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Evolution and present status of experimental manned ecological systems for long-term human life support - Bios, developed by the institute of biophysics of Russian academy of sciences in Krasnoyarsk (Siberia) / J. I. Gitelson, A. G. Degermendzhy // Proceedings of the International Astronautical Congress, IAC : International Astronautical Federation, IAF, 2015. - Vol. 1: 66th International Astronautical Congress 2015: Space - The Gateway for Mankind's Future, IAC 2015 (12 October 2015 through 16 October 2015, ) Conference code: 122921. - P243-250
Кл.слова (ненормированные):
Arid regions -- Biochemistry -- Biospherics -- Plant shutdowns -- Proteins -- Reconfigurable hardware -- Closed ecological systems -- Corrective actions -- Essential proteins -- Extreme conditions -- Human intelligence -- Long-term experiments -- Physiological effects -- Russian Academy of Sciences -- Ecology
Аннотация: Closed ecological systems are of two-fold interest - as models of the Earth's biosphere explorable in experiments and as a facility for long-term autonomous human life support beyond the Earth. Theoretical analysis and experimental implementation of highly closed manned systems has been the subject of studies at the Institute of Biophysics (Russian Academy of Sciences, Siberian Branch) for many years. BIOS systems of increasing complexity with complete regeneration of atmosphere, water and partially food have been realized. In BIOS-3 experiments the system inhabited by 2-3 researchers for 4-6 months maintained its metabolic equilibrium without any negative physiological effect on the crew, which proves its sustainable condition. Specific for BIOS-3 is internal control by the people inhabiting the system. So, BIOS-3 is the first experimental implementation of V.l. Vernadsky's idea about the noosphere - habitable Biosphere controlled by human intelligence. Contrary to predictions of many environmentalists the closedness of the ecosystem is a factor that does not reduce, but increases its sustainability and makes its use for reliable life support outside the Earth realistic. The system is sustainable owing to permanent feedback between the monitoring of few key parameters of the system and automatic corrective actions on them. Main object of control is photo-biosynthesis regenerating parameters of human habitat disturbed by his vital activities. This principle has been realized in BIOS system and proved its reliability in long-term experiments. A new challenge is specified-optimal increase of trophic closedness of the system by reproduction within it essential proteins (peptides and amino acids), lipids, vitamins and other essential compounds. Alternative lines of attack on this problem by state-of-the-art biotechnological methods, GMO including, are under analysis. Reduced BIOS version - without complete closure - can be a breakthrough instrument to improve the quality of life of people living under extreme conditions on the Earth - in polar latitudes (Arctic, Antarctic), in deserts, in high mountains.

Scopus
Держатели документа:
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Gitelson, J. I.; Degermendzhy, A. G.

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Battle of GLP-1 delivery technologies / M. Yu [et al.] // Adv. Drug Deliv. Rev. - 2018, DOI 10.1016/j.addr.2018.07.009 . - ISSN 0169-409X
Кл.слова (ненормированные):
Albumin fusion -- Exenatide -- Fatty acid conjugate -- Fc fusion -- GLP-1 receptor agonist -- Half-life -- Peptide delivery -- Pharmacokinetics
Аннотация: Glucagon-like peptide-1 receptor agonists (GLP-1 RAs) belong to an important therapeutic class for treatment of type 2 diabetes. Six GLP-1 RAs, each utilizing a unique drug delivery strategy, are now approved by the Food and Drug Administration (FDA) and additional, novel GLP-1 RAs are still under development, making for a crowded marketplace and fierce competition among the manufacturers of these products. As rapid elimination is a major challenge for clinical application of GLP-1 RAs, various half-life extension strategies have been successfully employed including sequential modification, attachment of fatty-acid to peptide, fusion with human serum albumin, fusion with the fragment crystallizable (Fc) region of a monoclonal antibody, sustained drug delivery systems, and PEGylation. In this review, we discuss the scientific rationale of the various half-life extension strategies used for GLP-1 RA development. By analyzing and comparing different approved GLP-1 RAs and those in development, we focus on assessing how half-life extending strategies impact the pharmacokinetics, pharmacodynamics, safety, patient usability and ultimately, the commercial success of GLP-1 RA products. We also anticipate future GLP-1 RA development trends. Since similar drug delivery strategies are also applied for developing other therapeutic peptides, we expect this case study of GLP-1 RAs will provide generalizable concepts for the rational design of therapeutic peptides products with extended duration of action. © 2018 Elsevier B.V.

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Держатели документа:
Department of Pharmaceutical Sciences, College of Pharmacy, University of Michigan, 428 Church St, Ann Arbor, MI, United States
Amneal Pharmaceuticals, 50 Horseblock Rd, Brookhaven, NY, United States
Siberian Federal University, 79 Svobodnuy Ave, Krasnoyarsk, Russian Federation
Institute of Biophysics SBRAS, 50 Akademgorodok, Russian Federation
Biointerfaces Institute, NCRC, 2800 Plymouth Rd, Ann Arbor, MI, United States
Department of Biomedical Engineering, 2200 Bonisteel Blvd, Ann Arbor, MI, United States

Доп.точки доступа:
Yu, M.; Benjamin, M. M.; Srinivasan, S.; Morin, E. E.; Shishatskaya, E. I.; Schwendeman, S. P.; Schwendeman, A.

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Molecular insights into ligand recognition and G protein coupling of the neuromodulatory orphan receptor GPR139 / Y. L. Zhou, H. Daver, B. Trapkov [et al.] // Cell Res. - 2021, DOI 10.1038/s41422-021-00591-w. - Cited References:16. - This work was supported by the CAS Strategic Priority Research Program XDB37030104 (Z.-J.L.), the National Science Fund for Distinguished Young Scholars 32022038 (T.H.), the National Natural Science Foundation of China grants 31930060 (Z.-J.L.) and 31870744 (T.H.), and the Shanghai Rising-Star Program 20QA1406500 (T. H.), the Lundbeck Foundation R163-2013-16327 (D.E.G.), the Novo Nordisk Foundation NNF18OC0031226 (D.E.G.) and Independent Research Fund Denmark | Natural Sciences 8021-00173B (D.E.G.), the Lundbeck Foundation R355-2020-949 (B.T.) and the Carlsberg Foundation CF20-0248 (H.B.-O.). D.E.G. is a member of the Integrative Structural Biology at the University of Copenhagen (ISBUC). The cryo-EM data were collected at the Bio-Electron Microscopy Facility, ShanghaiTech University, with the assistance of Q.-Q. Sun, D.-D. Liu, Z.-H. Zhang and Y.-H. Liu. We thank the Assay Core, the assistance of F.-F. Zhou and Q.-W. Tan and the Cell Expression, Cloning and Purification Core Facilities of iHuman Institute for their support. . - Article in press. - ISSN 1001-0602. - ISSN 1748-7838

РУБ Cell Biology
Рубрики:
DISCOVERY
PEPTIDES
ALPHA

WOS
Держатели документа:
ShanghaiTech Univ, iHuman Inst, Shanghai, Peoples R China.
ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai, Peoples R China.
Univ Chinese Acad Sci, Beijing, Peoples R China.
Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, CAS Ctr Excellence Mol Cell Sci, Shanghai, Peoples R China.
Univ Copenhagen, Dept Drug Design & Pharmacol, Univ Pk 2, Copenhagen, Denmark.
Krasnoyarsk Sci Ctr SB RAS, Fed Res Ctr, Inst Biophys SB RAS, Photobiol Lab, Akad Gorodok 50-50, Krasnoyarsk, Russia.

Доп.точки доступа:
Zhou, Yali; Daver, Henrik; Trapkov, Boris; Wu, Lijie; Wu, Meng; Harpsoe, Kasper; Gentry, Patrick R.; Liu, Kaiwen; Larionova, Marina; Liu, Junlin; Chen, N.a.; Brauner-Osborne, Hans; Gloriam, David E.; Hua, Tian; Liu, Zhi-Jie; CAS Strategic Priority Research Program [XDB37030104]; National Science Fund for Distinguished Young ScholarsNational Natural Science Foundation of China (NSFC)National Science Fund for Distinguished Young Scholars [32022038]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31930060, 31870744]; Shanghai Rising-Star Program [20QA1406500]; Lundbeck FoundationLundbeckfonden [R355-2020-949, R163-2013-16327]; Novo Nordisk FoundationNovo Nordisk FoundationNovocure Limited [NNF18OC0031226]; Independent Research Fund Denmark | Natural Sciences [8021-00173B]; Carlsberg FoundationCarlsberg Foundation [CF20-0248]

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Novel Mechanism of Bioluminescence: Oxidative Decarboxylation of a Moiety Adjacent to the Light Emitter of Fridericia Luciferin [Text] / M. A. Dubinnyi [et al.] // Angew. Chem.-Int. Edit. - 2015. - Vol. 54, Is. 24. - P7065-7067, DOI 10.1002/anie.201501668. - Cited References:15. - We thank Dr. K.V. Antonov for acquisition of LC-HRMS spectra and Prof. Gary Schuster for fruitful discussion. This work was supported by the Russian Science Foundation grant 14-50-00131. M.S.B. acknowledges support by a stipend program of the President of the Russian Federation. K.M.S. acknowledges generous support from the National Science Foundation (CHE-1213047). This research was carried out using the equipment provided by IBCH core facility (CKP IBCH). . - ISSN 1433-7851. - ISSN 1521-3773

РУБ Chemistry, Multidisciplinary
Рубрики:
STRUCTURE ELUCIDATION
CHEMILUMINESCENCE
CYPRIDINA
Кл.слова (ненормированные):
bioluminescence -- bioorganic chemistry -- luciferin -- oxidative -- decarboxylation -- peptides
Аннотация: A novel luciferin from a bioluminescent Siberian earthworm Fridericia heliota was recently described. In this study, the Fridericia oxyluciferin was isolated and its structure elucidated. The results provide insight into a novel bioluminescence mechanism in nature. Oxidative decarboxylation of a lysine fragment of the luciferin supplies energy for light generation, while a fluorescent CompX moiety remains intact and serves as the light emitter.

WOS
Держатели документа:
Russian Acad Sci, Inst Bioorgan Chem, Moscow 117997, Russia.
Pirogov Russian Natl Res Med Univ, Moscow 117997, Russia.
Russian Acad Sci, Akademgorodok, Siberian Branch, Lab Photobiol,Inst Biophys, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Branch Shemyakin, Pushchino 142290, Russia.
Russian Acad Sci, Ovchinnikov Inst Bioorgan Chem, Pushchino 142290, Russia.

Доп.точки доступа:
Dubinnyi, Maxim A.; Kaskova, Zinaida M.; Rodionova, Natalja S.; Baranov, Mikhail S.; Gorokhovatsky, Andrey Yu.; Kotlobay, Alexey; Solntsev, Kyril M.; Tsarkova, Aleksandra S.; Petushkov, Valentin N.; Yampolsky, Ilia V.; Russian Science Foundation [14-50-00131]; President of the Russian Federation; National Science Foundation [CHE-1213047]

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CONFORMATIONAL FEATURES OF GAMMA-GLUTAMYL-CONTAINING PEPTIDES [Текст] / T. P. SANDALOVA, P. I. BELOBROV // Bioorg. Khim. - 1983. - Vol. 9, Is. 8. - С. 1013-1020. - Cited References: 23 . - 8. - ISSN 0132-3423

РУБ Biochemistry & Molecular Biology + Chemistry, Organic

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

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CONFORMATIONAL FEATURES OF GAMMA-GLUTAMYL-CONTAINING PEPTIDES [Текст] / T. P. SANDALOVA, P. I. BELOBROV // Bioorg. Khim. - 1983. - Vol. 9, Is. 8. - P. 1013-1020. - Cited References: 23 . - ISSN 0132-3423

РУБ Biochemistry & Molecular Biology + Chemistry, Organic

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

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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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