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Burgess Т. L., Kelly R. В. Constitutive and regulated secretion of proteins. Annu. Rev. Cell. Biol., 3, 243-293, 1987.

 

Dingwall C., Laskey R. A. Protein import into the cell nucleus. Annu. Rev. Cell Biol., 2, 367-390, 1986.

 

Kornfeld S. Trafficking of lysosomal enzymes. FASEB J., 1, 462-468, 1987.

 

Pfeffer S. R., Rothman J. E. Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu. Rev. Biochem., 56, 829-852, 1987.

 

Verner K., Schatz G. Protein translocation across membranes. Science, 241, 1307-1313, 1988.

 

1. Bolender R. P. Stereological analysis of the guinea pig pancreas. J. Cell Biol., 61, 269 287. 1974.

 

Palade J. E., Farquhar M. G. Cell biology. In: Pathophysiology: The Biological Principles of Disease (L. H. Smith, S. D. Thier, eds.), pp. 1-56.

 

Philadelphia, Saunders, 1981.

 

Weibel E. R., Staubli W., GnagiH.R., Hess F. A. Correlated morphometric and biochemical studies on the liver cell. J. Cell Biol., 42, 68 91, 1969.

 

2. Blobel G. Intracellular protein topogenesis. Proc. Nail. Acad. Sci. USA, 77, 1496-1500, 1980.

 

Grav M. W., Doolinle W. F. Has the endosymbiont hypothesis been proven? Microbiol. Rev., 46, 1-42, 1982.

 

Schwarz R. M., Davhoff M. 0. Origins of the prokaryotes, eukaryotes, mitochondria, and chloroplasts. Science, 199, 395-403, 1978.

 

3. Palade G. Intracellular aspects of the process of protein synthesis. Science, 189, 347-358, 1975.

 

4. Kelly R. B. Pathways of protein secretion in eukaryotes. Science, 230, 25-31, 1985.

 

Sabatini D. D., Kreibich G., Morimoto Т., Adesnik M. Mechanisms for the incorporation of proteins in the membranes and organelles. J. Cell Biol., 92, 1 -22, 1982.

 

5. Pfeffer S. R., Rothman J. E. Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu. Rev. Biochem., 56, 829

852, 1987.

 

Wickner W. Т., LodishH.E. Multiple mechanisms of protein insertion into and across membranes. Science, 230, 400-406, 1985.

 

 


 

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.

 

6. Blobel G. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA, 77, 1496-1500, 1980.

 

Garoff H. Using recombinant DNA techniques to study protein targeting in the eukaryotic cell. Annu. Rev. Cell Biol., 1, 403-445, 1985.

 

7. Warren G. Membrane traffic and organelle division. Trends Biochem. Sci., 10, 439-443, 1985.

 

8. Alien R.D. The microtubule as an intracellular engine. Sci. Am., 238(2), 42-49, 1987.

 

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

 

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

 

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

 

9. Chock P. В., Rhee S. G., Stadtman E. R. Interconvertible enzyme cascades in cellular regulation. Annu. Rev. Biochem., 49, 813-843, 1980.

 

Holt G. D. et a/. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J. Cell Biol., 104, 1157-

1164, 1987.

 

Wold F. In vivo chemical modification of proteins (post-translational modification). Annu. Rev. Biochem., 50, 783-814, 1981.

 

10. Kamps M.P., Buss J.E., Sefton B.M. Mutation of NH2-terminal glycine of p60srс prevents both myristoylation and morphological transformation.

 

Proc. Ntl. Acad. Sci. USA, 82, 4625-4628, 1985.

 

Schutltz A. M., Henderson L. E., Orozlan S. Fatty acylation of proteins. Annu. Rev. Cell Biol., 4, 611-648, 1988.

 

Willumsen B. M., Harris K., Papayeorye A. G., Hubbert N. L., Lowy D. R. Harvey murine sarcoma virus p21ras protein: biological and biochemical significance of the cysteine nearest the carboxy terminus. EM BO J., 3, 2582-2585, 1984.

 

11. Dice J. F. Molecular determinants of protein half-lives in eukaryotic cells. FASEB J., 1, 349-357, 1987.

 

Goldbera A.L., GoffS.A. The selective degradation of abnormal proteins in bacteria. In: Maximizing Gene Expression (W. Reznikoff, L. Gold, eds.), pp. 287-314. Stoneham, MA, Butterworth, 1986.

 

12. Bachmair A., Finley D., Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Science, 234, 179 186, 1986.

 

Hershko A., Ciechanover A. The ubiquitin pathway for the degradation of intranuclear proteins. Prog. Nucleic Acid Res. Мо.. Biol., 33, 19-56, 1986.

 

Rechsteiner M. Ubiquitin-mediated pathways for intracellular proteolysis. Annu. Rev. Cell Biol., 3, 1 30, 1987.

 

13. Auyen J., Wold F. How much sequence information is needed for the regulation of amino-terminal acetylation of eukaryotic proteins? Trends Biochem. Sci,, 11, 494-497, 1986.

 

Ferber S., Ciechanover A. Role of arginine-tRNA in protein degradation by the ubiquitin pathway. Nature, 326, 808-811, 1987.

 

Varshavsky A., Bachmair A., Finlev D., Gonda D., Wunniny I. The N-end rule of selective protein turnover: mechanistic aspects and functional implications. In: Ubiquitin (M. Rechsteiner, ed.), pp. 284 324. New York, Plenum, 1988.

 

14. Craiy E.A. The heat-shock response. CRC Crit. Rev. Biochem., 18, 239-280, 1985.

 

Lindquist S. The heat-shock response. Annu. Rev. Biochem., 55, 1151-1191, 1986.

 

Pelham H. R. B. Speculations on the functions of the major hat shock and glucose-regulated proteins. Cell, 46, 959-961, 1986.

 

15. Franke W.W., Scheer U.. Krohne G., Jarash E.D. The nuclear envelope and the architecture of the nuclear periphery. J. Cell Biol., 91, 39s 50s, 1981.

 

Newport J. W., Forbes D.J. The nucleus: structure, function, and dynamics. Annu. Rev. Biochem., 56, 535 565, 1987.

 

16. Banner W.M. Protein migration and accumulation in nuclei. In: The Cell Nucleus (H. Busch, ed.), Vol. 6, Part C, pp. 97-148. New York, Academic, 1978.

 

Lang L, Schol: M., Peters R. Molecular mobility and nucleocytoplasmic flux in hepatoma cells. J. Cell Biol., 102, 1183-1190, 1986.

 

17. Dingwall C., Laskey R.A. Protein import into the cell nucleus. Annu. Rev. Cell Biol., 2, 367-390, 1986.

 

Feldherr C. M., Kallenbach E., Schult: N. Movement of a karyophilic protein through the nuclear pores of oocytes. J. Cell Bol., 99, 2216-2222, 1984.

 

Newmeyer D.D., Forbes D.J. Nuclear import can be separated into distinct steps in vitro: nuclear pore binding and translocation. Cell, 52, 641-

653, 1988.

 

18. Goldfarb D.S., Gariepy J., Schoolnik G., Kornbery R.D. Synthetic peptides as nuclear localization signals. Nature, 322, 641-644, 1986.

 

Kalderon D., Roberts B. L., Richardson W. D., Smith A. E. A short amino acid sequence able to specify nuclear location. Cell, 39, 499-509, 1984.

 

Lanford R. E., Bute/ J. S. Construction and characherization of an SV40 mutant defective in nuclear transport of Т antigen. Cell, 37, 801-813, 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.

 

19. Clawson G.A., Feldherr C.M., Smuckler E. A. Nucleocytoplasmic RNA transport. Мо.. Cell. Biochem., 67, 87-100, 1985.

 

Dworetzky S. I., Feldherr С. М. Translocation of RNA-coated gold particles through the nuclear pores of oocytes. J. Cell Biol., 106, 575 584, 1988.

 

20. Attardi G., Schatz G. Biogenesis of mitochondria. Annu. Rev. Cell Biol., 4, 289-333, 1988.

 

Tzayoloff A. Mitochondria. New York, Plenum, 1982.

 

21. Hawlitschek G. et al. Mitochondrial protein import: identification of processing peptidase and of PEP, a procesing enchancing protein. Cell, 53, 795-806, 1988.

 

Hurt E.G., van Loon A.P.G.M. How proteins fnd mitochondria and intramitochondrial compartments. Trends Biochem. Sci. 11, 204-207, 1986.

 

Pfanner N.. Neupert W. Biogenesis of mitochondrial energy transducing complexes. Curr. Top. Bioenerg., 15, 177-219, 1987.

 

Raise D., Schatz G. Mitochondrial presequences. J. Biol. Chem., 263, 4509-4511, 1988.

 

22. Eilers M., Schatz G. Protein unfolding and the energetics of protein translocation across biological membranes. Cell, 52, 481-483, 1988.

 

Pfanner N.. Neupert W. Transport of proteins into mitochondria: a potassium diffusion potential is able to drive the import of ADP/ATP carrier.

 

EM BO J., 4, 2819-2825, 1985.

 

Raise D., Horvath S.J., Tomich J.M., Richards J.H., Schatz G. A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers. EM BO J., 5. 1327 1334. 1986.

 

23. Schleyer M., Neupert W. Transport of proteins into mitochondria: translocational intermediates spanning contact sites between outer and inner membranes. Cell, 43, 339-350, 1985.

 

Schwaiger M., Herzog V., Neupert W. Characterization of translocation contact sites involved in the import of mitochondrial proteins. J. Cell Biol., 105, 235-246, 1987.

 

24. Deshaies R. J., Koch B. D., Werner-Washburne M., Craig E. A., Schekman R. A subfamily of stress proteins facilitates translocation of secretory and mitochonrial precursor polypeptides. Nature, 332, 800-805, 1988.

 

Eilers M., Schatz G. Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria, Nature, 322, 228-232, 1986.

 

Pfanner N.. Tropschug M., Neupert W. Mitochondrial protein import: nucleoside triphosphates are involved in conferring import competence to precursors. Cell, 49, 815-823, 1987.

 

25. Hartl F. U., Ostermann J., Guiard В., Neupert W. Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptids. Cell, 51, 1027-1037, 1987.

 

van Loon A. P. G. M., Brandli A. W., Schatz G. The presequences of two imported mitochondrial proteins contain information for intracellular and intramitochon-drial sorting. Cell, 44, 801-812, 1986.

 

26. Pfaller R., Neupert W. High-affinity binding sites involved in the import of porin into mitochondria. EMBO J., 6, 2635 2642, 1987.

 

Pfanner N. et al. Role of ATP in mitochondrial protein import. J. Biol. Chem., 263, 4049-4051, 1988.

 

27. Boutry M., Nagy F., Polsen G., Aoyagi K., Chua N. H. Targeting of bacterial chloramphenicol acetyltranferase to mitochondria in transgenic plants. Nature, 328, 340 342, 1987.

 

Pain D., Kanwar Y.S., Blobel G. Identification of a receptor for protein import into chloroplasts and its localization to envelope contact zones.

 

Nature, 331, 232-237, 1988.

 

Schmidt G. W., Mishkind M. L. The transport of proteins into chloroplasts. Annu. Rev. Biochem. 55, 879-912, 1986.

 

Smeekens S., Bauerie C., Hageman J., Keegstra K., Weisbeek P. The role of the transit peptide in the routing of precursors toward different chloroplast compartments. Cell 46, 365 375, 1986.

 

28. de Duve C. Microbodies in the living cell. Sci. Am., 248(5), 74 84, 1983.

 

de Duve C.. Baudhuin P. Peroxisomes (microbodies and related particles). Physiol. Rev. 46, 323-357, 1966.

 

Fahimi H. D., Sies H., eds. Peroxisomes in Biology and Medicine. Heidelberg, Springer, 1987.

 

29. Tolbert N. E.. Essner E. Microbodies: peroxisomes and glyoxysomes. J. Cell Biol., 91, 271s-283s, 1981.

 

Veenbuis M., Van Dijken J. P., Harder W. The significance of peroxisomes in the metabolism of one-carbon compounds in yeasts. Adv.

 

Microb. Physiol., 24, 1 -82, 1983.

 

30. Could S. J., KellerG.A., Subramani S. Identification of a peroxisomal targeting


 

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.

 

signal at the carboxy terminus of four peroxisomal proteins. J. Cell Biol., 107, 897-905, 1988.

 

Imanaka Т., Small G. M., Lazarow P. B. Translocation of acyl-CoA oxidase into peroxisomes requires ATP hydrolysis but not a membrane potential. J. Cell Biol., 105, 2915-2922, 1987.

 

Lazarow P. В., Fujiki Y. Biogenesis of peroxisomes. Annu. Rev. Cell Biol., 1, 489-530, 1985.

 

31. DePierre J. W., Dallner G. Structural aspects of the membrane of the endoplasmicreticulum. Biochim. Biophys. Acta, 415, 411-472, 1975.

 

Fawcett D. The Cell, 2nd ed., pp. 303-352. Philadelphia, Saunders, 1981.

 

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

 

32. Adelman M. R.. Sabatini D. D., Blobel G. Ribosome-membrane interaction: nondestructive disassembly of rat liver rough microsomes into ribosomal and membranous components. J. Cell Biol., 56, 206-229, 1973.

 

Blobel G., Dohberstein B. Transfer of proteins across membranes. J. Cell Biol., 67, 852-862, 1975.

 

33. Jones A. L., Fawcett D. W. Hypertrophy of the agranular endoplasmic reticulum in hamster liver induced by phenobarbital. J. Histochem.

 

Cytochem., 14, 215-232, 1966.

 

Mori H., Christensen A. K. Morphometric analysis of Leydig cells in the normal rat testis. J. Cell Biol., 84, 340-354, 1980.

 

34. Dallner G. Isolation of rough and smooth microsomes - general. Methods Enzymol., 31, 191-201, 1974.

 

de Duve C. Tissue fractionation past and present. J. Cell Biol., 50, 20d 55d, 1971.

 

35. Hortsch M., Avossa D., Meyer D.I. Characterization of secretory protein transloca-tion: ribosome-membrane interaction in endoplasmic reticulum. J. Cell Biol., 103, 241-253, 1986.

 

Kreibich G., Ulrick B. L., Sabatini D. D. Proteins of rough microsomal membranes related to ribosome binding. J. Cell Biol., 77, 464 487, 1978.

 

36. Blobel G., Dobberstein B. Transfer of proteins across membranes. J. Cell Biol., 67, 835-851, 1975.

 

Garoff H. Using recombinant DNA techniques to study protein targeting in the eucaryotic cell. Annu. Rev. Cell Biol., 1, 403-445, 1985.

 

Milstein C., Brownlee G., Harrison Т., Mathews M. B. A possible precursor of immunoglobulin light chains. Nature New Biol., 239, 117-120, 1972. van Heijne G. Signal sequences: the limits of variation. J. Мо.. Biol., 184, 99-105, 1985.

 

37. Meyer D. L, Krause E., Dobberstein B. Secretory protein translocation across membranes-the role of the "docking protein". Nature, 297, 647-

650, 1982.

 

Tajima S., Lauffer L., Rath V.L.. Walter P. The signal recognition particle receptor is a complex that contains two distinct polypeptide chains. J.

 

Cell Biol., 103, 1167-1178, 1986.

 

Walter P., Blobel G. Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum.

 

Nature, 299, 691-698, 1982.

 

Walter P., Lingappa V. R. Mechanism of protein translocation across the endoplasmic reticulum membrane. Annu. Rev. Cell Biol., 2, 499-516, 1986.

 

Wiedmann M., Kurzchalia T. V., Hartmann E., Rapoport T. A. A signal sequence receptor in the endoplasmic reticulum membrane. Nature, 328, 830- 833, 1987.

 

38. Chirico W.J., Waters M. G., Blobel G. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature, 332, 805-810, 1988.

 

Perara E., Rothman R. E., Lingappa, V. R. Uncoupling translocation from translation: implications for transport of proteins across membranes.

 

Science, 232, 348-352, 1986.

 

Zimmermann R., Meyer D.I. 1986 A year of new insights into how proteins cross membranes. Trends Biochem. Sci., 11, 512-515, 1986.

 

39. Rapoport T. A. Extensions of the signal hypothesis sequential insertion model versus amphipatic tunnel hypothesis. FEES Lett., 187, 1-10, 1985.

 

Wickner W.T., Lodish H.F. Multiple mechanisms of protein insertion into and across membranes. Science, 230, 400-406, 1985.

 

40. Engelman D. M., Steitz T. A.. Goldman A. Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev.

 

Biophys. Biophys. Chem., 15, 321-353, 1986.

 

Kaiser C. A., Preuss D., Grisafl P., Botstein D. Many random sequences functionally replace the secretion signal sequence of yeast invertase.

 

Science, 235, 312-317, 1987.

 

Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J. Мо.. Biol., 157, 105-132, 1982.

 

Zerial M., Huylebroeck D., Garoff H. Foreign transmembrane peptides replacing the


 

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.

 

internal signal sequence of transferrin receptor allow its translocation and membrane binding. Cell, 48, 147 155, 1987.

 

41. Bole D. G., Hendershof L.M., KearnyJ.F. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecrcting and secreting hybridomas. J. Cell Bol., 102, 1558 1566, 1986.

 

Lodish H. F. Transport of secretory and membrane glycoproteins from the rough endoplasmic reticulum to the Golgi. J. Biol. Chem., 263, 2107-2110, 1988.

 

Мито S., Pelham H. R. B. A C-terminal signal prevents secretion of luminal ER proteins. Cell, 48, 899 907, 1987.

 

42. Freedman R. Native disulphide bond formation in protein biosynthesis: evidence for the role of protein disulphide isomerase. Trends Biochem., Sci., 9, 438-441, 1984.

 

Holmgren A. Thioredoxin. Annu. Rev. Biochem., 54, 237-272, 1985.

 

43. Hirschberg С. В.. Snider M. D. Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus. Annu. Rev. Biochem., 56, 63-87, 1987.

 

Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem., 54, 631 664, 1985.

 

Torres C., Hart G. Topography and polypeptide distribution of terminal N-acetyl-glucosamine residues on the suface on intact lymphocytes. J.

 

Biol. Chem., 259, 3308-3317, 1984.

 

44 Cross G. A. M. Eukaryotic protein modification and membrane attachment via phosphatidylinositol. Cell, 48, 179-181, 1987.

 

Ferguson M. A.J., Williams A. F. Cell-surface anchoring of proteins via glycosil-phosphatidylinositol structures. Annu. Rev. Biochem., 57, 285-320, 1988.

 

Loif M. G., Sa/tiel A. R. Structural and functional roles of glycosil-phosphatidylino-sitol in membranes. Science, 239, 268-275, 1988.

 

45. Bishop W. R., Bell R. M. Assembly of phospholipids into cellular membranes: biosynthesis, transmembrane movement, and intracellular translocation. Annu. Rev. Cell Biol., 4, 579-610, 1988.

 

Bishop W. R., Bell R. M. Assembly of the endoplasmic reticulum phospholipid bilayer: the phosphatidylcholine transporter. Cell, 42, 51-60, 1985.

 

Dawidowic: E. A. Dynamics of membrane lipid metabolism and turnover. Annu. Rev. Biochem., 56, 43-61, 1987.

 

Pagano R. E., Sleight R. G. Defining lipid transport pathways in animal cells. Science, 229, 1051 1057, 1985.

 

Rothman J.E., Lenard J. Membrane asymmetry. Science, 195, 743-753, 1977.

 

46. Dawidowic: E. A. Lipid exchange: transmembrane movement, spontaneous movement, and protein-mediated transfer of lipids and cholesterol.

 

Curr. Top. Memb. Transp., 29, 175-202, 1987.

 

Yaffe M. P.. Kennedy E. P. Intracellular phospholipid movement and the role of phospholipid transfer proteins in animal cells. Biochemistry, 22, 1497-1507, 1983.

 

47. Farqulmr M.G., PaladeG.E. The Golgi apparatus (complex)-(1954 1981)-from artifact to center stage. J. Cell. Biol., 91, 77s-103s, 1981.

 

Pavelka M. Functional morphology of the Golgi apparatus. Adv. Anat. EmbryolCell Biol, 106, 1-94, 1987.

 

Rothman J. E. The compartmental organization of the Golgi apparatus Sci Am 253(3), 74-89, 1985.

 

48. Hubbard S. C, Ivatt R. J. Synthesis and processing of asparagine-linked oligosaccharides. Annu. Rev. Biochem., 50, 555-583, 1981.

 

Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu Rev. Biochem., 54, 631 664, 1985.

 

Schachter H., Roseman S. Mammalian glycosyltransferases: their role in the synthesis and function of complex carbohydrates and glicolipids.

 

In: The Biochemistry of Glycoproteins and Proteoglycanes (W.J. Lennarz, ed.), Chapter 3 New York Plenum, 1980. '

49. Elbein A. D. Inhibitors of the biosynthesis and processing of N-linked oligosacchande chains. Annu. Rev. Biochem., 56, 497-534, 1987.

 

Stanley P. Glycosylation mutants and the functions of mammalian carbohydrates Trends Genet., 3, 77-81, 1987.

 

West C. M. Current ideas on the significance of protein glycosylation. Мо. Cell Biochem., 72, 3-20, 1986.

 

50. Hassel J. R.. Kimura J. H., Hascal V. C. Proteoglycan core protein families Annu Rev. Biochem., 55, 539-567, 1986.

 

Huttner W. B. Tyrosine sulfation and the secretory pathway. Annu. Rev. Physiol., 50, 363 - 376, 1998.

Ruoslahti F. Structure and biology of proteoglycans. Annu. Rev. Cell Biol., 4, 229- -255, 1988.

 

Wagh P. V., Bahl O. P. Sugar residues on proteins. CRC Crit. Rev. Biochem., 10, 307-377, 1981, 51. Douglass J., Civelli O., Herbert E. Polyprotein gene expression: generation of diversity of neuroendocrine peptides. Annu. Rev. Biochem., 53, 665-715,


 

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.

 

Orel L. et al. Conversion of proinsulin to insulin occurs coordinately with acidication of maturing secretory vesicles. J. Cell Biol., 103, 2273-

2281, 1986.

 

52. Dunphy W. G., Rothman J. E. Compartmental organization of the Golgi stack. Cell, 42, 13-21, 1985.

 

53. Bainton D. The discovery of lysosomes. J. Cell Biol., 91, 66s- 76s, 1981.

 

de Duve C. Exploring cells with a centrifuge. Science, 189, 186 194, 1975.

 

54. Holzman E. Lysosomes: A Survey. New York, Springer-Verlag, 1976.

 

55. Griffiths G., Holfack В., Simons K., Mellman /., Kornfeld S. The mannose 6-phosphate receptor and the biogenesis of lysosomes. Cell, 52, 329

341, 1988.

 

Helenius A., Mellman /., Wall D., Hubbard A. Endosomes. Trends Biochem. Sci., 8, 245-250, 1983.

 

Mayer R.J., Dohertv F. Intracellular protein catabolism: state of the art. FEBS Lett., 198, 181-193, 1986.

 

Mellman I., Fuchs R., Helenius A. Acidification of the endocytic and exocytic pathways. Annu. Rev. Biochem., 55, 663-700, 1986.

 

Silverstein S.C., Steinman R.M., Cohn Z.A. Endocytosis. AnhurRev. Biochem., 46, 669-722, 1977.

 

56. Dahms N. M., Label P., Breitmeyer J., Chirgwin J. M., Kornfeld S. 46 kd mannose 6-phosphate receptor: cloning, expression, and homology to the 215 kd mannose 6-phosphate receptor. Cell, 50, 181 192, 1987.

 

Kornfeld S. Trafficking of lysosomal enzymes. FASEB J., 1, 462-468, 1987.

 

Pfeffer S. R. Mannose 6-phosphate receptors and their role in targeting of proteins to lysosomes. J. Membr. Biol., 103, 7-16, 1988.

 

van Fiqura K., Hasilik A. Lysosomal enzymes and their receptors. Annu. Rev. Biochem., 55, 167-193, 1986.

 

57. Brown W.J., Goodhouse J.; Farquhar. M.G. Mannose 6-phosphate receptors for lysosomal enzymes cycle between the Golgi coplex and endosomes. J. Cell Biol., 103, 1235-1247, 1986.

 

Duncan J. R., Kornfeld S. Intracellular movement of two mannose 6-phosphate receptors: return to the Golgi apparatus. J. Cell Biol., 106, 617-

628, 1988.

 

Geuze H.J.. Slot J. W., Strous G.J.A.M., Hasilik A., van Figura K. Possible pathways for lysosomal enzyme delivery. J. Cell Biol., 101, 2253-

2262, 1985.

 

Rothman J. E., Schmid S. L. Enzymatic recycling of clathrin from coated vesicles. Cell, 46, 5-9, 1986.

 

58. Lane/ L., Reitman M., Tang J., Roberts R. M., Kornfeld S. Lysosomal enzyme phosphorylation. J. Biol. Chem., 259, 14663-14671, 1984.

 

Reitman M. L., Kornfeld S. Lysosomal enzyme targeting. N-acetylglucosaminyl-phosphotransferase selectively phosphorylates native lysosomal enzymes. J. Biol. Chem., 256, 11977 11980, 1981.

 

59. Kornfeld S. Trafficking of lysosomal enzymes in normal and disease states. J. Clin. Invest., 77, 1-6, 1986.

 

Neufeld E. F., Lim T. W., Shapiro L. J. Inherited disorders of lysosomal metabolism. Annu. Rev. Biochem. 44, 357 376, 1975.

 

60. Burgess T. L., Kelly R. B. Constitutive and regulated secretion of proteins. Annu. Rev. Cell Biol., 3, 243-293, 1987.

 

61. Griffiths G., Simons K. The trans-Golgi network: sorting at the exit site of the Golgi complex. Science, 234, 438-443, 1986.

 

Orci L. et a/. The trans-most cisternae of the Golgi complex: a compartment for sorting of secretory and plasma membrane proteins. Cell, 51, 1039-1051, 1987.

 

62. Herzoy V'., Farquhar M. G. Luminal membrane retrieved after exocytosis reaches most Golgi cisternae in secretory cells. Proc. Natl. Acad. Sci.

 

USA, 74, 5073-5077, 1977.

 

Snider M. D.. Rogers О. С. Membrane traffic in animal cells: cellular glycoproteins return to the site of Golgi mannosidase I. J. Cell Biol., 103, 265-275, 1986.

 

63. Lodish H. F. Transport of secretory and membrane glycoproteins from the rough endoplasmic reticulum to the Golgi. J. Biol. Chem., 263, 2107-

2110, 1988.

 

Rothman J. E. Protein sorting by selective retention in the endoplasmic reticulum and Golgi stack. Cell, 50, 521-522, 1987.

 

Wieland F. Т., Gleason M. L., Serafini T. A., Rothman J. E. The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell, 50, 289-300, 1987.

 

64. Bartles J. R.. Hubbard A. L. Plasma membrane protein sorting in epithelial cells: do secretory pathways hold the key? Trends Biochem. Sci., 13, 181 184, 1988.

 

Matlin K. S. The sorting of proteins to the plasma membrane in epithelial cells. J. Cell Biol., 103, 2565 2568, 1986.

 

Mostov K. E., Breitfeld P., Harris J. M. An anchor-minus form of the polymeric immunoglobulin receptor is secreted predominantly apically in Madin-Darby canine kidney cells. J. Cell Biol., 105, 2031-2036, 1987.

 

Simons K., Fuller S. D. Cell surface polarity in epithelia. Annu. Rev. Cell Biol., 1, 243-288, 1985.

 

 


 

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.

 

65. Simons К., Garoff Н., Helenius A. How an animal virus gets into and out of its.host cell. Sci. Am., 246(2), 58-66, 1982.

 

Simons K., Warren G. Semliki forest virus: a probe for membrane traffic in the animal cell. Adv. Protein Chem., 36, 79-132, 1984.

 

66. Rodriguez-Boulan F. J. Membrane biogenesis, enveloped RNA viruses, and epithelial polarity. In: Modern Cell Biology. Vol. 1 (J. R. Mcintosh, В. Н. Satir, eds.), pp. 119 170, 1983.

 

Rodriguez-Boulan E. J., Sabatini D. D. Asymmetric budding of viruses in epithelial monolayers: a model system for the study of epithelial polarity. Proc. Natl. Acad. Sci. USA, 75, 5071-5075, 1978.

 

Roth M. G., Sirnivas R. V., Compans R. W. Basolateral maturation of retroviruses in polarized epithelial cells. J. Virol., 45, 1065-1073, 1983.

 

Strauss E. G., Strauss J. H. Assembly of enveloped animal viruses. In: Virus Structure and Assembly (S. Casjens, ed.), Chapter 6. Boston, Jones and Bartlett, 1985.

 

67. Rothman J. E. Protein sorting by selective retention in the endoplasmic reticulum and Golgi stack. Cell, 50, 521-522, 1987.

 

68. Griffiths G., Pfeiffer S., Simons K., Mat/in K. Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane. J. Cell Biol., 101, 949-964, 1985.

 

Orci L., Click B. S., Rothman J. E. A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack. Cell, 46, 171-184, 1986.

 

69. Bourne H. Do GTPases direct membrane traffic in secretion? Cell, 53, 669-671, 1988.

 

Novick P., Field C., Schekman R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell, 21, 205-215, 1980.

 

Scheckman R. Protein localization and membrane traffic in yeast. Annu. Rev. Cell Biol., 1, 115-143, 1985.

 

70. Batch W. E., Dunphy W. G., Braell W. A., Rothman J. E. Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine. Cell, 39, 405-416, 1984.

 

Dunphy W. G. et al. Yeast and mamals utilize similar cytosolic components to drive protein transport through the Golgi complex. Proc. Natl.

 

Acad. Sci. USA, 83, 1622-1626, 1986.

 

Fries E., Rothman J. E. Transport of vesicular stomatitis virus glycoprotein in a cell-free extract. Proc. Natl. Acad. Sci. USA, 77, 3870-3874, 1980.

 

 


 

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.

 




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