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Journal articles on the topic 'Proteinaceou'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

О.В., Скрипко. "ИЗУЧЕНИЕ ФУНКЦИОНАЛЬНО-ТЕХНОЛОГИЧЕСКИХ СВОЙСТВ БЕЛКОВО-ВИТАМИННЫХ И БЕЛКОВО-УГЛЕВОДНЫХ ДОБАВОК НА ОСНОВЕ СОИ". Bulletin of KSAU, № 3 (19 березня 2020): 150–56. http://dx.doi.org/10.36718/1819-4036-2020-3-150-156.

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Цель исследования – изучение функционально-технологических свойств разработанных в ФГБНУ ВНИИ сои инновационных пищевых добавок в виде белково-витаминных концентратов (БВК) и белково-углеводных гранулятов (БУГ). Задачи исследования: определить растворимость в воде БВК в виде гранул и муки, а также БУГ в гранулированном виде; установить продолжительность набухания муки и гранул БУГ и БВК; определить водосвязывающую (ВСС) и водопоглотительную (ВПС) способность БВК и БУГ в гранулированном и диспергированном виде. В результате исследования изучены основные функционально-технологические свойства: р

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2

Fuxreiter, Monika, Ágnes Tóth-Petróczy, Daniel A. Kraut, et al. "Disordered Proteinaceous Machines." Chemical Reviews 114, no. 13 (2014): 6806–43. http://dx.doi.org/10.1021/cr4007329.

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3

Chandna, Sanya, Monarch Shah, and Ankit Agrawal. "PROTEINACEOUS COVID-19." Chest 158, no. 4 (2020): A551. http://dx.doi.org/10.1016/j.chest.2020.08.521.

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4

Akhunzada, Zahir S., Mario Hubert, Erinc Sahin, and James Pratt. "Separation, Characterization and Discriminant Analysis of Subvisible Particles in Biologics Formulations." Current Pharmaceutical Biotechnology 20, no. 3 (2019): 232–44. http://dx.doi.org/10.2174/1389201020666190214100840.

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Background:The presence of subvisible particles (SVPs) in parenteral formulations of biologics is a major challenge in the development of therapeutic protein formulations. Distinction between proteinaceous and non-proteinaceous SVPs is vital in monitoring formulation stability.Methods:The current compendial method based on light obscuration (LO) has limitations in the analysis of translucent/low refractive index particles. A number of attempts have been made to develop an unambiguous method to characterize SVPs, albeit with limited success.Results:Herein, we describe a robust method that chara

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Deaton, J., C. Savva, J. Sun, et al. "GroEL: A Proteinaceous “Surfactant” ?" Microscopy and Microanalysis 8, S02 (2002): 840–41. http://dx.doi.org/10.1017/s1431927602102558.

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6

Svensson, Birte, Kenji Fukuda, Peter K. Nielsen та Birgit C. Bønsager. "Proteinaceous α-amylase inhibitors". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1696, № 2 (2004): 145–56. http://dx.doi.org/10.1016/j.bbapap.2003.07.004.

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7

Gusakov, A. V. "Proteinaceous inhibitors of microbial xylanases." Biochemistry (Moscow) 75, no. 10 (2010): 1185–99. http://dx.doi.org/10.1134/s0006297910100019.

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8

Braun, R., E. Brachtl, and M. Grasmug. "Codigestion of Proteinaceous Industrial Waste." Applied Biochemistry and Biotechnology 109, no. 1-3 (2003): 139–54. http://dx.doi.org/10.1385/abab:109:1-3:139.

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9

Fuxreiter, Monika, Ágnes Tóth-Petróczy, Daniel A. Kraut, et al. "Correction to Disordered Proteinaceous Machines." Chemical Reviews 115, no. 7 (2015): 2780. http://dx.doi.org/10.1021/acs.chemrev.5b00150.

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10

Tarr, B. D., and S. H. Bixby. "Proteinaceous grain-based fat substitute." Trends in Food Science & Technology 6, no. 9 (1995): 317. http://dx.doi.org/10.1016/s0924-2244(00)89157-8.

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11

Carvalho, Luísa. "Entrepreneurship and Regional Development: State of the Art." Technology Transfer and Entrepreneurship 5, no. 2 (2019): 58–66. http://dx.doi.org/10.2174/2213809906666190102111108.

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The presence of subvisible particles (SVPs) in parenteral formulations of biologics is a major challenge in the development of therapeutic protein formulations. Distinction between proteinaceous and non-proteinaceous SVPs is vital in monitoring formulation stability.

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12

Halemejko, Grazyna Z., and Ryszard J. Chrost. "Enzymatic hydrolysis of proteinaceous particulate and dissolved material in an eutrophic lake." Archiv für Hydrobiologie 107, no. 1 (1986): 1–21. http://dx.doi.org/10.1127/archiv-hydrobiol/107/1986/1.

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13

OrdónTez, R. M., M. I. Isla, M. A. Vattuone, and A. R. Sampietro. "Invertase Proteinaceous Inhibitor ofCyphomandra BetaceaSendt Fruits." Journal of Enzyme Inhibition 15, no. 6 (2000): 583–96. http://dx.doi.org/10.3109/14756360009040712.

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14

Debowski, Dawid. "Natural Proteinaceous Inhibitors of Serine Proteases." Current Pharmaceutical Design 19, no. 6 (2012): 1068–84. http://dx.doi.org/10.2174/1381612811319060009.

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15

Debowski, Dawid. "Natural Proteinaceous Inhibitors of Serine Proteases." Current Pharmaceutical Design 19, no. 6 (2012): 1068–84. http://dx.doi.org/10.2174/138161281906140714121225.

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16

Peinado García, Jenifer, Julien Caballero Castro, and Sergio Zabala López. "Proteinaceous lymphadenopathy associated with splenic rupture." Medicina Clínica (English Edition) 154, no. 10 (2020): 419–20. http://dx.doi.org/10.1016/j.medcle.2019.04.041.

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17

Barone, Justin R., and Walter F. Schmidt. "Nonfood Applications of Proteinaceous Renewable Materials." Journal of Chemical Education 83, no. 7 (2006): 1003. http://dx.doi.org/10.1021/ed083p1003.

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18

Suslick, K. S., M. W. Grinstaff, K. J. Kolbeck, and M. Wong. "Characterization of sonochemically prepared proteinaceous microspheres." Ultrasonics Sonochemistry 1, no. 1 (1994): S65—S68. http://dx.doi.org/10.1016/1350-4177(94)90030-2.

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19

Tan, Kar-Chun, Richard P. Oliver, Peter S. Solomon, and Caroline S. Moffat. "Proteinaceous necrotrophic effectors in fungal virulence." Functional Plant Biology 37, no. 10 (2010): 907. http://dx.doi.org/10.1071/fp10067.

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The host–pathogen interface can be considered as a biological battlefront. Molecules produced by both the pathogen and the host are critical factors determining the outcome of the interaction. Recent studies have revealed that an increasing number of necrotrophic fungal pathogens produce small proteinaceous effectors that are able to function as virulence factors. These molecules can cause tissue death in host plants that possess dominant sensitivity genes, leading to subsequent pathogen colonisation. Such effectors are only found in necrotrophic fungi, yet their roles in virulence are poorly

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20

York, William S., Qiang Qin та Jocelyn K. C. Rose. "Proteinaceous inhibitors of endo-β-glucanases". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1696, № 2 (2004): 223–33. http://dx.doi.org/10.1016/j.bbapap.2003.07.003.

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21

Käsermann, Fabian, and Christoph Kempf. "Virus membrane proteins and proteinaceous pores." Future Virology 1, no. 6 (2006): 823–31. http://dx.doi.org/10.2217/17460794.1.6.823.

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22

Isla, Maria Ines, Marta Amelia Vattuone, and Antonio Rodolfo Sampietro. "Proteinaceous inhibitor from Solanum tuberosum invertase." Phytochemistry 30, no. 3 (1991): 739–43. http://dx.doi.org/10.1016/0031-9422(91)85244-t.

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23

Liu, Ting, Yong Chen, Shiping Tian, and Boqiang Li. "Crucial Roles of Effectors in Interactions between Horticultural Crops and Pathogens." Horticulturae 9, no. 2 (2023): 250. http://dx.doi.org/10.3390/horticulturae9020250.

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Horticultural crops suffer from bacterial, fungal, and oomycete pathogens. Effectors are one of the main weapons deployed by those pathogens, especially in the early stages of infection. Pathogens secrete effectors with diverse functions to avoid recognition by plants, inhibit or manipulate plant immunity, and induce programmed cell death. Most identified effectors are proteinaceous, such as the well-studied type-III secretion system effectors (T3SEs) in bacteria, RXLR and CRN (crinkling and necrosis) motif effectors in oomycetes, and LysM (lysin motifs) domain effectors in fungi. In addition,

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24

И.А., Чаплыгина, та Матюшев В.В. "ТЕХНОЛОГИЯ И ОБОРУДОВАНИЕ ПОЛУЧЕНИЯ БЕЛКОВО-ВИТАМИННОГО КОАГУЛЯТА ИЗ ЗЕЛЕНОГО СОКА ЛЮЦЕРНЫ". Bulletin of KSAU, № 11 (25 листопада 2019): 138–42. http://dx.doi.org/10.36718/1819-4036-2019-11-138-142.

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Цель исследований – разработка технологии и оборудования, позволяющих получать белково-витаминный коагулят из зеленого сока при щадящих температурных режимах. Задача исследований – получение белково-витаминного коагулята на экспериментальной установке. Объектом исследований являлись зеленая масса люцерны, коагулятор и белково-витаминный коагулят. Анализ качества исходного сырья и белково-витаминного коагулята проводился в НИИЦ ФГБОУ ВО Красноярский ГАУ, ФГБУ ГЦАС «Красноярский» и ФГБУ «Красноярский референтный центр Россельхознадзора». Полученный в результате механического обезвоживания листос

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25

Tran, Thi Ngoc, Chien Thang Doan, Van Bon Nguyen, Anh Dzung Nguyen, and San-Lang Wang. "Conversion of Fishery Waste to Proteases by Streptomyces speibonae and Their Application in Antioxidant Preparation." Fishes 7, no. 3 (2022): 140. http://dx.doi.org/10.3390/fishes7030140.

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Proteinaceous wastes from the fishery process are an abundant renewable resource for the recovery of a variety of high-value products. This work attempted to utilize several proteinaceous wastes to produce proteases using the Streptomyces speibonae TKU048 strain. Among different possible carbon and nitrogen sources, the protease productive activity of S. speibonae TKU048 was optimal on 1% tuna head powder. Further, the casein/gelatin/tuna head powder zymography of the crude enzyme revealed the presence of three/nine/six proteases, respectively. The crude-enzyme cocktail of S. speibonae TKU048

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26

NAGAI, HIROSHI. "Studies on the proteinaceous toxins from cnidarians." NIPPON SUISAN GAKKAISHI 77, no. 3 (2011): 368–71. http://dx.doi.org/10.2331/suisan.77.368.

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27

Sugiura, Grant, Helen Kühn, Max Sauter, Uwe Haberkorn, and Walter Mier. "Radiolabeling Strategies for Tumor-Targeting Proteinaceous Drugs." Molecules 19, no. 2 (2014): 2135–65. http://dx.doi.org/10.3390/molecules19022135.

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28

Juge, Nathalie, and Jan Delcour. "Proteinaceous Xylanase Inhibitors: Structure, Function and Evolution." Current Enzyme Inhibition 2, no. 1 (2006): 29–35. http://dx.doi.org/10.2174/157340806775473562.

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29

ISHIKAWA, Kazuhiko, and Hiroshi NAKATANI. "Proteinaceous .ALPHA.-Amylase Inhibitors in Wheat Gluten." Agricultural and Biological Chemistry 55, no. 11 (1991): 2891–92. http://dx.doi.org/10.1271/bbb1961.55.2891.

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30

Roark, E. B., T. P. Guilderson, R. B. Dunbar, S. J. Fallon, and D. A. Mucciarone. "Extreme longevity in proteinaceous deep-sea corals." Proceedings of the National Academy of Sciences 106, no. 13 (2009): 5204–8. http://dx.doi.org/10.1073/pnas.0810875106.

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31

Ishikawa, Kazuhiko, та Hiroshi Nakatani. "Proteinaceous α-Amylase Inhibitors in Wheat Gluten". Agricultural and Biological Chemistry 55, № 11 (1991): 2891–92. http://dx.doi.org/10.1080/00021369.1991.10856971.

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32

Gardiner, R. B., and A. W. Day. "Surface proteinaceous fibrils (fimbriae) on filamentous fungi." Canadian Journal of Botany 66, no. 12 (1988): 2474–84. http://dx.doi.org/10.1139/b88-336.

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Proteinaceous fibrils (fimbriae) of 4–10 nm diam. have been described in several lower eukaryotes, including yeast-like fungi and certain algae. Antibodies prepared against the fimbriae of Ustilago violacea cross react with antigens present on the surface of these same organisms. In this paper we extend these observations to a diverse group of filamentous fungi, representing the major groups. These fungi also produce surface fibrils of 6–10 nm diam. and have surface antigens that cross react with the antibodies of U. violacea fimbriae. We conclude that surface proteins of a conserved type are

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33

Hurme, Reini, Kurt D. Berndt, Staffan J. Normark, and Mikael Rhen. "A Proteinaceous Gene Regulatory Thermometer in Salmonella." Cell 90, no. 1 (1997): 55–64. http://dx.doi.org/10.1016/s0092-8674(00)80313-x.

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34

Kazakevičiūtė-Makovska, R., and H. Steeb. "Superelasticity and Self-Healing of Proteinaceous Biomaterials." Procedia Engineering 10 (2011): 2597–602. http://dx.doi.org/10.1016/j.proeng.2011.04.432.

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35

Gongadze, Georgy M., Alla S. Kostyukova, Margarita L. Miroshnichenko, and Elizaveta A. Bonch-Osmolovskaya. "Regular proteinaceous layers ofThermococcus stetteri cell envelope." Current Microbiology 27, no. 1 (1993): 5–9. http://dx.doi.org/10.1007/bf01576826.

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36

Paik, Woon Ki, Hyang Woo Lee, and Sangduk Kim. "Endogenous proteinaceous inhibitor for protein methylation reactions." Archives of Pharmacal Research 10, no. 3 (1987): 193–96. http://dx.doi.org/10.1007/bf02861913.

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37

Goesaert, Hans, Giles Elliott, Paul A. Kroon, et al. "Occurrence of proteinaceous endoxylanase inhibitors in cereals." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1696, no. 2 (2004): 193–202. http://dx.doi.org/10.1016/j.bbapap.2003.08.015.

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38

Juge, Nathalie, Birte Svensson, Bernard Henrissat, and Gary Williamson. "Plant proteinaceous inhibitors of carbohydrate-active enzymes." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1696, no. 2 (2004): 141. http://dx.doi.org/10.1016/j.bbapap.2003.11.002.

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39

Dunaevsky, Ya E., Dong Zhang, A. R. Matveeva, G. A. Belyakova, and M. A. Belozersky. "Degradation of proteinaceous substrates by xylotrophic basidiomycetes." Microbiology 75, no. 1 (2006): 35–39. http://dx.doi.org/10.1134/s0026261706010073.

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40

Iritani, Eiji, Masashi Iwata, and Toshiro Murase. "Concentration of Proteinaceous Solutions with Superabsorbent Hydrogels." Separation Science and Technology 28, no. 10 (1993): 1819–36. http://dx.doi.org/10.1080/01496399308029243.

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41

Ng, Tzi Bun, Randy Chi Fai Cheung, Jack Ho Wong, et al. "Fungal proteinaceous compounds with multiple biological activities." Applied Microbiology and Biotechnology 100, no. 15 (2016): 6601–17. http://dx.doi.org/10.1007/s00253-016-7671-9.

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42

Jung, Jung-Yeul, Ki-Taek Byun, and Ho-Young Kwak. "Proteinaceous bubble and nanoparticle flows in microchannels." Microfluidics and Nanofluidics 1, no. 2 (2004): 177–82. http://dx.doi.org/10.1007/s10404-004-0026-3.

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43

Evershed, R. "Proteinaceous Material from Potsherds and Associated Soils." Journal of Archaeological Science 23, no. 3 (1996): 429–36. http://dx.doi.org/10.1006/jasc.1996.0038.

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44

Tatun, Nujira, Tippawan Singtripop, Shingo Osugi, Siriluck Nachiangmai, Masafumi Iwami, and Sho Sakurai. "Possible involvement of proteinaceous and non-proteinaceous trehalase inhibitors in the regulation of hemolymph trehalose concentration in Bombyx mori." Applied Entomology and Zoology 44, no. 1 (2009): 85–94. http://dx.doi.org/10.1303/aez.2009.85.

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45

Asher, Anthony H., and Steven M. Theg. "Electrochromic shift supports the membrane destabilization model of Tat-mediated transport and shows ion leakage during Sec transport." Proceedings of the National Academy of Sciences 118, no. 12 (2021): e2018122118. http://dx.doi.org/10.1073/pnas.2018122118.

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The mechanism and pore architecture of the Tat complex during transport of folded substrates remain a mystery, partly due to rapid dissociation after translocation. In contrast, the proteinaceous SecY pore is a persistent structure that needs only to undergo conformational shifts between “closed” and “opened” states when translocating unfolded substrate chains. Where the proteinaceous pore model describes the SecY pore well, the toroidal pore model better accounts for the high-energy barrier that must be overcome when transporting a folded substrate through the hydrophobic bilayer in Tat trans

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46

Dastranj, M., E. Borzoui, A. R. Bandani, and O. L. Franco. "Inhibitory effects of an extract from non-host plants on physiological characteristics of two major cabbage pests." Bulletin of Entomological Research 108, no. 3 (2017): 370–79. http://dx.doi.org/10.1017/s0007485317000864.

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AbstractThe diamondback moth (Plutella xylostella) and small white cabbage butterfly (Pieris rapae) are the two main serious pests of cruciferous crops (Brassicaceae) that have developed resistance to chemical control methods. In order to avoid such resistance and also the adverse effects of chemical pesticides on the environment, alternative methods have usually been suggested, including the use of plant enzyme inhibitors. Here, the inhibitory effects of proteinaceous inhibitors extracted from wheat, canola, sesame, bean and triticale were evaluated against the digestive α-amylases, larval gr

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47

Hendriks, Wiljan, Annika Bourgonje, William Leenders, and Rafael Pulido. "Proteinaceous Regulators and Inhibitors of Protein Tyrosine Phosphatases." Molecules 23, no. 2 (2018): 395. http://dx.doi.org/10.3390/molecules23020395.

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48

Tong, P. S., D. M. Barbano, and W. K. Jordan. "Characterization of Proteinaceous Membrane Foulants from Whey Ultrafiltration." Journal of Dairy Science 72, no. 6 (1989): 1435–42. http://dx.doi.org/10.3168/jds.s0022-0302(89)79251-1.

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49

Simakhina, G., and L. Solodko. "Proteinaceous Food Concentrates From Green Mass of Plants." Advanced Science Journal 2015, no. 1 (2015): 57–60. http://dx.doi.org/10.15550/asj.2015.01.057.

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50

YOSHINAGA-KIRIAKE, AYA. "Biochemical study on proteinaceous toxins from venomous fish." NIPPON SUISAN GAKKAISHI 88, no. 4 (2022): 229–31. http://dx.doi.org/10.2331/suisan.wa2950.

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