bur, Krasnoyarsk Sci Ctr, Siberian Branch, Krasnoyarsk, Russia
[Shimomura, O.] Marine Biol Lab, Woods Hole, MA 02543 USA
ИБФ СО РАН
СКТБ Наука : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Bondar, V.S.; Puzyr', A.P.; Purtov, K.V.; Petunin, A.I.; Burov, A.E.; Rodicheva, E.K.; Medvedeva, S.E.; Shpak, B.A.; Tyaglik, A.B.; Shimomura, O...; Gitel'zon, I.I.; Program of the Government of the Russian Federation "On Measures to Attract the Leading Scientists to the Educational Institutions of Russia" [11, G34.31.0058]; Siberian Branch of the Russian Academy of Sciences [71]

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Isolation and comparative studies of two fluorescent flavoproteins of luminous bacteria Photobacterium leiognathi / A. A. Raibekas, V. N. Petushkov // Biofizika. - 1990. - Vol. 35, Is. 2. - С. 368-370 . - ISSN 0006-3029
Кл.слова (ненормированные):
flavoprotein -- fluorescence -- letter -- nonhuman -- Photobacterium leiognathi

Scopus
Держатели документа:
Institute of Biological Physics, Siberian Branch, Academy of Sciences of the USSR, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Raibekas, A.A.; Petushkov, V.N.

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Hydrogen-bond networks between the C-terminus and Arg from the first alpha-helix stabilize photoprotein molecules [Text] / E. V. Eremeeva [et al.] // Photochem. Photobiol. Sci. - 2014. - Vol. 13, Is. 3. - P541-547, DOI 10.1039/c3pp50369k. - Cited References: 22. - The work was supported by RFBR grant 12-04-00753-a, by the Program of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058). . - ISSN 1474-905X. - ISSN 1474-9092

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
GREEN FLUORESCENT PROTEIN
   CA2+-REGULATED PHOTOPROTEIN
   BIOLUMINESCENT IMMUNOASSAY
   COELENTERAZINE BINDING
   ANGSTROM RESOLUTION
   ENERGY-TRANSFER
   FUSION PROTEIN
   APO-OBELIN
   AEQUORIN
   EXPRESSION
Аннотация: Previous studies have stated that aequorin loses most of its bioluminescence activity upon modification of the C-terminus, thus limiting the production of photoprotein fusion proteins at its N-terminus. In the present work, we investigate the importance of the C-terminal proline and the hydrogen bonds it forms for photoprotein active complex formation, stability and functional activity. According to the crystal structures of obelin and aequorin, two Ca2+-regulated photoproteins, the carboxyl group of the C-terminal Pro forms two hydrogen bonds with the side chain of Arg21 (Arg15 in aequorin case) situated in the first a-helix. Whereas, deletion or substitution of the C-terminal proline could noticeably change the bioluminescence activity, stability or the yield of an active photoprotein complex. Therefore, modifications of the first alpha-helix Arg has a clear destructive effect on the main photoprotein properties. A C-terminal hydrogen-bond network is proposed to be important for the stability of photoprotein molecules towards external disturbances, when taking part in the formation of locked protein conformations and isolation of coelenterazine-binding cavities.

WOS
Держатели документа:
[Eremeeva, Elena V.
Burakova, Ludmila P.
Krasitskaya, Vasilisa V.
Kudryavtsev, Alexander N.
Frank, Ludmila A.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Burakova, Ludmila P.
Krasitskaya, Vasilisa V.
Kudryavtsev, Alexander N.
Shimomura, Osamu
Frank, Ludmila A.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Krasnoyarsk 660041, Russia
[Shimomura, Osamu] Marine Biol Lab, Woods Hole, MA 02543 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Burakova, L.P.; Krasitskaya, V.V.; Kudryavtsev, A.N.; Shimomura, O...; Frank, L.A.; RFBR [12-04-00753-a]; Government of Russian Federation [11.G34.31.0058]

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    Antimicrobial and antiradical activity of individual fractions of essential oil from seeds of heracleum dissectum ledeb. Of Siberian Region / A. A. Efremov, I. D. Zykova, N. S. Korosteleva // Khimiya Rastitel'nogo Syr'ya. - 2020. - Is. 2. - С. 79-85, DOI 10.14258/JCPRM.2020027029 . - ISSN 1029-5151
   Перевод заглавия: АНТИМИКРОБНАЯ И АНТИРАДИКАЛЬНАЯ АКТИВНОСТЬ ОТДЕЛЬНЫХ ФРАКЦИЙ ЭФИРНОГО МАСЛА ПЛОДОВ HERACLEUM DISSECTUM LEDEB. СИБИРСКОГО РЕГИОНА
Кл.слова (ненормированные):
2 -- 2-diphenyl-1-picrylhydrazyl -- Antimicrobial activity -- Antiradical activity -- Beans -- Essential oil -- Heracleum dissectum Ledeb
Аннотация: By the method of exhaustive hydroponically obtained essential oil from beans of Heracleum dissectum Ledeb., growing in the Krasnoyarsk region. Separate fractions of oil were obtained: the first after 45 minutes from the beginning of distillation, the second – after 2 hours, the third-after 5 hours, the fourth fraction was collected after the end of hydro-distillation. The component composition of both whole essential oil and its separate fractions was studied. The main components are octyl acetate (60.0%), octyl-2-methylpropanoate (10.2%), n-hexyl-2-methylbutanoate (9.0%). The main amount of octyl acetate (64.7%) is concentrated in the first fraction of the oil. The antimicrobial activity of various fractions of essential oil of borscht dissected against strains of opportunistic microorganisms: Escherichia coli, Pseudomonas aeruginosa, Klebsiella pneumoniae, Staphylococcus aureus 209p, MRSA, Proteus vulgaris. It was found that, depending on the duration of isolation, the antimicrobial activity of essential oil fractions in relation to Staphylococcus aureus 209p, MRSA and Pseudomonas aeruginosa decreases, and in relation to Escherichia coli, Klebsiella pneumoniae and Proteus vulgaris increases. The most pronounced inhibitory effect of the third and fourth fractions of essential oil against Klebsiella pneumonia. The antiradical activity of all studied samples of borscht essential oil dissected in reaction with stable free 2,2-diphenyl-1-picrylhydrazyl radical was established. The first fraction showed minimal antiradical activity (15.1%), the fourth – maximum (49.2%). © 2020 Altai State University. All rights reserved.

Scopus
Держатели документа:
Siberian Federal University, pr. Svobodnyy, 79, Krasnoyarsk, 660049, Russian Federation
Special Design and Technology Bureau “Science”, Federal Research Center of the KSC SB RAS, Akademgorodok, 50/45, Krasnoyarsk, 660036, Russian Federation
Institute of Biophysics, Federal Research Center, KSC SB RAS, Akademgorodok, 50/50, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Efremov, A. A.; Zykova, I. D.; Korosteleva, N. S.

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10.

Extraction of Nanochitin from Marine Resources and Fabrication of Polymer Nanocomposites: Recent Advances / B. Joseph, R. M. Sam, P. Balakrishnan [et al.] // Polymers. - 2020. - Vol. 12, Is. 8. - Ст. 1664, DOI 10.3390/polym12081664. - Cited References:128. - This study was financially supported by project "Agro preparations of the new generation: a strategy of construction and realization" (agreement number 074-02-2018-328) in accordance with resolution number 220 of the Government of the Russian Federation of 9 April 2010, "On measures designed to attract leading scientists to the Russian institutions of higher learning." S.C.M.F. is the recipient of an E2S UPPA Research Partnership Chair (MANTA: Marine Materials) supported by the "Investissements d'Avenir" French program managed by ANR (ANR-16-IDEX-0002), the Region Nouvelle-Aquitaine and the Communaute d'Agglomeration du Pays Basque, France. . - ISSN 2073-4360

РУБ Polymer Science
Рубрики:
NATURAL-RUBBER NANOCOMPOSITES
ELECTROSPUN PVDF MEMBRANE
ALPHA-CHITIN
Кл.слова (ненормированные):
nanochitin -- biodegradable -- marine -- reinforcement -- polysaccharides
Аннотация: Industrial sea food residues, mainly crab and shrimp shells, are considered to be the most promising and abundant source of chitin. In-depth understanding of the biological properties of chitin and scientific advancements in the field of nanotechnology have enabled the development of high-performance chitin nanomaterials. Nanoscale chitin is of great economic value as an efficient functional and reinforcement material for a wide range of applications ranging from water purification to tissue engineering. The use of polymers and nanochitin to produce (bio) nanocomposites offers a good opportunity to prepare bioplastic materials with enhanced functional and structural properties. Most processes for nanochitin isolation rely on the use of chemical, physical or mechanical methods. Chitin-based nanocomposites are fabricated by various methods, involving electrospinning, freeze drying, etc. This review discusses the progress and new developments in the isolation and physico-chemical characterization of chitin; it also highlights the processing of nanochitin in various composite and functional materials.

WOS
Держатели документа:
Mahatma Gandhi Univ, Int & Inter Univ Ctr Nanosci & Nanotechnol, Kottayam 686560, Kerala, India.
Bishop Moore Coll, Res & Post Grad Dept Chem, Mavelikara 690110, Kerala, India.
Plant Lipids Pvt Ltd, Cochin 682311, Kerala, India.
Siberian Fed Univ, Russian Acad Sci, Inst Biophys, Krasnoyarsk 660041, Russia.
Univ Pau & Pays Adour, Inst Interdisciplinary Res Environm & Mat IPREM, IPREM, CNRS,E2S UPPA, F-64600 Anglet, France.
Mahatma Gandhi Univ, Sch Energy Mat, Kottayam 686560, Kerala, India.

Доп.точки доступа:
Joseph, Blessy; Sam, Rubie Mavelil; Balakrishnan, Preetha; Maria, Hanna J.; Gopi, Sreeraj; Volova, Tatiana; Fernandes, Susana C. M.; Thomas, Sabu; Government of the Russian Federation [074-02-2018-328, 220]; "Investissements d'Avenir" French programFrench National Research Agency (ANR) [ANR-16-IDEX-0002]; Region Nouvelle-AquitaineRegion Nouvelle-Aquitaine; Communaute d'Agglomeration du Pays Basque, France

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11.

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, DOI 10.3390/ijms21217846. - Cited References:53. - This work was supported by grants from Centre National de la Recherche Scientifique (AAP Prematuration CNRS 2016, to A.B. and N.P.; equipment transfer to S.P. and B.L.), from Agence Nationale de la Recherche (AAP Prematuration FCS/IDEX Paris Saclay, to A.B. and N.P., France BioImaging infrastructure ANR-10-INBS-04, ANR-11-EQPX-029 to N.P.), from Fondation pour la Recherche sur le Cerveau/Rotary Club de France (B.L.), and from RFBR (project number 20-04-00085 to N.P.M. and E.S.V.). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
IN-VIVO
   PHOTOPROTEIN AEQUORIN
   CA2+-REGULATED PHOTOPROTEINS
   SPREADING
Кл.слова (ненормированные):
bioluminescence -- aequorin -- calcium sensor -- BRET -- mutagenesis -- GPCR -- assay -- 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.

WOS
Держатели документа:
Ctr Natl Rech Sci CNRS, Inst Neurobiol Alfred Fessard, UPR 3294, Ave Terrasse, F-91198 Gif Sur Yvette, France.
Univ Paris Saclay, BioEmergences Unit, CNRS, USR 3695, Ave Terrasse, F-91198 Gif Sur Yvette, France.
Sorbonne Univ, Inst Biol Paris Seine NPS IBPS, INSERM, Neurosci Paris Seine,CNRS,UMR8246,U1130,UM119, F-75005 Paris, France.
Inst Biophys SB RAS, Fed Res Ctr, Photobiol Lab, Krasnoyarsk Sci Ctr SB RAS, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Bakayan, Adil; Picaud, Sandrine; Malikova, Natalia P.; Tricoire, Ludovic; Lambolez, Bertrand; Vysotski, Eugene S.; Peyrieras, Nadine; Vysotski, Eugene; Centre National de la Recherche ScientifiqueCentre National de la Recherche Scientifique (CNRS); Agence Nationale de la RechercheFrench National Research Agency (ANR) [ANR-10-INBS-04, ANR-11-EQPX-029]; Fondation pour la Recherche sur le Cerveau/Rotary Club de France; RFBRRussian Foundation for Basic Research (RFBR) [20-04-00085]

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12.

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.

Scopus
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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13.

Phylogeny of Salmonoid Fishes (Salmonoidei) Based on mtDNA COI Gene Sequences (Barcoding) / V. S. Artamonova [et al.] // Contemp. Probl. Ecol. - 2018. - Vol. 11, Is. 3. - P271-285, DOI 10.1134/S1995425518030022. - Cited References:102. - We are very grateful to colleagues who helped collect samples: E.G. Berestovskii, I.N. Bolotov, E.A. Borovikova, I.V. Vikhrev, L.A. Glushchenko, V.V. Ignatenko, D.P. Karabanov, A.P. Novoselov, V.M. Spitsyn, V.A. Shirokov, and I.L. Shchurov; employees of Trout Hatchery "Adler", the Federal Breeding and Genetic Center for Fish Culture, and Vygsky and Kemsky fish hatcheries; and residents of Barabash-Levada, Len-lu, and Chupa settlements. We also thank S.S. Alekseev for identifying sharp-snouted and blunt-snouted lenoks. This work was supported by the Russian Science Foundation, project no. 16-14-10001. . - ISSN 1995-4255. - ISSN 1995-4263

РУБ Ecology
Рубрики:
MOLECULAR DATING ANALYSIS
GROWTH-HORMONE INTRONS
SALMONIFORMES
Кл.слова (ненормированные):
evolution -- network -- molecular clock -- amino acid sequence -- reproductive -- isolation -- immobilization -- fishes
Аннотация: We have analyzed the partial sequences of the mitochondrial COI gene along with the amino acid sequences of cytochrome oxidase subunit I, encoded by this gene region, in representatives of 11 genera of salmonoid fish. For amino acid sequences, two alternative networks are constructed with outgroups represented by either Esocoidei or Osmeroidei as the supposed ancestral groups. This way, Osmeroidei appear to be closer to the salmonoid fish than Esocoidei, and their presence in the network as an outgroup explains the available data on the morphology and karyology of salmonoids much better. A number of the results of this study are fundamentally new. In particular, the slowing down of the molecular evolution of the grayling (Thymallidae) is shown. We conclude that the charr (Salvelinus) is one of the modern genera of salmonoids closest to their ancestor. The hypothesis of the phylogenetic proximity of the genera Brachymystax, Hucho, and Salmo has been confirmed. We also discuss the possibility that it is namely the changes in the amino acid sequence of cytochrome oxidase subunit I that lead to postzygotic reproductive isolation between taxa.

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Держатели документа:
Russian Acad Sci, Severtsov Inst Ecol & Evolut, Moscow 119071, Russia.
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Artamonova, V. S.; Kolmakova, O. V.; Kirillova, E. A.; Makhrov, A. A.; Russian Science Foundation [16-14-10001]

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14.

    Isolation, Study and Application of Organosolv Lignins / B. N. Kuznetsov [и др.] // J. Sib. Fed. Univ.-Chem. - 2016. - Vol. 9, Is. 4. - С. 454-482, DOI 10.17516/1998-2836-2016-9-4-454-482. - Cited References:137 . - ISSN 1998-2836. - ISSN 2313-6049
Рубрики:
SIZE-EXCLUSION CHROMATOGRAPHY
   MOLECULAR-WEIGHT DISTRIBUTION
Кл.слова (ненормированные):
organosolv lignin -- isolation -- structure -- catalytic depolymerization -- molecular weight -- application -- liquid hydrocarbons -- aerogels
Аннотация: The analysis of the literature on the methods of soluble organosolv lignins isolation, their physical-chemical study and on the method of their processing to porous aerogels and liquid hydrocarbons was carried out. A review of the literature allowed us to choice of the most important areas of research. For isolation from wood the soluble lignins free from sulfur the methods of catalytic peroxide delignification at mild conditions (temperature <= 100 degrees C, atmospheric pressure) and methods of lignin extraction by supercritical organic solvents were used. Molecular mass and molecular-mass distribution of ethanol-lignin samples isolated from aspenwood and abies-wood were studied by gel-permeation chromatography. Weighted molecular mass of ethanol-lignin from abies wood is 478 Da and that from aspen wood ethanol-lignin - 750 Da. Thus, the studied samples of ethanol-lignin have rather low molecular mass, what should facilitate their further processing to liquid hydrocarbons and aerogels. For the depolymerization of organosolv lignins to liquid hydrocarbons the processes of their catalytic conversion in supercritical alcohols have good prospects for the use. In the processes of lignin thermal conversion alcohols can to extract the products of lignin depolymerization and to alkylate these products, preventing their repolymerization to high molecular mass substances. To obtain a new class of nanoporous materials based on lignin the methods of organic aerogels synthesis from mixtures of lignin with other natural polymers and crosslinking agents were applied. It was found that the structure and properties of porous materials of aerogel type depend not only from the reaction mixture composition but from the method of drying. Drying in subcritical conditions leads to the formation of xerogels, in supercritical conditions - to the formation aerogels and the freezdrying - of cryogels. Obtained porous materials can have very low density (around 0.2 g/cm(3)), high specific surface area (to 500 m(2)/g) and the pore volume near 5 cm(3)/g.

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FRC Krasnoyarsk Sci Ctr SB RAS, Inst Chem & Chem Technol SB RAS, 50-24 Akademgorodok, Krasnoyarsk 660036, Russia.
FRC Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, 50-50 Akademgorodok, Krasnoyarsk 660036, Russia.
Univ Lorraine, CNRS, UMR 7198, Inst Jean Lamour,ENSTIB, 27 Rue Philippe Seguin,CS 60036, F-88026 Epinal, France.

Доп.точки доступа:
Kuznetsov, Boris N.; Malyar, Yuriy N.; Kuznetsova, Svetlana A.; Grishechko, Lyudmila I.; Kazachenko, Alexander S.; Levdansky, Alexander V.; Pestunov, Andrey V.; Boyandin, Anatoly N.; Celzard, Alan

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15.

Extracellular Oxidases of Basidiomycete Neonothopanus nambi: Isolation and Some Properties / N. O. Ronzhin, O. A. Mogilnaya, K. S. Artemenko [et al.] // Dokl. Biochem. Biophys. - 2020. - Vol. 490, Is. 1. - P38-42, DOI 10.1134/S1607672920010135. - Cited References:15 . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
PEROXIDASE-ACTIVITY
LIGHT-EMISSION
Кл.слова (ненормированные):
extracellular oxidases -- basidiomycete Neonothopanus nambi -- beta-glucosidase -- gel-filtration chromatography -- veratryl alcohol -- phenol -- FAD
Аннотация: Using the original technique of treating biomass with beta-glucosidase, a pool of extracellular fungal enzymes was obtained for the first time from the mycelium of basidiomycete Neonothopanus nambi. Two protein fractions containing enzymes with oxidase activity were isolated from the extract by gel-filtration chromatography and conventionally called F1 and F2. Enzyme F1 has a native molecular weight of 80-85 kDa and does not contain chromophore components; however, it catalyzes the oxidation of veratryl alcohol with K-m = 0.52 mM. Probably, this enzyme is an alcohol oxidase. Enzyme F2 with a native molecular weight of approximately 60 kDa is a FAD-containing protein. It catalyzes the cooxidation of phenol with 4-aminoantipyrine without the addition of exogenous hydrogen peroxide, which distinguishes it from the known peroxidases. It was assumed that this enzyme may be a mixed-function oxidase. F2 oxidase has K-m value 0.27 mM for phenol. The temperature optimums for oxidases F1 and F2 are 22-35 and 55-70 degrees C, and pH optimums are 6 and 5, respectively.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci, Inst Biophys,Fed Res Ctr, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Ronzhin, N. O.; Mogilnaya, O. A.; Artemenko, K. S.; Posokhina, E. D.; Bondar, V. S.

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16.

Isolation and Purification of Fungal Luciferase from Neonothopanus nimbi / K. V. Purtov [et al.] // Dokl. Biochem. Biophys. - 2018. - Vol. 480, Is. 1. - P177-180, DOI 10.1134/S1607672918030134. - Cited References:6. - The study was supported by Russian Science Foundation Grant No. 16-14-00052. This research was carried out using the equipment provided by the Collective Use Center (CKP IBCH, ID of the agreement with Ministry of Education and Science of the Russian Federation: RFMEFI 62117X0018). . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics

Аннотация: This is the first study to obtain a high-purity luciferase from the fungus Neonothopanus nambi bio-mass that is suitable for subsequent sequencing.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Krasnoyarsk Res Ctr, Inst Biophys, Krasnoyarsk 630036, Russia.
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia.

Доп.точки доступа:
Purtov, K. V.; Gorokhovatsky, A. Yu.; Kotlobay, A. A.; Osipova, Z. M.; Petushkov, V. N.; Rodionova, N. S.; Tsarkova, A. S.; Chepurnykh, T. V.; Yampolsky, I. V.; Gitelson, J. I.; Russian Science Foundation [16-14-00052]

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17.

Isolation and comparative study of two fluorescent flavoproteins of the luminous bacteria Photobacterium leiognathi / A. A. Raibekas, V. N. Petushkov // Biophysics. - 1990. - Vol. 35, Is. 2. - P377-379 . - ISSN 0006-3509

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

Доп.точки доступа:
Raibekas, A.A.; Petushkov, V.N.

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18.

Effect of bacterial population density on germination wheat seeds and dynamics of simple artificial ecosystems / L.A Somova [et al.] // Advances in Space Research. - 2001. - Vol. 27, Is. 9. - P1611-1615, DOI 10.1016/S0273-1177(01)00257-5 . - ISSN 0273-1177
Кл.слова (ненормированные):
Bacteria -- Biomass -- Ecosystems -- Plants (botany) -- Seed -- Artificial soil -- Germination -- Photoassimilation -- Space research -- artificial ecosystem -- article -- comparative study -- ecosystem -- germination -- growth, development and aging -- isolation and purification -- microbiology -- physiology -- plant root -- plant seed -- Pseudomonas fluorescens -- Pseudomonas putida -- wheat -- Ecosystem -- Germination -- Plant Roots -- Pseudomonas fluorescens -- Pseudomonas putida -- Seeds -- Triticum
Аннотация: Effect of the size of rhizospheric bacterial populations on germination of seeds and development of simple terrestrial "wheat plants - rhizospheric microorganisms - artificial soil" and "wheat plants - artificial soil" systems has been studied. Experiments demonstrated that within specify ranges in the inoculate, the rhizospheric bacteria are capable of increasing the yield of germinated seeds and stimulate the growth of plantlets. Germination of seeds inoculated with bacteria was either stimulated, or inhibited or remained at control levels depending on the amount of bacteria. Plant biomass growth and total photoassimilation has been found to depend on the amount of bacteria on the plant roots: the higher the amount of bacteria on plant roots, the smaller is the biomass of plants but the total photoassimilation is, higher. Thus, depending on the amount of bacteria on the roots of plants the system either increases the biomass of plants or increases the total photoassimilation, i.e. "pumps" carbon through itself involving bacteria. В© 2001 COSPAR. Published by Elsevier Science Ltd. All rights reserved.

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

Доп.точки доступа:
Somova, L.A; Pechurkin, N.S.; Sarangova, A.B.; Pisman, T.I.

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19.

Isolation of bioluminescent functions from Photobacterium leiognathi: analysis of luxA, luxB, luxG and neighboring genes / B. A. Illarrionov [et al.] // Gene. - 1990. - Vol. 86, Is. 1. - P89-94 . - ISSN 0378-1119
Кл.слова (ненормированные):
Bioluminescence -- expression in E. coli -- luciferase -- molecular evolution -- nucleotide sequence -- protein alignment -- recombinant DNA -- luciferase -- amino acid sequence -- article -- bioluminescence -- fungus -- gene structure -- genetic engineering -- heredity -- nonhuman -- nucleotide sequence -- priority journal -- vibrionaceae -- Acyltransferases -- Amino Acid Sequence -- Bacterial Proteins -- Base Sequence -- Cloning, Molecular -- DNA, Bacterial -- Genes, Structural, Bacterial -- Luciferase -- Luminescence -- Molecular Sequence Data -- Operon -- Photobacterium -- Restriction Mapping -- Escherichia coli -- Fungi -- Photobacterium leiognathi -- Vibrio harveyi -- Vibrionaceae
Аннотация: Genes encoding luminescence of Photobacterium leiognathi have been cloned in Escherichia coli. The luminescent clones were readily apparent. Among them, a clone containing a recombinant plasmid with a 13.5-kb insertion was identified. This DNA fragment contained all of the luminescence-encoding genes. The luciferase-encoding genes (lux) in this DNA fragment were localized. We have sequenced a part of the cloned lux region and identified the luxA, luxB and luxG genes encoding the ? and ? subunits of luciferase and a ? protein with an Mr of 26 180, respectively. The analysis of deduced amino acid sequences and comparison with known luciferase sequences from Vibrio harveyi, indicate the common origin of these proteins. В© 1990.

Scopus
Держатели документа:
Krasnoyarsk State University, Krasnoyarsk, 660062, Russian Federation
All-Union Research Institute of Molecular Biology, Novosibirsk Region, 633159, Russian Federation
Institute of Biophysics, Krasnoyarsk, 660036, Russian Federation
Institute of Clinical and Experimental Medicine, Novosibirsk, Russian Federation
Novosibirsk Institute of Bioorganic Chemistry, Novosibirsk, 630090, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Illarrionov, B.A.; Blinov, V.M.; Douchenko, A.P.; Protopopova, M.V.; Karginov, V.A.; Mertvetsov, N.P.; Gitelson, J.I.

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20.

BIOLUMBASE - The database of natural and transgenic bioluminescent organisms / S. E. Medvedeva [et al.] // Luminescence. - 2005. - Vol. 20, Is. 2. - P90-96, DOI 10.1002/bio.809 . - ISSN 1522-7235
Кл.слова (ненормированные):
Bioluminescence -- Database -- Luminous bacteria -- lux gene -- Marine -- article -- bacterial strain -- bacterium culture -- bacterium isolation -- bioluminescence -- data base -- gene construct -- medical information -- transgenics -- wide area network -- Bacteria -- Bacterial Proteins -- Databases, Factual -- Ecology -- Luminescence -- Luminescent Proteins -- Marine Biology -- Organisms, Genetically Modified -- Photobacterium -- Transgenes
Аннотация: The Institute of Biophysics SB RAS hosts and maintains a specialized collection of luminous bacteria (CCIBSO 836) containing over 700 strains isolated in various regions of the world's oceans. The culture collection is a source of lux genes and biologically active substances. The wide application of bioluminescence in medicine and ecology has given importance to analys-ing information on the structure and functioning of bioluminescence systems in natural and transgenic microorganisms, as well as on their features that are closely interrelated with bioluminescence. The aims of our BIOLUMBASE database are: gathering information on microorganisms with lux genes, their analysis and free access, and distribution of this data throughout the global network. The database includes two sections, natural and transgenic luminous microorganisms, and is updated by our own experimental results, the published literature and internet resources. For the future, a publicly available internet site for BIOLUMBASE is planned. This will list the strains and provide comprehensive information on the properties and functions of luminous bacteria, the mechanisms of regulation of bioluminescence systems, constructs with lux genes, and applications of bioluminescence in microbiology, ecology, medicine and biotechnology. It is noteworthy that this database will also be useful for evaluation of biological hazards of transgenic strains. Users will be able to carry out bibliographic and strain searches starting from any feature of interest. Copyright В© 2005 John Wiley & Sons, Ltd.

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

Доп.точки доступа:
Medvedeva, S.E.; Boyandin, A.; Lankin, Y.; Kotov, D.; Rodicheva, E.; Popova, L.

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