{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,6]],"date-time":"2026-05-06T13:39:53Z","timestamp":1778074793521,"version":"3.51.4"},"reference-count":25,"publisher":"SAGE Publications","issue":"3","license":[{"start":{"date-parts":[[2013,6,1]],"date-time":"2013-06-01T00:00:00Z","timestamp":1370044800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["Monoclonal Antibodies in Immunodiagnosis &amp; Immunotherapy"],"published-print":{"date-parts":[[2013,6]]},"abstract":"<jats:p>\n                    Tyrosyl-tRNA synthetase (TyrRS) is one of the key enzymes of protein biosynthesis. In addition to its basic role, this enzyme reveals some important non-canonical functions. Under apoptotic conditions, the full-length enzyme splits into two fragments having distinct cytokine activities, thereby linking protein synthesis to cytokine signaling pathways. The NH\n                    <jats:sub>2<\/jats:sub>\n                    -terminal catalytic fragment, known as miniTyrRS, binds strongly to the CXC-chemokine receptor CXCR1 and, like interleukin 8, functions as a chemoattractant for polymorphonuclear leukocytes. On the other hand, an extra COOH-terminal domain of human TyrRS has cytokine activities like those of a mature human endothelial monocyte-activating polypeptide II (EMAP II). Moreover, the etiology of specific diseases (cancer, neuronal pathologies, autoimmune disorders, and disrupted metabolic conditions) is connected to specific aminoacyl-tRNA synthetases. Here we report the generation and characterization of monoclonal antibodies specific to N- and C-terminal domains of TyrRS. Recombinant TyrRS and its N- and C-terminal domains were expressed as His-tag fusion proteins in bacteria. Affinity purified proteins have been used as antigens for immunization and hybridoma cell screening. Monoclonal antibodies specific to catalytic N-terminal module and C-terminal EMAP II-like domain of TyrRS may be useful as tools in various aspects of TyrRS function and cellular localization.\n                  <\/jats:p>","DOI":"10.1089\/mab.2012.0096","type":"journal-article","created":{"date-parts":[[2013,6,10]],"date-time":"2013-06-10T10:36:23Z","timestamp":1370860583000},"page":"200-204","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":2,"title":["Monoclonal Antibodies Against Tyrosyl-tRNA Synthetase and Its Isolated Cytokine-Like Domain"],"prefix":"10.1177","volume":"32","author":[{"given":"Iuliia","family":"Kondratiuk","sequence":"first","affiliation":[{"name":"Institute of Molecular Biology and Genetics","place":["Ukraine"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Antonina","family":"Khoruzenko","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biology and Genetics","place":["Ukraine"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Olga","family":"Cherednyk","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biology and Genetics","place":["Ukraine"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Valeriy","family":"Filonenko","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biology and Genetics","place":["Ukraine"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aleksander","family":"Kornelyuk","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biology and Genetics","place":["Ukraine"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","published-online":{"date-parts":[[2013,6]]},"reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.46.29295"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibs.2005.08.004"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1080\/15216540600735974"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.012602099"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibs.2004.03.002"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1086\/375039"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng1727"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng0197-91"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng2013"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.3181\/00379727-153-39526"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.1999.0141"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.2169\/internalmedicine.44.527"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0802862105"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.7124\/bc.0004DF"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.33.23155"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.284.5411.147"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.7124\/bc.000516"},{"key":"e_1_3_3_19_2","first-page":"33","article-title":"Optimization of biosynthesis process of catalytic module of mammalian tyrosyl-tRNA synthetase and its research by immunochemical methods","volume":"56","author":"Kondratiuk I","year":"2010","unstructured":"Kondratiuk I, , Babaryk MA, , Sidorik LL, , Kornelyuk OI. Optimization of biosynthesis process of catalytic module of mammalian tyrosyl-tRNA synthetase and its research by immunochemical methods. J Taras Shevchenko Natl Univ Kyiv Biol, 2010; 56:33\u201335.","journal-title":"J Taras Shevchenko Natl Univ Kyiv Biol"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.7124\/bc.00016B"},{"key":"e_1_3_3_21_2","first-page":"6","article-title":"Optimization of bacterial expression of mammalian tyrosyl-tRNA synthetase on cultivation strain Escherichia coli BL21 (DE3) pLysE","volume":"4","author":"Kondratiuk I","year":"2009","unstructured":"Kondratiuk I, , Babaryk MA, , Kornelyuk AI. Optimization of bacterial expression of mammalian tyrosyl-tRNA synthetase on cultivation strain Escherichia coli BL21 (DE3) pLysE. Microbiol Biotechnol, 2009; 4:6\u201312.","journal-title":"Microbiol Biotechnol"},{"key":"e_1_3_3_22_2","volume-title":"Antibodies: A Laboratory Manual","author":"Harlow E","year":"1998","unstructured":"Harlow E, , Lane D. Antibodies: A Laboratory Manual. Cold Spring Harbor Press: Cold Spring Harbor, NY, 1998."},{"key":"e_1_3_3_23_2","unstructured":"Hurrell JGR. Monoclonal Hybridoma Antibodies: Techniques Application. CRC Press: Boca Raton FL 1982."},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.2876518"},{"key":"e_1_3_3_26_2","first-page":"250","article-title":"Cytokine-like activities of some aminoacyl-tRNA synthetases and auxiliary p43 cofactor of aminoacylation reaction and their role in oncogenesis","volume":"26","author":"Ivakhno SS","year":"2004","unstructured":"Ivakhno SS, , Kornelyuk AI. Cytokine-like activities of some aminoacyl-tRNA synthetases and auxiliary p43 cofactor of aminoacylation reaction and their role in oncogenesis. 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