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1.


   
    A heuristic neural network model in the research of properties of evolutionary trajectories / S. Bartsev, P. Baturina // INTERNATIONAL WORKSHOP ADVANCED TECHNOLOGIES IN MATERIAL SCIENCE, : IOP PUBLISHING LTD, 2019. - Vol. 537: International Workshop on Advanced Technologies in Material Science, (APR 04-06, 2019, Krasnoyarsk, RUSSIA). - Ст. 042001. - (IOP Conference Series-Materials Science and Engineering), DOI 10.1088/1757-899X/537/4/042001. - Cited References:21 . -
РУБ Engineering, Mechanical + Materials Science, Multidisciplinary
Рубрики:
SEQUENCE SPACE
Аннотация: There is considerable data on molecular evolution, but there remains no approach to systematizing them within the framework of the key problems of biology. To search for the most common properties of evolving systems, the heuristic method has been proposed. Artificial networks of formal neurons were chosen as the heuristic model object. The paper examines the divergent component of evolutionary trajectory formation. As a result of the simulation, the dependence of the potential variability parameter on the position of the fitness function landscape was obtained. The simulation results are in agreement with the real data of molecular evolution experiments.

WOS
Держатели документа:
RAS, SB, Inst Biophys, Fed Res Ctr,Krasnoyarsk Sci Ctr, 50 Akad Gorodok, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, 79 Svobodny Pr, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Bartsev, S.; Baturina, P.

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2.


   
    A heuristic neural network model in the research of properties of evolutionary trajectories / S. Bartsev, P. Baturina // IOP Conference Series: Materials Science and Engineering : Institute of Physics Publishing, 2019. - Vol. 537: International Workshop on Advanced Technologies in Material Science, Mechanical and Automation Engineering - MIP: Engineering-2019 (4 April 2019 through 6 April 2019, ) Conference code: 149243, Is. 4, DOI 10.1088/1757-899X/537/4/042001
Кл.слова (ненормированные):
Molecular biology -- Artificial networks -- Common property -- Evolving systems -- Fitness functions -- Heuristic model -- Molecular evolution -- Neural network model -- Trajectory formation -- Heuristic methods
Аннотация: There is considerable data on molecular evolution, but there remains no approach to systematizing them within the framework of the key problems of biology. To search for the most common properties of evolving systems, the heuristic method has been proposed. Artificial networks of formal neurons were chosen as the heuristic model object. The paper examines the divergent component of evolutionary trajectory formation. As a result of the simulation, the dependence of the potential variability parameter on the position of the fitness function landscape was obtained. The simulation results are in agreement with the real data of molecular evolution experiments. © Published under licence by IOP Publishing Ltd.

Scopus,
Смотреть статью
Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center, Krasnoyarsk Scientific Center SB RAS, 50, Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, 79 Svobodny pr., Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Bartsev, S.; Baturina, P.

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3.


   
    A new composite material based on alumina nanofibers and detonation nanodiamonds: synthesis, characterization, and sensing application / N. O. Ronzhin, E. D. Posokhina, E. V. Mikhlina [et al.] // J. Nanopart. Res. - 2021. - Vol. 23, Is. 9. - Ст. 199, DOI 10.1007/s11051-021-05309-y. - Cited References:57. - This work is partially supported by the Russian Foundation for Basic Research, Project 18-29-19078 (E. V. Mikhlina, M. M. Simunin, I. Ryzhkov). . - ISSN 1388-0764. - ISSN 1572-896X
РУБ Chemistry, Multidisciplinary + Nanoscience & Nanotechnology + Materials
Рубрики:
ELECTROCHEMICAL ENERGY-STORAGE
   SELECTIVE DETECTION

   PHENOL DETECTION

Кл.слова (ненормированные):
Nanodiamonds -- Alumina nanofibers -- Composite -- Indicator system -- Phenol
Аннотация: The development of inexpensive, easy-to-produce, and easy-to-use analytical tools for detection of harmful and toxic substances is a relevant research problem with direct applications in environmental monitoring and protection. In this work, we propose a novel composite material based on alumina nanofibers and detonation nanodiamonds for detection of phenol in aqueous medium. The composite material was obtained by mixing an aqueous suspension of alumina nanofibers with a diameter of 10-15 nm and a length of several microns and a hydrosol of nanodiamonds with an average cluster size of 70 nm. The mechanisms underlying the interaction of these nanomaterials are clarified and the physicochemical properties of the composite are investigated. The SEM and TEM studies show that the obtained composite has a network structure, in which clusters of nanodiamonds (10-20 nm in diameter) are distributed over the surface of nanofibers. Coupling of nanomaterials occurs due to opposite signs of their zeta potentials, which results in electrostatic attraction and subsequent chemical bonding as indicated by the X-ray photoelectron spectroscopy and simultaneous thermal analysis. The bonding apparently occurs between functional groups (mainly carboxyl) on the surface of nanodiamonds and amphoteric hydroxyl groups on the surface of alumina nanofibers. The proposed composite allows an easy-to-perform colorimetric analysis for qualitative and quantitative determination of phenol in aqueous samples with linear response over a wide range of concentrations (0.5-106 mu M). Multiple tests have shown that the composite is reusable and retains its catalytic function for at least 1 year during storage at room temperature.

WOS
Держатели документа:
Inst Biophys SB RAS, Akademgorodok 50-50, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Svobodny 79, Krasnoyarsk 660041, Russia.
Inst Computat Modelling SB RAS, Akademgorodok 50-44, Krasnoyarsk 660036, Russia.
Inst Chem & Chem Technol SB RAS, Akademgorodok 50-24, Krasnoyarsk 660036, Russia.
Fed Res Ctr KSC SB RAS, Akademgorodok 50-38, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Ronzhin, Nikita O.; Posokhina, Ekaterina D.; Mikhlina, Elena, V; Mikhlin, Yuri L.; Simunin, Mikhail M.; Tarasova, Lyudmila S.; Vorobyev, Sergey A.; Bondar, Vladimir S.; Ryzhkov, Ilya I.; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-29-19078]

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4.


   
    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.

Scopus
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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5.


   
    Bioluminescent and spectroscopic properties of His-Trp-Tyr triad mutants of obelin and aequorin / E. V. Eremeeva [et al.] // Photochem. Photobiol. Sci. - 2013. - Vol. 12, Is. 6. - P1016-1024, DOI 10.1039/c3pp00002h. - Cited References: 46. - The work was supported by RFBR grant 12-04-00131, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" (grant 1044.2012.2). E.V.E. was supported by Wageningen University Sandwich PhD-Fellowship Program. . - ISSN 1474-905X
РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
   CA2+-BINDING PHOTOPROTEIN

   SEQUENCE-ANALYSIS

   CRYSTAL-STRUCTURE

   VIOLET BIOLUMINESCENCE

   ANGSTROM RESOLUTION

   MNEMIOPSIS-LEIDYI

   LIGHT-EMISSION

   W92F OBELIN

   CLONING

Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine organisms, mostly coelenterates. The photoproteins consist of a single polypeptide chain to which an imidazopyrazinone derivative (2-hydroperoxycoelenterazine) is tightly bound. According to photoprotein spatial structures the side chains of His175, Trp179, and Tyr190 in obelin and His169, Trp173, Tyr184 in aequorin are at distances that allow hydrogen bonding with the peroxide and carbonyl groups of the 2-hydroperoxycoelenterazine ligand. We replaced these amino acids in both photoproteins by residues with different hydrogen bond donor-acceptor capacity. All mutants exhibited luciferase-like bioluminescence activity, hardly present in the wild-type photoproteins, and showed low or no photoprotein activity, except for aeqH169Q (24% of wild-type activity), obeW179Y (23%), obeW179F (67%), obeY190F (14%), and aeqY184F (22%). The results clearly support the supposition made from photoprotein spatial structures that the hydrogen bond network formed by His-Trp-Tyr triad participates in stabilizing the 2-hydroperoxy adduct of coelenterazine. These residues are also essential for the positioning of the 2-hydroperoxycoelenterazine intermediate, light emitting reaction, and for the formation of active photoprotein. In addition, we demonstrate that although the positions of His-Trp-Tyr residues in aequorin and obelin spatial structures are almost identical the substitution effects might be noticeably different.

Держатели документа:
[Eremeeva, Elena V.
Markova, Svetlana V.
Frank, Ludmila A.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Visser, Antonie J. W. G.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Markova, Svetlana V.
Frank, Ludmila A.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; Frank, L.A.; Visser, AJWG; van Berkel, WJH; Vysotski, E.S.

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6.


   
    Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents / E. V. Eremeeva, T. Y. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446, DOI 10.3390/ijms21155446. - Cited References:50. - The reported study was funded by RFBR and NSFC according to the research project No. 20-54-53011 (E.V.E. and N.P.M.), Russian Foundation for Basic Research (No. 18-44-242001), Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science (E.S.V.), the National Natural Science Foundation of China (No. 81874308), and the Shandong Natural Science Foundation (No. ZR2018ZC0233) (M.L.). . - ISSN 1422-0067
РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
   SPECTROSCOPIC PROPERTIES

Кл.слова (ненормированные):
photoprotein -- obelin -- aequorin -- coelenterazine -- analogues
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues.

WOS
Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photobiol Lab, Fed Res Ctr, Krasnoyarsk 660036, Russia.
Shandong Univ, Sch Pharmaceut Sci, Dept Med Chem, Key Lab Chem Biol MOE, Jinan 250012, Peoples R China.
Shandong Univ, Helmholtz Inst Biotechnol, State Key Lab Microbial Technol, Qingdao 266237, Peoples R China.

Доп.точки доступа:
Eremeeva, Elena, V; Jiang, Tianyu; Malikova, Natalia P.; Li, Minyong; Vysotski, Eugene S.; RFBRRussian Foundation for Basic Research (RFBR); NSFCNational Natural Science Foundation of China (NSFC) [20-54-53011]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-44-242001]; Krasnoyarsk Regional Fund of Science; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [81874308]; Shandong Natural Science FoundationNatural Science Foundation of Shandong Province [ZR2018ZC0233]; Government of Krasnoyarsk Territory

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7.


   
    Bioluminescent properties of semi-synthetic obelin and aequorin activated by coelenterazine analogues with modifications of C-2, C-6, and C-8 substituents / E. V. Eremeeva, T. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446. - P1-21, DOI 10.3390/ijms21155446 . - ISSN 1661-6596
Кл.слова (ненормированные):
Aequorin -- Analogues -- Coelenterazine -- Obelin -- Photoprotein
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
Key Laboratory of Chemical Biology (MOE), Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, Jinan, Shandong 250012, China
State Key Laboratory of Microbial Technology, Shandong University–Helmholtz Institute of Biotechnology, Shandong University, Qingdao, Shandong 266237, China

Доп.точки доступа:
Eremeeva, E. V.; Jiang, T.; Malikova, N. P.; Li, M.; Vysotski, E. S.

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8.


   
    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 J. - 2014. - Vol. 281, Is. 5. - P1432-1445, DOI 10.1111/febs.12715 . - ISSN 1742-4658
Кл.слова (ненормированные):
aequorin -- bioluminescence -- coelenterazine, obelin -- 6 (4 hydroxyphenyl) derivative -- aequorin -- benzene derivative -- calcium ion -- hydromedusan -- mutant protein -- obelin -- oxygen -- photoprotein -- unclassified drug -- amino acid substitution -- article -- bioluminescence -- calcium transport -- crystal structure -- fluorescence -- hydrogen bond -- priority journal -- protein conformation -- protein structure -- wild type -- Coelenterata -- aequorin -- bioluminescence -- Ca2+-regulated photoprotein -- coelenterazine, obelin -- Amino Acid Substitution -- Animals -- Conserved Sequence -- Crystallography, X-Ray -- Hydrogen Bonding -- Hydrozoa -- Luminescent Proteins -- Models, Molecular -- Mutagenesis, Site-Directed -- Mutant Proteins -- Protein Conformation -- Spectrophotometry
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine coelenterates. All hydromedusan photoproteins are a single-chain polypeptide to which 2- hydroperoxycoelenterazine is tightly but non-covalently bound. Bioluminescence results from oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. The bioluminescence spectral maxima of recombinant photoproteins vary in the range 462-495 nm, despite a high degree of identity of amino acid sequences and spatial structures of these photoproteins. Based on studies of obelin and aequorin mutants with substitution of Phe to Tyr and Tyr to Phe, respectively [Stepanyuk GA et al. (2005) FEBS Lett 579, 1008-1014], it was suggested that the spectral differences may be accounted for by an additional hydrogen bond between the hydroxyl group of a Tyr residue and an oxygen atom of the 6-(p-hydroxyphenyl) substituent of coelenterazine. Here, we report the crystal structures of two conformation states of the F88Y obelin mutant that has bioluminescence and product fluorescence spectra resembling those of aequorin. Comparison of spatial structures of the F88Y obelin conformation states with those of wild-type obelin clearly shows that substitution of Phe to Tyr does not affect the overall structures of either F88Y obelin or its product following Ca2+ discharge, compared to the conformation states of wild-type obelin. The hydrogen bond network in F88Y obelin being due to the Tyr substitution clearly supports the suggestion that different hydrogen bond patterns near the oxygen of the 6-(p-hydroxyphenyl) substituent are the basis for spectral modifications between hydromedusan photoproteins. Comparison of spatial structures and the hydrogen bond network formed into the substrate-binding cavity of WT obelin, F88Y obelin, and aequorin clearly shows that the main cause determining different light emission colors of hydromedusan photoproteins is a different arrangement of the hydrogen-bond network near OH group of 6-(p-hydroxyphenyl) substituent of coelenterazine due to the presence of either Phe or Tyr residue. © 2014 FEBS.

Scopus
Держатели документа:
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Krasnoyarsk 660036, Russian Federation
Laboratory of Bioluminescence Biotechnology, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Russian Federation
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United States
IHuman Institute, ShanghaiTech University, Shanghai, China : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Natashin, P.V.; Markova, S.V.; Lee, J.; Vysotski, E.S.; Liu, Z.-J.

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9.


   
    Ecology of purple sulfur bacteria in the highly stratified meromictic Lake Shunet (Siberia, Khakassia) in 2002-2009 / D. Y. Rogozin, V. V. Zykov, A. G. Degermendzhi // Microbiology (Russian Federation). - 2012. - Vol. 81, Is. 6. - P727-735, DOI 10.1134/S0026261712060148 . - ISSN 0026-2617
Кл.слова (ненормированные):
bacteriochlorophyll a -- chemocline -- meromictic lake -- purple sulfur bacteria -- seasonal dynamics -- Bacteria (microorganisms) -- Chromatiaceae
Аннотация: Phototrophic sulfur bacteria form dense accumulations in the chemocline zones of stratified lakes where light reaches the sulfide-containing layers of water. Many works are dedicated to the ecophysiology of these microorganisms in meromictic lakes. However, the role of these microorganisms in the trophic network of these ecosystems, the ways of biomass utilization, and the contribution to the turnover of biogenic elements have so far been insufficiently understood. This work deals with the analysis of many years' seasonal dynamics of the biomass of purple sulfur bacteria and the physicochemical conditions of their environment in Lake Shunet (Siberia, Khakassia, Russia), unraveling the causes of their anomalous development in the chemocline of this lake, as well as the comparative analysis of such type of ecosystems. Lake Shunet is characterized by markedly pronounced stratification and the high density of purple sulfur bacteria (PSB) in the chemocline, which is comparable to that of Lake Mahoney (Canada) where the number of PSB is the greatest among those known in the world. It was shown that, in the period 2002-2009, the total amount of bacterio-chlorophyll a in the water column of Lake Shunet increased and did not correlate with the seasonal variations in temperature and illumination in the chemocline. It was established that PSB cells in the purple layer experienced the effect of self-shading. The sedimentation rate of purple sulfur bacteria in Lake Shunet was low due to the pronounced density gradient in the chemocline zone. Thus, the high number of PSB in the chemocline was due to the combination of strong illumination, a high sulfide concentration, and a high water density gradient, which was responsible for stable stratification and contributed to the accumulation of the cells in a narrow layer. The data obtained could be useful for the paleoreconstruction of climatically deter-mined changes in the level of the lake and its periods of meromixis by the presence of carotenoids and bacte-riochlorophylls in the bottom sediments. В© 2012 Pleiades Publishing, Ltd.

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

Доп.точки доступа:
Rogozin, D.Y.; Zykov, V.V.; Degermendzhi, A.G.

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10.


   
    Essence of life and multiformity of its realization: expected signatures of life [Text] / S. I. Bartsev ; ed. G Horneck [et al.] // SPACE LIFE SCIENCES: SEARCH FOR SIGNATURES OF LIFE, AND SPACE FLIGHT ENVIRONMENTAL EFFECTS ON THE NERVOUS SYSTEM. Ser. ADVANCES IN SPACE RESEARCH-SERIES : PERGAMON-ELSEVIER SCIENCE LTD, 2004. - Vol. 33: 2nd World Space Congress/34th COSPAR Scientific Assembly (OCT 10-19, 2002, HOUSTON, TX), Is. 8. - P. 1313-1317, DOI 10.1016/j.asr.2003.08.032. - Cited References: 23 . - ISBN 0273-1177
РУБ Engineering, Aerospace + Astronomy & Astrophysics + Biophysics + Geosciences, Multidisciplinary + Meteorology & Atmospheric Sciences
Рубрики:
COMPLEX NETWORKS
   EMERGENCE

   EVOLUTION

Кл.слова (ненормированные):
astrobiology -- signatures of life -- essence of life -- multiformity of life
Аннотация: The question on the essence of life as phenomenon is the key one for astrobiology, since the answer to this question determines "breadth of our outlook". Taking Earth's version of life as the pattern extremely under-estimates our estimation of the probability of life origin and respectively expected probability of extraterrestrial life discovery. In the paper the hypothetical key attribute of life in general is selected on the base of comparative analyses and deductive inference. Simulation conducted on the base of neural network model shows that the same function could be realized by means of great variety of structures, which originated in the course of an evolutionary process. So multiplicity of evolutionary outcomes essentially increases the probability of final result - realization of an integrated function providing fitness to environment. Life as the integrated function can be realized via great variety of development ways and structures. A logical consequence of definitions for life as phenomenon is suggested. Final one is "Life is specific organization of informational and energetic processes coupling, enabling choice-making, and displayed as anomalies of different kinds". Anomalies of visible form, mechanical movement, chemical composition and noticeable response are considered. Presented in the paper sweeping generalization is not rigorously proven, however it can play heuristic role in increasing the level of specificity of searching for extraterrestrial life. (C) 2004 COSPAR. Published by Elsevier Ltd. All rights reserved.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bartsev, S.I.; Horneck, G \ed.\; LevasseurRegourd, AC \ed.\; Rabin, BM \ed.\; Rabin, \ed.\

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11.


   
    Gene pool maintenance and the prospects for using a special-purpose luminous bacteria collection / E. K. Rodicheva [et al.] // Applied Biochemistry and Microbiology. - 1998. - Vol. 34, Is. 1. - P70-76 . - ISSN 0003-6838
Аннотация: The culture collection maintained at the Institute of Biophysics (IB), Siberian Division, Russian Academy of Sciences, is the only deposit in Russia and CIS which contains about 700 strains of five species of marine luminous bacteria sampled in various sites of the World Ocean. The strains collected are used for identification of luminous bacteria; studying their physiology, biochemistry, and cytology; and developing concepts of organization and metabolism of luminous bacteria under natural and laboratory conditions. Methods of their storage and practical use are developed. The results of these studies are summarized in a data bank, which will be incorporated into the general network of data banks on microbial cultures kept in Russia and into the international network of data banks on microorganisms (MSDN). Systematization of information on luminous bacteria possessing a unique visual marker allows their extensive use in basic research and genetic engineering, for environmental and medical applications, and for biotechnological purposes.

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

Доп.точки доступа:
Rodicheva, E.K.; Medvedeva, S.E.; Vydryakova, G.A.; Chugaeva, Yu.V.; Kuznetsov, A.M.

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12.


   
    H2O-Bridged Proton-Transfer Channel in Emitter Species Formation in Obelin Bioluminescence / S. F. Chen, E. S. Vysotski, Y. J. Liu // J. Phys. Chem. B. - 2021. - Vol. 125, Is. 37. - P10452-10458, DOI 10.1021/acs.jpcb.1c03985. - Cited References:50. - This work was supported by the Program of Shanghai Institute of Technology (no. YJ2016-42), the National Natural Science Foundation of China (21973005 and 21911530094), and the Russian Foundation for Basic Research (20-04-00085 and 19-14-53004). . - ISSN 1520-6106. - ISSN 1520-5207
РУБ Chemistry, Physical
Рубрики:
CHEMILUMINESCENT DECOMPOSITION
   FLUORESCENCE-SPECTRA

   MECHANISM

   QM/MM

Аннотация: Bioluminescence of a number of marine organisms is conditioned by Ca2+-regulated photoprotein (CaRP) with coelenterazine as the reaction substrate. The reaction product, coelenteramide, at the first singlet excited state (S-1) is the emitter of CaRP. The S-1-state coelenteramide is produced via the decomposition of coelenterazine dioxetanone. Experiments suggested that the neutral S-1-coelenteramide is the primary emitter species. This supposition contradicts with theoretical calculations showing that the anionic S-1-coelenteramide is a primary product of the decomposition of coelenterazine dioxetanone. In this study, applying molecular dynamic (MD) simulations and the hybrid quantum mechanics/molecular mechanics (QM/MM) method, we investigated a proton-transfer (PT) process taking place in CaRP obelin from Obelia longissima for emitter formation. Our calculations demonstrate a concerted PT process with a water molecule as a bridge between anionic S-1-coelenteramide and the nearest histidine residue. The low activation barrier as well as the strong hydrogen-bond network between the proton donor and the proton acceptor suggests a fast PT process comparable with that of the lifetime of excited anionic S-1-coelenteramide. The existence of the PT process eliminates the discrepancy between experimental and theoretical studies. The fast PT process at emitter formation can also take place in other CaRPs.

WOS
Держатели документа:
Shanghai Inst Technol, Sch Chem & Environm Engn, Shanghai 201418, Peoples R China.
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photo Biol Lab, Krasnoyarsk 660036, Russia.
Beijing Normal Univ Zhuhai, Ctr Adv Mat Res, Adv Inst Nat Sci, Zhuhai 519087, Peoples R China.
Beijing Normal Univ, Coll Chem, Key Lab Theoret & Computat Photochem, Minist Educ, Beijing 100875, Peoples R China.

Доп.точки доступа:
Chen, Shu-Feng; Vysotski, Eugene S.; Liu, Ya-Jun; Vysotski, Eugene; Program of Shanghai Institute of Technology [YJ2016-42]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [21973005, 21911530094]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085, 19-14-53004]

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13.


   
    H2O-Bridged Proton-Transfer Channel in Emitter Species Formation in Obelin Bioluminescence / S. -F. Chen, E. S. Vysotski, Y. -J. Liu // J Phys Chem B. - 2021, DOI 10.1021/acs.jpcb.1c03985 . - Article in press. - ISSN 1520-6106
Кл.слова (ненормированные):
Amino acids -- Excited states -- Hydrogen bonds -- Molecular dynamics -- Molecular modeling -- Molecules -- Phosphorescence -- Proton transfer -- Quantum theory -- Fast protons -- Marine organisms -- Photoproteins -- Primary products -- Proton transfer process -- Quantum mechanics/molecular mechanics -- Reaction substrates -- Singlet excited state -- Theoretical calculations -- Transfer channel -- Bioluminescence
Аннотация: Bioluminescence of a number of marine organisms is conditioned by Ca2+-regulated photoprotein (CaRP) with coelenterazine as the reaction substrate. The reaction product, coelenteramide, at the first singlet excited state (S1) is the emitter of CaRP. The S1-state coelenteramide is produced via the decomposition of coelenterazine dioxetanone. Experiments suggested that the neutral S1-coelenteramide is the primary emitter species. This supposition contradicts with theoretical calculations showing that the anionic S1-coelenteramide is a primary product of the decomposition of coelenterazine dioxetanone. In this study, applying molecular dynamic (MD) simulations and the hybrid quantum mechanics/molecular mechanics (QM/MM) method, we investigated a proton-transfer (PT) process taking place in CaRP obelin from Obelia longissima for emitter formation. Our calculations demonstrate a concerted PT process with a water molecule as a bridge between anionic S1-coelenteramide and the nearest histidine residue. The low activation barrier as well as the strong hydrogen-bond network between the proton donor and the proton acceptor suggests a fast PT process comparable with that of the lifetime of excited anionic S1-coelenteramide. The existence of the PT process eliminates the discrepancy between experimental and theoretical studies. The fast PT process at emitter formation can also take place in other CaRPs. © 2021 American Chemical Society.

Scopus
Держатели документа:
School of Chemical and Environmental Engineering, Shanghai Institute of Technology, Shanghai, 201418, China
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center, Krasnoyarsk Science Center SB RAS, Krasnoyarsk, 660036, Russian Federation
Center for Advanced Materials Research, Advanced Institute of Natural Sciences, Beijing Normal University at Zhuhai, Zhuhai, 519087, China
Key Laboratory of Theoretical and Computational Photochemistry, Ministry of Education, College of Chemistry, Beijing Normal University, Beijing, 100875, China

Доп.точки доступа:
Chen, S. -F.; Vysotski, E. S.; Liu, Y. -J.

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14.


   
    High-resolution structures of scytalone dehydratase-inhibitor complexes crystallized at physiological pH [Text] / Z. . Wawrzak [et al.] // Proteins. - 1999. - Vol. 35, Is. 4. - P. 425-439, DOI 10.1002/(SICI)1097-0134(19990601)35:4425::AID-PROT63.0.CO;2-1. - Cited References: 33 . - ISSN 0887-3585
РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
MAGNAPORTHE-GRISEA
   HEMAGGLUTININ

   GLYCOPROTEIN

   REFINEMENT

   MELANIN

   DISEASE

   SITE

Кл.слова (ненормированные):
structure-based design -- enzyme inhibitors -- X-ray crystallography -- fungicides -- melanin biosynthesis
Аннотация: Scytalone dehydratase is a molecular target of inhibitor design efforts aimed at preventing the fungal disease caused by Magnaporthe grisea. A method for cocrystallization of enzyme with inhibitors at neutral pH has produced several crystal structures of enzyme-inhibitor complexes at resolutions ranging from 1.5 to 2.2 Angstrom Four high resolution structures of different enzyme-inhibitor complexes are described. In contrast to the original X-ray structure of the enzyme, the four new structures have well-defined electron density for the loop region comprising residues 115-119 and a different conformation between residues 154 and 160. The structure of the enzyme complex with an aminoquinazoline inhibitor showed that the inhibitor is in a position to form a hydrogen bond with the amide of the Asn131 side chain and with two water molecules in a fashion similar to the salicylamide inhibitor in the original structure, thus confirming design principles. The aminoquinazoline structure also allows for a more confident assignment of donors and accepters in the hydrogen bonding network, The structures of the enzyme complexes with two dichlorocyclopropane carboxamide inhibitors showed the two chlorine atoms nearly in plane with the amide side chain of Asn131. The positions of Phe53 and Phe158 are significantly altered in the new structures in comparison to the two structures obtained from crystals grown at acidic pH, The multiple structures help define the mobility of active site amino acids critical for catalysis and inhibitor binding. Proteins 1999;35:425-439. (C) 1999 Wiley-Liss, Inc.

WOS
Держатели документа:
Dupont Co, Stine Haskell Res Ctr, Agr Prod, Newark, DE 19714 USA
Dupont Co, Expt Stn, Life Sci, Wilmington, DE USA
Karolinska Inst, Dept Med Biochem & Biophys, Stockholm, Sweden
Russian Acad Sci, Inst Biophys, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Wawrzak, Z...; Sandalova, T...; Steffens, J.J.; Basarab, G.S.; Lundqvist, T...; Lindqvist, Y...; Jordan, D.B.

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15.


   
    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. - 2018. - Vol. 8. - P435-436. - Cited References:0. - This work was supported by RFBR grant 17-04-00764 and a China-Russia international collaboration grant from the Chinese Academy of Sciences and the Natural Science Foundation of China. . - ISSN 2211-5463
РУБ Biochemistry & Molecular Biology


WOS
Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Fed Res Ctr, Photobiol Lab, Inst Biophys SB RAS, Krasnoyarsk, Russia.
ShanghaiTech Univ, IHuman Inst, Shanghai, Peoples R China.
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA.
Доп.точки доступа:
Vysotski, E.; Markova, S.; Natashin, P.; Stepanyuk, G.; Lee, J.; Malikova, N.; Liu, Z.; RFBR [17-04-00764]; China-Russia international collaboration grant from Chinese Academy of Sciences; Natural Science Foundation of China

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16.


   
    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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17.


   
    Naturally deducing estimate for the coefficient of CELSS closure [Text] / S. I. Bartsev ; ed. M Nelson [et al.] // SPACE LIFE SCIENCES: CLOSED ARTIFICIAL ECOSYSTEMS AND LIFE SUPPORT SYSTEMS. Ser. ADVANCES IN SPACE RESEARCH : PERGAMON-ELSEVIER SCIENCE LTD, 2003. - Vol. 31: Meeting of F4 1 Session of the 34th Scientific Assembly of COSPAR (OCT, 2002, HOUSTON, TEXAS), Is. 7. - P. 1675-1682, DOI 10.1016/S0273-1177(03)00107-8. - Cited References: 4 . - ISBN 0273-1177
РУБ Engineering, Aerospace + Astronomy & Astrophysics + Ecology + Geosciences, Multidisciplinary + Meteorology & Atmospheric Sciences

Аннотация: The term Closed Ecological System (CES) is in wide use. However there is no generally accepted measure of the closure of ecological systems. In order to obtain reproducibility of experiments with natural and man-made CES (with respect to degree of closure) some universal estimate needs to be developed. Understanding ecological systems as a network and closure as the degree of matter recycling allows the use of matrix graphs. Graphs are very natural forms for the presentation of the network of matter flows in ecosystems. An estimate equal to the sum of products of weights of oriented edges that constitute contour is suggested as a measure of the degree of closure in ecosystems. It is shown that this estimate can be uniformly applied to ecosystems of arbitrary size and configuration of flows. (C) 2003 COSPAR. Published by Elsevier Science Ltd. All rights reserved.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bartsev, S.I.; Nelson, M \ed.\; Pechurkin, NS \ed.\; Dempster, WF \ed.\; Somova, LA \ed.\; Somo, , LA \ed.\

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18.


   
    Neural networks playing 'matching pennies' with each other: reproducibility of game dynamics / T. Dolgova, S. Bartsev // INTERNATIONAL WORKSHOP ADVANCED TECHNOLOGIES IN MATERIAL SCIENCE, : IOP PUBLISHING LTD, 2019. - Vol. 537: International Workshop on Advanced Technologies in Material Science, (APR 04-06, 2019, Krasnoyarsk, RUSSIA). - Ст. 042002. - (IOP Conference Series-Materials Science and Engineering), DOI 10.1088/1757-899X/537/4/042002. - Cited References:18 . -
РУБ Engineering, Mechanical + Materials Science, Multidisciplinary
Рубрики:
REPRESENTATIONS
   CONSCIOUSNESS

Аннотация: Reflection is an essential feature of consciousness and possibly the single most important one. This fact allows us to simplify the objective of the concept of 'neural correlates of consciousness' and to focus investigations on reflection itself. Reflexive games are the concentrated and pure embodiment of reflection manifestation without the addition of other higher cognitive functions. In this paper, we use the game 'matching pennies' ("Odd-Even") in order to trace the strategies and possible patterns of recurrent neural network operation. Experimental results show the splitting of all considered game patterns into two groups. A significant difference was observed in these groups of patterns, indicating a qualitative difference in game dynamics apparently due to the qualitatively different dynamic patterns of neuron excitations of the networks. A similar splitting of all players into two groups was found by other authors for human players, which differ in terms of the reflection availability. By this, we can assume that one of the causes of the splitting is that the presence of reflection in a particular group of recurrent neural networks dramatically changes the game meta-strategy.

WOS
Держатели документа:
Siberian Fed Univ, 79 Svobodny Pr, Krasnoyarsk 660041, Russia.
RAS, SB, Inst Biophys, Fed Res Ctr,Krasnoyarsk Sci Ctr, 50 Akad Gorodok, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Dolgova, T.; Bartsev, S.

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19.


   
    Neural networks playing 'matching pennies' with each other: Reproducibility of game dynamics / T. Dolgova, S. Bartsev // IOP Conference Series: Materials Science and Engineering : Institute of Physics Publishing, 2019. - Vol. 537: International Workshop on Advanced Technologies in Material Science, Mechanical and Automation Engineering - MIP: Engineering-2019 (4 April 2019 through 6 April 2019, ) Conference code: 149243, Is. 4, DOI 10.1088/1757-899X/537/4/042002
Кл.слова (ненормированные):
Condensed matter physics -- Engineering -- Industrial engineering -- Materials science -- Cognitive functions -- Dynamic patterns -- Essential features -- Meta strategies -- Neural correlates of consciousness -- Neuron excitation -- Qualitative differences -- Reproducibilities -- Recurrent neural networks
Аннотация: Reflection is an essential feature of consciousness and possibly the single most important one. This fact allows us to simplify the objective of the concept of 'neural correlates of consciousness' and to focus investigations on reflection itself. Reflexive games are the concentrated and pure embodiment of reflection manifestation without the addition of other higher cognitive functions. In this paper, we use the game 'matching pennies' ("Odd-Even") in order to trace the strategies and possible patterns of recurrent neural network operation. Experimental results show the splitting of all considered game patterns into two groups. A significant difference was observed in these groups of patterns, indicating a qualitative difference in game dynamics apparently due to the qualitatively different dynamic patterns of neuron excitations of the networks. A similar splitting of all players into two groups was found by other authors for human players, which differ in terms of the reflection availability. By this, we can assume that one of the causes of the splitting is that the presence of reflection in a particular group of recurrent neural networks dramatically changes the game meta-strategy. © Published under licence by IOP Publishing Ltd.

Scopus,
Смотреть статью
Держатели документа:
Siberian Federal University, 2 79 Svobodny pr., Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Federal Research Center, Krasnoyarsk Scientific Center SB RAS, 50, Akademgorodok, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Dolgova, T.; Bartsev, S.

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20.


   
    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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Смотреть статью,
Scopus
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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