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1Academic Journal
Πηγή: IX Всероссийская Пущинская конференция «Биохимия, физиология и биосферная роль микроорганизмов».
Θεματικοί όροι: гетерологичная экспрессия, фитостерин, биотрансформация стероидов, тестостерон, миколицибактерии, 3-кетостероид-1(2)-дегидрогеназа, 17β-гидроксистероиддегидрогеназа
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2Academic Journal
Πηγή: Вестник защиты растений, Vol 107, Iss 3 (2024)
Θεματικοί όροι: 0301 basic medicine, гетерологичная экспрессия, 0303 health sciences, 03 medical and health sciences, поликлональные антитела, Plant culture, биологическая защита растений, SB1-1110
Σύνδεσμος πρόσβασης: https://doaj.org/article/f8d7c16bccb442979cbf84d3084108b2
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3Academic Journal
Συγγραφείς: V. V. Bykov, A. A. Vologzhannikova, M. V. Trunilina, T. A. Kudryashov, A. S. Sokolov, Yu. S. Lapteva, В. В. Быков, А. А. Вологжанникова, М. В. Трунилина, Т. А. Кудряшов, А. С. Соколов, Ю. С. Лаптева
Συνεισφορές: Работа выполнена при финансовой поддержке Российского научного фонда, грант № 23-24-00563 (Соколов А.С.).
Πηγή: Acta Biomedica Scientifica; Том 9, № 5 (2024); 75-83 ; 2587-9596 ; 2541-9420
Θεματικοί όροι: удаление N-концевого метионина, Thermus thermophilus, heterologous expression, removal of N-terminal methionine, гетерологичная экспрессия
Περιγραφή αρχείου: application/pdf
Relation: https://www.actabiomedica.ru/jour/article/view/5036/2902; Gamerdinger M, Deuerling E. Cotranslational sorting and processing of newly synthesized proteins in eukaryotes. Trends Biochem Sci. 2024; 49(2): 105-118. doi:10.1016/j.tibs.2023.10.003; Chen L, Kashina A. Post-translational modifications of the protein termini. Front Cell Dev Biol. 2021; 9: 719590. doi:10.3389/fcell.2021.719590; Nguyen KT, Kim JM, Park SE, Hwang CS. N-terminal methionine excision of proteins creates tertiary destabilizing N-degrons of the Arg/N-end rule pathway. J Biol Chem. 2019; 294(12): 4464-4476. doi:10.1074/jbc.RA118.006913; Wingfield PT. N-terminal methionine processing. Curr Protoc Protein Sci. 2017; 88: 6.14.1-6.14.3. doi:10.1002/cpps.29; Arif A, Mohammed K, Nadeem MS. Biochemical and in silico evaluation of recombinant E. coli aminopeptidase and in vitro processed human interferon alpha-2b. Turk J Biol. 2018; 42(3): 240-249. doi:10.3906/biy-1801-83; Rawlings ND. Using the MEROPS database for investigation of lysosomal peptidases, their inhibitors, and substrates. Methods Mol Biol. 2017; 1594: 213-226. doi:10.1007/978-1-4939-6934-0_14; Roderick SL, Matthews BW. Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: A new type of proteolytic enzyme. Biochemistry. 1993; 32(15): 3907-3912. doi:10.1021/bi00066a009; D’souza VM, Bennett B, Copik AJ, Holz RC. Divalent metal binding properties of the methionyl aminopeptidase from Escherichia coli. Biochemistry. 2000;39(13):3817-3826. doi:10.1021/bi9925827; Meng L, Ruebush S, D’souza VM, Copik AJ, Tsunasawa S, Holz RC. Overexpression and divalent metal binding properties of the methionyl aminopeptidase from Pyrococcus furiosus. Biochemistry. 2002; 41(23): 7199-7208. doi:10.1021/bi020138p; Bala S, Reddi B, Addlagatta A. A single amino acid difference between archaeal and human type 2 methionine aminopeptidases differentiates their affinity towards ovalicin. Biochim Biophys Acta Proteins Proteom. 2023; 1871(2): 140881. doi:10.1016/j.bbapap.2022.140881; Bala SC, Haque N, Pillalamarri V, Reddi R, Kashyap R, Marapaka AK, et al. Discovery of a new class of type 1 methionine aminopeptidases that have relaxed substrate specificity. Int J Biol Macromol. 2019; 129: 523-529. doi:10.1016/j.ijbiomac.2019.02.055; Arya T, Reddi R, Kishor C, Ganji RJ, Bhukya S, Gumpena R, et al. Identification of the molecular basis of inhibitor selectivity between the human and streptococcal type I methionine aminopeptidases. J Med Chem. 2015; 58(5): 2350-2357. doi:10.1021/jm501790e; Goya Grocin A, Kallemeijn WW, Tate EW. Targeting methionine aminopeptidase 2 in cancer, obesity, and autoimmunity. Trends Pharmacol Sci. 2021; 42(10): 870-882. doi:10.1016/j.tips.2021.07.004; Friese-Hamim M, Ortiz Ruiz MJ, Bogatyrova O, Keil M, Rohdich F, Blume B, et al. Novel methionine aminopeptidase 2 inhibitor M8891 synergizes with VEGF receptor inhibitors to inhibit tumor growth of renal cell carcinoma models. Mol Cancer Ther. 2024; 23(2): 159-173. doi:10.1158/1535-7163.MCT-23-0102; Watanabe N, Saito-Nakano Y, Kurisawa N, Otomo K, Suenaga K, Nakano K, et al. Fumagillin inhibits growth of the enteric protozoan parasite Entamoeba histolytica by covalently binding to and selectively inhibiting methionine aminopeptidase 2. Antimicrob Agents Chemother. 2023; 67(11): e0056023. doi:10.1128/aac.00560-23; Carducci MA, Wang D, Habermehl C, Bödding M, Rohdich F, Lignet F, et al. A first-in-human, dose-escalation study of the methionine aminopeptidase 2 inhibitor M8891 in patients with advanced solid tumors. Cancer Res Commun. 2023; 3(8): 1638-1647. doi:10.1158/2767-9764.CRC-23-0048; Steinberg E, Esa R, Schwob O, Stern T, Orehov N, Zamir G, Hubert A, et al. Methionine aminopeptidase 2 as a potential target in pancreatic ductal adenocarcinoma. Am J Transl Res. 2022; 14(9): 6243-6255.; Helgren TR, Chen C, Wangtrakuldee P, Edwards TE, Staker BL, Abendroth J, et al. Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents. Bioorg Med Chem. 2017; 25(3): 813-824. doi:10.1016/j.bmc.2016.11.013; Zhang M, He S, Han X, Cui J, Wang H, Huo X, et al. Discovery of potential antituberculosis agents targeted methionine aminopeptidase 1 of Mycobacterium tuberculosis by the developed fluorescent probe. Anal Chem. 2023; 95(44): 16210-16215. doi:10.1021/acs.analchem.3c02952; Ye M, Xiong L, Dong Y, Xie C, Zhang Z, Shen L, et al. The potential role of the methionine aminopeptidase gene PxMetAP1 in a cosmopolitan pest for Bacillus thuringiensis toxin tolerance. Int J Mol Sci. 2022; 23(21): 13005. doi:10.3390/ijms232113005; Reddi B, Kishor C, Jangam A, Bala S, Rajeswari Batchu U, Gundla R, et al. Regioselectivity in inhibition of peptide deformylase from Haemophilus influenzae by 4- vs 5-azaindole hydroxamic acid derivatives: Biochemical, structural and antimicrobial studies. Bioorg Chem. 2022; 128: 106095. doi:10.1016/j.bioorg.2022.106095; Bala S, Yellamanda KV, Kadari A, Ravinuthala VSU, Kattula B, Singh OV, et al. Selective inhibition of Helicobacter pylori methionine aminopeptidase by azaindole hydroxamic acid derivatives: Design, synthesis, in vitro biochemical and structural studies. Bioorg Chem. 2021; 115: 105185. doi:10.1016/j.bioorg.2021.105185; Nandan A, Nampoothiri KM. Therapeutic and biotechnological applications of substrate specific microbial aminopeptidases. Appl Microbiol Biotechnol. 2020; 104(12): 5243-5257. doi:10.1007/s00253-020-10641-9; Pasquini M, Grosjean N, Hixson KK, Nicora CD, Yee EF, Lipton M, et al. Zng1 is a GTP-dependent zinc transferase needed for activation of methionine aminopeptidase. Cell Rep. 2022; 39(7): 110834. doi:10.1016/j.celrep.2022.110834; Baker RT, Catanzariti AM, Karunasekara Y, Soboleva TA, Sharwood R, Whitney S, et al. Using deubiquitylating enzymes as research tools. Methods Enzymol. 2005; 398: 540-554. doi:10.1016/S0076-6879(05)98044-0; Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 1995; 4(11): 2411-2423. doi:10.1002/pro.5560041120; You C, Lu H, Sekowska A, Fang G, Wang Y, Gilles AM, et al. The two authentic methionine aminopeptidase genes are differentially expressed in Bacillus subtilis. BMC Microbiol. 2005; 5: 57. doi:10.1186/1471-2180-5-57; Sievers F, Higgins DG. Clustal Omega for making accurate alignments of many protein sequences. Protein Sci. 2018; 27(1): 135-145. doi:10.1002/pro.3290; Reddi R, Arya T, Kishor C, Gumpena R, Ganji RJ, Bhukya S, et al. Selective targeting of the conserved active site cysteine of Mycobacterium tuberculosis methionine aminopeptidase with electrophilic reagents. FEBS J. 2014; 281(18): 4240-4248. doi:10.1111/febs.12847; Irfan I, Ali A, Reddi B, Khan MA, Hasan P, Ahmed S, et al. Design, synthesis and mechanistic studies of novel isatin-pyrazole hydrazone conjugates as selective and potent bacterial MetAP inhibitors. Antibiotics (Basel). 2022; 11(8): 1126. doi:10.3390/antibiotics11081126; Lapteva YS, Bykov VV, Trunilina MV, Boldaevsky IS, Kudryashov TA, Vologzhannikova AA, et al. Obtaining overstable methionine aminopeptidase for the removal of methionine from recombinant proteins. Journal Biomed. 2023; 19(3E): 47-51. doi:10.33647/2713-0428-19-3Е-47-51; https://www.actabiomedica.ru/jour/article/view/5036
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4Academic Journal
Συγγραφείς: M. A. Vinter, I. S. Kazlouski, A. I. Zinchenko, М. А. Винтер, И. С. Казловский, А. И. Зинченко
Πηγή: Doklady of the National Academy of Sciences of Belarus; Том 66, № 5 (2022); 509-516 ; Доклады Национальной академии наук Беларуси; Том 66, № 5 (2022); 509-516 ; 2524-2431 ; 1561-8323 ; 10.29235/1561-8323-2022-66-5
Θεματικοί όροι: цикло-ди-АМФ, genetic engineering, recombinant strain, Bacillus thuringiensis, heterologous gene expression, inclusion bodies, diadenylate cyclase, cyclo-di-AMP, генная инженерия, рекомбинантный штамм, гетерологичная экспрессия гена, тельца включения, диаденилатциклаза
Περιγραφή αρχείου: application/pdf
Relation: https://doklady.belnauka.by/jour/article/view/1090/1093; A decade of research on the second messenger c-di-AMP / W. Yin [et al.] // FEMS Microbiol. Rev. – 2020. – Vol. 44, N 6. – P. 701–724. https://doi.org/10.1093/femsre/fuaa019; Intranasal delivery of influenza rNP adjuvanted with c-di-AMP induces strong humoral and cellular immune responses and provides protection against virus challenge / M. V. Sanchez [et al.] // PLoS ONE. – 2014. – Vol. 9, N 8. – Art. e104824. https://doi.org/10.1371/journal.pone.0104824; Cyclic di-adenosine monophosphate: a promising adjuvant candidate for the development of neonatal vaccines / D. Lirussi [et al.] // Pharmaceutics. – 2021. – Vol. 13, N 2. – Art. 188. https://doi.org/10.3390/ pharmaceutics13020188; Yan, H. The Promise and challenges of cyclic dinucleotides as molecular adjuvants for vaccine development / H. Yan, W. Chen // Vaccines. – 2021. – Vol. 9, N 8. – Art. 917. https://doi.org/10.3390/vaccines9080917; Chemical synthesis, purification, and characterization of 3′-5′-linked canonical cyclic dinucleotides (CDNs) / C. Wang [et al.] // Meth. Enzymol. – 2019. – Vol. 625. – P. 41−59. https://doi.org/10.1016/bs.mie.2019.04.022; Villaverde, A. Protein aggregation in recombinant bacteria: Biological role of inclusion bodies / A. Villaverde, M. M. Carrio // Biotechnol. Lett. – 2003. – Vol. 25, N 17. – P. 1385–1395. https://doi.org/10.1023/a:1025024104862; Schramm, F. D. Protein aggregation in bacteria / F. D. Schramm, K. Schroeder, K. Jonas // FEMS Microbiol. Rev. – 2020. – Vol. 44, N 1. – P. 54–72. https://doi.org/10.1093/femsre/fuz026; Enzymatic synthesis of 2′-ara and 2′-deoxy analogues of c-di-GMP / A. S. Shchokolova [et al.] // Nucleos. Nucleot. Nucl. Acids. – 2015. – Vol. 34, N 6. – P. 416–423. https://doi.org/10.1080/15257770.2015.1006775; Thermostable adenosine 5′-monophosphate phosphorylase from Thermococcus kodakarensis forms catalytically active inclusion bodies / S. Kamel [et al.] // Sci. Rep. – 2021. – Vol. 11, N 1. – Art. 16880. https://doi.org/10.1038/s41598- 021-96073-5; Re-engineered BCG overexpressing cyclic di-AMP augments trained immunity and exhibits improved efficacy against bladder cancer / A. K. Singh [et al.] // Nat. Commun. – 2022. – Vol. 13, N 1. – Art. 878. https://doi.org/10.1038/s41467- 022-28509-z; Cyclic di-AMP homeostasis in Bacillus subtilis: both lack and high level accumulation of the nucleotide are detrimental for cell growth / F. M. Mehne [et al.] // J. Biol. Chem. – 2013. – Vol. 288, N 3. – P. 2004–2017. https://doi.org/10.1074/jbc. m112.395491; Создание рекомбинантного штамма Escherichia coli – продуцента диаденилатциклазы и ее использование для синтеза цикло-ди-АМФ / И. С. Казловский [и др.] // Вес. Нац. акад. навук Беларусi. Сер. бiял. навук. – 2015. – № 4. – С. 51–55.; Green, M. R. Molecular cloning. A laboratory manual. 4th ed. / M. R. Green, J. Sambrook. – New York, 2012. – 630 p.; Quan, J. Circular polymerase extension cloning of complex gene libraries and pathways / J. Quan, J. Tian // PLoS ONE. – 2009. – Vol. 4, N 7. – Art. e6441. https://doi.org/10.1371/journal.pone.0006441; Challenges associated with the formation of recombinant protein inclusion bodies in Escherichia coli and strategies to address them for industrial applications / A. Bhatwa [et al.] // Front. Bioeng. Biotechnol. – 2021. – Vol. 9. – Art. 630551. https:// doi.org/10.3389/fbioe.2021.630551; https://doklady.belnauka.by/jour/article/view/1090
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5Academic Journal
Συγγραφείς: O. L. Terekhina, A. V. Lobanov, O. P. Dmitrenko, N. N. Lobanova, M. K. Nurbekov
Πηγή: Nauchno-prakticheskii zhurnal «Patogenez». :148-152
Θεματικοί όροι: recombinant protein S100B, аналитическая и препаративная экспрессия белков, рекомбинантный белок S100B, cloning and expression strategy, metal affinity protein chromatography, disulfide bonds, фолдинг белка, 3. Good health, 03 medical and health sciences, 0302 clinical medicine, Genome compiler, protein folding, металл-аффинная хроматография белков, гетерологичная экспрессия кДНК, pBT7-N-His vector system, стратегия клонирования и экспрессии, дисульфидные связи, analytical and preparative protein expression, векторная система pBT7-N-His, heterologous cDNA expression
Σύνδεσμος πρόσβασης: http://pathogenesis.pro/index.php/pathogenesis/article/download/253/221
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6Academic Journal
Συγγραφείς: D. M. Davidov, O. P. Dmitrenko, O. L. Terekhina, M. K. Nurbekov
Πηγή: Nauchno-prakticheskii zhurnal «Patogenez». :161-164
Θεματικοί όροι: recombinant protein S100B, аналитическая и препаративная экспрессия белков, рекомбинантный белок S100B, cloning and expression strategy, metal affinity protein chromatography, оптимизация гетерологичной экспрессии, фолдинг белка, 03 medical and health sciences, 0302 clinical medicine, Genome compiler, protein folding, металл-аффинная хроматография белков, гетерологичная экспрессия кДНК, рекомбинантная плазмида, pBT7-N-His vector system, analytical and preparative protein expression, векторная система pBT7-N-His, heterologous cDNA expression
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7Academic Journal
Συγγραφείς: A. V. Nezhdanova, M. A. Slugina, E. A. Dyachenko, A. M. Kamionskaya, E. Z. Kochieva, A. V. Shchennikova, А. В. Нежданова, М. А. Слугина, Е. А. Дьяченко, А. М. Камионская, Е. З. Кочиева, А. В. Щенникова
Συνεισφορές: This work was supported by the Russian Foundation for Basic Research (No. 18-29-07007) and the Ministry of Science and Higher Education of the Russian Federation, and was performed using the experimental climate control facility in the Institute of Bioengineering (Research Center of Biotechnology, Russian Academy of Sciences).
Πηγή: Vavilov Journal of Genetics and Breeding; Том 25, № 5 (2021); 492-501 ; Вавиловский журнал генетики и селекции; Том 25, № 5 (2021); 492-501 ; 2500-3259 ; 10.18699/VJ21.052
Θεματικοί όροι: SlMADS5, Nicotiana tabacum, heterologous gene expression, MADS-domain transcription factors, SEPALLATA, гетерологичная экспрессия гена, MADS-транскрипционные факторы
Περιγραφή αρχείου: application/pdf
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DOI 10.1023/a:1025001402838.; Castillejo C., Romera-Branchat M., Pelaz S. A new role of the Arabidopsis SEPALLATA3 gene revealed by its constitutive expression. Plant J. 2005;43(4):586-596. DOI 10.1111/j.1365-313X.2005.02476.x.; Coen E.S., Meyerowitz E.M. The war of the whorls: genetic interactions controlling flower development. Nature. 1991;353(6339):31-37. DOI 10.1038/353031a0.; Ditta G., Pinyopich A., Robles P., Pelaz S., Yanofsky M.F. The SEP4 gene of Arabidopsis thaliana functions in floral organ and meristem identity. Curr. Biol. 2004;14(21):1935-1940. DOI 10.1016/j.cub.2004.; Dong T., Hu Z., Deng L., Wang Y., Zhu M., Zhang J., Chen G. A tomato MADS-box transcription factor, SlMADS1, acts as a negative regulator of fruit ripening. Plant Physiol. 2013;163(2):1026-1036. DOI 10.1104/pp.113.224436.; Dyachenko E.A., Slugina М.А. Intraspecific variability of the Sus1 sucrose synthase gene in Pisum sativum accessions. 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8Academic Journal
Συγγραφείς: Ширшикова, Галина, Хуснутдинова, Анна, Цыганков, Анатолий, Бутанаев, Александр
Θεματικοί όροι: NI-FE ГИДРОГЕНАЗА, ГЕТЕРОЛОГИЧНАЯ ЭКСПРЕССИЯ, ПУРПУРНЫЕ БАКТЕРИИ
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9Academic Journal
Πηγή: Известия Тульского государственного университета. Естественные науки.
Θεματικοί όροι: NI-FE ГИДРОГЕНАЗА, ГЕТЕРОЛОГИЧНАЯ ЭКСПРЕССИЯ, ПУРПУРНЫЕ БАКТЕРИИ
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Συγγραφείς: Шарипова Маргарита Рашидовна
Συνεισφορές: Институт фундаментальной медицины и биологии, Казанский федеральный университет
Θεματικοί όροι: клонирование, трансформация, гетерологичная экспрессия, вектор экспрессии, вертор-амплификатор, фьюжн-вектор, векторы для отбора, интегративный вектор, челночный вектор, Биология
Διαθεσιμότητα: https://openrepository.ru/article?id=440591
