<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE root>
<article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="other" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Advances in Molecular Oncology</journal-id><journal-title-group><journal-title xml:lang="en">Advances in Molecular Oncology</journal-title><trans-title-group xml:lang="ru"><trans-title>Успехи молекулярной онкологии</trans-title></trans-title-group></journal-title-group><issn publication-format="print">2313-805X</issn><issn publication-format="electronic">2413-3787</issn><publisher><publisher-name xml:lang="en">Publishing House ABV Press</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">83</article-id><article-id pub-id-type="doi">10.17650/2313-805X-2017-4-1-17-23</article-id><article-categories><subj-group subj-group-type="toc-heading" xml:lang="en"><subject>REVIEW ARTICLES</subject></subj-group><subj-group subj-group-type="toc-heading" xml:lang="ru"><subject>ОБЗОРНЫЕ СТАТЬИ</subject></subj-group><subj-group subj-group-type="article-type"><subject></subject></subj-group></article-categories><title-group><article-title xml:lang="en">The thymidine kinase-1 as a potential tumor marker: structure, function, activity in normal and malignant tissues</article-title><trans-title-group xml:lang="ru"><trans-title>Тимидинкиназа 1 как потенциальный опухолеассоциированный маркер: структура, функции, активность в нормальных и опухолевых тканях</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Sergeeva</surname><given-names>N. S.</given-names></name><name xml:lang="ru"><surname>Сергеева</surname><given-names>Н. С.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p>Department of Conservative Treatment Prognosis</p><p>3 2nd Botkinskiy Proezd, Moscow 125284, Russia</p><p>1 Ostrovityanovа St., Moscow 117997, Russia</p></bio><bio xml:lang="ru"><p>Отделение прогноза эффективности консервативного лечения</p><p>Россия, 125284 Москва, 2-й Боткинский проезд, 3</p><p>Россия, 117997 Москва, ул. Островитянова, 1</p></bio><email>prognoz.06@mail.ru</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Parilova</surname><given-names>N. K.</given-names></name><name xml:lang="ru"><surname>Парилова</surname><given-names>Н. К.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p>Department of Conservative Treatment Prognosis</p><p>3 2nd Botkinskiy Proezd, Moscow 125284, Russia</p></bio><bio xml:lang="ru"><p>Отделение прогноза эффективности консервативного лечения</p><p>Россия, 125284 Москва, 2-й Боткинский проезд, 3</p></bio><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Marshutina</surname><given-names>N. V.</given-names></name><name xml:lang="ru"><surname>Маршутина</surname><given-names>Н. В.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p>Department of Conservative Treatment Prognosis</p><p>3 2nd Botkinskiy Proezd, Moscow 125284, Russia</p></bio><bio xml:lang="ru"><p>Отделение прогноза эффективности консервативного лечения</p><p>Россия, 125284 Москва, 2-й Боткинский проезд, 3</p></bio><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Meysner</surname><given-names>I. S.</given-names></name><name xml:lang="ru"><surname>Мейснер</surname><given-names>И. С.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p>1 Ostrovityanovа St., Moscow 117997, Russia</p></bio><bio xml:lang="ru"><p>Россия, 117997 Москва, ул. Островитянова, 1</p></bio><xref ref-type="aff" rid="aff3"/></contrib></contrib-group><aff-alternatives id="aff1"><aff><institution xml:lang="en">P.A. Hertzen Moscow Oncology Research Institute – branch of the National Medical Research Radiological Center, Ministry of Health of Russia&#13;
&#13;
N.I. Pirogov Russian National Research Medical University, Ministry of Health of Russia</institution></aff><aff><institution xml:lang="ru">Московский научно-исследовательский онкологический институт им. П.А. Герцена – филиала ФГБУ «Национальный медицинский исследовательский радиологический центр» Минздрава России&#13;
&#13;
ФГБОУ ВО «Российский национальный исследовательский медицинский университет им. Н.И. Пирогова» Минздрава России</institution></aff></aff-alternatives><aff-alternatives id="aff2"><aff><institution xml:lang="en">P.A. Hertzen Moscow Oncology Research Institute – branch of the National Medical Research Radiological Center, Ministry of Health of Russia</institution></aff><aff><institution xml:lang="ru">Московский научно-исследовательский онкологический институт им. П.А. Герцена – филиала ФГБУ «Национальный медицинский исследовательский радиологический центр» Минздрава России</institution></aff></aff-alternatives><aff-alternatives id="aff3"><aff><institution xml:lang="en">N.I. Pirogov Russian National Research Medical University, Ministry of Health of Russia</institution></aff><aff><institution xml:lang="ru">ФГБОУ ВО «Российский национальный исследовательский медицинский университет им. Н.И. Пирогова» Минздрава России</institution></aff></aff-alternatives><pub-date date-type="pub" iso-8601-date="2017-01-15" publication-format="electronic"><day>15</day><month>01</month><year>2017</year></pub-date><volume>4</volume><issue>1</issue><issue-title xml:lang="en"/><issue-title xml:lang="ru"/><fpage>17</fpage><lpage>23</lpage><history><date date-type="received" iso-8601-date="2017-04-18"><day>18</day><month>04</month><year>2017</year></date><date date-type="accepted" iso-8601-date="2017-04-18"><day>18</day><month>04</month><year>2017</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2017, Sergeeva N.S., Parilova N.K., Marshutina N.V., Meysner I.S.</copyright-statement><copyright-statement xml:lang="ru">Copyright ©; 2017, Сергеева Н.С., Парилова Н.К., Маршутина Н.В., Мейснер И.С.</copyright-statement><copyright-year>2017</copyright-year><copyright-holder xml:lang="en">Sergeeva N.S., Parilova N.K., Marshutina N.V., Meysner I.S.</copyright-holder><copyright-holder xml:lang="ru">Сергеева Н.С., Парилова Н.К., Маршутина Н.В., Мейснер И.С.</copyright-holder><ali:free_to_read xmlns:ali="http://www.niso.org/schemas/ali/1.0/"/><license><ali:license_ref xmlns:ali="http://www.niso.org/schemas/ali/1.0/">https://creativecommons.org/licenses/by/4.0</ali:license_ref></license></permissions><self-uri xlink:href="https://umo.abvpress.ru/jour/article/view/83">https://umo.abvpress.ru/jour/article/view/83</self-uri><abstract xml:lang="en"><p>In the review the role of the thymidine kinase (TK) to ensure the replication of DNA de novo and spare (salvage the) way in health and activate alternate ways in carcinogenesis is described. The structure of cytoplasmic TK (TК-1), also called fetal, and the level of regulation of its activity in the cells and their change during the cell cycle is described. Considering the data about the absence of TK-1 in resting (G0) cells, TK-1 is positioned as a marker of proliferating cells, which activity is recorded from late G1 phase, peaking in S-phase, it is stored in the G2 and mitosis, quickly decreasing to undetectable levels in the early G1 phase. Data on the expression TK-1 (as compared with Ki-67 and PCNA (proliferating cell nuclear antigen)) in tumor tissues (colorectal, breast, cervical, lung, renal, prostate and ovarian cancer), as well as some benign and precancerous pathological processes in relation to the clinical and diagnostic features of these processes are systemized. These data suggest that the proliferative index studies on TK-1 (antibody to the domain HRA-210) should be used together with Ki-67 and PCNA, for a more complete assessment of the proliferative status of malignant tumors and pre-cancerous and benign conditions, with the aim of prognosis of the tumor process and treatment planning.</p></abstract><trans-abstract xml:lang="ru"><p/></trans-abstract><kwd-group xml:lang="en"><kwd>thymidine kinase 1 (TK-1)</kwd><kwd>Ki-67</kwd><kwd>PCNA</kwd><kwd>cell cycle</kwd><kwd>carcinogenesis</kwd></kwd-group><kwd-group xml:lang="ru"><kwd>тимидинкиназа 1 (ТК-1)</kwd><kwd>Ki-67</kwd><kwd>PCNA</kwd><kwd>клеточный цикл</kwd><kwd>канцерогенез</kwd></kwd-group><funding-group/></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><citation-alternatives><mixed-citation xml:lang="en">1. Силаева С.А. Раздел 10. Обмен нуклеотидов. В кн.: Биохимия. Учебник для вузов. Под ред. Е.С. Северина, 2003. 779 с. С. 521–44. [Silaeva S.A. Section 10. Nucleotide metabolism. In: Biochemistry. University textbook. Ed. by E.S. Severin, 2003. 779 p. Pp. 521– 44. (In Russ.)].</mixed-citation><mixed-citation xml:lang="ru">Силаева С.А. Раздел 10. Обмен нуклеотидов. В кн.: Биохимия. Учебник для вузов. Под ред. Е.С. Северина, 2003. 779 с. С. 521–44. [Silaeva S.A. Section 10. Nucleotide metabolism. In: Biochemistry. University textbook. Ed. by E.S. Severin, 2003. 779 p. Pp. 521– 44. (In Russ.)].</mixed-citation></citation-alternatives></ref><ref id="B2"><label>2.</label><citation-alternatives><mixed-citation xml:lang="en">2. Welin M., Kosinska U., Mikkelsen N.-E. et al. Structures of thymidine kinase 1 of human and mycoplasma origin. Proc Natl Acad Sci U S A 2004;101(52): 17970–5.</mixed-citation><mixed-citation xml:lang="ru">Welin M., Kosinska U., Mikkelsen N.-E. et al. Structures of thymidine kinase 1 of human and mycoplasma origin. Proc Natl Acad Sci U S A 2004;101(52): 17970–5.</mixed-citation></citation-alternatives></ref><ref id="B3"><label>3.</label><citation-alternatives><mixed-citation xml:lang="en">3. Jordan A., Reichard P. Ribonucleotide reductases. Annu Rev Biochem 1998;67:71–98.</mixed-citation><mixed-citation xml:lang="ru">Jordan A., Reichard P. Ribonucleotide reductases. Annu Rev Biochem 1998;67:71–98.</mixed-citation></citation-alternatives></ref><ref id="B4"><label>4.</label><citation-alternatives><mixed-citation xml:lang="en">4. Arner E.S., Eriksson S. Mammalian deoxyribonucleoside kinases. Pharmacol Ther 1995;67(2):155–86. DOI: 10.1016/0163-7258(95)00015-9.</mixed-citation><mixed-citation xml:lang="ru">Arner E.S., Eriksson S. Mammalian deoxyribonucleoside kinases. Pharmacol Ther 1995;67(2):155–86. DOI: 10.1016/0163-7258(95)00015-9.</mixed-citation></citation-alternatives></ref><ref id="B5"><label>5.</label><citation-alternatives><mixed-citation xml:lang="en">5. Bello L.J. Regulation of thymidine kinase synthesys in human cells. Exp Cell Res 1974;89(2):263–74.</mixed-citation><mixed-citation xml:lang="ru">Bello L.J. Regulation of thymidine kinase synthesys in human cells. Exp Cell Res 1974;89(2):263–74.</mixed-citation></citation-alternatives></ref><ref id="B6"><label>6.</label><citation-alternatives><mixed-citation xml:lang="en">6. Munch-Petersen B., Tyrsted G. Induction of thymidine kinases in phytohaemagglutinin- stimulated human lymphocytes. Biochim Biophys Acta 1977;478(3): 364–75.</mixed-citation><mixed-citation xml:lang="ru">Munch-Petersen B., Tyrsted G. Induction of thymidine kinases in phytohaemagglutinin- stimulated human lymphocytes. Biochim Biophys Acta 1977;478(3): 364–75.</mixed-citation></citation-alternatives></ref><ref id="B7"><label>7.</label><citation-alternatives><mixed-citation xml:lang="en">7. Sherley J.L., Kelly T.J. Regulation of human thymidine kinase during the cell cycle. J Biol Chem 1988;263(17):8350–8.</mixed-citation><mixed-citation xml:lang="ru">Sherley J.L., Kelly T.J. Regulation of human thymidine kinase during the cell cycle. J Biol Chem 1988;263(17):8350–8.</mixed-citation></citation-alternatives></ref><ref id="B8"><label>8.</label><citation-alternatives><mixed-citation xml:lang="en">8. Segura-Pena D., Lichter J., Trani M. et al. Quaternary structure change as a mechanism for the regulation of thymidine kinase 1-like enzymes. Structure 2007;15(12):1555–66. DOI: 10.1016/j.str.2007.09.025. PMID: 18073106.</mixed-citation><mixed-citation xml:lang="ru">Segura-Pena D., Lichter J., Trani M. et al. Quaternary structure change as a mechanism for the regulation of thymidine kinase 1-like enzymes. Structure 2007;15(12):1555–66. DOI: 10.1016/j.str.2007.09.025. PMID: 18073106.</mixed-citation></citation-alternatives></ref><ref id="B9"><label>9.</label><citation-alternatives><mixed-citation xml:lang="en">9. Kornberg A., Lehman I.R., Simms E.S. Polydeoxyribosides in the synthesis of polynucleotides. Fed Proc 1956;15: 291–2.</mixed-citation><mixed-citation xml:lang="ru">Kornberg A., Lehman I.R., Simms E.S. Polydeoxyribosides in the synthesis of polynucleotides. Fed Proc 1956;15: 291–2.</mixed-citation></citation-alternatives></ref><ref id="B10"><label>10.</label><citation-alternatives><mixed-citation xml:lang="en">10. Reichard P., Estborn B. Utilization of desoxyribosides in the synthesis of polynucleotides. J Biol Chem 1951;188(2):839–46. PMID: 14824173.</mixed-citation><mixed-citation xml:lang="ru">Reichard P., Estborn B. Utilization of desoxyribosides in the synthesis of polynucleotides. J Biol Chem 1951;188(2):839–46. PMID: 14824173.</mixed-citation></citation-alternatives></ref><ref id="B11"><label>11.</label><citation-alternatives><mixed-citation xml:lang="en">11. Mathews C.K. Enzymatic channeling of DNA precursors. Basic Life Sci 1985;31:47–66.</mixed-citation><mixed-citation xml:lang="ru">Mathews C.K. Enzymatic channeling of DNA precursors. Basic Life Sci 1985;31:47–66.</mixed-citation></citation-alternatives></ref><ref id="B12"><label>12.</label><citation-alternatives><mixed-citation xml:lang="en">12. Leeds J.M., Mathews C.K. Cell cycledependent effects on deoxyribonucleotide and DNA labeling by nucleoside precursors in mammalian cells. Mol Cell Biol 1987;7(1):532–4.</mixed-citation><mixed-citation xml:lang="ru">Leeds J.M., Mathews C.K. Cell cycledependent effects on deoxyribonucleotide and DNA labeling by nucleoside precursors in mammalian cells. Mol Cell Biol 1987;7(1):532–4.</mixed-citation></citation-alternatives></ref><ref id="B13"><label>13.</label><citation-alternatives><mixed-citation xml:lang="en">13. Nicander B., Reichard P. Dynamics of pyrimidine deoxynucleoside triphosphate pools in relationship to DNA synthesis in 3T6 mouse fibroblasts. Proc Natl Acad Sci U S A 1983;80(5): 1347–51.</mixed-citation><mixed-citation xml:lang="ru">Nicander B., Reichard P. Dynamics of pyrimidine deoxynucleoside triphosphate pools in relationship to DNA synthesis in 3T6 mouse fibroblasts. Proc Natl Acad Sci U S A 1983;80(5): 1347–51.</mixed-citation></citation-alternatives></ref><ref id="B14"><label>14.</label><citation-alternatives><mixed-citation xml:lang="en">14. Bollum F.J., Van Potter R. Incorporation of thymidine into deoxyribonucleic acid by enzymes from rat tissues. J Biol Chem 1958;233:478–82.</mixed-citation><mixed-citation xml:lang="ru">Bollum F.J., Van Potter R. Incorporation of thymidine into deoxyribonucleic acid by enzymes from rat tissues. J Biol Chem 1958;233:478–82.</mixed-citation></citation-alternatives></ref><ref id="B15"><label>15.</label><citation-alternatives><mixed-citation xml:lang="en">15. Bollum F.J., Van Potter R. Nucleic acid metabolism in regenerating rat liver. Soluble enzymes which convert thymidine to thymidine phosphates and DNA. Cancer Res 1959;19:561–5.</mixed-citation><mixed-citation xml:lang="ru">Bollum F.J., Van Potter R. Nucleic acid metabolism in regenerating rat liver. Soluble enzymes which convert thymidine to thymidine phosphates and DNA. Cancer Res 1959;19:561–5.</mixed-citation></citation-alternatives></ref><ref id="B16"><label>16.</label><citation-alternatives><mixed-citation xml:lang="en">16. Weissman S.M., Smellie R.M., Paul J. Studies on the biosynthesis of deoxyribonucleic acid by extracts of mammalian cells. IV. The phosphorylation of thymidine. Biochim Biophys Acta 1960;45:101–10.</mixed-citation><mixed-citation xml:lang="ru">Weissman S.M., Smellie R.M., Paul J. Studies on the biosynthesis of deoxyribonucleic acid by extracts of mammalian cells. IV. The phosphorylation of thymidine. Biochim Biophys Acta 1960;45:101–10.</mixed-citation></citation-alternatives></ref><ref id="B17"><label>17.</label><citation-alternatives><mixed-citation xml:lang="en">17. Okazaki R., Kornberg A. Deoxythymidine kinase of Escherichia coli. I. Purification and some properties of the enzyme. J Biol Chem 1964; 239:269–74.</mixed-citation><mixed-citation xml:lang="ru">Okazaki R., Kornberg A. Deoxythymidine kinase of Escherichia coli. I. Purification and some properties of the enzyme. J Biol Chem 1964; 239:269–74.</mixed-citation></citation-alternatives></ref><ref id="B18"><label>18.</label><citation-alternatives><mixed-citation xml:lang="en">18. Hotta Y., Stern H. Molecular facets of mitotic regulation 1. Synthesis of thymidine kinase. Proc Natl Acad Sci U S A 1963;49(5):648–54.</mixed-citation><mixed-citation xml:lang="ru">Hotta Y., Stern H. Molecular facets of mitotic regulation 1. Synthesis of thymidine kinase. Proc Natl Acad Sci U S A 1963;49(5):648–54.</mixed-citation></citation-alternatives></ref><ref id="B19"><label>19.</label><citation-alternatives><mixed-citation xml:lang="en">19. Chello P.L., Jaffe J.J. Comparative properties of trypanosomal and mammalian thymidine kinases. Comp Biochem Physiol 1972;43(3):543–62.</mixed-citation><mixed-citation xml:lang="ru">Chello P.L., Jaffe J.J. Comparative properties of trypanosomal and mammalian thymidine kinases. Comp Biochem Physiol 1972;43(3):543–62.</mixed-citation></citation-alternatives></ref><ref id="B20"><label>20.</label><citation-alternatives><mixed-citation xml:lang="en">20. Kit S., Dubbs D.R. Acquisition of thymidine kinase activity by Herpes simplex infected mouse fibroblast cells. Biochem Biophys Res Commun 1963;11:55–9.</mixed-citation><mixed-citation xml:lang="ru">Kit S., Dubbs D.R. Acquisition of thymidine kinase activity by Herpes simplex infected mouse fibroblast cells. Biochem Biophys Res Commun 1963;11:55–9.</mixed-citation></citation-alternatives></ref><ref id="B21"><label>21.</label><citation-alternatives><mixed-citation xml:lang="en">21. Littlefield J.W. The periodic synthesis of thymidine kinase in mouse fibroblasts. Biochim Biophys Acta 1966;114(2): 398–403.</mixed-citation><mixed-citation xml:lang="ru">Littlefield J.W. The periodic synthesis of thymidine kinase in mouse fibroblasts. Biochim Biophys Acta 1966;114(2): 398–403.</mixed-citation></citation-alternatives></ref><ref id="B22"><label>22.</label><citation-alternatives><mixed-citation xml:lang="en">22. Berk A.J., Clayton D.A. A genetically distinct thymidine kinase in mammalian mitochondria. Exclusive labeling of mitochondrial deoxyribonucleic acid. J Biol Chem 1973;248(8):2722–9.</mixed-citation><mixed-citation xml:lang="ru">Berk A.J., Clayton D.A. A genetically distinct thymidine kinase in mammalian mitochondria. Exclusive labeling of mitochondrial deoxyribonucleic acid. J Biol Chem 1973;248(8):2722–9.</mixed-citation></citation-alternatives></ref><ref id="B23"><label>23.</label><citation-alternatives><mixed-citation xml:lang="en">23. Berk A.J., Meyer B.J., Clayton D.A. Mitochondrial-specific thymidine kinase. Arch Biochem Biophys 1973;154(2): 563–5.</mixed-citation><mixed-citation xml:lang="ru">Berk A.J., Meyer B.J., Clayton D.A. Mitochondrial-specific thymidine kinase. Arch Biochem Biophys 1973;154(2): 563–5.</mixed-citation></citation-alternatives></ref><ref id="B24"><label>24.</label><citation-alternatives><mixed-citation xml:lang="en">24. Elsevier S.M., Kucherlapati R.S., Nichols E.A. et al. Assignment of the gene for galactokinase to human chromosome 17 and its regional localisation to band q21-22. Nature 1974;251(5476):633–6.</mixed-citation><mixed-citation xml:lang="ru">Elsevier S.M., Kucherlapati R.S., Nichols E.A. et al. Assignment of the gene for galactokinase to human chromosome 17 and its regional localisation to band q21-22. Nature 1974;251(5476):633–6.</mixed-citation></citation-alternatives></ref><ref id="B25"><label>25.</label><citation-alternatives><mixed-citation xml:lang="en">25. Kuo W.L., Hirschhorn R., Huie M.L., Hirschhorn K. Localization and ordering of acid alpha- glucosidase (GAA) and thymidine kinase (TK1) by fluorescence in situ hybridization. Hum Genet 1996;97(3):404–6.</mixed-citation><mixed-citation xml:lang="ru">Kuo W.L., Hirschhorn R., Huie M.L., Hirschhorn K. Localization and ordering of acid alpha- glucosidase (GAA) and thymidine kinase (TK1) by fluorescence in situ hybridization. Hum Genet 1996;97(3):404–6.</mixed-citation></citation-alternatives></ref><ref id="B26"><label>26.</label><citation-alternatives><mixed-citation xml:lang="en">26. Schoen R.C., Cox S.H., Wagner R.P. Thymidine-kinase activity of cultured cells from individuals with inherited galactokinase deficiency. Am J Hum Genet 1984;36(4):815–22.</mixed-citation><mixed-citation xml:lang="ru">Schoen R.C., Cox S.H., Wagner R.P. Thymidine-kinase activity of cultured cells from individuals with inherited galactokinase deficiency. Am J Hum Genet 1984;36(4):815–22.</mixed-citation></citation-alternatives></ref><ref id="B27"><label>27.</label><citation-alternatives><mixed-citation xml:lang="en">27. Bradshaw H.D. Jr, Deininger P.L. Human thymidine kinase gene: molecular cloning and nucleotide sequence of a cDNA expressible in mammalian cells. Mol Cell Biol 1984;4(11):2316–20.</mixed-citation><mixed-citation xml:lang="ru">Bradshaw H.D. Jr, Deininger P.L. Human thymidine kinase gene: molecular cloning and nucleotide sequence of a cDNA expressible in mammalian cells. Mol Cell Biol 1984;4(11):2316–20.</mixed-citation></citation-alternatives></ref><ref id="B28"><label>28.</label><citation-alternatives><mixed-citation xml:lang="en">28. Murphy P.D., Kidd J.R., Castiglione C.M. et al. A frequent polymorphism for the cytosolic thymidine kinase gene, TK1, (17q21–q22) detected by the enzyme TaqI. Nucleic Acids Res 1986;14(10):4381.</mixed-citation><mixed-citation xml:lang="ru">Murphy P.D., Kidd J.R., Castiglione C.M. et al. A frequent polymorphism for the cytosolic thymidine kinase gene, TK1, (17q21–q22) detected by the enzyme TaqI. Nucleic Acids Res 1986;14(10):4381.</mixed-citation></citation-alternatives></ref><ref id="B29"><label>29.</label><citation-alternatives><mixed-citation xml:lang="en">29. Dutrillaux B., Muleris M. Induction of increased salvage pathways of nucleotide synthesis by dosage effect due to chromosome imbalances may be fundamental in carcinogenesis: the example of colorectal carcinoma. Ann Genet 1986;29(1):11–5.</mixed-citation><mixed-citation xml:lang="ru">Dutrillaux B., Muleris M. Induction of increased salvage pathways of nucleotide synthesis by dosage effect due to chromosome imbalances may be fundamental in carcinogenesis: the example of colorectal carcinoma. Ann Genet 1986;29(1):11–5.</mixed-citation></citation-alternatives></ref><ref id="B30"><label>30.</label><citation-alternatives><mixed-citation xml:lang="en">30. Hanan S., Jagarlamudi K.K., Liya W. et al. Quaternary structures of recombinant, cellular, and serum forms of thymidine kinase 1 from dogs and humans. BMC Biochem 2012;13:12. DOI: 10.1186/1471-2091-13-12. PMID: 22741536.</mixed-citation><mixed-citation xml:lang="ru">Hanan S., Jagarlamudi K.K., Liya W. et al. Quaternary structures of recombinant, cellular, and serum forms of thymidine kinase 1 from dogs and humans. BMC Biochem 2012;13:12. DOI: 10.1186/1471-2091-13-12. PMID: 22741536.</mixed-citation></citation-alternatives></ref><ref id="B31"><label>31.</label><citation-alternatives><mixed-citation xml:lang="en">31. Karlström A.R., Neumüller M., Gronowitz J.S., Källander C.F. Molecular forms in human serum of enzymes synthesizing DNA precursors and DNA. Mol Cell Biochem 1990;92(1):23–35.</mixed-citation><mixed-citation xml:lang="ru">Karlström A.R., Neumüller M., Gronowitz J.S., Källander C.F. Molecular forms in human serum of enzymes synthesizing DNA precursors and DNA. Mol Cell Biochem 1990;92(1):23–35.</mixed-citation></citation-alternatives></ref><ref id="B32"><label>32.</label><citation-alternatives><mixed-citation xml:lang="en">32. Birringer M.S., Claus M.T., Folkers G. et al. Structure of a type II thymidine kinase with bound dTTP. FEBS Lett 2005;579(6):1376–82. DOI: 10.1016/j.febslet.2005.01.034.</mixed-citation><mixed-citation xml:lang="ru">Birringer M.S., Claus M.T., Folkers G. et al. Structure of a type II thymidine kinase with bound dTTP. FEBS Lett 2005;579(6):1376–82. DOI: 10.1016/j.febslet.2005.01.034.</mixed-citation></citation-alternatives></ref><ref id="B33"><label>33.</label><citation-alternatives><mixed-citation xml:lang="en">33. Munch-Petersen B., Cloos L., Jensen H.K., Tyrsted G. Human thymidine kinase 1. Regulation in normal and malignant cells. Adv Enzyme Regul 1995;35:69–89.</mixed-citation><mixed-citation xml:lang="ru">Munch-Petersen B., Cloos L., Jensen H.K., Tyrsted G. Human thymidine kinase 1. Regulation in normal and malignant cells. Adv Enzyme Regul 1995;35:69–89.</mixed-citation></citation-alternatives></ref><ref id="B34"><label>34.</label><citation-alternatives><mixed-citation xml:lang="en">34. Li C.L., Lu C.Y., Ke P.Y., Chang Z.F. Perturbation of ATP-induced tetramerization of human cytosolic thymidine kinase by substitution of serine-13 with aspartic acid at the mitotic phosphorylation site. Biochem Biophys Res Commun 2004;313(3):587–93.</mixed-citation><mixed-citation xml:lang="ru">Li C.L., Lu C.Y., Ke P.Y., Chang Z.F. Perturbation of ATP-induced tetramerization of human cytosolic thymidine kinase by substitution of serine-13 with aspartic acid at the mitotic phosphorylation site. Biochem Biophys Res Commun 2004;313(3):587–93.</mixed-citation></citation-alternatives></ref><ref id="B35"><label>35.</label><citation-alternatives><mixed-citation xml:lang="en">35. He Q., Wang N., Skog S. et al. Characterization of a peptide antibody against a Cterminal part of human and mouse cytosolic thymidine kinase, which is a marker for cell proliferation. Eur J Cell Biol 1996;70(2):117–24.</mixed-citation><mixed-citation xml:lang="ru">He Q., Wang N., Skog S. et al. Characterization of a peptide antibody against a Cterminal part of human and mouse cytosolic thymidine kinase, which is a marker for cell proliferation. Eur J Cell Biol 1996;70(2):117–24.</mixed-citation></citation-alternatives></ref><ref id="B36"><label>36.</label><citation-alternatives><mixed-citation xml:lang="en">36. Wang N., He Q., Skog S. et al. Investigation on cell proliferation with new antibody against thymidine kinase 1. Anal Cell Pathol 2001;23(1):11–9.</mixed-citation><mixed-citation xml:lang="ru">Wang N., He Q., Skog S. et al. Investigation on cell proliferation with new antibody against thymidine kinase 1. Anal Cell Pathol 2001;23(1):11–9.</mixed-citation></citation-alternatives></ref><ref id="B37"><label>37.</label><citation-alternatives><mixed-citation xml:lang="en">37. Wu C., Yang R., Zhou J. et al. Production and characterisation of a novel chicken IgY antibody raised against C-terminal peptide from human thymidine kinase 1. J Immunol Methods 2003;277(1–2): 157–69.</mixed-citation><mixed-citation xml:lang="ru">Wu C., Yang R., Zhou J. et al. Production and characterisation of a novel chicken IgY antibody raised against C-terminal peptide from human thymidine kinase 1. J Immunol Methods 2003;277(1–2): 157–69.</mixed-citation></citation-alternatives></ref><ref id="B38"><label>38.</label><citation-alternatives><mixed-citation xml:lang="en">38. Eriksson S. New exposed proliferation related peptide, ligands and methods employing the same. PCT application WO 2008:142664.</mixed-citation><mixed-citation xml:lang="ru">Eriksson S. New exposed proliferation related peptide, ligands and methods employing the same. PCT application WO 2008:142664.</mixed-citation></citation-alternatives></ref><ref id="B39"><label>39.</label><citation-alternatives><mixed-citation xml:lang="en">39. Gasparri F., Wang N., Skog S. et al. Thymidine kinase 1 expression defines as activated G1 state of cell cycle as revealed with site-specific antibodies and ArrayScan assays. Eur J Cell Biol 2009;88(12):779–85.</mixed-citation><mixed-citation xml:lang="ru">Gasparri F., Wang N., Skog S. et al. Thymidine kinase 1 expression defines as activated G1 state of cell cycle as revealed with site-specific antibodies and ArrayScan assays. Eur J Cell Biol 2009;88(12):779–85.</mixed-citation></citation-alternatives></ref><ref id="B40"><label>40.</label><citation-alternatives><mixed-citation xml:lang="en">40. Coppock D.L., Pardee A.B. Control of thymidine kinase mRNA during the cell cycle. Mol Cell Biol 1987;7(8):2925–32.</mixed-citation><mixed-citation xml:lang="ru">Coppock D.L., Pardee A.B. Control of thymidine kinase mRNA during the cell cycle. Mol Cell Biol 1987;7(8):2925–32.</mixed-citation></citation-alternatives></ref><ref id="B41"><label>41.</label><citation-alternatives><mixed-citation xml:lang="en">41. Gerdes J., Schwab U., Lemke H., Stein H. Production of a mouse monoclonal antibody reactive with a human nuclear antigen associated with cell proliferation. Int J Cancer 1983;31(1):13–20.</mixed-citation><mixed-citation xml:lang="ru">Gerdes J., Schwab U., Lemke H., Stein H. Production of a mouse monoclonal antibody reactive with a human nuclear antigen associated with cell proliferation. Int J Cancer 1983;31(1):13–20.</mixed-citation></citation-alternatives></ref><ref id="B42"><label>42.</label><citation-alternatives><mixed-citation xml:lang="en">42. Gross M.K., Kainz M.S., Merrill G.F. The chicken thymidine kinase gene is transcriptionally repressed during terminal differentiation: the associated decline in TK mRNA cannot account fully for the disappearance of TK enzyme activity. Dev Biol 1987;122(2):439–51.</mixed-citation><mixed-citation xml:lang="ru">Gross M.K., Kainz M.S., Merrill G.F. The chicken thymidine kinase gene is transcriptionally repressed during terminal differentiation: the associated decline in TK mRNA cannot account fully for the disappearance of TK enzyme activity. Dev Biol 1987;122(2):439–51.</mixed-citation></citation-alternatives></ref><ref id="B43"><label>43.</label><citation-alternatives><mixed-citation xml:lang="en">43. Kauffman M.G., Kelly T.J. Cell cycle regulation of thymidine kinase: residues near the carboxyl terminus are essential for the specific degradation of the enzyme at mitosis. Mol Cell Biol 1991;11(5):2538– 46.</mixed-citation><mixed-citation xml:lang="ru">Kauffman M.G., Kelly T.J. Cell cycle regulation of thymidine kinase: residues near the carboxyl terminus are essential for the specific degradation of the enzyme at mitosis. Mol Cell Biol 1991;11(5):2538– 46.</mixed-citation></citation-alternatives></ref><ref id="B44"><label>44.</label><citation-alternatives><mixed-citation xml:lang="en">44. Sutterluety H., Bartl S., Karlseder J. et al. Carboxy-terminal residues of mouse thymidine kinase are essential for rapid degradation in quiescent cells. J Mol Biol 1996;259(3):383–92.</mixed-citation><mixed-citation xml:lang="ru">Sutterluety H., Bartl S., Karlseder J. et al. Carboxy-terminal residues of mouse thymidine kinase are essential for rapid degradation in quiescent cells. J Mol Biol 1996;259(3):383–92.</mixed-citation></citation-alternatives></ref><ref id="B45"><label>45.</label><citation-alternatives><mixed-citation xml:lang="en">45. Hu C.M., Chang Z.F. Mitotic control of dTTP pool: a necessity or coincidence? J Biomed Sci 2007;14(4):491–7.</mixed-citation><mixed-citation xml:lang="ru">Hu C.M., Chang Z.F. Mitotic control of dTTP pool: a necessity or coincidence? J Biomed Sci 2007;14(4):491–7.</mixed-citation></citation-alternatives></ref><ref id="B46"><label>46.</label><citation-alternatives><mixed-citation xml:lang="en">46. Ke P.Y., Kuo Y.Y., Hu C.M., Chang Z.F. Control of dTTP pool size by anaphase promoting complex/cyclosome is essential for the maintenance of genetic stability. Genes Dev 2005;19(16):1920–33.</mixed-citation><mixed-citation xml:lang="ru">Ke P.Y., Kuo Y.Y., Hu C.M., Chang Z.F. Control of dTTP pool size by anaphase promoting complex/cyclosome is essential for the maintenance of genetic stability. Genes Dev 2005;19(16):1920–33.</mixed-citation></citation-alternatives></ref><ref id="B47"><label>47.</label><citation-alternatives><mixed-citation xml:lang="en">47. Dobrovolsky V.N., Bucci T., Heflich R.H. et al. Mice deficient for cytosolic thymidine kinase gene develop fatal kidney disease. Mol Genet Metab 2003;78(1):1–10.</mixed-citation><mixed-citation xml:lang="ru">Dobrovolsky V.N., Bucci T., Heflich R.H. et al. Mice deficient for cytosolic thymidine kinase gene develop fatal kidney disease. Mol Genet Metab 2003;78(1):1–10.</mixed-citation></citation-alternatives></ref><ref id="B48"><label>48.</label><citation-alternatives><mixed-citation xml:lang="en">48. Ke P.Y., Chang Z.F. Mitotic degradation of human thymidine kinase 1 is dependent on the anaphase-promoting complex/ cyclosome-CDH1-mediated pathway. Mol Cell Biol 2004;24(2):514–26.</mixed-citation><mixed-citation xml:lang="ru">Ke P.Y., Chang Z.F. Mitotic degradation of human thymidine kinase 1 is dependent on the anaphase-promoting complex/ cyclosome-CDH1-mediated pathway. Mol Cell Biol 2004;24(2):514–26.</mixed-citation></citation-alternatives></ref><ref id="B49"><label>49.</label><citation-alternatives><mixed-citation xml:lang="en">49. Zhou J., He E., Skog S. The proliferation marker thymidine kinase 1 in clinical use. Mol Clin Oncol 2013;1(1):18–28.</mixed-citation><mixed-citation xml:lang="ru">Zhou J., He E., Skog S. The proliferation marker thymidine kinase 1 in clinical use. Mol Clin Oncol 2013;1(1):18–28.</mixed-citation></citation-alternatives></ref><ref id="B50"><label>50.</label><citation-alternatives><mixed-citation xml:lang="en">50. Kuroiwa N., Nakayama M., Fukuda T. et al. Specific recognition of cytosolic thymidine kinase in the human lung tumor by monoclonal antibodies raised against recombinant human thymidine kinase. J Immunol Methods 2001;253(1–2):1–11.</mixed-citation><mixed-citation xml:lang="ru">Kuroiwa N., Nakayama M., Fukuda T. et al. Specific recognition of cytosolic thymidine kinase in the human lung tumor by monoclonal antibodies raised against recombinant human thymidine kinase. J Immunol Methods 2001;253(1–2):1–11.</mixed-citation></citation-alternatives></ref><ref id="B51"><label>51.</label><citation-alternatives><mixed-citation xml:lang="en">51. Mao Y., Wu J., Wang N. et al. A comparative study: immunohistochemical detection of cytosolic thymidine kinase and proliferating cell nuclear antigen in breast cancer. Cancer Invest 2002;20(7–8): 922–31.</mixed-citation><mixed-citation xml:lang="ru">Mao Y., Wu J., Wang N. et al. A comparative study: immunohistochemical detection of cytosolic thymidine kinase and proliferating cell nuclear antigen in breast cancer. Cancer Invest 2002;20(7–8): 922–31.</mixed-citation></citation-alternatives></ref><ref id="B52"><label>52.</label><citation-alternatives><mixed-citation xml:lang="en">52. He Q., Mao Y., Wu J. et al. Cytosolic thymidine kinase is a specific histopathologic tumour marker for breast carcinomas. Int J Oncol 2004;25(4):945–53.</mixed-citation><mixed-citation xml:lang="ru">He Q., Mao Y., Wu J. et al. Cytosolic thymidine kinase is a specific histopathologic tumour marker for breast carcinomas. Int J Oncol 2004;25(4):945–53.</mixed-citation></citation-alternatives></ref><ref id="B53"><label>53.</label><citation-alternatives><mixed-citation xml:lang="en">53. Guan H., Sun Y., Zan Q. et al. Thymidine kinase 1 expression in atypical ductal hyperplasia significantly differs from usual ductal hyperplasia and ductal carcinoma in situ: A useful tool in tumor therapy management. Mol Med Rep 2009;2(6):923–9. DOI: 10.3892/mmr_00000193.</mixed-citation><mixed-citation xml:lang="ru">Guan H., Sun Y., Zan Q. et al. Thymidine kinase 1 expression in atypical ductal hyperplasia significantly differs from usual ductal hyperplasia and ductal carcinoma in situ: A useful tool in tumor therapy management. Mol Med Rep 2009;2(6):923–9. DOI: 10.3892/mmr_00000193.</mixed-citation></citation-alternatives></ref><ref id="B54"><label>54.</label><citation-alternatives><mixed-citation xml:lang="en">54. Chen G., He C., Li L. et al. Nuclear TK1 expression is an independent prognostic factor for survival in pre-malignant and malignant lesions of the cervix. BMC Cancer 2013;13:249. DOI: 10.1186/1471-2407-13-249.</mixed-citation><mixed-citation xml:lang="ru">Chen G., He C., Li L. et al. Nuclear TK1 expression is an independent prognostic factor for survival in pre-malignant and malignant lesions of the cervix. BMC Cancer 2013;13:249. DOI: 10.1186/1471-2407-13-249.</mixed-citation></citation-alternatives></ref><ref id="B55"><label>55.</label><citation-alternatives><mixed-citation xml:lang="en">55. Liu C., Gao Q., Shi Q.L. et al. Significance of TK1 and Ki-67 expression in ovarian serous adenocarcinoma. J Clin Exp Pathol 2011;27:1289–93.</mixed-citation><mixed-citation xml:lang="ru">Liu C., Gao Q., Shi Q.L. et al. Significance of TK1 and Ki-67 expression in ovarian serous adenocarcinoma. J Clin Exp Pathol 2011;27:1289–93.</mixed-citation></citation-alternatives></ref><ref id="B56"><label>56.</label><citation-alternatives><mixed-citation xml:lang="en">56. Mao Y., Wu J., Skog S. et al. Expression of cell proliferating genes in patients with non- small cell lung cancer by immunohistochemistry and cDNA profiling. Oncol Rep 2005;13(5): 837–46.</mixed-citation><mixed-citation xml:lang="ru">Mao Y., Wu J., Skog S. et al. Expression of cell proliferating genes in patients with non- small cell lung cancer by immunohistochemistry and cDNA profiling. Oncol Rep 2005;13(5): 837–46.</mixed-citation></citation-alternatives></ref><ref id="B57"><label>57.</label><citation-alternatives><mixed-citation xml:lang="en">57. Xu Y., Liu B., Shi Q.L. et al. Thymidine kinase 1 is a better prognostic marker than Ki-67 for pT1 adenocarcinoma of the lung. Int J Clin Exp Med 2014;7(8):2120–8.</mixed-citation><mixed-citation xml:lang="ru">Xu Y., Liu B., Shi Q.L. et al. Thymidine kinase 1 is a better prognostic marker than Ki-67 for pT1 adenocarcinoma of the lung. Int J Clin Exp Med 2014;7(8):2120–8.</mixed-citation></citation-alternatives></ref><ref id="B58"><label>58.</label><citation-alternatives><mixed-citation xml:lang="en">58. Xu Y., Shi Q.L., Ma H. et al. High thymidine kinase 1 (TK1) expression is a predictor of poor survival in patients with pT1 of lung adenocarcinoma. Tumour Biol 2012;33(2):475–83. DOI: 10.1007/s13277-011-0276-0.</mixed-citation><mixed-citation xml:lang="ru">Xu Y., Shi Q.L., Ma H. et al. High thymidine kinase 1 (TK1) expression is a predictor of poor survival in patients with pT1 of lung adenocarcinoma. Tumour Biol 2012;33(2):475–83. DOI: 10.1007/s13277-011-0276-0.</mixed-citation></citation-alternatives></ref><ref id="B59"><label>59.</label><citation-alternatives><mixed-citation xml:lang="en">59. Wu J., Mao Y., He L. et al. A new cell proliferating marker: cytosolic thymidine kinase as compared to proliferating cell nuclear antigen in patients with colorectal carcinoma. Anticancer Res 2000;20(6C):4815–20.</mixed-citation><mixed-citation xml:lang="ru">Wu J., Mao Y., He L. et al. A new cell proliferating marker: cytosolic thymidine kinase as compared to proliferating cell nuclear antigen in patients with colorectal carcinoma. Anticancer Res 2000;20(6C):4815–20.</mixed-citation></citation-alternatives></ref><ref id="B60"><label>60.</label><citation-alternatives><mixed-citation xml:lang="en">60. Wei J.W., Xu C.R., Zen D.Z., Chen Y. Analysis on the content of TK1 of patients with colonic polyps. Lab Med Clin 2011;8:769.</mixed-citation><mixed-citation xml:lang="ru">Wei J.W., Xu C.R., Zen D.Z., Chen Y. Analysis on the content of TK1 of patients with colonic polyps. Lab Med Clin 2011;8:769.</mixed-citation></citation-alternatives></ref><ref id="B61"><label>61.</label><citation-alternatives><mixed-citation xml:lang="en">61. Gakis G., Hennenlotter J., Scharpf M. et al. XPA210: a new proliferation marker to characterize tumor biology and progression of renal cell carcinoma. World J Urol 2011;29(6):801–6. DOI: 10.1007/s00345-010-0621-8.</mixed-citation><mixed-citation xml:lang="ru">Gakis G., Hennenlotter J., Scharpf M. et al. XPA210: a new proliferation marker to characterize tumor biology and progression of renal cell carcinoma. World J Urol 2011;29(6):801–6. DOI: 10.1007/s00345-010-0621-8.</mixed-citation></citation-alternatives></ref><ref id="B62"><label>62.</label><citation-alternatives><mixed-citation xml:lang="en">62. Kruck S., Hennenlotter J., Vogel U. et al. Exposed proliferation antigen 210 (XPA- 210) in renal cell carcinoma (RCC) and oncocytoma: clinical utility and biological implications. BJU Int 2012;109(4):634–8. DOI: 10.1111/j.1464-410X.2011.10392.x.</mixed-citation><mixed-citation xml:lang="ru">Kruck S., Hennenlotter J., Vogel U. et al. Exposed proliferation antigen 210 (XPA- 210) in renal cell carcinoma (RCC) and oncocytoma: clinical utility and biological implications. BJU Int 2012;109(4):634–8. DOI: 10.1111/j.1464-410X.2011.10392.x.</mixed-citation></citation-alternatives></ref><ref id="B63"><label>63.</label><citation-alternatives><mixed-citation xml:lang="en">63. Luo P., Wang N., He E. et al. The proliferation marker thymidine kinase 1 level is high in normal kidney tubule cells compared to other normal and malignant renal cells. Pathol Oncol Res 2010;16(2):277–83. DOI: 10.1007/s12253-009-9222-5.</mixed-citation><mixed-citation xml:lang="ru">Luo P., Wang N., He E. et al. The proliferation marker thymidine kinase 1 level is high in normal kidney tubule cells compared to other normal and malignant renal cells. Pathol Oncol Res 2010;16(2):277–83. DOI: 10.1007/s12253-009-9222-5.</mixed-citation></citation-alternatives></ref><ref id="B64"><label>64.</label><citation-alternatives><mixed-citation xml:lang="en">64. Rausch S., Hennenlotter J., Teepe K. et al. Muscle-invasive bladder cancer is characterized by overexpression of thymidine kinase 1. Urol Oncol 2015;33(10):426.e21–9. DOI: 10.1016/j.urolonc.2015.06.007.</mixed-citation><mixed-citation xml:lang="ru">Rausch S., Hennenlotter J., Teepe K. et al. Muscle-invasive bladder cancer is characterized by overexpression of thymidine kinase 1. Urol Oncol 2015;33(10):426.e21–9. DOI: 10.1016/j.urolonc.2015.06.007.</mixed-citation></citation-alternatives></ref><ref id="B65"><label>65.</label><citation-alternatives><mixed-citation xml:lang="en">65. Ye F.P., Xie Q.L., Liu X.L. et al. Expression of TK1 and Ki67 in prostate diseases. J Clin Exp Pathol 2008;24:644–67.</mixed-citation><mixed-citation xml:lang="ru">Ye F.P., Xie Q.L., Liu X.L. et al. Expression of TK1 and Ki67 in prostate diseases. J Clin Exp Pathol 2008;24:644–67.</mixed-citation></citation-alternatives></ref><ref id="B66"><label>66.</label><citation-alternatives><mixed-citation xml:lang="en">66. Aufderklamm S., Hennenlotter J., Todenhoefer T. et al. XPA-210: a new proliferation marker determines locally advanced prostate cancer and is a predictor of biochemical recurrence. World J Urol 2012;30(4):547–52. DOI: 10.1007/s00345-011-0768-y.</mixed-citation><mixed-citation xml:lang="ru">Aufderklamm S., Hennenlotter J., Todenhoefer T. et al. XPA-210: a new proliferation marker determines locally advanced prostate cancer and is a predictor of biochemical recurrence. World J Urol 2012;30(4):547–52. DOI: 10.1007/s00345-011-0768-y.</mixed-citation></citation-alternatives></ref></ref-list></back></article>
