Статті в журналах з теми "Biopharmaceutical proteins"
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Liu, Shulei, and Benjamin L. Schulz. "Biopharmaceutical quality control with mass spectrometry." Bioanalysis 13, no. 16 (August 2021): 1275–91. http://dx.doi.org/10.4155/bio-2021-0123.
Повний текст джерелаTodorovic, Zoran, and Dragana Protic. "Bioethical issues in the development of biopharmaceuticals." Filozofija i drustvo 23, no. 4 (2012): 49–56. http://dx.doi.org/10.2298/fid1204049t.
Повний текст джерелаBarolo, Lorenzo, Raffaela M. Abbriano, Audrey S. Commault, Jestin George, Tim Kahlke, Michele Fabris, Matthew P. Padula, Angelo Lopez, Peter J. Ralph, and Mathieu Pernice. "Perspectives for Glyco-Engineering of Recombinant Biopharmaceuticals from Microalgae." Cells 9, no. 3 (March 5, 2020): 633. http://dx.doi.org/10.3390/cells9030633.
Повний текст джерелаZhang, Fangrong, Gesa Richter, Benjamin Bourgeois, Emil Spreitzer, Armin Moser, Andreas Keilbach, Petra Kotnik, and Tobias Madl. "A General Small-Angle X-ray Scattering-Based Screening Protocol for Studying Physical Stability of Protein Formulations." Pharmaceutics 14, no. 1 (December 28, 2021): 69. http://dx.doi.org/10.3390/pharmaceutics14010069.
Повний текст джерелаNielsen, Jens. "Production of biopharmaceutical proteins by yeast." Bioengineered 4, no. 4 (July 2013): 207–11. http://dx.doi.org/10.4161/bioe.22856.
Повний текст джерелаWebber, Matthew J., Eric A. Appel, Brittany Vinciguerra, Abel B. Cortinas, Lavanya S. Thapa, Siddharth Jhunjhunwala, Lyle Isaacs, Robert Langer, and Daniel G. Anderson. "Supramolecular PEGylation of biopharmaceuticals." Proceedings of the National Academy of Sciences 113, no. 50 (November 28, 2016): 14189–94. http://dx.doi.org/10.1073/pnas.1616639113.
Повний текст джерелаOwczarek, B., A. Gerszberg, and K. Hnatuszko-Konka. "A Brief Reminder of Systems of Production and Chromatography-Based Recovery of Recombinant Protein Biopharmaceuticals." BioMed Research International 2019 (January 8, 2019): 1–13. http://dx.doi.org/10.1155/2019/4216060.
Повний текст джерелаBuyel, Johannes Felix, and Rainer Fischer. "Downstream processing of biopharmaceutical proteins produced in plants." Bioengineered 5, no. 2 (February 3, 2014): 138–42. http://dx.doi.org/10.4161/bioe.28061.
Повний текст джерелаHoward, John A. "Commercialization of Biopharmaceutical and Bioindustrial Proteins from Plants." Crop Science 45, no. 2 (March 2005): 468–72. http://dx.doi.org/10.2135/cropsci2005.0468.
Повний текст джерелаCreamer, Jessica S., Nathan J. Oborny, and Susan M. Lunte. "Recent advances in the analysis of therapeutic proteins by capillary and microchip electrophoresis." Anal. Methods 6, no. 15 (2014): 5427–49. http://dx.doi.org/10.1039/c4ay00447g.
Повний текст джерелаHamrang, Zahra, Nicholas J. W. Rattray, and Alain Pluen. "Proteins behaving badly: emerging technologies in profiling biopharmaceutical aggregation." Trends in Biotechnology 31, no. 8 (August 2013): 448–58. http://dx.doi.org/10.1016/j.tibtech.2013.05.004.
Повний текст джерелаTolbert, William R. "Manufacture of biopharmaceutical proteins by mammalian cell culture systems." Biotechnology Advances 8, no. 4 (January 1990): 729–39. http://dx.doi.org/10.1016/0734-9750(90)91994-r.
Повний текст джерелаMartin, Pauline L., and Gerhard F. Weinbauer. "Developmental Toxicity Testing of Biopharmaceuticals in Nonhuman Primates." International Journal of Toxicology 29, no. 6 (October 6, 2010): 552–68. http://dx.doi.org/10.1177/1091581810378896.
Повний текст джерелаSasaki, Tetsuji, and Akiyoshi Taniguchi. "Development of a Non-protein and Lipid Medium Adopted Cell Line for Biopharmaceutical Recombinant Protein Expression." Open Biotechnology Journal 7, no. 1 (February 22, 2013): 1–6. http://dx.doi.org/10.2174/1874070701307010001.
Повний текст джерелаOnoue, Satomi, Hiroki Suzuki, and Yoshiki Seto. "Formulation Approaches to Overcome Biopharmaceutical Limitations of Inhaled Peptides/Proteins." Current Pharmaceutical Design 21, no. 27 (September 17, 2015): 3867–74. http://dx.doi.org/10.2174/1381612821666150820110826.
Повний текст джерелаRodger, Alison, and Doug Marshall. "Beginners guide to circular dichroism." Biochemist 43, no. 2 (March 26, 2021): 58–64. http://dx.doi.org/10.1042/bio_2020_105.
Повний текст джерелаHandl, Alina, Ángela I. López-Lorente, René Handrick, Boris Mizaikoff, and Friedemann Hesse. "Infrared attenuated total reflection and 2D fluorescence spectroscopy for the discrimination of differently aggregated monoclonal antibodies." Analyst 144, no. 21 (2019): 6334–41. http://dx.doi.org/10.1039/c9an00424f.
Повний текст джерелаBolje, Aljoša, and Stanislav Gobec. "Analytical Techniques for Structural Characterization of Proteins in Solid Pharmaceutical Forms: An Overview." Pharmaceutics 13, no. 4 (April 11, 2021): 534. http://dx.doi.org/10.3390/pharmaceutics13040534.
Повний текст джерелаCastro, Leonor S., Guilherme S. Lobo, Patrícia Pereira, Mara G. Freire, Márcia C. Neves, and Augusto Q. Pedro. "Interferon-Based Biopharmaceuticals: Overview on the Production, Purification, and Formulation." Vaccines 9, no. 4 (April 1, 2021): 328. http://dx.doi.org/10.3390/vaccines9040328.
Повний текст джерелаShanmugaraj, Balamurugan, Christine Joy I. Bulaon, and Waranyoo Phoolcharoen. "Plant Molecular Farming: A Viable Platform for Recombinant Biopharmaceutical Production." Plants 9, no. 7 (July 4, 2020): 842. http://dx.doi.org/10.3390/plants9070842.
Повний текст джерелаGerszberg, Aneta, and Katarzyna Hnatuszko-Konka. "Compendium on Food Crop Plants as a Platform for Pharmaceutical Protein Production." International Journal of Molecular Sciences 23, no. 6 (March 17, 2022): 3236. http://dx.doi.org/10.3390/ijms23063236.
Повний текст джерелаSamiec, M., and M. Skrzyszowska. "Transgenic mammalian species, generated by somatic cell cloning, in biomedicine, biopharmaceutical industry and human nutrition/dietetics - recent achievements." Polish Journal of Veterinary Sciences 14, no. 2 (May 1, 2011): 317–28. http://dx.doi.org/10.2478/v10181-011-0050-7.
Повний текст джерелаSaraswat, Mayank, Luca Musante, Alessandra Ravidá, Brian Shortt, Barry Byrne, and Harry Holthofer. "Preparative Purification of Recombinant Proteins: Current Status and Future Trends." BioMed Research International 2013 (2013): 1–18. http://dx.doi.org/10.1155/2013/312709.
Повний текст джерелаHu, Jianwen, Jizhong Han, Haoran Li, Xian Zhang, Lan lan Liu, Fei Chen, and Bin Zeng. "Human Embryonic Kidney 293 Cells: A Vehicle for Biopharmaceutical Manufacturing, Structural Biology, and Electrophysiology." Cells Tissues Organs 205, no. 1 (2018): 1–8. http://dx.doi.org/10.1159/000485501.
Повний текст джерелаIbrahim, Yousif H.-E. Y., Géza Regdon, Elnazeer I. Hamedelniel, and Tamás Sovány. "Review of recently used techniques and materials to improve the efficiency of orally administered proteins/peptides." DARU Journal of Pharmaceutical Sciences 28, no. 1 (December 6, 2019): 403–16. http://dx.doi.org/10.1007/s40199-019-00316-w.
Повний текст джерелаHefferon, Kathleen Laura. "Plant virus expression vectors set the stage as production platforms for biopharmaceutical proteins." Virology 433, no. 1 (November 2012): 1–6. http://dx.doi.org/10.1016/j.virol.2012.06.012.
Повний текст джерелаZalar, Matja, Hristo L. Svilenov, and Alexander P. Golovanov. "Binding of excipients is a poor predictor for aggregation kinetics of biopharmaceutical proteins." European Journal of Pharmaceutics and Biopharmaceutics 151 (June 2020): 127–36. http://dx.doi.org/10.1016/j.ejpb.2020.04.002.
Повний текст джерелаEaton, Leslie C. "Quantitation of residual Escherichia coli DNA in recombinant biopharmaceutical proteins by hybridization analysis." Journal of Pharmaceutical and Biomedical Analysis 7, no. 5 (January 1989): 633–38. http://dx.doi.org/10.1016/0731-7085(89)80230-4.
Повний текст джерелаBugelskil, P. J., D. J. Herzykl, S. Rehm, A. G. Harmsen, E. V. Gore, D. M. Williams, B. E. Maleeff, et al. "Preclinical development of keliximab, a Primatized™ anti-CD4 monoclonal antibody, in human CD4 transgenic mice: characterization of the model and safety studies." Human & Experimental Toxicology 19, no. 4 (April 2000): 230–43. http://dx.doi.org/10.1191/096032700678815783.
Повний текст джерелаKeller, G.-A. "Cell Imaging in Drug Discovery and Development." Microscopy and Microanalysis 7, S2 (August 2001): 620–21. http://dx.doi.org/10.1017/s1431927600029172.
Повний текст джерелаCabal, Ace Bryan Sotelo, and Tzong-Yuan Wu. "Recombinant Protein Technology in the Challenging Era of Coronaviruses." Processes 10, no. 5 (May 10, 2022): 946. http://dx.doi.org/10.3390/pr10050946.
Повний текст джерелаBischoff, Rainer, Kees J. Bronsema, Nico C. van de Merbel, Kees J. Bronsema, and Nico C. van de Merbel. "Analysis of biopharmaceutical proteins in biological matrices by LC-MS/MS I. Sample preparation." TrAC Trends in Analytical Chemistry 48 (July 2013): 41–51. http://dx.doi.org/10.1016/j.trac.2012.11.015.
Повний текст джерелаBush, David R., Li Zang, Arseniy M. Belov, Alexander R. Ivanov та Barry L. Karger. "High Resolution CZE-MS Quantitative Characterization of Intact Biopharmaceutical Proteins: Proteoforms of Interferon-β1". Analytical Chemistry 88, № 2 (24 грудня 2015): 1138–46. http://dx.doi.org/10.1021/acs.analchem.5b03218.
Повний текст джерелаCardona-Ospina, Jaime A., Juan C. Sepúlveda-Arias, L. Mancilla, and Luis G. Gutierrez-López. "Plant expression systems, a budding way to confront chikungunya and Zika in developing countries?" F1000Research 5 (August 31, 2016): 2121. http://dx.doi.org/10.12688/f1000research.9502.1.
Повний текст джерелаIbeanu, Nkiruka, Raphael Egbu, Lesley Onyekuru, Hoda Javaheri, Peng Tee Khaw, Gareth R. Williams, Steve Brocchini, and Sahar Awwad. "Injectables and Depots to Prolong Drug Action of Proteins and Peptides." Pharmaceutics 12, no. 10 (October 21, 2020): 999. http://dx.doi.org/10.3390/pharmaceutics12100999.
Повний текст джерелаKeysberg, Christoph, Oliver Hertel, Louise Schelletter, Tobias Busche, Chiara Sochart, Jörn Kalinowski, Raimund Hoffrogge, Kerstin Otte, and Thomas Noll. "Exploring the molecular content of CHO exosomes during bioprocessing." Applied Microbiology and Biotechnology 105, no. 9 (May 2021): 3673–89. http://dx.doi.org/10.1007/s00253-021-11309-8.
Повний текст джерелаBracewell, Daniel G., Victoria Smith, Mike Delahaye, and C. Mark Smales. "Analytics of host cell proteins (HCPs): lessons from biopharmaceutical mAb analysis for Gene therapy products." Current Opinion in Biotechnology 71 (October 2021): 98–104. http://dx.doi.org/10.1016/j.copbio.2021.06.026.
Повний текст джерелаTitchener-Hooker, N. J., P. Dunnill, and M. Hoare. "Micro biochemical engineering to accelerate the design of industrial-scale downstream processes for biopharmaceutical proteins." Biotechnology and Bioengineering 100, no. 3 (2008): 473–87. http://dx.doi.org/10.1002/bit.21788.
Повний текст джерелаKim, Nam Ah, Bora Heo, and Seong Hoon Jeong. "Rapid methodology for basal system selection of therapeutic proteins during the early stage biopharmaceutical development." Journal of Pharmaceutical Investigation 50, no. 4 (September 11, 2019): 363–72. http://dx.doi.org/10.1007/s40005-019-00461-z.
Повний текст джерелаKotapati, Srikanth, Madhura Deshpande, Aarti Jashnani, Dharam Thakkar, Hongwu Xu, and Gavin Dollinger. "The role of ligand-binding assay and LC–MS in the bioanalysis of complex protein and oligonucleotide therapeutics." Bioanalysis 13, no. 11 (June 2021): 931–54. http://dx.doi.org/10.4155/bio-2021-0009.
Повний текст джерелаVan Manen-Brush, Kathleen, Jacob Zeitler, John R. White, Paul Younge, Samantha Willis, and Marisa Jones. "Improving Chinese hamster ovary host cell protein ELISA using Ella®: an automated microfluidic platform." BioTechniques 69, no. 3 (September 2020): 186–92. http://dx.doi.org/10.2144/btn-2020-0074.
Повний текст джерелаZhong, Xiaotian, and Jill F. Wright. "Biological Insights into Therapeutic Protein Modifications throughout Trafficking and Their Biopharmaceutical Applications." International Journal of Cell Biology 2013 (2013): 1–19. http://dx.doi.org/10.1155/2013/273086.
Повний текст джерелаDewi, Kartika Sari, and Asrul Muhamad Fuad. "Improving the Expression of Human Granulocyte Colony Stimulating Factor in Escherichia coli by Reducing the GC-content and Increasing mRNA Folding Free Energy at 5’-Terminal End." Advanced Pharmaceutical Bulletin 10, no. 4 (August 9, 2020): 610–16. http://dx.doi.org/10.34172/apb.2020.073.
Повний текст джерелаBenedé, Sara, and Elena Molina. "Chicken Egg Proteins and Derived Peptides with Antioxidant Properties." Foods 9, no. 6 (June 3, 2020): 735. http://dx.doi.org/10.3390/foods9060735.
Повний текст джерелаInouye, Masaharu, and Thierry Burnouf. "The Role of Nanofiltration in the Pathogen Safety of Biologicals: An Update." Current Nanoscience 16, no. 3 (April 2, 2020): 413–24. http://dx.doi.org/10.2174/1573413715666190328223130.
Повний текст джерелаGebauer, Michaela, and Arne Skerra. "Engineered Protein Scaffolds as Next-Generation Therapeutics." Annual Review of Pharmacology and Toxicology 60, no. 1 (January 6, 2020): 391–415. http://dx.doi.org/10.1146/annurev-pharmtox-010818-021118.
Повний текст джерелаThoring, Zemella, Wüstenhagen, and Kubick. "Accelerating the Production of Druggable Targets: Eukaryotic Cell-Free Systems Come into Focus." Methods and Protocols 2, no. 2 (April 16, 2019): 30. http://dx.doi.org/10.3390/mps2020030.
Повний текст джерелаGagnon, Pete, and Tsutomu Arakawa. "Editorial [Hot Topic: Aggregation Detection and Removal Biopharmaceutical Proteins (Guest Editors: Pete Gagnon & Tsutomu Arakawa)]." Current Pharmaceutical Biotechnology 10, no. 4 (June 1, 2009): 347. http://dx.doi.org/10.2174/138920109788488923.
Повний текст джерелаHopfgartner, Gérard, Antoine Lesur, and Emmanuel Varesio. "Analysis of biopharmaceutical proteins in biological matrices by LC-MS/MS II. LC-MS/MS analysis." TrAC Trends in Analytical Chemistry 48 (July 2013): 52–61. http://dx.doi.org/10.1016/j.trac.2013.03.008.
Повний текст джерелаKouwen, Thijs R. H. M., Jean-Yves F. Dubois, Roland Freudl, Wim J. Quax, and Jan Maarten van Dijl. "Modulation of Thiol-Disulfide Oxidoreductases for Increased Production of Disulfide-Bond-Containing Proteins in Bacillus subtilis." Applied and Environmental Microbiology 74, no. 24 (October 24, 2008): 7536–45. http://dx.doi.org/10.1128/aem.00894-08.
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