Peptide Self-Regulation of Living Systems (Facts and Hypotheses) - Shataeva L. K. 2003

References

Adamson A. Water-polymer interface // Water in Polymers. Moscow: Mir, 1984. P. 91—114.

Alekseenko L. P., Orekhovich V. N. New developments in cardiovascular regulation: Endocrine function of The Heart // Vopr. Med. Khimii. 1987. Vol. 33, no. 3. P. 1-15.

Amasiatsi D. Unnecessary for the Uneducated. Moscow: Nauka, 1990. 880 p. (Ser. Scientific Heritage; vol. 13).

Anisimov V. N., Arutyunyan A. V., Khavinson V. Kh. Effect of melatonin and epithalamin on The activity of the antioxidant defense system in rats // Dokl. RAN. 1997. Vol. 352, no. 6. P. 831—833.

(Anisimov V. N., Bondarenko L. A., Khavinson V. Kh.) Anisimov V. N., Bondarenko L. A., Khavinson V. Kh. Effect of pineal peptide preparation (epithalamin) on life span and pineal and serum melatonin level in old rats // Ann. N. Y. Acad. Sci. 1992. Vol. 673. P. 53-57.

Anisimov V. N., Solovyov M. V. Evolution of Concepts in Gerontology. St. Petersburg: Eskulap, 1999. 130 p.

Anisimov V. N., Khavinson V. Kh. Effect of a polypeptide pineal preparation on the life span and spontaneous tumor incidence in old female rats // Dokl. AN SSSR. 1991. Vol. 319, no. 1. P. 250-253.

Anisimov V. N., Khavinson V. Kh., Alimova I. N. et al. Epitalon inhibits tumor development and HER-2/NEU oncogene expression in mammary tumors of accelerated-senescence Transgenic Mice // Byul. Eksperim. Biologii i Meditsiny. 2002a. Vol. 133, no. 2, P. 199-202.

(Anisimov V. N., Khavinson V. Kh., Mikhalsky A. I., Yashin A. I.) Anisimov V. N., Khavinson V. Kh., Mikhalski A. I., Yashin A. I. Effect of synthetic thymic and pineal Peptides on biomarkers of ageing, survival and spontaneous tumor incidence in female CBA mice // Mech. Ageing Develop. 2001. Vol. 122, no. 1. P. 41—68.

Anisimov V. N., Khavinson V. Kh., Morozov V. G. The Role of pineal peptides in Homeostasis regulation: Twenty years of research experience // Uspekhi Sovrem. Biologii. 1993. Vol. 113, no. 6. P. 752—762.

(Anisimov V. N., Khavinson V. Kh., Morozov V. G.) Anisimov V. N., Khavinson V. Kh., Morozov V. G. Twenty years of study on effect of pineal peptide preparation: epithalamin in experimental gerontology and oncology // Ann. N.Y. Acad. Sci. 1994. Vol. 719. P. 483—493.

(Anisimov V. N., Khavinson V. Kh., Popovich I. G., Zabezhinsky M. A.) Anisimov V. N., Khavinson V. Kh., Popovich I. G., Zabezhinski M. A. Inhibitory effect of peptide Epitalon in colon carcinogenesis induced by 1,2-dimethylhydrazine in rats // Cancer Lett. 2002b. Vol. 183. P. 1-8.

Anisimov S. V., Boheler K. R., Khavinson V. Kh., Anisimov V. N. Investigation of The Effect of vilon and epitalon peptides on Gene Expression IN the mouse heart using microarray technology // Byul. Eksperim. Biologii i Meditsiny. 2002. Vol. 133, no. 3. P. 340-347.

Ashmarin I. P., Kamenskaya M. A. Neuropeptides in Synaptic Transmission. Moscow: VINITI, 1988. 184 p. (Itog Nauki i Tekhniki. Ser. Fiziologiya Cheloveka i Zhivotnykh; vol. 34).

Ashmarin I. P., Karazeeva E. P. Neuropeptides // Brain Biochemistry. St. Petersburg: St. Petersburg Univ. Press, 1999. P. 232-266.

Ashmarin I. P., Lelekova T. V., Sanzhieva L. Ts. On the efficacy of ultramall doses and concentrations of biologically active compounds // Izv. RAN. Ser. Biol. 1992. no. 4. P. 531—536.

Ashmarin I. P., Obukhova M. F. Regulatory peptides: A functionally continuous ensemble // Biokhimiya. 1986. Vol. 51, no. 4. P. 531-544.

Balázs A., Blažek I. Endogenous Inhibitors of Cell Proliferation. Moscow: Mir, 1982. 302 p.

Bell R. The Proton in Chemistry. Moscow: Mir, 1977. 382 p.

(Belokrylov G. A., Popova O. Ya., Derevnina O. N. et al.) Belokrylov G. A., Popova O. Ya., Derevnina O. N. et al. Immuno-, phagocytosis modulating and antitoxic properties of Amino Acids and peptide preparations // Drug Develop. Ind. Pharm. 1998. Vol. 24, no. 2. P. 115-127.

Bernal J. D. THE ORIGIN OF Life. Moscow: Mir, 1969. 357 p.

Introduction/36.html">Biological Membranes: A Practical Approach / Ed. by J. Findlay and W. Evans. Moscow: Mir, 1990. 424 p.

Birshtein T. M. Dipole moment of a coil-like polypeptide chain // Vysokomolekul. Soedineniya. 1975. Ser. A. Vol. 17, no. 1. P. 58-61.

Biryuzova V. I. Ultrastructural Organization OF THE Yeast Cell: An Atlas. Moscow: Nauka, 1993. Vol. 3. 224 p.

Boguslavsky L. I. Bioelectrochemical Phenomena and Phase Boundaries. Moscow: Nauka, 1978. 360 p.

Bochkov, N. P., Solovyova, D. V., Strekalov, D. L., & Khavinson, V. K. (2002). The role of molecular genetic Diagnostics in predicting and preventing age-related pathology. Clinical Medicine, 2, 4–8.

Brown, G., & Walken, J. (1982). Liquid crystals and biological structures. Moscow: Mir Publ., 198 p.

Brillouin, L. (1966). Scientific uncertainty and information. Moscow: Mir Publ., 272 p.

Brodsky, V. Y., Khavinson, V. K., Zolotarev, Y. A., et al. (2001). Rhythm of Protein Synthesis in hepatocyte cultures of rats of various ages. Norm and effect of the livagen peptide. Proceedings of the Russian Academy of Sciences. Biological Series, 5, 517–521.

Bulyenkov, N. F. (1990). Self-organizing triplet structures of ideal fractals of “bound” water with D3 and T Symmetry. Crystallography Reports, 35(1), 147–149.

Valuev, I. L., Valuev, L. I., & Platov, N. A. (1998). On the MECHANISM OF ACTION of immobilized Insulin preparations for oral administration. Reports of the Russian Academy of Sciences, 360(1), 57–60.

Wegner, R. E., Rituma, I. R., & Chipens, G. I. (1984). Structure and biological properties of thymopoietin II, thymosin a₁, their fragments and analogues. Proceedings of the Academy of Sciences of the Latvian SSR, 12, 63–76.

Vernadsky, V. I. (1988). Philosophical thoughts of a naturalist. Moscow: Nauka Publ., 520 p.

Wiener, N. (1983). Cybernetics: Or control and communication in the animal and the machine. Moscow: Nauka Publ., 344 p.

Vitvitsky, V. N., Soboleva, L. S., & Shevchenko, V. A. (2000). Alteration of cytotoxic and cytogenetic effects of radiation upon administration of RNA preparations isolated from various Tissues into the Organism. Proceedings of the Russian Academy of Sciences. Biological Series, 3, 290–293.

Vlasov, G. P., Izvarina, N. Y., Illarionova, N. G., et al. (1988). Effect of polymer modification of insulin on its Enzymatic Hydrolysis and conformational properties. Applied Biochemistry and Microbiology, 24(1), 56–61.

Volkenshtein, M. V. (1981). Biophysics. Moscow: Nauka Publ., 576 p.

Volkenshtein, M. V., & Fishman, S. I. (1967). Theory of the effect of ionization on the degree of the a-helix conformation of a polypeptide. Biophysics, 12(1), 14–17.

Gabuda, S. P. (1982). Bound water. Facts and hypotheses. Novosibirsk: Nauka Publ., 160 p.

Gabuda, S. P., & Rzhavin, A. F. (1976). Detection of age-related Changes in the molecular structure of Collagen. Molecular Biology, 10(5), 998–1001.

Gabuda, S. P., & Rzhavin, A. F. (1978). Nuclear magnetic Resonance in crystal hydrates and hydrated Proteins. Novosibirsk: Nauka Publ., 160 p.

Gavrilov, L. A., & Gavrilova, N. S. (1986). Biology of lifespan. Moscow: Nauka Publ., 168 p.

Galperin, Y. M., & Lazarev, P. I. (1986). Digestion and homeostasis. Moscow: Nauka Publ., 304 p.

Glebov, R. N. (1987). Endocytosis and Exocytosis. Moscow: Vysshaya Shkola Publ., 96 p.

Govyrin, V. A., & Zhorov, B. S. (1994). Ligand-receptor interactions in molecular physiology. Saint Petersburg: Nauka Publ., 240 p.

Goldanskii, V. I. (1979). Molecular chemical tunneling — facts and hypotheses. Chernogolovka: Institute of Chemical Physics of the USSR Academy of Sciences, 45 p.

Gomazkov, O. A. (1995). Physiologically active peptides: A reference guide. Moscow: IPGM, 144 p.

Gomazkov, O. A. (1997). The brain and neuropeptides: A reference and information publication. Moscow: Institute of Biomedical Chemistry of the Russian Academy of Medical Sciences, 170 p.

Gorizontov, P. D. (Ed.). (1981). Homeostasis. Moscow: Meditsina Publ., 576 p.

Grushka, Z., Tyračková, V., Tishchenko, G. A., & Shataeva, L. K. (1988). Structure and permeability of composite carboxylic membranes based on polyacrylonitrile. Collection of Czechoslovak Chemical Communications, 53, 3089–3095.

Davydov, A. S. 1984. Solitons in Molecular Systems. Kiev: Naukova Dumka. 288 p.

Debabov, V. G. 1997. DNA vaccination and Gene Therapy based on transient expression of Nucleic Acids in somatic Cells of humans and animals. Molecular Biology, vol. 31, no. 2, pp. 209-215.

De Duve, C. 1987. A Guided Tour of the Living Cell. Moscow: Mir. 256 p.

Djaliashvili, T. A. 1989. The Mechanism of the Modulatory Action of Peptides. Tbilisi: Metsniereba. 224 p.

Dilman, V. M. 1981. The Big Biological Clock: An Introduction to Integrative Medicine. Moscow: Znanie. 207 p.

Dilman, V. M. 1987. Four Models of Medicine. Moscow: Meditsina. 288 p.

Dobretsov, G. E. 1989. Fluorescent Probes in the Study of Cells, Membranes, and Lipoproteins. Moscow: Nauka. 276 p.

Egorov, E. E. 1999. Around telomerase. Molecular Biology, vol. 33, no. 3, pp. 385-392.

Zamyatnin, A. A. 1973. Dilatometry of Protein Solutions. Moscow: Nauka. 104 p.

Zamyatnin, A. A. 1990. Physicochemical features of endogenous regulatory oligopeptides. Biofizika, vol. 35, no. 4, pp. 555-559.

Saenger, W. 1984. Principles of Nucleic Acid Structure. New York: Springer-Verlag. (Russ. ed.: Moscow: Mir, 1987. 584 p.)

Zubova, S. G., and Okulov, V. B. 2001. The role of adhesion molecules in the recognition of foreign and transformed cells by mammalian macrophages. Uspekhi Sovremennoi Biologii, vol. 121, no. 1, pp. 59-66.

Ivanitskii, G. R., and Deev, A. A. 2001. The mechanism of wave interaction as a model of metered substance secretion. Doklady Akademii Nauk, vol. 381, no. 3, pp. 412-416.

Ivanov, V. T., and Berlin, Yu. A. 2000. Molecular biology in the year 2000: Forecasts, reality, and forecasts once again. Russian Journal of Bioorganic Chemistry, vol. 26, no. 10, pp. 752-755.

Ivanov, V. T., Karelin, A. A., Philippova, M. M. et al. 1997. Hemoglobin as a source of endogenous bioactive peptides: METABOLISM/2.html">THE CONCEPT OF tissue-specific peptide pool. Biopolymers (Peptide Science), vol. 43, no. 2, pp. 171-188.

Ivanova, M. A., Smolin, A. V., Shcherbakova, O. G., and Filatov, M. V. 1998. The effect of polyelectrolyte properties of DNA on cytosine protonation. Molecular Biology, vol. 32, no. 4, pp. 635-638.

Evans, E., and Skalak, R. 1982. Mechanics and Thermodynamics of Biomembranes. Moscow: Mir. 304 p.

Il'icheva, I. A., and Florent'ev, V. L. 1992. Four-stranded oligonucleotide complexes—quadruplexes. Molecular Biology, vol. 26, no. 3, pp. 512-531.

Immunophysiology. Ed. by E. A. Korneva. St. Petersburg: Nauka, 1993. 684 p.

Iogansen, A. V. 1981. Infrared Spectroscopy and spectral determination of Hydrogen bond energy. In: Hydrogen Bonding, ed. by N. D. Sokolov. Moscow: Nauka, pp.

Kabanov, A. V., and Kabanov, V. A. 1994. Interpolyelectrolyte complexes of Selection/9.html">NUCLEIC ACIDS AS a means for delivering genetic material into cells. Vysokomolekulyarnye Soedineniya, vol. 36, no. 2, pp. 198-211. Also published as: Kabanov, A. V., and Kabanov, V. A. 1995. DNA complexes with polycations for the delivery of genetic material into cells. Bioconjugate Chem., vol. 6, pp. 7-20.

Kabanov, A. V., Kiselev, V. I., Chikindas, M. Ya. et al. 1989. Enhancement of the transforming activity of plasmid DNA by its incorporation into an interpolyelectrolyte complex with a carbon-chain polycation. Doklady Akademii Nauk SSSR, vol. 306, no. 1, pp. 226-229.

Kagawa, Y. 1984. Biomembranes. Tokyo: Bureau. (Russ. ed.: Moscow: Vysshaya Shkola, 1985. 303 p.)

Karpov, R. S., Slepushkin, V. D., Mordovin, V. F. et al. 1985. The Use of Epiphysis Preparations in Clinical Practice. Tomsk: Tomsk University Press. 152 p.

Caplan, S. R., and Essig, A. 1983. Bioenergetics and Linear Nonequilibrium Thermodynamics: The Steady State. Harvard University Press. (Russ. ed.: Moscow: Mir, 1986. 382 p.)

Kiseleva, E. P., Ogurtsov, R. P., Popova, O. Y., et al. Comparative characteristics of two peptide immunomodulators. Immunologiya, 1999, no. 2, pp. 23–26.

Kiseleva, O. I., Pyshkina, O. A., Kumazawa, N., et al. Study of specific interactions in the DNA-histone system using model objects. Proc. II Int. Conf. “Chemistry of Highly Organized Substances and Scientific Foundations of Nanotechnology”. St. Petersburg: SRC for Chemistry of St. Petersburg State University, 1998, p. 104.

Klimov, P. K. Peptides and the Digestive System. Leningrad: Nauka, 1983, 272 p.

Klimov, P. K., Barashkova, G. M. Endogenous peptides as a unified system of regulatory substances. Sechenov Physiol. J. USSR, 1993, vol. 79, no. 3, pp. 80-87.

Klimontovich, Y. L. Entropy and information of open systems. Physics-Uspekhi, 1999, vol. 169, no. 4, pp. 443–452.

Knyazkin, I. V., Polyakova, V. O. The effect of vilon on the Thymus and Spleen in a radiation model of premature Aging. Advances in Gerontology, 2002, iss. 9, pp. 105–109.

Knyazkin, I. V., Yuzhakov, V. V., Chalisova, N. I., Grigoriev, E. I. Functional Morphology of organotypic rat spleen culture of various ages under the action of vilon. Advances in Gerontology, 2002, iss. 9, pp. 110–115.

Kokryakov, V. N. Biology of Animal-Derived Antibiotics. St. Petersburg: Nauka, 1999, 164 p.

Caughley, G. Analysis of Vertebrate Populations. Moscow: Mir, 1979, 364 p.

Komarov, F. I., Khavinson, V. K., Simonenkova, V. A., Merkuryeva, G. A. The use of epithalamin in Climacteric myocardiopathy. Clinical Medicine, 1995, vol. 73, no. 4, pp. 40–42.

Konyshev, V. A. Nutrition and Regulatory Systems of the Body. Moscow: Meditsina, 1985, 222 p.

Korkushko, O. V., Khavinson, V. K., Butenko, G. M., Shatilo, V. B.

Peptide Preparations of the Thymus and Pineal Gland in the Prevention of Accelerated Aging. St. Petersburg: Nauka, 2002, 204 p.

Korneva, E. A., Golovko, O. I., Kazakova, T. V. Molecular and biological aspects of the interaction between the nervous and immune systems. Problems of Medical Chemistry, 1999, vol. 43, no. 5, pp. 321–329.

Korneva, E. A., Shkhinek, E. K. Hormones and The Immune System. Leningrad: Nauka, 1988, 248 p.

Kravtsov, A. V., Alekseenko, I. R. Surfactants as Tools for Biomembrane Research. Kyiv: Naukova Dumka, 1993, 262 p.

Krichevskaya, A. A., Lukash, A. I., Shugaley, V. S., Bondarenko, T. I.

Amino Acids, Their Derivatives, and Metabolic Regulation. Rostov-on-Don: Rostov University Press, 1983, 112 p.

Kuvichkin, V. V. DNA-lipid interactions in vitro and in vivo. Biology Bulletin Reviews, 2000, vol. 120, no. 5, pp. 466–476.

Kuznik, B. I., Morozov, V. G., Khavinson, V. K. Cytomedins and their role in The regulation of physiological functions. Biology Bulletin Reviews, 1995, vol. 115, no. 3, pp. 353-367.

Kuznik, B. I., Morozov, V. G., Khavinson, V. K. Cytomedins: 25 Years of Experimental and Clinical Research. St. Petersburg: Nauka, 1998, 310 p.

Kuznik, B. I., Pinelis, I. S., Khavinson, V. K. The Use of Peptide BIOREGULATORS in Dentistry. St. Petersburg: Eskulap, 1999, 142 p.

Kulberg, A. Y. Cell Membrane Receptors. Moscow: Vysshaya Shkola, 1987, 104 p.

Kutsiy, M. P., Kuznetsova, E. A., Gazlev, A. I. The involvement of proteinases in apoptosis. Biochemistry (Moscow), 1999, vol. 64, no. 2, pp. 149–163.

Levitsky, D. O. Calcium and Biological Membranes. Moscow: Vysshaya Shkola, 1990, 124 p.

Lehninger, A. Biochemistry. Moscow: Mir, 1974. 958 p.

Lyshko, V. K., & Shevchenko, M. I. Membranes and Cell life. Kyiv: Naukova Dumka, 1987. 104 p.

Lyashenko, A. A., & Uvarov, V. Yu. On the systematization of cytokines. Advances in Modern Biology, 2001, vol. 121, no. 6, pp. 589–603.

Margolis, G. S., & Buse, D. V. The kallikrein–kinin system in the Kidneys. In: Hormones and the Kidney / Eds. B. M. Brenner and D. G. Stein. Moscow: Mir, 1983, pp. 139-173.

Martynkina, L. P., Kolesnikov, A. A., Streltsov, S. A., et al.

Electron microscopic studies of circular DNA compaction in model systems. 2. Complexes of the synthetic peptide tervaline with high molecular weight circular DNAs. Molecular Biology, 1998, vol. 32, no. 4, pp. 614–620.

Martynkina, L. P., Semyonov, T. E., & Vengerov, Yu. Yu. Electron microscopic Study of the compaction of individual DNA molecules in films upon interaction with histone H1. Molecular Biology, 1991, vol. 25, no. 5, pp. 1338–1344.

Martynov, V. F., Leontyeva, L. I., Sorochinskaya, E. I., et al. Induction of differentiation of human Blood and Bone Marrow T-cell precursors by synthetic fragments of thymic factors. Immunology, 1986, no. 4, pp. 24–26.

Maryanovich, A. T., & Polyakov, E. L. Neuropeptides and the blood-brain barrier. Advances in Physiology, 1991, vol. 22, no. 2, pp. 33–51.

Metzler, D. Biochemistry: The Chemical Reactions of Living Cells: In 3 vols. Moscow: Mir, 1980. Vol. 3. 378 p.

Morozov, V. G., Ryzhak, G. A., & Malinin, V. V. Cytamines (bioregulators of cellular metabolism). 2nd ed., rev. and enl. St. Petersburg: Foliant, 2000a. 119 p.

Morozov, V. G., & Khavinson, V. Kh. Effect of substances isolated from the Hypothalamus on immunogenesis and morphological blood composition. Experimental Surgery and Anesthesiology, 1973, no. 1, pp. 19–22.

Morozov, V. G., & Khavinson, V. Kh. A new Class of biological regulators of multicellular systems: Cytomedins. Advances in Modern Biology, 1983, vol. 96, no. 3(6), pp. 339–352.

Morozov, V. G., & Khavinson, V. Kh. The role of cellular mediators (cytomedins) in the regulation of genetic activity. Proceedings of the USSR Academy of Sciences. Biological Series, 1985, no. 4, pp. 581–587.

Morozov, V. G., & Khavinson, V. Kh. Peptide Bioregulators (25 Years of Experimental and Clinical Study). St. Petersburg: Nauka, 1996. 74 p.

(Morozov, V. G., Khavinson, V. Kh.) Morozov, V. G., & Khavinson, V. Kh.

Natural and synthetic thymic peptides as therapeutics for immune dysfunction. Int. J. Immunopharmacol., 1997. Vol. 19, N 9/10, pp. 501–505.

Morozov, V. G., Khavinson, V. Kh., & Malinin, V. V. Peptide thymomimetics. St. Petersburg: Nauka, 2000b. 158 p.

Morozov, V. G., Khavinson, V. Kh., & Pisarev, O. A. Isolation from the thymus and study of The Nature of an immunogenesis-stimulating factor. Doklady Akademii Nauk SSSR, 1977, vol. 233, no. 3, pp. 491-494.

Napalkov, N. P., Yakovlev, G. M., Anisimov, V. N., et al. Prospects for the use of thymus preparations in cancer prevention. Problems of Oncology, 1998, vol. 30, no. 5, pp. 515–521.

Fundamentals of Physiology / Ed. Academician A. D. Nozdrachev. St. Petersburg: Lan, 2001. 1088 p.

Nikiforova, A. A. Lecithin: Cholesterol acyltransferase of Blood Plasma. In: BIOCHEMISTRY OF Lipids and Their Role in Metabolism. Moscow: Nauka, 1981, pp. 85-105.

Paltsev, M. A., & Ivanov, A. A. Intercellular Interactions. Moscow: Meditsina, 1995. 224 p.

Panarin, E. F. Main types and principles of synthesis of biologically active polymers. In: Synthesis, Structure, and Properties of Polymers / Institute of Macromolecular Compounds, USSR Academy of Sciences. Leningrad: Nauka, 1989, pp. 187-198.

Panin, L. E., Kuzmenko, A. P., Poteryaeva, O. N., & Skryl, G. Sh. Detection of apolipoprotein A-I immunoreactivity in rat hepatocyte nuclear Chromatin. Biochemistry, 1992, vol. 57, no. 6, pp. 826–831.

Pankov, Yu. A. All animal and human Organs and tissues are endocrine and secrete Peptide Hormones into the blood // Vopr. Med. Khimii. 1996. Vol. 42, no. 3. P. 179—184.

Pankov, Yu. A., Pozdnyakov, V. I., & Tumanyan, V. G. Analysis of local similarity in primary structures of protein hormones // Molekulyar. Biologiya. 1976. Vol. 10, no. 2. P. 423—436.

Pansevich, L. I., & Barkovsky, E. V. Features of the distribution of amino acid residue combinations in the Primary Structure of calmodulin // Biophysics. 1990. Vol. 35, no. 4. P. 581—584.

Petrov, R. V., Mikhailova, A. A., Fomina, L. A., & Stepanenko, R. N. Myelopeptides. Moscow: Nauka, 2000. 181 p.

Petrov, R. V., & Khaitov, R. M. Immune Response and aging // Uspekhi Sovrem. Biologii. 1975. Vol. 79, no. 1. P. 111 — 127.

Pauling, L. General Chemistry. Moscow: Mir, 1964. 584 p.

Polyakov, L. M., & Panin, L. E. Lipoprotein Regulation of Metabolic processes // Uspekhi Sovrem. Biologii. 2000. Vol. 120, no. 3. P. 265-273.

Polyakova, V. O., Kvetnoy, I. M., Khavinson, V. Kh., et al. Thymus and aging // Uspekhi Gerontologii. 2001. Iss. 8. P. 50—57.

Ponomareva-Stepnaya, M. A., Nezavibatko, V. N., Antonova, L. V., et al. An ACTH (4—10) analogue as a prolonged-action learning stimulant // Khim.-Farmatsevt. Zhurn. 1984. Vol. 18, no. 7. P. 790— 795.

Popov, M. E. Structural organization of proteins. Moscow: Nauka, 1997. 604 p. (Protein Problem Series; Vol. 3).

Potaman, V. I., Arefeeva, I. A., Alfeeva, L. Yu., et al. A tuftsin analogue with a prolonged effect on the Central Nervous system of mammals // Biol. Membrany. 1992. Vol. 9, no. 10—11. P. 1082-1084.

Preparative Biochemistry of Lipids / Ed. by L. D. Bergelson and E. V. Dyatlovitskaya. Moscow: Nauka, 1981. 256 p.

Pushkina, N. V. Protein amidation during organism aging // Ukr. Biokhim. Zhurn. 1977. Vol. 51, no. 6. P. 680—683.

Rabinovich, M. I., & Trubetskov, D. I. Introduction to the Theory of Oscillations and Waves. Moscow: Nauka, 1984. 432 p.

Raikhlin, N. T., Kvetnoy, I. M., & Osadchuk, M. A. The APUD System (General Pathological and Oncological Aspects). Obninsk: Medical Radiological Research Center of the RAMS, 1993. Part 1. 127 p.

Rapoport, I. A. Induction of Immunity as the next task of chemical mutagenesis // Genes, Evolution, Breeding: Selected Works. Moscow: Nauka, 1996. P. 196—202.

Reikhardt, B. A., Kulikova, O. G., & Sapronov, N. S. Dynamics of disorders in brain neuron regulatory systems in age-related amnesia in rats // Psikhofarmakologiya i Biol. Narkologiya. 2001. Vol. 1, no. 1. P. 38-42.

Rosenkranz, A. A., Yachmenev, S. V., & Sobolev, A. S. The use of artificial constructs for the targeted transfer of genetic material into human cells via receptor-mediated endocytosis // Dokl. AN SSSR. 1990. Vol. 312, no. 2. P. 493—494.

Romanov, Yu. A., Ketlinsky, S. A., Antokhin, A. I., & Okulov, V. B.

Chalones and Regulation of Cell Division. Moscow: Meditsina, 1984. 208 p.

Rudzit, V. K. Diabetogenic Tryptophan Metabolites as a Cause of Diabetes Mellitus. Riga: Zinatne, 1981. 83 p.

Rumyantsev, S. N. Constitutional Immunity and Its Molecular-Ecological Foundations. Leningrad: Nauka, 1983. 212 p.

Rusanov, A. I. On the thermodynamics of nucleation on charged centers // Dokl. AN SSSR. 1978. Vol. 238, no. 4. P. 831-834.

Rybnikov, V. Yu., & Zakutsky, N. G. Peptide Regulation of Brain Functions / Ed. by V. Kh. Khavinson. St. Petersburg: Foliant, 2000. 40 p.

Ryzhak, G. A., Malinin, V. V., & Platonova, T. N. Cortexin and Regulation of Brain Functions / Ed. by A. A. Skoromets and V. Kh. Khavinson. St. Petersburg: Foliant, 2001. 160 p.

Ryadnova I. Yu., Chernova I. A., Shataeva L. K., Khavinson V. Kh. Affinity Chromatography of nucleoprotein complexes. Vopr. Med. Khim., 2001, vol. 47, no. 2, pp. 209–216.

Ryadnova I. Yu., Shataeva L. K., Khavinson V. Kh. Interaction of DNA with proteins in model systems. Vysokomolekul. Soedineniya, 2000a, vol. 42, no. 5, pp. 1–7.

Ryadnova I. Yu., Shataeva L. K., Khavinson V. Kh. Tissue-specific nucleoprotein complexes. Vopr. Med. Khim., 2000b, vol. 46, no. 1, pp. 62–71.

Sazanov L. A., Zaitsev S. V. Effect of ultra-low doses (10^-18–10^-14 M) of BIOLOGICALLY ACTIVE SUBSTANCES: General regularities, features, and possible mechanisms. Biokhimiya, 1992, vol. 57, no. 10, pp. 1443–1460.

Skurikhin I. M., Nechaev A. P. All About Food from a Chemist's Perspective. Moscow: Vysshaya Shkola Publ., 1991. 288 p.

Sudakov K. V. General Theory of Functional Systems. Moscow: Meditsina Publ., 1984. 224 p.

Sjakste N. I., Budylin A. V. Structural changes in chromatin at various levels of its organization during aging. Ontogenez, 1992, vol. 23, no. 3, pp. 242–253.

Trofimova S. V., Khavinson V. Kh. The retina and aging. Uspekhi Gerontologii, 2002, iss. 9, pp. 79–82.

Walford R., Meredith P., Chenie C. Immunoengineering: Prospects for the correction of age-related immunodeficiencies. In: Immunology and Aging, ed. T. Makinodan and E. Yunis. Moscow: Mir Publ., 1980, pp. 242–267.

Ursova N. I. Modern Treatment of Helicobacter pylori-associated PEPTIC ULCER DISEASE in children. Ros. Med. Zhurn., 2000, vol. 8, no. 17, pp. 707–710.

Fedorova T. A., Tereshchenko O. Ya., Mazurik V. K. Nucleic Acids and Proteins in the Organism under Radiation Injury. Moscow: Meditsina Publ., 1974. 408 p.

Filippov A. T. The Many-Faced Soliton. Moscow: Nauka Publ., 1990. 286 p. (Kvant Library, iss. 48).

Fox S., Dose K. Molecular Evolution and the Origin of Life. Moscow: Mir Publ., 1975. 375 p.

Franklin T., Snow J. Biochemistry of Antimicrobial Action. Moscow: Mir Publ., 1984. 240 p.

Frolkis V. V. Syndromes of aging. Vestn. AMN SSSR, 1990, no. 1, pp. 8–12.

Frolkis V. V., Muradyan H. K. Experimental Ways to Extend Life. Leningrad: Nauka Publ., 1988. 245 p.

Khavinson V. Kh. Peptide Regulation of Aging. Vestn. RAMN, 2001a, no. 12, pp. 16–20.

Khavinson V. Kh. Tissue-specific action of peptides. Byull. Eksperim. Biologii i Meditsiny, 2001b, vol. 132, no. 8, pp. 228–229.

Khavinson V. Kh., Anisimov V. N. Synthetic dipeptide vilon (L-Lys–L-Glu) increases life span and inhibits The Development of spontaneous tumors in mice. Dokl. RAN, 2000, vol. 372, no. 3, pp. 421–423.

Khavinson V. Kh., Ashmarin I. P., Malinin V. V. Age-related dynamics of regulatory peptides. Nauka Dolgoletiya, 2001a, no. 1, pp. 18–22.

Khavinson V. Kh., Golubev A. G. Aging of the pineal gland. Uspekhi Gerontologii, 2002, iss. 9, pp. 67–72.

Khavinson V. Kh., Goncharova N., Lapin B. Synthetic tetrapeptide epitalon restores distributed neuroendocrine regulation in senescent monkeys. Neuroendocrinology Lett., 2001b, vol. 22, pp. 251–254.

Khavinson V. Kh., Gorbunov A. A., Ryzhak G. A. The Effect of Peptide Bioregulators on the Morphology of Parenchymal Organs. St. Petersburg: Foliant Publ., 2000a. 79 p.

Khavinson V. Kh., Egorova V. V., Timofeeva N. M. et al. Effect of vilon and epitalon peptides on glucose and Glycine absorption in various PARTS OF THE Small Intestine in rats. Byull. Eksperim. Biologii i Meditsiny, 2002a, vol. 133, no. 5, pp. 570–573.

Khavinson V. Kh., Zhukov V. V. Thymus peptides and mechanisms of immunomodulation. Uspekhi Sovrem. Biologii i Meditsiny, 1992, vol. 112, no. 4, pp. 554–570.

(Khavinson V. Kh., Izmailov D. M., Obukhova L. K., Malinin V. V.) Khavinson V. Kh., Izmailov D. M., Obukhova L. K., Malinin V. V. Effect of epitalon on the lifespan increase in Drosophila melanogaster // Mech. Ageing Develop. 2006. Vol. 120. P. 141—149.

Khavinson V. Kh., Kvetnoy I. M. Peptide bioregulators inhibit apoptosis // Bull. Exp. Biol. Med. 2000. Vol. 130, no. 12. P. 657-659.

Khavinson V. Kh., Malinin V. V. Mechanisms of geroprotective action of peptides // Bull. Exp. Biol. Med. 2002. Vol. 133, no. 1. P. 4-10.

Khavinson V. Kh., Morozov V. G. Application of thymus peptides as geroprotective agents // Probl. Aging Longevity. 1991. Vol. 1, no. 2. P. 123-128.

Khavinson V. Kh., Morozov V. G. Epiphysis and thymus peptides in the regulation of aging. St. Petersburg: Foliant, 2001. 160 p.

(Khavinson V. Kh., Morozov V. G., Anisimov V. N.) Khavinson V. Kh., Morozov V. G., Anisimov V. N. Experimental studies of the pineal gland preparation Epithalamin // The pineal gland and cancer / Eds C. Bartsch et al. Berlin; Heidelberg: Springer-Verlag, 2001b. P. 294—306.

Khavinson V. Kh., Morozov V. G., Malinin V. V. et al. Effect of the Lys—Glu peptide on interleukin-2 gene expression in lymphocytes // Bull. Exp. Biol. Med. 2000c. Vol. 130, no. 9. P. 330-332.

Khavinson V. Kh., Morozov V. G., Chalisova N. I., Okulov V. B.

Effect of brain peptides on Nerve Tissue cells in vitro // Cytology. 1997. Vol. 39, no. 7. P. 571—575.

Khavinson V. Kh., Mylnikov S. V. Effect of the pineal tetrapeptide on the state of antioxidant defense in Drosophila melanogaster // Bull. Exp. Biol. Med. 2000. Vol. 129, no. 4. P. 420-422.

Khavinson V. Kh., Rybakina E. G., Malinin V. V. et al. Effect of short peptides on thymocyte blast transformation and signal Transduction via the sphingomyelin pathway // Bull. Exp. Biol. Med. 2002b. Vol. 133, no. 5. P. 574—577.

(Khavinson V. Kh., Solovieva D. V.) Khavinson V. Kh., Solovieva D. V.

New approach to the prophylaxis and treatment of age-related pathology // Rom. J. Geront. Geriat. 1998. Vol. 20, no. 1. P. 28—34.

Khavinson V. Kh., Chalisova N. I., Morozov V. G., Malinin V. V.

Role of thymus peptides in the regulation of lymphoid tissue growth in rats of different ages // Dokl. Akad. Nauk. 1999. Vol. 369, no. 5. P. 701—703.

Khavinson V. Kh., Chernyak S. I., Dyakonov M. M. Cytamins as a means of maintaining high professional fitness and longevity in military personnel // Mil. Med. J. 2001d. Vol. 322, no. 2. P. 26—28.

Khavinson V. Kh., Shutak T. S. Use of epithalamin in non-insulin-dependent diabetes mellitus. St. Petersburg: Foliant, 2000. 61 p.

Khavinson V. Kh., Yuzhakov V. V., Kvetnoy I. M. et al. Immunohistochemical and morphometric Analysis of the effect of vilon and epitalon on the functional morphology of radiosensitive organs // Bull. Exp. Biol. Med. 2001e. Vol. 131, no. 3. P. 338-346.

Khusainova R. S., Khusainov A. A., Popov V. I. et al. DNA-Ca²⁺-phosphatidylcholine // Dokl. Akad. Nauk. 1999. Vol. 367, no. 3. P. 416—419.

Chazov E. I., Isachenkov V. A. The pineal gland: place and role in the neuroendocrine regulation system. Moscow: Nauka, 1974. 238 p.

Chalisova N. I., Khavinson V. Kh., Penniyainen V. A., Grigoriev E. I. Effect of thymus peptide fractions on the development of organotypic culture of the thymus and spleen in rats // Cytology. 1999. Vol. 41, no. 10. P. 889-894.

Chang R. Physical chemistry with Applications to biological systems. Moscow: Mir, 1980. 462 p.

Chebotarev D. F., Korkushko O. V., Mankovsky N. B., Mints A. Ya. Atherosclerosis and age. Leningrad: Meditsina, 1982. 295 p.

(Chernova I. A., Gurevich K. Ya.) Chernova I. A., Gurevich K. Ya. Structure and sorption characteristics of bioaffinity membranes // J. Membrane Sci. 1996. Vol. 113. P. 161—167.

Shataeva L. K., Ryadnova I. Yu., Khavinson V. Kh. Interpolymer complexes of deoxyribonucleic acid with proteins // Russ. J. Appl. Chem. 1999. Vol. 72, no. 6. P. 982—985.

Shataeva L. K., Radnova I. Yu., Khavinson V. Kh. Investigation of the informational value of oligopeptide blocks in regulatory Peptides and Proteins // Uspekhi Sovrem. Biologii. 2002. Vol. 122, no. 3. P. 282-289.

Shataeva L. K., Chernova I. A., Samsonov G. V. et al. Isolation and properties of neuraminidase from cholera vibrios // Vopr. Med. Khimii. 1978. Vol. 24, no. 4. P. 569-572.

Shannon C. E. Prediction and entropy of printed English // The Mathematical Theory of Communication. Urbana: Univ. of Illinois Press, 1949. (Russ. ed.: Raboty po teorii informatsii i kibernetike. Moscow: Inostr. Lit., 1963. P. 669—686).

Schmalhausen I. I. Integration of biological systems and their self-regulation // Byul. MOIP. Otd. Biol. 1961. Vol. 66, iss. 2. P. 104—134.

Schmalhausen I. I. Cybernetic Questions in Biology. Novosibirsk: Nauka, 1968. 224 p.

Eigen M., Winkler R. The Laws of the Game: How the Rules of Nature Govern Destiny. New York: Knopf, 1981. (Russ. ed.: Igra zhizni. Moscow: Nauka, 1979. 94 p.).

Eigen M., Schuster P. The Hypercycle: A Principle of Natural Self-Organization. Berlin: Springer-Verlag, 1979. (Russ. ed.: Gipertsikl. Printsipy samoorganizatsii makromolekul. Moscow: Mir, 1982. 270 p.).

Yakovlev G. M., Novikov V. S., Khavinson V. Kh. Resistance, Stress, Regulation. Leningrad: Nauka, 1990. 238 p.

Yakovlev G. M., Khavinson V. Kh., Morozov V. G., Novikov V. S. Prospects for bioregulating therapy // Klin. Meditsina. 1991. Vol. 69, no. 5. P. 19-23.

Yamskoy I. A., Yamskova V. P. New-generation pharmacological preparations based on cellular microenvironment Glycoproteins // Ross. Khim. Zh. (Zh. VKhO im. D. I. Mendeleeva). 1998. Vol. 62, no. 3. P. 85-90.

Yankovsky O. Yu., Dovnar T. E. On The problem of the Specificity of regulatory peptide Cleavage from unspecialized precursor proteins // Zh. Evol. Biokhim. Fiziol. 1986. Vol. 22, no. 1. P. 11-16.

Yarilin A. A. Fundamentals of Immunology. Moscow: Meditsina, 1999. 608 p.

Yarilin A. A., Nikonova M. F., Yarilina A. A. et al. Apoptosis, its role in pathology and The Significance of its assessment in Clinical and immunological examination of patients // Med. Immunologiya. 2000. Vol. 2, no. 1. P. 7-16.

Adinolfi S., Bagni C., Morelli M. A. C. et al. Novel RNA-binding motif: the KH module // Biopolymers (Peptide Sci.). 1999. Vol. 51, no. 2. P. 153-164.

Akala E. A., Kopeckova P., Kopecek J. Novel pH sensitive hydrogels with adjustable Swelling kinetics // Biomaterials. 1998. Vol. 19. P. 1037—1047.

Alberts B., Bray D., Lewis J. et al. Molecular Biology of The Cell. 3rd ed. New York: Garland Publ., 1994. 1294 p.

Andersson L., Blomberg L., Flegel M. et al. Large-scale synthesis of peptides // Biopolymers (Peptide Sci.). 2000. Vol. 55. P. 227—250.

Antequera F., Bird A. CpG islands // Exs. 1993. Vol. 64. P. 169-185.

Arnott S., Chandrasekaran R., Hall L. H. et al. DNA secondary structures: helices, wrinkles and junctions // Cold Spring Harbor Symp. Quant. Biol. 1983. Vol. 47. P. 53-67.

Atchley W. R., Wollenberg K. R., Fitch W. M. et al. Correlation among amino acid sites in bHLH Protein domains: an information theoretic analysis // Mol. Biol. Evol. 2000. Vol. 17. P. 164—178.

Audhya T., Scheid M. P., Goldstein G. Contrasting biological activities of thymopoietin and splenin, two closely related polypeptide products of thymus and spleen // Proc. Natl. Acad. Sci. USA. 1984. Vol. 81, no. 9. P. 2847-2849.

Bairoch A., Bucher P., Hofman K. The PROSITE database, its status in 1995 // Nucleic Acids Res. 1996. Vol. 24. P. 189—196.

Baumann G. Growth-hormone binding proteins // Proc. Soc. Exp. Biol. Med. 1993. Vol. 202. P. 392-400.

Bell A., Kittler L., Löber G., Zimmer C. DNA binding properties of minor groove binders and their influence on the topoisomerase II cleavage reaction // J. Mol. Recognit. 1997. Vol. 10, no. 6. P. 245—255.

Bellamy D. The thymus in relation to problems of cellular growth and aging // Gerontologia. 1973. Vol. 19. P. 162—184.

Belli S. L., Rechnitz G. A. Biosensors based on native chemoreceptors // Frezenius Ztschr. Anal. Chem. 1989. Bd 331. S. 439—447.

Biochemical microcalorimetry / Ed. H. D. Brown. New York: Acad. Press, 1969. 338 p.

Biotechnology of Antibiotics / Ed. R. William. New York etc.: Strohl. Marcel Dekker, 1997. 842 p. (Drugs and the pharmaceutical sciences; Vol. 82).

Bird A. The essential of DNA Methylation // Cell. 1992. Vol. 70. P. 5-8.

Bloomfield V. A. DNA-Condensation by multivalent cations // Biopolymers. Nucl. Acids Sсi. 1997. Vol. 44, N 3. P. 269—282.

Boarends W. M. Histone ubiquitination and chromatin remodeling in mouse Spermatogenesis // Develop. Biol. 1999. Vol. 207, N 2. P. 322— 333.

Bodey В., Bodey В. J., Siegel S. E., Kaiser H. E. Involution of the mammalian thymus, one of the leading regulators of aging // In Vivo. 1997. Vol. 11, N 5. P. 421-440.

Bornstein M. V., Miller A., Slagle S. A pilot trial of COP-1 in exacerbiting-remitting multiple sclerosis // N. Engl. J. Med. 1987. Vol. 317, N 7. P. 408-414.

Burgess R. R. Use of polyethyleneimine in purification of DNA binding protein // Meth. Enzymol. “Protein—DNA interactions” / Ed. R. T. Sauer. 1991. Vol. 208. P. 3-9.

Cameron D. E., Sved S., Solyom L. et al. Effect of ribonucleic acid on memory defect in the aged // Amer. J. Psychiat. 1963. Vol. 120. P. 320-325.

Cattau D., Bourgoin D., Joly M. Change of conformation of DNA by association with proteins // Europ. J. Biochem. 1969. Vol. 8, N 4. P. 541-546.

Chien Y. W. Systemic delivery of pharmacologically active molecules across the Skin // Targeted Drug Delivery. Berlin etc.: Springer-Verlag, 1992. P. 181—230. (Handbook Exp. Pharmacol, and Ther.; Vol. 100).

Ching-Fa Wu, Wen-Yih Chen, Hwai-Shen Liu. Determination of the binding constant of imidazole and Histidine with immobilized Cu(II) by differential UV spectroscopy // J. Chem. Eng. Jap. 1995. Vol. 28, N 4. P. 419-423.

Choh Hao Li. Biologically active peptides // Biochemical and biophysical studies of proteins and nucleic acids. Berlin etc.: Elsevier, 1984. P. 1-10.

Claud H. Role of aromatic amino acid residues in the binding of Enzymes and proteins to nucleic acids // Nature. New Biol. 1971. Vol. 234, N 47. P. 120-121.

Coleman J. E. Zinc proteins: enzymes, storage proteins Transcription factors and Replication proteins // Annu. Rev. Biochem. 1992. Vol. 61. P. 897-946.

Conjugated oligomers, polymers, and dendrimers: from polyacetilene to DNA: Proc. of the 4th Francqui colloquium, Brusseles, 21—23 Oct. 1998 / Ed. J.-L. Bredas. Paris: De Berg Univ., 1998. 622 p.

Connor J., Schroit A. J. Transbilayer movement of phosphotidylserine in erythrocytes // Biochemistry. 1988. Vol. 27, N 3. P. 848— 851.

Cooper A. A., Stevens T. H. Protein splicing: self-splicing of genetically mobile elements at the protein level // TIBS. 1995. 20 Sept. P. 351-356.

Davis S. S. Overcoming barriers to the oral administration of peptide drugs // Trends Pharm. Sсi. 1990. Vol. 11, N 9. P. 353—355.

Dawson P. E., Muir T. W., Clark-Lewis I., Kent S. В. H. Synthesis of proteins by native chemical ligation // Science. 1994. Vol. 266, N 5186. P. 276-279.

De Bold A. J., Borrenstein H. B., Veress А. T., Sonnenberg H. А rapid and potent natriuretic responce to intravenous injection of atrial miocardial extract in rats // Life Sei. 1981. Vol. 28, N 1. P. 89—94.

Deenen L. L. M. Topology and dynamics of Phospholipids in membranes // FEBS Lett. 1981. Vol. 123, N 1. P. 3-15.

Deinum G., van Langen H., van Ginkel G., Levine Y. K. Molecular order and dynamics in planar lipid bilayers: effects of unsaturation and sterols // Biochemistry. 1988. Vol. 27, N 3. P. 852—860.

Denisov G., Wanaski S., Luan P. et al. Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidyl Inositol 4,5-biphosphate: an electrostatic model and experimental results // Biophys. J. 1998. Vol. 74, N 2. P. 731-744.

Dickson D. W. The Pathogenesis of senile plaques // J. Neuropathol. and Exp. Neurol. 1997. Vol. 56. P. 321-339.

Drubaix I., Giakoumakis A., Robert L., Robert A. M. Preliminary data on the age-dependent decrease in basic fibroblast growth factor and platelet-derived growth factor in the human vein wall and in their influence on cell proliferation // Gerontology. 1998. Vol. 44, N 1. P. 9—14.

Dumas F., Lebrun M. C., Tocanne J.-F. Is the protein/lipid hydrophobic matching principle relevant to membrane organisation and functions? // FEBS Lett. 1999. Vol. 458. P. 271—277.

Dynlacht B. D. Regulation of transcription by protein, that control the Cell Cycle // Nature. 1997. Vol. 389. P. 149—152.

Erlwanger R. H., Unmack M. A., Grondahl M. L. Effect of age on vasoactive intestinal polypeptide-induced short-circuit current in porcine jejunum // Comp. Biochem. Physiol, and Mol. Integrat. Physiol. 1999. Vol. 124, N 1. P. 29-33.

Erhan S., Mazzolf T., Cohen L. Amino acid neighborhood relationships in proteins // Intern. J. Bio-Med. Comput. 1980. Vol. 11, N 1. P. 67-75.

Etemadi A.-H. Membrane Asymmetry — a survey and critical appraisal of the methodology // Biochim. et biophys. acta. 1980. Vol. 604, N 3-4. P. 423-475.

Finch С. E., Kirkwood T. Chance, development, and aging. Oxford: Oxford Univ. Press, 2000. 256 p.

Fox S. V. A theory of macromolecular and cellular origins // Nature. 1965. Vol. 205. P. 238.

Furchgott R. F., Zavadski J. V. The obligatory role of the endothelial cells in the relaxation of arterial smooth Muscle by acetylholine // Nature. 1980. Vol. 288. P. 373-376.

Ginaldi L., De Martinis M., D’Ostilio A. et al. The immune system in the elderly. 2. Specific cellular immunity // Immunol. Res. 1999. Vol. 20, N 2. P. 109-115.

Goldknopt I. L., Wilson G., Rosenbaum F. et al. Dissappearance of protein A24 and ubiquitin during shatdown of transcription in avian erythroid cells // Fed. Proc. 1980. Vol. 39, N 6. P. 255.

Goldstein G., Scheid M., Hammerling U. et al. ISOLATION OF A polypeptide that has Lymphocyte-differentiating properties and is probably represented universally in living cells // Proc. Nat. Acad. Sсi. USA. 1975. Vol. 72, N 1. P. 11-15.

Graf J., Ogle R. C., Robey F. A. et al. Pentapeptide from the Laminin B1 chain mediates Cell Adhesion and binds the 67 000 Laminin receptor // Biochemistry. 1987. Vol. 26, N 22. P. 6896—6900.

Gunning M. E., Brenner В. M. Natriuretic peptides and the kidney, current concepts // Kidney Intern. 1992. Vol. 42, suppl. 38. P. 127— 133.

Halaas J. L., Gajiwala K. S., Maffei M. et al. Weight-reducing effects of the plasma protein encoded by the obese gene // Science. 1995. Vol. 269, N 7. P. 543-546.

Hannappel E., Davoust S., Horecker B. L. Isolation of peptides from calf thymus // Biochem. and Biophys. Res. Commns. 1982a. Vol. 104, N 1. P. 266-271.

Hannappel E., Davoust S., Horecker B. L. Thymosin ß8 and β9: two new peptides isolated from calf thymus homologous to thymosin ß₄ // Proc. Nat. Acad. Sсi. USA. 1982b. Vol. 82. P. 1708-1711.

Harrison S. C. A structural Taxonomy of DNA-binding domains // Nature. 1991. Vol. 353. P. 715-719.

Hartley R. V. L. Transmission of information // Bell System Techn. J. 1928. Vol. 7, N 3. P. 535-563.

Heijne G. von. A sequence correlation between oppositely charged residues in secreted proteins // Biochem. and Biophys. Res. Communs. 1980. Vol. 93, N 1. P. 82-86.

Heldin C. N., Heilman U., Ishikawa F., Miyazono K. Purification, cloning and expression of platelet—derived endothelial cell growth factor // Meth. Enzymol. 1991. Vol. 198. P. 383—391.

Herzei H., Ebeling W., Schnutt A. O. Entropies of biosequences: the role of repeats // Phys. Rev. E. 1994. Vol. 50, N 6. P. 5061—5071.

Herzei H., Grosse I. Measuring correlations in symbol sequences // Physica A. 1995. Vol. 216, N 6. P. 518-542.

Heymann J. B., Engel A. Structural clues in The sequence of the Aquaporins // J. Mol. Biol. 2000. Vol. 295, N 4. P. 1039—1053.

Hinkel L., McCaig C. D., Robinson K. R. The direction of growth of differentiating neurones and myoblasts from frog embryos in applied electric field // J. Physiol. 1981. Vol. 314. P. 121 — 135.

Hipkiss A. R., Worthington V. C., Himswoth D. T. M., Herwig W. Protective effect of camosine against protein modification mediated by malondialdehyde and hypochlorite // Biochim. et biophys. acta. 1998. Vol. 1380. P. 46-54.

Hippel P. H. von, McGhee J. D. DNA-Protein Interactions // Annu. Rev. Biochem. 1972. Vol. 41, N 1. P. 231—300.

Hirokawa K. The thymus and aging // Immunology and aging. New York; London: Acad. Press, 1977. P. 51—72.

Hopp T. P., Woods K. R. Prediction of Protein antigenic determinants from Amino acid sequences // Proc. Nat. Acad. Sei. USA. 1981. Vol. 78, N 6. P. 3824-3828.

Horlein A. J., Naar A. M., Heinzei T. et al. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor // Nature. 1995. Vol. 377. P. 397—404.

Immunostimulants / Eds I. Azuma and G. Jolles. Berlin; Paris; Tokyo: Jap. Sei. Soc. Press; Springer-Verlag, 1987. 258 p.

Israel L., Kozarevic Dj., Orgogozo J. M. Subjective and objective health in aging: problems of assessment // Modification of cell to cell signals during normal and pathological aging / Ed. S. Govoni and F. Battaini. Berlin etc.: Springer-Verlag, 1987. P. 261—285.

Iverson B. L. Betas are brought into the fold // Nature. 1997. Vol. 385, N 6612. P. 113-115.

Jacob F., Monod J. Genetic regulation mechanisms in the synthesis of proteins // J. Mol. Biol. 1961. Vol. 3. P. 318-356.

Jaffe L. F. The role of ionic currents in establishing developmental pattern // Phil. Trans. Roy. Soc. London B. 1981. Vol. 295. P. 553— 556.

Jasani B., Kreil G., Madder B. F., Stanworth D. R. Further studies on the structural requirements for polypeptide-mediated histamine release from rat must cells // Biochem. J. 1979. Vol. 181, N 3. P. 623— 632.

Kaiser E. T., K6zdy F. J. Amphiphilic Secondary structure: design of peptide hormones // Science. 1984. Vol. 223, N 4633. P. 249—255.

Kamo N. Characteristics of biomembranes and membrane transport // Liquid membranes. Chemical applications / Eds T. Araki and H. Tsukube. Florida, Boca Raton: C. R. C. Press Inc., 1990. 726 p.

Karlin S., Zuker M., Brocchieri L. Measuring residue associations in protein structures. Possible implication for protein folding // J. Mol. Biol. 1994. Vol. 239, N 2. P. 227-248.

Kaskоw J. W., Regmi A., Mulchahey J. J. Changes in brain corticotropin-releasing factor Messenger RNA expression in aged Fisher 344 rats // Brain Res. 1999. Vol. 822, N 1-2. P. 228-230.

Katan-Khaykovich Y., Shaul Y. RFX1, a single DNA-binding protein with a split dimerization domain, generates alternative complexes // J. Biol. Chem. 1998. Vol. 273, N 38. P. 24504-24512.

Kohl A., Volk H.-D., Diezel W. The dipeptide Lys—Pro restores the diminished wound healing following treatment with anti-T-helper cell monoclonal antibody // Intern. J. Immunopharmacol. 1989. Vol. 11, N 3. P. 237-240.

Kolusheva S., Shahal T., Jelinek R. Peptide-membrane interactions studied by a new phospholipid/polydiacetilene colorimetric vesicle assay // Biochemistry. 2000. Vol. 39. P. 15851 — 15859.

Knox D. G., Rosenberg A. Fluctuations of Protein Structure as expressed in distribution of hydrogen exchange rate constants // Biopolymers (Peptide Sсi.). 1980. Vol. 19, N 5. P. 1049-1069.

Kopelman R. Diffusion-controlled reaction kinetics // The fractal approach to heterogeneous chemistry / Ed. D. Avnir. New York etc.: John Wiley end Sons, 1992. P. 295-308.

Krauss E. M., Cowburn D. Anomalous exchange kinetics of peptide amide protons In aqueous solutions // Intern. J. Peptide and Protein Res. 1981, Vol. 17, N 1. P. 42-47.

Kreil G. D-aminoacids in animal peptides // Annu. Rev. Biochem. 1997. Vol. 66. P. 337-345.

Kroemer G., Petit P., Zamzami N. et al. The biochemistry of programmed cell death // FASEB J. 1995. Vol. 9, N 13. P. 1277-1287.

Lear J. D., Schneider J. P., Kenker P. K. Electrostatic effects on ion selectivity and rectification in designed ion channel peptides // J. Amer. Chem. Soc. 1997. Vol. 119, N 14. P. 3212-3217.

Lee D. H., Granja J. R., Martinez J. A. et al. A self replicating peptide // Nature. 1996. Vol. 382, N 6591. P. 525—528.

Leo A., Hansch C., Elkins D. Partition coefficients and their uses // Chem. Revs. 1971. N 6. P. 525-616.

Leonard D. A., Rajaram N., Kerppola T. K. Structural basis of DNA bending and oriented heterodimer binding by the basic leucine zipper domains of Fos and Jun // Proc. Nat. Acad. Sсi. USA. 1997. Vol. 94, N 10. P. 4913-4918.

Leszyk J., Dumasvala R., Potter J. D. et al. Bovine cardiac Troponin-T: aminoacid sequences of the two isoforms // Biochemistry. 1987. Vol. 26, N 22. P. 7035-7042.

Levi-Montalchini R. Developmental neurobiology and the natural history of NGF // Annu. Rev. Neurosci. 1982. Vol. 5. P. 341 — 356.

Levitt M. A simplified representation of protein Conformations for rapid simulation of protein folding // J. Mol. Biol. 1976. Vol. 104, N 1. P. 59-107.

Lieburg A. F. van, Knoers N. V., Deen P. M. Discovery of aquaporins: a breakthrough in research on renal water transport // Pediatr. Nephrol. 1995. N 9(2). P. 228-234.

Lin L.-F., Doherty D. H., Lile J. D. et al. GDNF: a glial cell line-derived neurotrophic factor for Midbrain dopaminergic Neurons // Science. 1993. Vol. 260. P. 1130-1132.

Louis J. M., Dyda F., Nashed N. T. et al. Hydrofilic peptides derived from the transframe region of Gag—Pol inhibit the HIV-protease // Biochemistry. 1998. Vol. 37, N 8. P. 2105—2110.

Luisi В., Orozco M., Sponer J., Luque F. On the potential role of the amino nitrogen atom as a hydrogen bond acceptor in macromolecules // J. Mol. Biol. 1998. Vol. 279, N 5. P. 1123-1136.

Lumry R., Rajender S. Enthalpy — entropy compensation phenomena in water solution of proteins and small molecules // Biopolymers (Reptide Sсi.). 1970. Vol. 9, N 10. P. 1125-1227.

Mao Y., Sun M., Desai S. D., Leroy F. L SUMO-1 conjugation to topoisomerase 1, a possible repair responce to topoisomerasemediated DNA demage // Proc. Nat. Acad. Sсi. USA. 2000. Vol. 97, N 8. P. 4046-4051.

Marks M. S., Ohne H., Kirchhausen T., Bonifacino S. J. Protein sorting by Tyrosine-based signals: adapting to the Ys and wherefores // Trends Cell Biol. 1997. Vol. 7. P. 124-128.

Marlow B. J., Fairhurst D., Pendse H. P. Colloid vibration potential and the electrokinetic characterisation of concentrated colloids // Langmuir. 1988. Vol. 4, N 3. P. 611-626.

McGhee J. D., Felsenfeld G. Nucleosome structure // Annu. Rev. Biochem. 1980. Vol. 49. P. 1115-1156.

McMurray W. C. Form and function of phospholipids / Ed. G. B. Ansell. Amsterdam: Elsevier Sсi. Publ. Co, 1973. 255 p..

McNamara S. H. Dietary supplements of botanicals and other substances: a new era regulation // Food and Drag Law J. 1995. Vol. 50, N 3. P. 341-348.

Meites J. Neuroendocrine aspects of aging II Modification of cell to cell signals during normal and pathological aging / Eds S. Govoni and F. Battaini. Berlin etc.: Springer-Verlag, 1987. P. 83—89.

Mitchell P. Vectorial chemistry and the molecular mechanics of Chemiosmotic Coupling: power transmission by proticity // Biochem. Soc. Transactions. 1976. Vol. 4, N 1. P. 399—430.

Mitchell P. J., Tjian R. Transcriptional Regulation in mammalian cells by sequence-specific DNA-binding proteins // Science. 1989. Vol. 245. P. 371-378.

Morris A. J. Lysophospholipid signaling // Trends Pharm. Sei. 1999. Vol. 20, N 3. P. 393-395.

Mosevitsky M. I., Novitskaya V. A., Plekhanov A. Yu, Skladchikova G. Yu. Neuronal protein GAP-43 is a member of novel group of brain acid-soluble proteins (BASPs) // Neurosci. Res. 1994. Vol. 19, N 2. P. 223-228.

Mousli M., Bueb J.-L., Bronner C., Rouot B., Landry Y. G-protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides // Trends Pharm. Sсi. 1990. Vol. 11, N 9. P. 358-362.

Nemeth-Cahalan K. L., Hall J. E. pH and calcium regulate the water permeability of aquaporin 0 // J. Biol. Chem. 2000. Vol. 275, N 10. P. 6777-6782.

Neuman J. В., Engel A. Structural clues in the sequences of the aquaporins // J. Mol. Biol. 2000. Vol. 295, N 4. P. 1039-1053.

Nucleic acid-protein recognition / Ed. H. J. Vogel. New-York: Acad. Press, 1977. 587 p.

Okouchi S., Ashida T., Sakaguchi S. et al. Dynamics of the Hydration of halogenoalcohols in aqueous solutions // Bull. Chem. Soc. Jap. 2002. Vol. 75, N 1. P. 59-63.

Olanow C. W., Tatton W. G. Etiology AND PATHOGENESIS of Parkinson’s disease // Annu. Rev. Neurosci. 1999. Vol. 22. P. 123—144.

Ouyang Q., Cicek G., Westendorp R. G. J., Remarque E. J. Reduced IFN-y production in elderly people following in vitro stimulation with Influenza vaccine and endotoxin // Mech. Ageing Develop. 2000. Vol. 121. P. 131-137.

Owen D., Evans P. R. A structural explanation for the recognition of tyrosine based endocytotic signals // Science. 1998. Vol. 282. P. 1327— 1332.

Oxford Dictionary of biochemistry and molecular biology. Oxford: Oxford Univ. Press, 1997. 746 p.

Pabo C. O., Sauer R. T. Transcription factors: structural families and principles of DNA recognition // Ann. Rev. Biochem. 1992. Vol. 61. P. 1053-1095.

Palmer M., Velicevic I., Saweljew P. et al. Streptolysin O: a proposed model of allosteric interaction between a pore forming protein and its target lipid bilayer // Biochemistry. 1998. Vol. 37, N 8. P. 2378—2383.

Pauling L. A molecular theory of general anesthesia // Science, 1961, Vol. 134, N 1. P. 15.

Pawelec G., Effros R. B., Caruso C. et al. T-cells and aging // Frontiers in Biosci. 1999. Vol. 4. P. 216—269.

Pecheur E. I., Martin I., Ruysschaert J. M. et al. Membrane fusion induced by 11 mer anionic and cationic peptides. A structure — function study // Biochemistry. 1998. Vol. 37, N 8. P. 2361—2371.

Pellegrini M., Mierke D. F. Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy // Biopolymers. (Peptide Sсi.). 1999. Vol. 51, N 3. P. 208-220.

Pickart L. The biological effects and mechanism of action of the plasma tripeptide Glycyl-Histidyl-Lysin // Lymphokines / Ed. E. Pick. New York; London: Acad. Press, 1983. Vol. 8. P. 425—446.

Pietrokovski S., Henikoff J. G., Henikoff S. The BLOCKS database — a system for Protein Classification // Nucl. Acid Res. 1996. Vol. 24. P. 197-200.

Protein targeting: A practical approach / Eds A. I. Magee and T. Willeman. Oxford: Oxford Univ. Press, 1993. 315 p.

Re F., Zanetti A., Sironi M. et al. Inhibition of anchorage-dependent cell spreading triggers apoptosis in cultured human endothelial cells // J. Cell Biol. 1994. Vol. 127, N 2. P. 537-546.

Reem G. H., Cook L. A., Henriksen D. M., Vilcek J. Gamma-interferon induction in human thymocytes activated by Lectins and B-cell lines // Infect. Immunol. 1982. Vol. 37, N 1. P. 216—221.

Regulatory peptides / Ed. J. M. Polak. Basel etc.: Birkhauser Verlag, 1989. 396 p.

Reutter W., Kottgen E., Bauer C., Gerok W. Biological Significance of sialic acids // Sialic acids / Ed. R. Schauer. Vien; New York: Springer-Verlag, 1982. P. 263—304. (Cell Biol. Monographs; Vol. 10).

Richardson G. Hair-cell regeneration: keep the noise down // Curr. Biol. 1993. Vol. 3. P. 759-762.

Rivier J., Kaiser R., Galyean R. Solid-phase synthesis of Somatostatin and Glucagon selective analogs in gram quantities // Biopolymers (Peptide Sсi.). 1978. Vol. 17, N 8. P. 1927-1938.

Robert L., Legeasis J. M., Robert A. M., Renard G. Corneal collagens // Pathol. Biol. (Paris). 2001. Vol. 49, N 49. P. 353—363.

Rytomaa M., Kinnunen P. K. J. Dissociation of cytochrom C from Liposomes by histone H1. Comparison with basic peptides // Biochemistry. 1996. Vol. 35, N 14. P. 4529-4539.

Sahu A., Kalra S. P. Absence of increased neuropeptide Y neuronal activity before and during the luteinizing hormone (LH) surge may underlie the attenuated preovulatory LH surge in middle-age rats // Endocrinology. 1998. Vol. 139, N 2. P. 696—702.

Schiffer M., Edmundson A. B. Use of helical wheels to represent the structures of proteins and to identify segments with helical potential // Biophys. J. 1967. Vol. 7, N 2. P. 121-135.

Schlesinger D. H., Goldstein G., Niall H. D. The complete Amino Acid Sequence of Ubiquitin, a adenilate cyclase stimulating polypeptide probably universal in living cells II Biochemistry. 1975. Vol. 14, N 10. P. 2214-2218.

Schmid S. L. Clatrin coated vesicle formation and protein sorting. An integrated process U Annu. Rev. Biochem. 1997. Vol. 66. P. 511—548.

Shannon C. Prediction and entropy of printed English // Bell System Techn. J. 1951. Vol. 30, N 1. P. 50—64.

Simon M. I. Summary: The cell surface regulates Information Flow, material transport, and cell identity // Cold Spring Harbor Symp. Quant. Biol. 1992. Vol. 57. P. 673—688.

Singer S. Y. The Structure and function of membranes, a personal memoir // J. Membran. Biol. 1992. Vol. 129, N 1. P. 3—12.

Stewart J., Stahmann M. Polyaminoacids, Polypeptides and proteins / Ed. M. Stahmann. Madison: Visconsin Univ. Acad. Press, 1962. P. 9—29.

Stone R. A., Glembotski C. C. Immunoreactive atrial natriuretic peptide in the rat eye U Biochem. and Biophys. Res. Communs. 1986. Vol. 134. P. 1022-1028.

Strous G. J., Govers R. The ubiquitin-proteosome system and endocytosis // J. Cell Sei. 1999. Vol. 112. P. 1417—423.

Suzuki T., Ichiyama A., Saitoh H. et al. A new 30 kDa ubiquitin-related SUMO-1 hydrolase from bovine brain // J. Biol. Chem. 1999. Vol. 274, N 44. P. 31131-31134.

Takemura A., Matsuda N., Taneguchi S. Regeneration accelerators for periodontal tissue and Materials / Jpn. KoKai ToKKyo Koho JP 06, 234,653 (Cl A61K37/02). 1994.

Tanaka K., Nishide J., Okasaki K. et al. Characterisation of fission yeast SUMO-1 homologue, Pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation // Nucl. Cell Biol. 1999. Vol. 19, N 12. P. 8660-8672.

Tanatani A., Fukutomi R., Ranuta H. et al. Novel DNA minor groove binders with an aromatic layered structure // Nucl. Acid Symp. Ser.

1998. Vol. 39. P. 31-32.

Tang L., Li J., Kotz D. S., Feng J.-A. Determining the DNA bending angle induced by non-specific high mobility group-1 (HMG-1) proteins — a novel method // Biochemistry. 2000. Vol. 39, N 11. P. 3052—3060.

Tang Y. A., Yuan J., Osapay G. et al. A cyclic antimicrobial peptide produced in primate leucocytes by the ligation of two truncated defensins // Science. 1999. Vol. 286. P. 498—502.

Tappia P. S., Padua R. R., Panagia V., Kardami E. Fibroblast growth-factor-2 stimulates phospholipase Cß in adult cardiomyocytes // Biochem. Cell Biol. 1999. Vol. 77, N 6. P. 569-575.

Teitelbaum D., Meshorer A., Hirshfeld H. et al. Copolymers for treatment of encephalomyelitis // Europ. J. Immunol. 1971. Vol. 1, N 1. P. 242-248

Teng C. S., Teng C. T., Allfrey V. G. Studies of nuclear acidic proteins // J. Biol. Chem. 1971. Vol. 246, N 11. P. 3597-3609.

Tomas T., Thomas G., McLendon C. et al. ß-Amyloid — mediated vasoactivity and vascular endothelial damage // Nature. 1996. Vol. 380, N 6570. P. 168-171.

Tomoaia-Cotisel M. Acid dissociation constants diphytanylglycerol phosphorylglycerol methylphosphate // Chem. and Phys. Lipids. 1999. Vol. 100, N 1-2. P. 41-54.

Unwin P. N. T., Ennis K. Two configurations of a channel-forming membrane protein // Nature. 1984. Vol. 307. P. 609—612.

Van Holde К. E. Chromatin. New York; London: Springer-Verlag, 1988. 497 p.

Wainer P. K., Langridge R., Blaney J. M., Kollman P. A. Electrostatic potential molecular surfaces // Proc. Nat. Acad. Sei. USA. 1982. Vol. 79, N 12. P. 3754-3758.

Wakim В. T., Alexander K. A., Masure H. R. et al. Amino acid sequence of P-57, a neurospecific calmodulin-binding protein // Biochemistry. 1987. Vol. 26, N 23. P. 7466-7470.

Weiss O., Jimenez-Montano M. A., Herzel H. Information content of protein sequences // J. Theor. Biol. 2000. Vol. 206. P. 379—386.

W. H. O. Working group: Preventing disability in the elderly. Copenhagen: WHO Regional office for Europe, 1982. EURO Reports and studies N 65.

Wilkinson K. D., Audhya T. K. Stimulation of ATP-dependent proteolysis requires Ubiquitin with the COO-terminal sequence Arg— Gly-Gly // J. Biol. Chem. 1981. Vol. 256, N 17. P. 9235-9241.

Willeman T., Harding C., Stahl P. Receptor-mediated endocytosis // Biochem. J. 1985. Vol. 232, N 1. P. 1-14.

Wolffe A. P. Architectural transcription factors // Science. 1994. Vol. 264. P. 1100-1101.

Yamamoto N. Antihypertensive peptides derived from food proteins // Biopolymers (Peptide Sсi.). 1997. Vol. 43, N 2. P. 129—138.

Yuasa K., Michibata H., Omori K., Yanaka N. A novel interaction of cGMP-dependent protein kinase I with troponin T // J. Biol. Chem.

1999. Vol. 274, N 52. P. 37429-37434.

Yuqiu J., Juang C.-В., Keller D. et al. Mechanical, electrical, and chemical manipulation of single DNA molecules // Nanotechnology. 1992. Vol. 3, N 1. P. 16-20.

Zhang S., Holmes T., Lockshin C., Rich A. Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane // Proc. Nat. Acad. Sсi. USA. 1993. Vol. 90, N 8. P. 3334— 3338.

Zhou N. E., Kay С. M., Hodges R. S. Synthetic model proteins: the relative contribution of leucine residues at the nonequivalent positions of the 3—4 hydrophobic repeat to the Stability of the two-stranded a-helical coiled-coil // Biochemistry. 1992. Vol. 31, N 25. P. 5739-5746.