Студопедия

КАТЕГОРИИ:


Архитектура-(3434)Астрономия-(809)Биология-(7483)Биотехнологии-(1457)Военное дело-(14632)Высокие технологии-(1363)География-(913)Геология-(1438)Государство-(451)Демография-(1065)Дом-(47672)Журналистика и СМИ-(912)Изобретательство-(14524)Иностранные языки-(4268)Информатика-(17799)Искусство-(1338)История-(13644)Компьютеры-(11121)Косметика-(55)Кулинария-(373)Культура-(8427)Лингвистика-(374)Литература-(1642)Маркетинг-(23702)Математика-(16968)Машиностроение-(1700)Медицина-(12668)Менеджмент-(24684)Механика-(15423)Науковедение-(506)Образование-(11852)Охрана труда-(3308)Педагогика-(5571)Полиграфия-(1312)Политика-(7869)Право-(5454)Приборостроение-(1369)Программирование-(2801)Производство-(97182)Промышленность-(8706)Психология-(18388)Религия-(3217)Связь-(10668)Сельское хозяйство-(299)Социология-(6455)Спорт-(42831)Строительство-(4793)Торговля-(5050)Транспорт-(2929)Туризм-(1568)Физика-(3942)Философия-(17015)Финансы-(26596)Химия-(22929)Экология-(12095)Экономика-(9961)Электроника-(8441)Электротехника-(4623)Энергетика-(12629)Юриспруденция-(1492)Ядерная техника-(1748)

Цитированная. Bershadsky A.D., Vasiliev J.M




Общая

Bershadsky A.D., Vasiliev J.M. Cytoskeleton. New York. Plenum Press, 1988.

 

Lackie J. M. Cell Movement and Cell Behaviour. London, Alien and Unvvin, 1985.

 

Schliwa M. The Cytoskeleton. New York, Springer-Verlag, 1986.

 

Shcterline P. Mechanisms of Cell Motility. London, Academic Press, 1983.

 

 


 

Албертс Б., Брей Д., Льюис Дж., Рэфф М., Робертс К. Уотсон Дж. Д. Молекулярная биология клетки: В 3-х т. 2-е изд. перераб. и доп. Т. 2.: Пер. с англ. – М.: Мир, 1993. – 539 с.

 

1. Amos L. A. Structure of muscle filaments studied by electron microscopy. Annu. Rev. Biophys. Biophys. Chem., 14, 291-313, 1985.

 

Huxley A. F. Reflections on Muscle. Princeton, NJ, Princeton University Press, 1980.

 

Squire J. M. Muscle: Design, Diversity and Disease. Menlo Park CA, Benjamin-Cummings, 1986.

 

2. Cooke R. The mechanism of muscle contraction. CRC Crit. Rev. Biochem., 21, 53-118, 1986.

 

Huxley H, E. The mechanism of muscular contraction. Science, 164, 1356-1366, 1969.

 

3. Cohen C., Parry D. A. D.. -Helical coiled coils a widespread motif in proteins. Trends Biochem. Sci., 11, 245-248, 1986.

 

Davis J. S. Assembly processes in vertebrate skeletal thick filament formation. Annu. Rev. Biophys. Biophys. Chem., 17, 217 239, 1988.

 

4. Bessman S. P., Carpenter C. L. The creatine-creatine phosphate energy shuttle. Annu. Rev. Biochem., 54, 831-862, 1985.

 

5. Warrick H.M., Spudich J.A. Myosin structure and function in cell motility. Annu. Rev. Cell Biol., 3, 379-421, 1987.

 

6. Pollard Т.О., Cooper J.A. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu. Rev. Biochem., 55, 987-

1035, 1986.

 

7. Irring M. Muscle mechanics and probes of the crossbridge cycle. In: Fibrous Protein Structure (J. M. Squire, P. J. Vibert, eds.). San Diego, CA, Academic Press, 1987.

 

Pollard Т.О. The myosin crossbridge problem. Cell, 48, 909, 910, 1987.

 

8. Katz B. Nerve, Muscle and Synapse. New York, MaGraw-Hill, 1966. [Имеется перевод: Катц Б. Нерв, мышца и синапс. М.: Мир, 1969].

 

LaiF.A., Erickson H.P., Rousseau Е., Liu O.-Y., Meissner G. Purification and reconstruction of the calcium release channel from skeletal muscle. Nature, 331, 315-319, 1988.

 

Saito A., Inui M., Radermacher M., Frank J., Fleischer S. Ultrastructure of the calcium release channel of sarcoplasmatic reticulum. J. Cell Biol., 107, 211 219, 1988.

 

9. Murray J. M., Weber A. The cooperative action of muscle proteins. Sci. Am., 230(2), 59-71, 1974.

 

Phillips G. N., Fillers J. P., Cohen C. Tropomyosin crystal structure and muscle regulation. J. Мо.. Biol., 192, 111-131, 1986.

 

Zot A.S., Potter J. D. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu. Rev. Biophys. Chem., 16, 535-559, 1987.

 

10. Wang K. Sarcomere-associated cytoskeletal lattices in striated muscle. Review and hypothesis. In: Cell and Muscle Motility (J.W. Shay, ed.).

 

Vol. 6, pp. 315-369. New York, Plenum Press, 1985.

 

11. Fawcett D.W. A Textbook of Histology, llth ed. Philadelphia, Saunders, 1986.

 

12. Korn E.D., Hammer J.A. Myosins of nonmuscle cells. Annu. Rev. Biophys. Biophys. Chem., 17, 23-45, 1988.

 

Sellers J. R., Adelstein R. S. Regulation of contractile activity. In: The Enzymes (P. Bover, E.G. Krebs, ed), Vol. 18, pp. 381-418. San Diego, CA, Academic Press, 1987.

 

13. Citi S., Kendrick-Jones J. Regulation of non-muscle myosin structure and function. Bioessays, 7, 155- 159, 1987.

 

14. ByersH.R., Fujiwara K. Stress fibers in cells in situ: immunofluorescence visualization with anti-actin, anti-myosin and anti-alpha-actinin. J.

 

Cell Biol., 93, 804-811, 1982.

 

Langanger B. et al. The molecular organization of myosin in stress fibers of cultured cells. J. Cell Biol., 102, 200-209, 1986.

 

Schroeder Т.Е. Actin in dividing cells: contractile ring filaments bind heavy meromyosin. Proc. Natl. Acad. Sci. USA, 70, 1688-1692, 1973.

 

15. Buckingham M.E. Actin and myosin multigene families: their expression during the formation of skeletal muscle. Essays Biochem., 20, 77-109, 1985.

 

Emerson C. P., Bernstein S. I. Molecular genetics of myosin. Annu. Rev. Biochem., 56, 695-726, 1987.

 

Otey C.A., Kalnoski M.H., Bulinski J.C. Identification and quantification of actin isoforms in vertebrate cells and tissues. J. Cell. Biochem., 34, 113-124, 1987.

 

16. Breitbart R.E., Andreadis A., Nadal-Ginard B. Alternative splicing: a ubiquitous mechanism for the generation of multiple protein isoforms from single genes. Annu. Rev. Biochem., 56, 467-495, 1987.

 

17. Bray D., Heath J., Moss D. The membrane-associated "cortex" of animal cells: its structure and mechanical properties. J. Cell Sci. Suppl. 4, 71-

88, 1986.

 

 


 

Албертс Б., Брей Д., Льюис Дж., Рэфф М., Робертс К. Уотсон Дж. Д. Молекулярная биология клетки: В 3-х т. 2-е изд. перераб. и доп. Т. 2.: Пер. с англ. – М.: Мир, 1993. – 539 с.

 

Коrn Е. D. Actin polymerization and its regulation by proteins from nonmuscle cells. Physiol. Rev., 62, 672-737, 1982.

 

Pollard Т.О., Cooper J. A. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu. Rev. Biochem., 55, 987-

1035, 1986.

 

Tilney L. G. Interactions between actin filaments and membranes give spatial organization to cells. In: Modern Cell Biology, Vol. 2. Spatial Organization of Eukaryotic Cells (J. R. Mclntosh, В. Н. Satir esdl.) pp. 163-199. New York: Liss, 1983.

 

18. Sato M., Schwartz W.H., Pollard Т.О. Dependence of the mechanical properties of actin/alpha-actinin gels on deformation rate. Nature, 325, 828-830, 1987.

 

Stossel T. P. et el. Non-muscle actin binding proteins. Annu. Rev. Cell Biol., 1, 353-402, 1985.

 

19. Matsudaira P., Janmev P. Pieces in the actin-severing protein puzzle. Cell, 54, 139-140, 1988.

 

Yin H. L. Gelsolin: calcium and polyphosphoinositide-regulated actin modulating protein. Bioessays, 7, 176 179, 1987.

 

20. Korn E. D., Hammer J. A. Myosins of nonmuscle cells. Annu. Rev. Biophys. Biophys. Chem., 17, 23-45, 1988.

 

Warrick H.M., Spudlich J.A. Myosin structure and function in cell motility. Annu. Rev. Cell Biol., 3, 379-421, 1987.

 

21. Adams R. J., Pollard T.D. Propulsion of organelles isolated from Acanthamoeha along actin filaments by myosin-I. Nature, 322, 754 756, 1986.

 

Sheetz M. P., Spudich J. A. Movement of myosin-coated fluorescent beads on actin cables in vitro. Nature, 303, 31-35, 1983.

 

22. Bennett V. The membrane skeleton of human erythrocytes and its implications for more complex cells. Annu. Rev. Biochem., 54, 273-304, 1985.

 

23. Conzelman K.A., Mooseker M.S. The 110-kD protein-calmodulin complex of the intestinal microvillus in an actin-activated MgATPase. J. Cell Biol., 105, 313-324, 1987.

 

Mooseker M. S. Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border. Annu. Rev. Cell. Biol., 1, 209-241, 1985.

 

24. Burridae K. et al. Focal adhesions: transmembrane junctions between the extracellular matrix and cytoskleton. Annu. Rev. Cell Biol., 4, 487-

525, 1988.

 

Horwitz A., Duyaan K., Buck C., Beckerle M.C., Bur ridge К. Interaction of plasma membrane fibronectin receptor with talin-a transmembrane linkage. Nature, 320, 531-533, 1986.

 

25. Bonder E. M., Fishkind D.J., Mooseker M.S. Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament. Cell, 34, 491-501, 1983.

 

Korn E.D., Carlier M.-F., Pantaloni D. Actin polymerization and ATP hydrolysis. Science, 238, 638-644, 1987.

 

26. Abercrombie M. The crawling movement of metazoan cells. Proc. R. Soc. Lond. (Biol.), 207, 129-147, 1980.

 

Small J. V., Rinnerthaler G., Hinssen H. Organization of actin meshworks in cultured cells: the leading edge. Cold Spring Harbor Symp.

 

Quant. Biol., 46, 599-611, 1982.

 

Wany Y. Exhange of actin subunits at the leading adge of living fibroblasts: possible role of treadmiling. J. Cell Biol., 101, 597 602, 1985.

 

27. Tilney L. G., Inoue S. Acrosomal reaction of Thyone sperm. II. The kinetics and possible mechanism of acrosomal process elongation. J. Cell Biol., 93, 820-827, 1982.

 

28. Carson M., Weber A., Zigmond S. H. An actin-nucleating activity in poly-morphonuclear leukocytes is modulated by chcrnotactic peptides, J.

 

Cell Biol., 103, 2707-2714, 1986.

 

Devreotes P., Zigmond S. Chemotaxis in eukaryotic cells. Annu. Rev. Cell Biol., 4, 649-686, 1988.

 

Tilney L. G., Bonder E. M., DeRosier D.J. Actin filaments elongate from their membrane-associated ends. J. Cell Biol., 90, 485-494, 1981.

 

29. Cooper J.A. Effects of cytochalasin and phalloidin on actin. J. Cell Biol., 105, 1473-1478, 1987.

 

30. Dustin P. Microtubules, 2nd ed., pp. 127-164. New York, Springer-Verlag, 1984.

 

Gibbons I.R. Cilia and flagella of eukaryotes. J. Cell Biol., 91, 107s-124s, 1981.

 

Roberts K., Hyams J.S., eds. Microtubules. New York. Academic Press, 1979. Satir P. How cilia move. Sci. Am., 231(4), 44-63, 1974.

 

31. Amos L. A., Baker T.S. The three dimensional structure of tubulin protofilaments. Nature, 279, 607-612, 1979.

 

Mandelkow E.-M., Schultheiss R., Rapp R., Muller M., Mandelkow E. On the surface lattice of microtubules: helix starts, protofilament number, seam and handedness. J. Cell Biol., 102, 1067-1073, 1986.

 

RaffE.C. Genetics of microtubule systems. J. Cell Biol., 99, 1-10, 1984.

 

 


 

Албертс Б., Брей Д., Льюис Дж., Рэфф М., Робертс К. Уотсон Дж. Д. Молекулярная биология клетки: В 3-х т. 2-е изд. перераб. и доп. Т. 2.: Пер. с англ. – М.: Мир, 1993. – 539 с.

 

Sulivan К. F. Structure and utilization of tubulin isotypes. Annu. Rev. Cell Biol., 4, 687-716, 1988.

 

32. Linck R. W., Amos W. B. Localization of tektin filaments in microtubules of sea urchin sperm flagella by immunoelectron microscopy, J. Cell Biol., 100, 126-135, 1985.

 

33. Goodenough U. W., Heuser J. E. Substructure of inner dynein arms, radial spokes, and the central pair/projection complex of cilia and flagella.

 

J. Cell Biol., 100, 2008 2018, 1985.

 

34. Summers K. E., Gibbons 1. R. ATP-induced sliding of tubules in trypsin-treated flagella of sea urchin sperm. Proc. Natl. Acad. Sci. UDA, 68, 3092-3096, 1971. Warner F. D., Satir P. The structural basis of ciliary bend formation. J. Cell Biol., 63, 35-63, 1974.

 

35. Johnson K. A. Pathway of the microtubule-dynein ATPase and structure of dynein: a comparison with actomyosin. Annu. Rev. Biophys.

 

Biophys. Chem., 14, 161-188, 1985.

 

36. Brokaw C.J. Future directions for studies of mechanisms for generating flagellar bending waves. J. Cell Sci., Suppl. 4, 103 113, 1986.

 

Brokaw C. J., Luck D. J. L., Huang B. Analysis of the movement of Chlamydomonas flagella: the function of the radial-spoke system is revealed by comparison of wild-type and mutant flagella. J. Cell Biol., 92, 722-732, 1982.

 

37. Afzelius B. A. The immotile-cilia syndrome: a microtubule-associated defect. CRC Crit. Rev. Biochem., 19, 63-87, 1985.

 

Huang B. Chlanydomonas reinhardtii: a model system for genetic analysis of flagellar structure and motility. Int. Rev. Cytol., 99, 181 215, 1986.

 

Luck D. J. L. Genetic and biochemical dissection of the eucaryotic flagellum. J. Cell Biol., 98, 789 794, 1984.

 

38. Lefebvre P. A., Rosenbaum J. L. Regulation of the synthesis and assembly of ciliary and flagellar proteins during regeneration. Annu. Rev. Cell Biol., 2, 517-546, 1986.

 

Wheatley D. N. The Centriole: A Central Enigma of Cell Biology. New York, Elsevier, 1982.

 

39. Karsenti E., Мого В. Centrosomes and the spatial distribution of microtubules in animal cells. Trends Biochem. Sci., 11, 460-463, 1986.

 

Ramanis Z., Luck D. J. L. Loci affecting flagellar assembly and function map to an unusual linkage group in Chlamydomonas reinhardtii. Proc.

 

Natl. Acad. Sci. USA, 83, 423 436, 1986.

 

Vorobjev LA., Chentsov Y.S. Centrioles in the cell cycle. 1. Epithelial cells. J. Cell Biol., 93, 938 949, 1982.

 

40. Dustin P. Microtubules, 2nd ed. Berlin, Springer-Verlag, 1984.

 

41. De Brabander M. et al. Microtubule dynamics during the cell cycle: the effects of taxol and nocodazole on the microtubule system of Ptk2 cells at different stages of the mitotic cycle. Int. Rev. Cytol., 101, 215-274, 1986.

 

Inoue S. Cell division and the mitotic spindle. J. Cell Biol., 91, 13Is-147s, 1981.

 

Salmon E. D., McKeel M., Hays T. Rapid rate of tubulin dissociation from microtubules in the mitotic spindle in vivo measured by blocking polymerization with colchicine. J. Cell Biol., 99, 1066-1075, 1984.

 

42. Farrell K. W., Jordan M.A., Miller H.P., Wilson L. Phase dynamics at microtubule ends: the coexistence of microtubule length changes and treadmilling. J. Cell Biol., 104, 1035-1046, 1987.

 

Mclntosh J. R., Euteneuer U. Tubulin hooks as probes for microtubule polarity: an analysis of the method and evaluation of data on microtubule polarity in the mitotic spindle. J. Cell Biol., 98, 525 533, 1984.

 

43. Carlier M.-F. Role of nucleotide hydrolysis in the polymerization of actin and tubulin. Cell Biophys., 12, 105-117, 1988.

 

Horio H. Hotani H. Visualization of the dynamic instability of individual microtubules by dark field microscopy. Nature, 321, 605-607, 1986.

 

Mitchison Т., Kirschner M. Dynamic instability of microtubule growth. Nature, 312, 237-342, 1984.

 

44. Karsenti E., Maro B. Centrosomes and the spatial distribution of microtubules in animal cells. Trends Biochem. Sci., 11, 460-463, 1986.

 

Mitchison Т., Kirschner M. Microtubule assembly nucleated by isolated Centrosomes. Nature, 312, 232-237, 1984.

 

45. Kirschner M., Mitchison T. Beyond self-assembly: from microtubules to morphogenesis. Cell, 45, 329-342, 1986.

 

Sammak P. J., Borisy G. G. Direct observation of microtubule dynamics in living cells. Nature, 332, 724-726, 1988.

 

46. Barra H. S., Arce C. A., Argarana С. Е. Posttranslational tyrosination and detyrosination of tubulin. Molec. Neurobiol., 2, 133-153, 1988.

 

Gundersen G. G., Khawja S., Bulinski J. C. Postpolymerization detyrosination of [α]-tubulin: a mechanism for subcellular differentiation of microtubules. J. Cell Biol., 105, 251-264, 1987.

 

 


 

Албертс Б., Брей Д., Льюис Дж., Рэфф М., Робертс К. Уотсон Дж. Д. Молекулярная биология клетки: В 3-х т. 2-е изд. перераб. и доп. Т. 2.: Пер. с англ. – М.: Мир, 1993. – 539 с.

 

Maruta Н., Greer К., Rosenbaum J. L. The acetylation of a-tubulin and its relationships to the assembly and disassembly of microtubules. J.

 

Cell Biol., 103, 571-579, 1986.

 

Schulze E., Asai D. J., Bulinski J. C., Kirschner M. Post-translational modification and microtubule stability. J. Cell Biol., 105, 2167-2177, 1987.

 

47. Olmstcd J. B. Microtubule-associated proteins. Annu. Rev. Cell Biol., 2, 421-457, 1986.

 

ValleeR.B., Bloom G. S., Theurkauf W. E. Microtutbule-associated proteins: subunits of the cytomatrix. J. Cell Biol., 99, 38s-44s, 1984.

 

48. Alien R.D. The microtubule as an intracellular engine. Sci. Am., 256(2), 42-49, 1987.

 

Alien R.D. ct al. Gliding movement of and bidirectional transport along single native microtubules from squid axoplasm: evidence for an active role of microtubules in cytoplasmic transport. J. Cell Biol., 100, 1736 1752, 1985.

 

49. Vale R. Intracellular transport using microtubule-based motors. Annu. Rev. Cell Biol., 3, 347-378, 1987.

 

Vale R.D., Reese T.S., SheetzM.P. Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell, 42, 39 50, 1985.

 

Vallee R. В., Wall J. S., Paschal B. M., Shpetner H. S. Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein. Nature, 332, 561 563, 1988.

 

50. Allan V.J., Kreis Т.Е. A microtubule-binding protein associated with membranes of the Golgi apparatus. J. Cell Biol., 103, 2229-2239, 1986.

 

Dabora S. L., Sheet- M. P. The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extracts. Cell, 54, 27-35, 1988.

 

Lee C., Chen L. B. Dynamic behavior of endoplasmic reticulum in living cells. Cell, 54, 37-46, 1988.

 

Lucocq J. M., Warren G. Fragmentation and partitioning of the Golgi apparatus during mitosis in HeLa cells. EMBO J., 6, 3239-3246, 1987.

 

51. Geiger B. Intermediate filaments: looking for a function. Nature, 329, 392-393, 1987. Steinert P. M., Roop D. R. Molecular and cellular biology of intermediate filaments. Annu. Rev. Biochem., 57, 593-626, 1988.

 

Traub P. Intermediate Filaments: A Review. New York, Springer-Verlag, 1985. Wang E., Fischman D., Liem B.K.H., Sun T.-T., eds.

Intermediate Filaments. Ann. N.Y. Acad. Sci., 455, 1985.

 

52. Osborn M., Weber K. Tumor diagnosis by intermediate filament typing: a novel tool for surgical pathology. Lab. Invest., 48, 372-394, 1983.

 

53. Ip W., Hartzer M. K., Pang S. Y.-Y., Robson R. M. Assembly of vimentin in vitro and its implications concerning the structure of intermediate filaments. J. Моl. Biol., 183, 365-375, 1985.

 

Quintan R. A. ct al. Characterization of dimer subunits of intermediate filament proteins. J. Моl. Biol., 192, 337-349, 1986.

 

54. Geuens G., De Brabander M., Nuydens R., De Mey J. The interaction between microtubules and intermediate filaments in cultured cells treated with taxol and nocodazole. Cell Biol. Int. Rep., 7, 35-47, 1983.

 

Goldman R. et al. Intermediate filaments: possible functions as cytoskeletal connecting links between the nucleus and the cell surface. Ann. N.

 

Y. Acad. Sci., 45, 1-17, 1985.

 

55. Geisler N., Weber K. Phosphorylation of desmin in vitro inhibits formation of intermediate filaments: identification of three kinase A sites in the aminoterminal head domain. EMBO J., 7, 15 20, 1988.

 

Inagaki M., Nishi Y., Nishizawa K., Matsuyama M., Sato C. Site-specific phosphorylation induces disassembly of vimentin filaments in vitro.

 

Nature, 328, 649 652, 1987.

 

56. Aebi U., Cohn J., Buhle L., Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature, 323, 560-564, 1986.

 

McKeon F.D., Kirschner M. W., Caput D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature, 319, 463-468, 1986.

 

57. Abercrombie M. The crawling movement of metazoan cells. Proc. R. Soc. Lond. (Biol.), 207, 129-147, 1980.

 

Bridgman P. Structure of cytoplasm as revealed by modern electron microscopy techniques. Trends Neurosci., 10, 321-325, 1987.

 

Singer S. J., Kupfer A. The directed migration of eukaryotic cells. Annu. Rev. Cell Biol., 2, 337-365, 1986.

 

Trinkaus J. P. Cells into Organs: The Forces that Shape the Embryo. 2nd ed. Englewood Clifis, NJ, Prentice-Hall, 1984.

 

58. Bridgman P. C., Reese T. S. The structure of cytoplasm in directly frozen cultured cells. 1. Filamentous meshworks and the cytoplasmic ground substance. J. Cell Biol., 99, 1655-1668, 1984.

 

 


 

Албертс Б., Брей Д., Льюис Дж., Рэфф М., Робертс К. Уотсон Дж. Д. Молекулярная биология клетки: В 3-х т. 2-е изд. перераб. и доп. Т. 2.: Пер. с англ. – М.: Мир, 1993. – 539 с.

 

Heuser J., Kirschner M. W. Filament organization revealed in platinum replicas of freeze-dried cytoskeletons. J. Cell Biol., 86, 212-234, 1980.

 

59. Fulton A.B. How crowded is the cytoplasm? Cell, 30, 345-347, 1982.

 

Luby-Phelps K., Taylor D. L., Lanni F. Probing the structure of the cytoplasm. J. Cell Biol., 102, 2015-2022, 1986.

 

60. Kolega J. Effects of mechanical tension on protrusive activity and microfilament and intermediate filament organization in an epidermal epithelium moving in culture. J. Cell Biol., 102, 1400 1411, 1986.

 

Trinkam J. P. Cells into Organs: The Forces That Shape the Embryo, 2nd ed., pp. 157 244. Englewood Cliffs, NJ. Prentice-Hall, 1984.

 

61. Bray D., Hollcnbeck P.J. Growth cone motility and guidance. Annu. Rev. Cell Biol., 4, 43-62, 1988.

 

Euteneuer U., Schliwa M. Persistent, directional motility of cells and cytoplasmic fragments in the absence of microtubules. Nature, 310, 58-

61, 1984.

 

Malawista S. E., De Boisfleury Chevance A. The cytokinetoplast: purified, stabile, and functional motile machinery from human blood polymorphonuclear leukocytes. J. Cell Biol., 95, 960-973, 1982.

 

Marsh L., Letourneau P. C. Growth of neurites without filopodial or lamellipodial activity in the presence of cytochalasin B. J. Cell Biol., 99, 2041-2047, 1084.

 

Vasiliev J. M. et at. Effect of colcemid on the locomotion of fibroblasts. J. Embryol. Exp. Morphol., 24, 625-640, 1970.

 

62. Bray D., White J.G. Cortical flow in animal cells. Science, 239, 883-888, 1988.

 

De Lozannc A., Spudich J.A. Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science, 236, 1086-

1091, 1987.

 

Knecht D. A., Loomis W. F. Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum. Science, 236, 1081 1086, 1987.

 

63. Bergmann J.E., Kupfer A., Singer S.J. Membrane insertion at the leading edge of motile fibroblasts. Proc. Natl. Acad. Sci., USA, 80, 1367-

1371, 1983.

 

Bretscher M.S. How animal cells move. Sci. Am., 257(6), 72 90, 1987.

 

64. Lackie J.M. Cell Movement and Cell Behaviour, pp. 253-275. London, Alien and Unwin, 1986.

 

Trinkaus J. P. Cells into Organs: The Forces That Shape the Embryo, 2nd ed., pp. 157 244. Englewood Cliffs, NJ. Prentice-Hall, 1984.

 

65. Ode/I G. M., Oster G., Alberch P., Burnside B. The mechanical basis of morphogenesis. 1. Epithelial folding and invagination. Dev. Biol., 85, 446-462, 1981.

 

66. Tilncy L. G., Tilney M. S., Cotanche D. A. Aclin filaments, stereocilia, and hair cells of the cochlea. V. How the staircase pattern of stereociliary lengths in generated. J. Cell Biol., 106, 355-365, 1988.

 

Tilney L. G., De Rosier D. J. Actin filaments, stereocilia, and hair cells of the bird cochlea. IV. How the actin filaments become organized in developing stereocilia and in the cuticular plate. Dev. Biol., 116, 119-129, 1986.

 

 


 

Албертс Б., Брей Д., Льюис Дж., Рэфф М., Робертс К. Уотсон Дж. Д. Молекулярная биология клетки: В 3-х т. 2-е изд. перераб. и доп. Т. 2.: Пер. с англ. – М.: Мир, 1993. – 539 с.

 




Поделиться с друзьями:


Дата добавления: 2015-08-31; Просмотров: 578; Нарушение авторских прав?; Мы поможем в написании вашей работы!


Нам важно ваше мнение! Был ли полезен опубликованный материал? Да | Нет



studopedia.su - Студопедия (2013 - 2024) год. Все материалы представленные на сайте исключительно с целью ознакомления читателями и не преследуют коммерческих целей или нарушение авторских прав! Последнее добавление




Генерация страницы за: 0.043 сек.