Статті в журналах з теми "Recombinant monoclonal antibody"
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Siegel, D. L. "Recombinant monoclonal antibody technology." Transfusion Clinique et Biologique 9, no. 1 (January 2002): 15–22. http://dx.doi.org/10.1016/s1246-7820(01)00210-5.
Повний текст джерелаLiu, Hongcheng, Georgeen Gaza-Bulseco, and Chris Chumsae. "Glutamine deamidation of a recombinant monoclonal antibody." Rapid Communications in Mass Spectrometry 22, no. 24 (December 30, 2008): 4081–88. http://dx.doi.org/10.1002/rcm.3831.
Повний текст джерелаEltarhoni, Khadiga, Faddy Kamel, Katrina Ihebunezie, Pasha Nisar, and Mikhail Soloviev. "Therapeutic Antibodies in Cancer Treatment in the UK." International Journal of Molecular Sciences 23, no. 23 (November 23, 2022): 14589. http://dx.doi.org/10.3390/ijms232314589.
Повний текст джерелаBrichta, J., M. Hnilova, and T. Viskovic. "generation of hapten-specific recombinant antibodies: antibody phage display technology: a review." Veterinární Medicína 50, No. 6 (March 28, 2012): 231–52. http://dx.doi.org/10.17221/5620-vetmed.
Повний текст джерелаLubkin, Margaret, Matthew Shallice, Julie Nyhus, Louis Leong, and Birte Aggeler. "Recombinant Rabbit Monoclonal Antibodies to Study Apoptosis and Apoptotic Pathways (132.4)." Journal of Immunology 184, no. 1_Supplement (April 1, 2010): 132.4. http://dx.doi.org/10.4049/jimmunol.184.supp.132.4.
Повний текст джерелаBoonham, N., and I. Barker. "Virus Strain Discrimination Using Recombinant Antibodies." Disease Markers 16, no. 1-2 (2000): 95–97. http://dx.doi.org/10.1155/2000/815852.
Повний текст джерелаAmbrogelly, Alexandre, Stephen Gozo, Amit Katiyar, Shara Dellatore, Yune Kune, Ram Bhat, Joanne Sun, et al. "Analytical comparability study of recombinant monoclonal antibody therapeutics." mAbs 10, no. 4 (March 20, 2018): 513–38. http://dx.doi.org/10.1080/19420862.2018.1438797.
Повний текст джерелаSchrader, John W., and Gary R. McLean. "Multispecificity of a recombinant anti-ras monoclonal antibody." Journal of Molecular Recognition 31, no. 2 (November 8, 2017): e2683. http://dx.doi.org/10.1002/jmr.2683.
Повний текст джерелаGreunke, Kerstin, Edzard Spillner, Ingke Braren, Henning Seismann, Sabine Kainz, Ulrich Hahn, Thomas Grunwald, and Reinhard Bredehorst. "Bivalent monoclonal IgY antibody formats by conversion of recombinant antibody fragments." Journal of Biotechnology 124, no. 2 (July 2006): 446–56. http://dx.doi.org/10.1016/j.jbiotec.2005.12.032.
Повний текст джерелаEwers, Helge. "Open-source recombinant monoclonal secondary nanobodies." Journal of Cell Biology 217, no. 3 (February 14, 2018): 809–11. http://dx.doi.org/10.1083/jcb.201802025.
Повний текст джерелаGong, Siqi, Seijal Gautam, Joshua D. Coneglio, Hanna B. Scinto, and Ruth M. Ruprecht. "Antibody Light Chains: Key to Increased Monoclonal Antibody Yields in Expi293 Cells?" Antibodies 11, no. 2 (May 18, 2022): 37. http://dx.doi.org/10.3390/antib11020037.
Повний текст джерелаAki, Yuichi, Yuta Katsumata, Hirofumi Kakihara, Koichi Nonaka, and Kenshu Fujiwara. "4-(2,5-Dimethyl-1H-pyrrol-1-yl)-N-(2,5-dioxopyrrolidin-1-yl) benzamide improves monoclonal antibody production in a Chinese hamster ovary cell culture." PLOS ONE 16, no. 4 (April 22, 2021): e0250416. http://dx.doi.org/10.1371/journal.pone.0250416.
Повний текст джерелаZonneveld, Anton-Jan van, Harry Veerman, Just P. J. Brakenhoff, Lucien A. Aarden, Jean-Francois Cajot, and Hans Pannekoek. "Mapping of Epitopes on Human Tissue-Type Plasminogen Activator with Recombinant Deletion Mutant Proteins." Thrombosis and Haemostasis 57, no. 01 (1987): 082–86. http://dx.doi.org/10.1055/s-0038-1651067.
Повний текст джерелаVancutsem, E., F. Echahidi, K. Van Geel, G. Muyldermans, O. Soetens, and A. Naessens. "Production of Recombinant Antigens of Ureaplasma parvum Serotypes 3 and 6 for Development of a Serological Assay." Clinical and Vaccine Immunology 15, no. 3 (December 19, 2007): 447–51. http://dx.doi.org/10.1128/cvi.00379-07.
Повний текст джерелаDe Logu, Alessandro, R. Anthony Williamson, Roman Rozenshteyn, Fernando Ramiro-Ibañez, Cindy D. Simpson, Dennis R. Burton, and Pietro Paolo Sanna. "Characterization of a Type-Common Human Recombinant Monoclonal Antibody to Herpes Simplex Virus with High Therapeutic Potential." Journal of Clinical Microbiology 36, no. 11 (1998): 3198–204. http://dx.doi.org/10.1128/jcm.36.11.3198-3204.1998.
Повний текст джерелаWang, Dongdong, Christine Nowak, Bruce Mason, Amit Katiyar, and Hongcheng Liu. "Analytical artifacts in characterization of recombinant monoclonal antibody therapeutics." Journal of Pharmaceutical and Biomedical Analysis 183 (May 2020): 113131. http://dx.doi.org/10.1016/j.jpba.2020.113131.
Повний текст джерелаMayani, Mukesh, Carlos D. M. Filipe, Michael D. McLean, J. Christopher Hall, and Raja Ghosh. "Purification of transgenic tobacco-derived recombinant human monoclonal antibody." Biochemical Engineering Journal 72 (March 2013): 33–41. http://dx.doi.org/10.1016/j.bej.2012.12.007.
Повний текст джерелаGaza-Bulseco, Georgeen, and Hongcheng Liu. "Fragmentation of a Recombinant Monoclonal Antibody at Various pH." Pharmaceutical Research 25, no. 8 (May 13, 2008): 1881–90. http://dx.doi.org/10.1007/s11095-008-9606-3.
Повний текст джерелаKim, Eun-Jung, Gyu-Min Im, Chang-Soo Lee, Yun-Gon Kim, Byoung Joon Ko, Hee-Jin Jeong, and Byung-Gee Kim. "Generation of Monoclonal Antibodies for Sensitive Detection of Pro-Inflammatory Protein S100A9." Applied Sciences 11, no. 10 (May 19, 2021): 4659. http://dx.doi.org/10.3390/app11104659.
Повний текст джерелаMohammadian, Omid, Masoumeh Rajabibazl, Hadi Bayat, and Azam Rahimpour. "Transient Expression of a Recombinant Monoclonal Antibody in HEK293T Cells." Pharmaceutical Sciences 24, no. 3 (September 23, 2018): 207–12. http://dx.doi.org/10.15171/ps.2018.30.
Повний текст джерелаYurkov, S. G., S. P. Zhivoderov, A. Y. Koltsov, R. A. Khamitov, N. V. Stratonova, and N. A. Litvinova. "Evaluation of the Virus Elimination and Inactivation at Different Stages of the Model Biotechnological Process for the Production of a Drug Based on the Monoclonal Antibody Fab-Fragment." Biotekhnologiya 37, no. 1 (2021): 69–80. http://dx.doi.org/10.21519/0234-2758-2021-37-1-69-80.
Повний текст джерелаLyubarskaya, Yelena, Damian Houde, James Woodard, David Murphy, and Rohin Mhatre. "Analysis of recombinant monoclonal antibody isoforms by electrospray ionization mass spectrometry as a strategy for streamlining characterization of recombinant monoclonal antibody charge heterogeneity." Analytical Biochemistry 348, no. 1 (January 2006): 24–39. http://dx.doi.org/10.1016/j.ab.2005.10.003.
Повний текст джерелаBatista, Cassiano Martin, Lia Carolina Soares Medeiros, Iriane Eger, and Maurilio José Soares. "mAb CZP-315.D9: An Antirecombinant Cruzipain Monoclonal Antibody That Specifically Labels the Reservosomes ofTrypanosoma cruziEpimastigotes." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/714749.
Повний текст джерелаDesogus, Alessandra, Roberto Burioni, Angela Ingianni, Francesca Bugli, Raffaello Pompei, and Giovanni Fadda. "Production and Characterization of a Human Recombinant Monoclonal Fab Fragment Specific for Influenza A Viruses." Clinical Diagnostic Laboratory Immunology 10, no. 4 (July 2003): 680–85. http://dx.doi.org/10.1128/cdli.10.4.680-685.2003.
Повний текст джерелаZheng, Ling, Shucheng Zhang, Charles Wood, Sanjay Kapil, Graham E. Wilcox, Thomas A. Loughin, and H. C. Minocha. "Differentiation of Two Bovine Lentiviruses by a Monoclonal Antibody on the Basis of Epitope Specificity." Clinical Diagnostic Laboratory Immunology 8, no. 2 (March 1, 2001): 283–87. http://dx.doi.org/10.1128/cdli.8.2.283-287.2001.
Повний текст джерелаOrlandi, R., M. Cattaneo, F. Troglio, M. Campiglio, I. Biunno, and S. Ménard. "Production of a Monoclonal Antibody Directed against the Recombinant SEL1L Protein." International Journal of Biological Markers 17, no. 2 (April 2002): 104–11. http://dx.doi.org/10.1177/172460080201700205.
Повний текст джерелаKoo, Kai, Peggy M. Foegeding, and Harold E. Swaisgood. "Construction and Expression of a Bifunctional Single-Chain Antibody against Bacillus cereusSpores." Applied and Environmental Microbiology 64, no. 7 (July 1, 1998): 2490–96. http://dx.doi.org/10.1128/aem.64.7.2490-2496.1998.
Повний текст джерелаKojic, Snezana, Elisa Medeot, and Georgine Faulkner. "Characterization of antibodies directed against the Ankrd2 human muscle protein." Archives of Biological Sciences 61, no. 4 (2009): 683–91. http://dx.doi.org/10.2298/abs0904683k.
Повний текст джерелаKOLB, ANDREAS F., and STUART G. SIDDELL. "Expression of a Recombinant Monoclonal Antibody From a Bicistronic mRNA." Hybridoma 16, no. 5 (October 1997): 421–26. http://dx.doi.org/10.1089/hyb.1997.16.421.
Повний текст джерелаvan Duijnhoven, Hans L. P., Torik A. Y. Ayoubi, Erika D. J. Timmera, Anneke A. M. Braks, Anton J. M. Roebroek, Gerard J. M. Martens, and Wim J. M. van de Ven. "Development of a monoclonal antibody against recombinant neuroendocrine 7B2 protein." FEBS Letters 255, no. 2 (September 25, 1989): 372–76. http://dx.doi.org/10.1016/0014-5793(89)81125-1.
Повний текст джерелаKAMIHIRA, MASAMICHI, ICHIROU KAWAKUBO, MASAYUKI TANIGUCHI, SHINJI IIJIMA, and TAKESHI KOBAYASHI. "Production and characterization of monoclonal antibody to recombinant .ALPHA.-amylase." Journal of Chemical Engineering of Japan 21, no. 4 (1988): 357–62. http://dx.doi.org/10.1252/jcej.21.357.
Повний текст джерелаLiu, Hongcheng, Christine Nowak, Mei Shao, Gomathinayagam Ponniah, and Alyssa Neill. "Impact of cell culture on recombinant monoclonal antibody product heterogeneity." Biotechnology Progress 32, no. 5 (August 3, 2016): 1103–12. http://dx.doi.org/10.1002/btpr.2327.
Повний текст джерелаBeck, Alain, Christine Nowak, Deborah Meshulam, Kristina Reynolds, David Chen, Dennis B. Pacardo, Samantha B. Nicholls, et al. "Risk-Based Control Strategies of Recombinant Monoclonal Antibody Charge Variants." Antibodies 11, no. 4 (November 20, 2022): 73. http://dx.doi.org/10.3390/antib11040073.
Повний текст джерелаChargelegue, Daniel, Pascal M. W. Drake, Patricia Obregon, Alessandra Prada, Neil Fairweather, and Julian K.-C. Ma. "Highly Immunogenic and Protective Recombinant Vaccine Candidate Expressed in Transgenic Plants." Infection and Immunity 73, no. 9 (September 2005): 5915–22. http://dx.doi.org/10.1128/iai.73.9.5915-5922.2005.
Повний текст джерелаBrena, Sonia, Miren J. Omaetxebarría, Natalia Elguezabal, Jonathan Cabezas, María D. Moragues, and José Pontón. "Fungicidal Monoclonal Antibody C7 Binds to Candida albicans Als3." Infection and Immunity 75, no. 7 (April 23, 2007): 3680–82. http://dx.doi.org/10.1128/iai.01840-06.
Повний текст джерелаGinsburg, David, Paula L. Bockenstedt, Elizabeth A. Allen, David A. Fox, Paul A. Foster, Zaverio M. Ruggeri, Theodore S. Zimmerman, et al. "Fine Mapping of Monoclonal Antibody Epitopes on Human von Willebrand Factor Using a Recombinant Peptide Library." Thrombosis and Haemostasis 67, no. 01 (1992): 166–71. http://dx.doi.org/10.1055/s-0038-1648400.
Повний текст джерелаLiu, Dong, Mandy Tseng, Linda F. Epstein, Lydia Green, Brian Chan, Brian Soriano, Desiree Lim, et al. "Evaluation of recombinant monoclonal antibody SVmab1 binding to NaV1.7 target sequences and block of human NaV1.7 currents." F1000Research 5 (November 25, 2016): 2764. http://dx.doi.org/10.12688/f1000research.9918.1.
Повний текст джерелаBurrin, J. M., J. L. Paterson, P. S. Sharp, and T. H. Yeo. "Monoclonal and polyclonal antibodies compared for radioimmunoassay of somatomedin-C in patients with acromegaly or hypopituitarism." Clinical Chemistry 33, no. 9 (September 1, 1987): 1593–96. http://dx.doi.org/10.1093/clinchem/33.9.1593.
Повний текст джерелаWoźniakowski, Grzegorz, and Elżbieta Samorek-Salamonowicz. "In Vitro Replication of Recombinant Marek’S Disease Viruses Constructed from Field Strains Lacking Meq and Vtr Oncogenes." Bulletin of the Veterinary Institute in Pulawy 57, no. 2 (June 1, 2013): 141–47. http://dx.doi.org/10.2478/bvip-2013-0027.
Повний текст джерелаAlves, Bryce, Mary Anne Jelinek, Yanan Lu, Melissa Ritland, Patricia Velasco, Xi Zhao, Eddie Adams, and Joseph Fernandez. "Single B cell isolation and cloning from rabbits to generate recombinant antibodies." Journal of Immunology 204, no. 1_Supplement (May 1, 2020): 159.53. http://dx.doi.org/10.4049/jimmunol.204.supp.159.53.
Повний текст джерелаHigo-Moriguchi, Kyoko, Yasushi Akahori, Yoshitaka Iba, Yoshikazu Kurosawa, and Koki Taniguchi. "Isolation of Human Monoclonal Antibodies That Neutralize Human Rotavirus." Journal of Virology 78, no. 7 (April 1, 2004): 3325–32. http://dx.doi.org/10.1128/jvi.78.7.3325-3332.2004.
Повний текст джерелаBaharudeen, Zamrina, Rahmah Noordin, Lim Theam Soon, Dinesh Balachandra, Nor Suhada Anuar, Fatin Hamimi Mustafa, and Anizah Rahumatullah. "Isolation and Production of Human Monoclonal Antibody Proteins against a Toxocara canis Excretory–Secretory Recombinant Antigen." Pathogens 11, no. 11 (October 25, 2022): 1232. http://dx.doi.org/10.3390/pathogens11111232.
Повний текст джерелаBraren, Ingke, Simon Blank, Henning Seismann, Susanne Deckers, Markus Ollert, Thomas Grunwald, and Edzard Spillner. "Generation of Human Monoclonal Allergen-Specific IgE and IgG Antibodies from Synthetic Antibody Libraries." Clinical Chemistry 53, no. 5 (May 1, 2007): 837–44. http://dx.doi.org/10.1373/clinchem.2006.078360.
Повний текст джерелаMay, Kenneth F., Bettina Franz, Christopher Harvey, F. Stephen Hodi, Glenn Dranoff, and Kai Wucherpfennig. "Isolation of human anti-MICA antibody from cancer patients responding to immunotherapies." Journal of Clinical Oncology 30, no. 15_suppl (May 20, 2012): 2502. http://dx.doi.org/10.1200/jco.2012.30.15_suppl.2502.
Повний текст джерелаSaijo, Masayuki, Marie-Claude Georges-Courbot, Philippe Marianneau, Victor Romanowski, Shuetsu Fukushi, Tetsuya Mizutani, Alain-Jean Georges, Takeshi Kurata, Ichiro Kurane, and Shigeru Morikawa. "Development of Recombinant Nucleoprotein-Based Diagnostic Systems for Lassa Fever." Clinical and Vaccine Immunology 14, no. 9 (July 18, 2007): 1182–89. http://dx.doi.org/10.1128/cvi.00101-07.
Повний текст джерелаTanaka, Tetsuya, Ichiro Nakamura, Nai-Yuan Lee, Haruto Kumura, and Kei-ichi Shimazaki. "Expression of bovine lactoferrin and lactoferrin N-lobe by recombinant baculovirus and its antimicrobial activity against Prototheca zopfii." Biochemistry and Cell Biology 81, no. 5 (October 1, 2003): 349–54. http://dx.doi.org/10.1139/o03-062.
Повний текст джерелаOrlandi, R., M. Cattaneo, F. Troglio, M. Campiglio, I. Biunno, and S. Mnard. "Production of a monoclonal antibody directed against the recombinant SEL1L protein." International Journal of Biological Markers 17, no. 2 (2002): 104–11. http://dx.doi.org/10.5301/jbm.2008.4015.
Повний текст джерелаIizuka, Masashi, Shingo Ogawa, Atsushi Takeuchi, Shinichi Nakakita, Yuhki Kubo, Yoshitaka Miyawaki, Jun Hirabayashi, and Masahiro Tomita. "Production of a recombinant mouse monoclonal antibody in transgenic silkworm cocoons." FEBS Journal 276, no. 20 (September 9, 2009): 5806–20. http://dx.doi.org/10.1111/j.1742-4658.2009.07262.x.
Повний текст джерелаLam, Xanthe M., Janet Y. Yang, and Jeffrey L. Cleland. "Antioxidants for Prevention of Methionine Oxidation in Recombinant Monoclonal Antibody HER2." Journal of Pharmaceutical Sciences 86, no. 11 (November 1997): 1250–55. http://dx.doi.org/10.1021/js970143s.
Повний текст джерелаGreiner, J., F. Guadagni, P. Noguchi, S. Pestka, D. Colcher, P. Fisher, and J. Schlom. "Recombinant interferon enhances monoclonal antibody-targeting of carcinoma lesions in vivo." Science 235, no. 4791 (February 20, 1987): 895–98. http://dx.doi.org/10.1126/science.3580039.
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