MS – Moscow University. PhD, DSc – Engelhardt Institute of Molecular Biology, Russian Academy of Sceinces.
I am a cell and molecular biologist interested in the biology of growth factors and cytokines and their roles in vascular, metabolic and oncologic pathologies. My specific fields of studies are:
1. Nonclassical secretion of proteins devoid of signal peptide (e.g. FGF1 and IL1), its mechanisms, genetic regulation and effects on cardiovascular system status and cancer growth.
2. Cell memory: ability of cells to “remember” transient interactions with growth factors and thus modulate their response to repeated stimulation. In particular, “FGF memory” discovered in our laboratory could regulate wound repair and tumor incapsulation.
3. Regulation of adipogeneis by growth factors and cytokines (e.g. FGF1, Cthrc1).
1.While most extracellular proteins has in their structure a special signal peptide, required for their export through endoplasmic reticulum and Golgi, a large group of secreted proteins are devoid of signal peptides, and they are exported through insufficiently studied nonclassical mechanisms. Our laboratory studies the stress-induced nonclassical export, of FGF1 and IL1alpha, two ubiquitous pro-angiogenic and pro-inflammatory molecules. The goals of this project is to understand how multiprotein release complexes are formed, how the released proteins are transported to the cell membrane and how they exit to the extracellular compartment without using the classical mechanism of exocytosis. The understanding of these processes will facilitate the development of new clinical approaches to the regulation of angiogenesis, inflammation and tumor growth.
We also study the interactions between FGF/FGFR, Jagged(Delta)/Notch and thrombin/PAR1 signaling, three major regulatory systems involved in practically all of the aspects of organism development and organ formation. In particular, thrombin stimulation and downregulation of Notch signaling induce FGF1 expression and release, and the acquisition of the angiogenic phenotype by the cells. The aim is to understand molecular mechanisms underlying the cross-talk between FGF, Notch and thrombin signaling and to use this knowledge for the treatment of cardiovascular and oncological disorders.
We developed transgenic mouse models with conditional expression of FGF1 in endothelial cells and monocytes/macrophages. These models are being used to study the regulation of FGF1 export in vivo and its effects on tumor formation and tissue repair after ischemia.
2.Another topic of our studies is the molecular mechanisms, which regulate cell proliferative response to individual growth factors, including FGFs. We discovered that non-malignant cells respond to FGF by just one proliferative cycle and then indefinitely reside in the G1 phase of the second cycle.
Interestingly, transient treatment with FGF results in a sustained long-term inhibition of proliferative response to FGF, PDGF and EGF. This phenomenon termed “FGF memory” is dependent on histone deacetylase activity and pro-inflammatory NFkappaB signaling. Apparently, the limitation of proliferative response to growth factors may be needed in the organism to prevent tissue hyperplasia, and we are exploring the molecular processes underlying this limitation.
3. Recently we began the studies of molecular mechanisms underlying the regulation of adipogenesis by FGFs and by a novel hormone-like polypeptide Cthrc1 (discovered by our colleague, MMCRI faculty member Volkhard Lindner).
- 30. Soldi, R., Mandinova, A., Venkataraman, K., Hla, T., Vadas, M., Pitson, S., Duarte, M., Graziani, I., Kolev, V., Kacer, D., Kirov, A., Maciag, T. Prudovsky, I., “Sphingosine Kinase 1 is a critical component of the copper-dependent FGF1 export pathway.” Exper. Cell Res., 2007; In press
- 1. Kirov A., Kacer D., Conley B. A., Vary C. P., Prudovsky I. AHNAK2 Participates in the Stress-Induced Nonclassical FGF1 Secretion Pathway. J Cell Biochem. 2015, Epub ahead of print.
- 2. Wang T, Green LA, Gupta SK, Kim C, Wang L, Almodovar S, Flores SC, Prudovsky IA, Jolicoeur P, Liu Z, Clauss M. Transfer of Intracellular HIV Nef to Endothelium Causes Endothelial Dysfunction. PLoS One. 2014 Mar 7;9(3):e91063
- 3. Poole A, Knowland N, Cole R, Wang R, Booth L, Kacer D, Tarantini F, Friesel R, Prudovsky I. Transitory FGF treatment results in the long-lasting suppression of the proliferative response to repeated FGF stimulation. J Cell Biochem. 2013, 155:874-88.
- 4. Gong Y, Yang X, He Q, Gower L, Prudovsky I, Vary CP, Brooks PC, Friesel RE. Sprouty4 regulates endothelial cell migration via modulating integrin β3 stability through c-Src. Angiogenesis. 2013, 16:861-75.
- 5. Danza G, Di Serio C, Ambrosio MR, Sturli N, Lonetto G, Rosati F, Rocca BJ, Ventimiglia G, Del Vecchio MT, Prudovsky I, Marchionni N, Tarantini F. Notch3 is activated by chronic hypoxia and contributes to the progression of human prostate cancer. Int J Cancer. 2013, 133: 2577-86
- 6. Sterling SM, Allgeyer ES, Fick J, Prudovsky I, Mason MD, Neivandt DJ. Phospholipid Diffusion Coefficients of Cushioned Model Membranes Determined via Z-Scan Fluorescence Correlation Spectroscopy. Langmuir. 2013 Jun 6. [Epub ahead of print]
- 7. Prudovsky I. Nonclassically secreted regulators of angiogenesis. Angiology: Online Access 2013, 1:1-5.
- 8. Prudovsky I, Kumar TK, Sterling S, Neivandt D. Protein-phospholipid interactions in nonclassical protein secretion: problem and methods of study. Int J Mol Sci. 2013 14(2):3734-72. PMCID in process.
- 9. Lopez-Castejon G, Luheshi NM, Compan V, High S, Whitehead RC, Flitsch SL, Kirov A, Prudovsky I, Swanton E, Brough D. Deubiquitinases regulate the activity of caspase-1 and IL-1β secretion via assembly of the inflammasome. J Biol Chem 2012. 288: 2721-2733. PMCID: PMC3554938
- 10. Meng H, Zhang X, Yu G, Lee SJ, Chen YE, Prudovsky I, Wang MM. Biochemical characterization and cellular effects of CADASIL mutants of NOTCH3. PLoSOne 2012, 7: e44964 PMCID: PMC3445613
- 11. Kirov A, Maria Duarte M, Guay J, Karolak M, Yan C, Oxburgh L, Prudovsky I. Transgenic expression of nonclassically secreted FGF suppresses kidney repair. PloS One. 2012, 7: e36485. PMCID: PMC3351418
- 12. Prudovsky I, Vary C, Markaki I, Olins A, Olins D.. Phosphatidylserine co-localizes with epichromatin in interphase nuclei and mitotic chromosomes. Nucleus. 2012, 3:200-210. PMCID: PMC3383575.
- 13. Danza G, Di Serio C, Rosati F, Lonetto G, Sturli N, Kacer D, Pennella A, Ventimiglia G, Barucci R, Piscazzi A, Prudovsky I, Landriscina M, Marchionni N, Tarantini F. 2012. Notch signaling modulates hypoxia-induced neuroendocrine differentiation of human prostate cancer cells. Mol Cancer Res, 10: 230-238. PMCID: PMC3433043.
- 14. Kirov A, Al-Hashimi H, Solomon P, Mazur C, Thorpe PE, Sims PJ, Tarantini F, Kumar TK, Prudovsky I. Phosphatidylserine externalization and membrane blebbing are involved in the nonclassical export of FGF1. J Cellular Biochem. 2012, 113:956-66, PMCID: PMC3264788
- 15. Kacer D, McIntire C, Kirov A, Kany E, Roth J, Liaw L, Small D, Friesel R, Basilico C, Tarantini F, Verdi J, Prudovsky I. Regulation of nonclassical FGF1 release and FGF-dependent cell transformation by CBF1-mediated Notch signaling. J Cellular Physiol 2011; 226 :3064-75. PMCID: PMC3126874
- 16. Massi D, Landriscina M, Piscazzi A, Cosci E, Kirov A, Paglierani M, Di Serio C, Mourmouras V, Fumagalli S, Biagioli M, Prudovsky I, Miracco C, Santucci M, Marchionni N, Tarantini F.. S100A13 is a new angiogenic marker in human melanoma. Modern Pathology. 2010, 23: 804-813. PMCID: PMC2882157
- 17. Mouta-Bellum C, Kirov A, Miceli-Libby L, Mancini ML, Petrova TV, Liaw L, Prudovsky I, Thorpe PE, Miura N, Cantley LC, Alitalo K, Fruman DA, Vary CP. “Organ-specific lymphangiectasia, arrested lymphatic sprouting, and maturation defects resulting from gene-targeting of the PI3K regulatory isoforms p85alpha, p55alpha, and p50alpha.” 2009; Dev Dyn., 238: 2670-9.
- 18. Graziani I, Doyle A, Sterling S, Kirov A, Tarantini F, Landriscina M, Kumar TSK, Neivandt D, Prudovsky I. “Protein folding does not prevent the nonclassical export of FGF1 and S100A13.” Biochem Biophys Res Commun. 2009; 381:350-354.
- 19. Kathir KM, Gao L, Dakshinamurthy R, Daily AE, Brixey S., Liu, H.; Davis D., Adams P., Prudovsky I., Kumar TSK. “Characterization of the copper and lipid interactions of the C2B domain of synaptotagmin 1 ‑ relevance to the non‑classical secretion of the human acidic fibroblast growth factor.” BBA ‑ Biomembranes, 2009 [Epub. ahead of print].
- 21. Prudovsky, I, and Donato, R. “S100A13.” Nature Molecular Pages (electronic publication), 2009.
- 20. Duarte, M, Kolev, V, Kacer, D, Mouta-Bellum, C, Soldi, R, Graziani, I, Kirov, A, Friesel, R, Liaw, L, Small, D, Verdi, J, Maciag, T, Prudovsky, I. “Novel Cross-Talk between Three Cardiovascular Regulators: Thrombin cleavage fragment of Jagged 1 induces FGF1 expression and release.” 2008, Mol. Biol. Cell., 19:4863-4874.
- 22. Prudovsky, I., Tarantini, F., Landriscina, M., Neivandt, D., Soldi, R., Kirov, A., Small, D., Kathir, KM, Rajalingam D., and Kumar, TKS. “Secretion without Golgi.” J Cell Biochem. 2008, 3,: 1327-43.
- 23. Lee, CW, Raskett, CM, Prudovsky, I, Altieri, DC. Molecular Dependence of Estrogen Receptor-Negative Breast Cancer on a Notch-Survivin Signaling Axis. Cancer Res., 2008, 68: 5273-81.
- 24. Di Serio, C, Doria, L, Pellerito, S, Prudovsky, I, Micucci, I, Massi , D, Landriscina, M, Marchionni, N, Masotti, G., Tarantini, F. The Release of Fibroblast Growth Factor-1 from Melanoma Cells Requires Copper Ions and is Mediated by Phosphatidylinositol 3-kinase/Akt Intracellular Signaling Pathway. Cancer Letters, 2008, 267:67-74. PMID: 18400376
- 25. Urs S, Roudabush A, O’Neill CF, Pinz I, Prudovsky I, Kacer D, Tang Y, Liaw L, Small D. Soluble forms of the Notch ligands Delta1 and Jagged1 promote in vivo tumorigenicity in NIH3T3 fibroblasts with distinct phenotypes. Am J Pathol., 2008; 173:865-878.
- 26. Nikopoulos, GN, Adams, TL, Adams, D, Oxburgh, L, Prudovsky, I, Verdi, JM. The Use of Endo-Porter to Deliver Morpholinos in Kidney Organ Culture. Biotechniques, 2008: 44: 547-549. PMID: 18476819
- 27. Leclair, RJ, Wang, Q, Benson, MA, Prudovsky, I, Lindner, V. Intracellular Localization of Cthrc1 Characterizes Differentiated Smooth Muscle Cells.” Arterioscler Thromb Vasc Biol., 2008; 28:1332-1338.
- 28. Nikopoulos GN, Duarte M, Kubu CJ, Bellum, S., Friesel, R., Maciag, T., Prudovsky, I, Verdi, JM. “Soluble Jagged1 Attenuates Lateral Inhibition Allowing for the Clonal Expansion of Neural Crest Stem Cells.” Stem Cells. 2007 , 25: 3133-3142
- 29. Rajalingam, D., Graziani, I., Prudovsky, I., Yu, C., Kumar, TK. Relevance of partically structured states in the non-classical secretion of acidic fibroblast growth factor. 2007. Biochemistry, 46; 9225-9238.
- 31. Rajalingam, D., Kacer, D., Prudovsky, I., Thallapuranam, S.K.K.T., “Molecular cloning, overexpression and characterization of interleukin 1 alpha.” Biochem. Biophys. Res. Comm., 2007, 360: 604-8.
- 32. Di Serio, C., Pellerito, S., Duarte, M., Massi, D., Naldini, A., Cirino, G., Prudovsky, I., Santucci, M., Geppetti, P., Marchionni, N., Masotti, G., Tarantini, F. “Protease-activated receptor (PAR) 1 selective antagonist SCH7997 inhibits cell proliferation and induces apoptosis, by a PAR-1 independent mechanism.” Basic and Clin. Pharmacology and Toxicology, 2007, 267: 67-74.
- Biochim Biophys Acta. 2007 , 1768: 3080-89.
- 34. Graziani I, Bagala C. Duarte M, Soldi R, Kolev V, Tarantini F, Kumar TK, Doyle A, Neivandt D, Yu V, Maciag T, Prudovsky I. “Release of FGF1 and p40 synapttotagmin 1 correlates with their membrane destabilizing ability.” Biochem Biophys Res Commun., 2006; 349:192-99.
- 35. Duarte M, Kolev V, Soldi R, Kirov A, Graziani I, Marta Oliveira S, Kacer D, Friesel R, Maciag T, Prudovsky I. “Thrombin induces rapid PAR1-mediated non-classical FGF1 release.” Biochem Biophys Res Commun., 2006; 350:604-609
- 36. Sivaraja V, Suresh Kumar TK, Rajalingam D, Graziani I, Prudovsky I, Yu C. “Copper Binding Affinity of S100A13, a Key Component of the FGF-1 Non-Classical Copper-Dependent Release Complex.” Biophys. J., 2006; 91:1832-43.
- 37. Landriscina M, Schinzari G, Di Leonardo G, Quirino M, Cassano A, D’Argento E, Lauriola L, Scerrati M, Prudovsky I, Barone C. “S100A13, a new marker of angiogenesis in human astrocytic gliomas.” J.Neurooncol, 2006; 80:251-259.
- 38. Omoto, Atsushi; Kawahito, Yutaka; Prudovsky, Igor; Tubouchi, Yasunori; Kimura, Mizuho; Ishino, Hidetaka; Wada, Makoto; Yoshida, Makie; Yoshimura, Rikio; Yoshikawa, Toshikaru; Sano, Hajime. “Copper chelation with Tetrathiomolybdate suppresses adjuvant-induced arthritis and inflammation-associated cachexia in rats.” Arthritis Research and Therapy, Arthritis Research and Therapy, 2005; 7:R1174-1182.
- 39. Rajalingam, D.; Kumar, TKS; Soldi, R.; Graziani, I.; Prudovsky, I.; and Yu Chin, “Molecular Mechanism of Inhibition of Non-Classical FGF-1 Export.” Biochemistry, 2005, 44:15472-15479.
- 40. Vihren Kolev, Doreen Kacer, Radiana Trifonova, Deena Small, Maria Duarte, Raffaella Soldi, Irene Graziani, Olga Sideleva, Barry Larman, Thomas Maciag and Igor Prudovsky “The Intracellular Domain of Notch Ligand Delta1 Induces Cell Growth Arrest”, FEBS Letters, 2005; 579:5798-5802.
- 41. Sivaraja, Vaithiyalingam; Kumar, Krishnaswamy Suresh; Prudovsky, Igor; Yu, Chin. Three-Dimensional Solution “Structure of Mouse S100A13, a Component of the Fibroblast Growth Factor 1 Non-Classical Release Pathway.” Biochem. Biophys. Res. Comm., 2005; 335:1140-1148.
- 42. Doyle, A., Fick, J., Himmelhaus, M., Eck, W., Graziani, I., Prudovsky, I., Grunze, M., Maciag, T. and Neivandt, D. “Protein Deformation of Lipid Hybrid Bilayer Membranes studied by Sum Frequency Generation Vibrational Spectroscopy (SFS).” Langmuir, 2004; 20:8961-8965.
- 43. Andreeva, V., Prudovsky I., Maciag, T., “Stimulation of Quiescent Cells by Individual Polypeptide Growth Factors is Limited to One Cell Cycle.” Eur. J. Cell Biol., 2004; 327-335.
- 44. Peng. H., Sahni, A., Fay, P.J., Bellum, S., Prudovsky, I., Maciag, T. and Francis, C.W. “Identification of a binding site on human FGF-2 for fibrinogen.” Blood, 2004; 103:2114-2120.
- 45. Trifonova, R., Small, D., Kacer, D., Kovalenko, D., Kolev, V., Mandinova, A., Soldi, R., Liaw, L., Prudovsky, I., Maciag, T. “The non-transmembrane form of Delta1 but not of Jagged1 induces normal migratory behavior accompanied by FGF receptor 1-dependent transformation.” J. Biol. Chem., 2004; 279:13285-88.
- 46. Prudovsky, I., Mandinova, A., Soldi, R., Bagalá, C., Graziani, I., Landriscina, M., Tarantini, F., Duarte, M., Bellum, S., Doherty, H. and Maciag, T. “The non-classical export routes: IL1α and FGF1 point the way.” J. Cell Sci., 2003; 116:4871-4881.
- 47. Small, D., Kovalenko, D., Soldi, R., Mandinova, A., Kolev, V., Trifonova, R., Bagalá, C., Kacer, D., Liaw, L., Prudovsky, I. and Maciag, T. “Notch activation suppresses FGF-dependent cellular transformation.” J. Biol. Chem., 2003; 278:16405-16413.
- 48. Mandinova, A., Soldi, R., Graziani, I., Bagalá, C., Bellum, S., Landriscina, M., Tarantini, F., Prudovsky, I. and Maciag, T. “S100A13 mediates the copper-dependent stress-induced release of IL1α from both human U937 and murine NIH 3T3 Cells.” J. Cell Sci., 2003; 116:2687-2696.
- 49. Mandinov, L., Mandinova, A., Kyurkchiev, S., Kyurkchiev, D., Kehayov, I., Kolev, V., Soldi, R., Bagala, C., deMuink, E., Lindner, V., Post, M., Simons, M., Bellum, S., Prudovsky, I. and Maciag, T. “Copper chelation represses the vascular response to injury.” Proc. Natl. Acad. Sci. USA, 2003; 100:6700-6705.
- 50. Mandinov, L., Mandinova, A., Soldi, R., Graziani, I., Bagalá, C., Prudovsky, I., and Maciag, T. “Interleukin 1: The choreographer for the restenotic ballet.” Thromb. Haem. Vasc. Biol., 2003; 90:369-71.
- 51. Bagalá, C., Kolev, V, Mandinova, A., Soldi, R., Mouta, C., Graziani, I., Prudovsky, I., and Maciag, T., “The alternative translation of synaptotagmin 1 mediates the non-classical release of FGF1.” BBRC, 2003; 310:1041-1047.
- 52. Prudovsky, I., Bagalá, C., Tarantini, F., Mandinova, A., Soldi, R., Bellum, S., and Maciag, T., “The intracellular translocation of the components of the FGF1 release complex precedes their assembly prior to export.” J. Cell Biol., 2002; 156:201-208.
- 53. Prudovsky, I, Popov, K., Akimov, S., Serov, S., Zelenin, A., Meinhardt, G., Baier, P., Sohn, C., Hass, R. “Antisense CD11b integrin inhibits the development of a differentiated monocyte/macrophage phenotype in human leukemia cells.” Eur. J. Cell Biol. 2002; 81:36-42.
- 54. Carreira, C.M., Landriscina, M., Bellum, S., Prudovsky, I., Maciag, T. “The comparative release of FGF1 by hypoxia and temperature stress.” Growth Factors. 2001; 18:277-85.
- 55. Lindner, V., Booth, C., Prudovsky, I., Small, D., Maciag, T., and Liaw, L. “Members of the Jagged/Notch gene families are expressed in injured arteries and regulate cell phenotype via alterations in cell matrix and cell-cell interaction.” Am. J. Pathol., 2001; 159: 875-83.
- 56. Landriscina, M., Bagalá, C., Mandinova, A., Soldi, R., Micucci, I., Bellum, S., Prudovsky, I., and Maciag, T. “Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress.” J. Biol. Chem., 2001; 276:25549-57.
- 57. Small, D., Kovalenko, D., Kacer, D., Liaw, L., Landriscina, M., Di Serio, C., Prudovsky, I., and Maciag, T. “ Soluble Jagged 1 represses the function of its transmembrane form to induce the formation of the Src-dependent chord-like phenotype.” J. Biol. Chem., 2001; 276:32022-30.
- 58. Landriscina, M., Soldi, R., Bagalá, C., Micucci, I,., Bellum, S., Tarantini, F., Prudovsky, I., and Maciag, T. “S100A13 participates in the release of fibroblast growth factor 1 in response to heat shock in vitro.” J. Biol. Chem., 2001; 276:22544-52.
- 59. Tarantini, F., Micucci, I., Bellum. S., Landriscina, M., Garfinkel, S., Prudovsky, I. and Maciag, T. “The precursor but not the mature form of IL1α blocks the release of FGF1 in response to heat shock.” J. Biol. Chem., 2001; 276:5147-5151.
- 60. Landriscina, M., Prudovsky, I., Mouta-Carreira C., Soldi, R., Tarantini, F., and Maciag, T. “Amlexanox reversibly inhibits cell migration and proliferation and induces the Src-dependent disassembly of actin stress fibers in vivo.” J.Biol. Chem., 2000; 275:32753-32762.
- 61. Wong M.K.K., Prudovsky, I., Vary, C., Booth, C., Liaw, L., Mousa S., Small, D., and Maciag, T. “A non-transmembrane form of Jagged-1 regulates the formation of matrix-dependent cord-like structures.” BBRC, 2000; 268:853-859.
- 62. Vartanian, A., Alexandrov, I., Prudovsky, I., McLennan, A., and Kisselev, L. “Ap4A induces apoptosis in human cultured cells.” FEBS Lett., 1999; 456:175-180.
- 63. Yegorov, Y., Akimov, S., Hass, R., Zelenin, A., and Hass, R., Prudovsky, I.A. “Endogenous beta-galactosidase activity in continuously non-proliferating cells.” Exper. Cell Res., 1998; 243:207-211.
- 64. LaVallee T., Prudovsky, I.A., McMahon, G., Hu, X. and Maciag, T., “The activation of MAP kinase pathway by FGF-1 correlates with proliferation while activation of the Src pathway correlates with migration.” J. Cell Biol., 1998; 141:1647-1658.
- 65. Akimov, S., Maciag, T., Popov, K., Kapnik, E., Zelenin, A., and Prudovsky, I. “The interchangeability of growth factors in early G0-G1.” Proc. Russian Acad. Sci., 1998; 359:557-560.
- 66. Yegorov, Y.E., Chernov, D.N., Akimov, S.S., Akhmalisheva, A.K., Popov, K.V., Hass, R., Prudovsky, I.A., and Zelenin, A.V., “Telomerase activity of the cells during alteration of their proliferative status.” Biol. Membrany, 1998; 15:630-638.
- 67. McMahon, G., Garfinkel, S., Prudovsky, I.A., and Maciag, T., “Intracellular precursor Interleukin (IL)-1αbut not mature IL-1α is able to regulate human endothelial cell migration in vivo.” J.Biol. Chem. (Rapid Comm.), 1997; 272:2802-28205.
- 68. Hass, R., Prudovsky, I. and Kruhoffer, M., “Differential effects of phorbol ester on signalling and gene expression in human leukemia cells.” Leuk. Res., 1997; 21:589-594.
- 69. Vartanian, A., Prudovsky, I., Suzuki, H., Dal Pra, I., and Kisselev, L. “Opposite effects of cell differentiation and apoptosis on Ap3A/Ap4A ratio in human cell cultures.” FEBS Lett., 1997; 415:160-162.
- 70. Prudovsky, I.A., Savion, N., LaVallee, T.M. and Maciag, T., “The nuclear trafficking of extracellular fibroblast growth factor (FGF)-1 correlates with the perinuclear association of the FGF receptor-1α isoforms but not the FGF receptor-1β isoforms.” J. Biol. Chem., 1996; 271:14198-14205.
- 71. Garfinkel, S., Hu, X., Prudovsky, I.A., McMahon, G., Kapnik, E.M., McDowell, S.D., and Maciag, T., “FGF-1-dependent proliferative and migratory responses are impaired in senescent human umbilical vein endothelial cells and correlate with the inability to signal tyrosine phosphorylation of fibroblast growth factor receptor-1 substrates.” J. Cell Biol., 1996; 134: 783-791.
- 72. Prudovsky, I., Savion, N., Friesel, R., Xu, J., Hou, J., McKeehan, W., Maciag, T., “Intact and functional FGFR-1 trafficks near the nucleus in response to FGF-1.” J. Biol. Chem., 1994; 269:13720-13724.
- 73. Maciag, T., Zhan, X., Garfinkel, S., Friedman, S., Prudovsky, I., Jackson, A., Wessendorf, J., Hu, X., Gamble, S., Shi, J., Brown, S., Tarantini, F., Zimrin, A., “Novel mechanisms of fibroblast growth factor 1 function.” Recent Prog. Horm. Res., 1994; 49:105-123.
- 74. Fedorov, Yu.V., Prudovsky, I.A., Yegorov, Ye.E. and Zelenin, A.V., “The comparison of DNA synthesis inducibility by high potassium treatment in various non-proliferating cells.” Exper. Cell. Res., 1993; 209:156-159.
- 75. Prudovsky, I.A., Kosimov, R.B., Prasolov, V.S., Pospelova, T.V., Sukharev, S.I and Zelenin, A.V., “The control of DNA replication in hybrids between neutrophils and fibroblasts.” Cell. Prolif., 1993; 26:221-233.
- 76. Prudovsky, I.A., Yegorov, Ye.E., Kosimov, R.B., Gumeniuk, R.R., Khodiakov, A.L., and Tsong, T.Y., “Positive and negative regulation of replication in hybrid cells.” Mol. Biol. (Mosk.), 1991; 25:1157-1180.
- 77. Prudovsky, I.A., and Tsong, T.Y., “Fusion of fibroblasts with differentiated and nondifferentiated leukaemia cells resulting in blockage of DNA synthesis.” Dev. Biol., 1991; 144:232-239.
- 78. Kosimov, R.B., Sukharev, S.I., Pospelova, T.V., Prudovsky, I.A., and Zelenin, A.V. “DNA synthesis in heterokaryons obtained by the fusion of polymoprphonuclear leukocytes and cultured cells possessing different proliferative potentials.” Cytologia, 1991; 33:48-55.
- 79. Zelenin, A.V., Prudovsky, I.A., Gumeniuk, R.R., Yegorov, Ye. E., Kapnik, E.M., Kosimov, R.B., and Fedorov, Yu. V., “The nature of proliferation blockage in differentiated cells studied on heterokaryons as a model: various types of absence of proliferation in cells at terminal differentiation.” Ontogenez, 1990; 21:32-40.
- 80. Prudovsky, I.A., Kapnik, E.M., Fedorov, Yu.V., Barbul, A.I., and Zelenin, A.V., “Differential regulation of DNA synthesis in heterokaryons between chicken erythrocytes and culture cells with various proliferative potentials ‘. Eur. J. Cell Biol., 1990; 54:347-352.
- 81. Prudovsky, I.A., Gumeniuk, R.R., Yegorov, Ye. E., and Zelenin, A.V., “Resident macrophages specifically inhibit DNA synthesis in the nuclei of transformed cells in heterokaryons.” Int. J. Cancer, 1989; 44:1005-1008.
- 82. Prudovsky, I.A., Gumeniuk, R.R., Yegorov, Ye, E., Poletayev, A.I. and Zelenin, A.V., “Immortalized phenotype and the presence of active oncogenes correlate with the capacity of culture cells to induce reactivation of DNA synthesis in macrophage nuclei in heterokaryons.” Cell Differ. Dev., 1989; 26:221-228.
- 83. Zelenin, A.V., and Prudovsky, I.A., “Regulation of DNA synthesis investigated on heterokaryons of dividing and nondividing cells.” Int. Rev. Cytol., 1989; 117:179-213.
- 84. Kapnik, E.M., Prudovsky, I.A., Fedorov, Yu, V., Barbul, A.I., and Zelenin, A.V., “Study of the proliferation blockage in nucleate erythrocytes by a cellular hybridization method.” Proc. Acad. Sci. USSR, 1989; 308:982-986.
- 85. Khodjakov, A.L., Prudovsky, I.A., Onishchenko, G.E., Zelenin, A.V., and Chentsov, Yu, S., “Ultrastructure of cellular fragments isolated by mass enucleation method without the use of special chemical agents.” Proc. Natl. Acad. Sci. USSR, 1988; 301:448-450.
- 86. Gumeniuk, R.R., Prudovsky, I.A., Prasolov, V.S. and Zelenin, A.V., “Inhibition of DNA synthesis in nuclei of malignant cells after fusion with macrophages.” Proc. Natl. Acad. Sci. USSR, 1988; 298:985-987.
- 87. Yegorov, Ye. E., Gumeniuk, R. R., Prudovsky, I. A., and Zelenin, A.V., “DNA synthesis in the hybrids of macrophages and various cells with the limited ability to proliferate.” Biopolymeri I Kletka, 1987; 3:313-317.
- 88. Gumeniuk, R.R., Prudovsky, I.A., Topol, L.Z., Chumakov, P.M., and Zelenin, A.V. “Regulation of DNA synthesis in heterokaryons between macrophages and cells immortalized with oncogenes.” Proc. Natl. Acad. Sci. USSR, 1987; 294:230-233.
- 89. Gumeniuk, R.R., Prudovsky, I.A., Poletayev, A.I., and Zelenin, A.V., “Reactivation of DNA synthesis in heterokaryons of macrophages and cells transformed with a ts-mutant virus SV40 is temperature-dependent.” Proc. Nat. Acad. Sci. USSR, 1986; 291:221-224.
- 90. Zelenin, A.V., and Prudovsky, I.A., “Regulation of replication in heterokaryons and its relation to oncogenes activity.” Uspekhi Sovremennoj Biologii, 1985; 100:340-356.
- 91. Kerkis, A.Yu, Bajborodin, S.I., Prudovsky, I.A., Christoljubova, N.B., and Zelenin, A.V., “The use of cell enucleation for studying the stability of cytoplasmic organelles and cytoplasm organization.” Tsitologia, 1985; 27:792-796.
- 92. Yegorov, Ye.E., Prudovsky, I.A., and Zelenin, A.V., “Macrophages do not inhibit the entry into DNA synthesis of the nuclei of non-malignant proliferating cells in heterokaryons.” Proc. Natl. Acad. Sci. USSR, 1985; 280:1016-1019.
- 93. Prudovsky, I.A., Yegorov, Ye.E., and Zelenin, A.V., “DNA synthesis in the heterokaryons of non-dividing differentiated cells and culture cells with various proliferative potentials.” Cell Differ., 1985, 17:239-246.
- 94. Yegorov, Ye.E, Prudovsky, I.A., and Zelenin, A.V., “DNA synthesis in the hybrids of macrophages and culture cells with various proliferative activities.” Proc. Natl. Acad. Sci. USSR, 1984; 276:961-965.
- 95. Zelenin, A.V., and Prudovsky, I.A., ‘Why take nucleus from the cell.” Priroda, 1983; #7, 15-25.
- 96. Yegorov, Ye.E., Prudovsky, I.A., and Zelenin, A.V., “The comparative study of L cell cytoplasts obtained with the use of cytochalasin and without it.” Proc. Natl. Acad. Sci. USSR, 1982; 264:969-974.
- 97. Zelenin, A.V., Kushch, A.A., Nijazmatov, A.A., and Prudovsky, I.A., “Rapid entry into the S-period of lymph node lymphocytes in heterokaryons and reconstituted cells.” Proc. Natl. Acad. Sci. USSR, 1979; 246:1489-1492.
- 98. Kushch, A.A., Prudovsky, I.A., and Zelenin, A.V., “Chromatin activation in peritoneal exudate leukocytes after fusion with L cell cytoplasts.” Cytobiologie, 1978; 18:59-66.
- 99. Prudovsky, I.A., and Zelenin, A.V., “Effect of enucleation on the structural and functional state of the cytoplasm in L cells.” Tsitologia, 1978; 20:952-956.
- 100. Prudovsky, I.A., Kushch, A.A., and Zelenin, A.V., “Reactivation of the nuclei of peritoneal exudate leukocytes in enucleated L cells.” Proc. Natl. Acad. Sci. USSR, 1977; 237:211-214.
Since 2011, I have been supervising the module “Stress and adaptation” and presenting part of the lectures of this module.