Главная страница

Молекулярная биология клетки. Том 1. Молекулярная биология клетки 2Molecular Bruce Alberts, Dennis Bray,Biology


Скачать 25.6 Mb.
НазваниеМолекулярная биология клетки 2Molecular Bruce Alberts, Dennis Bray,Biology
АнкорМолекулярная биология клетки. Том 1.pdf
Дата22.04.2017
Размер25.6 Mb.
Формат файлаpdf
Имя файлаМолекулярная биология клетки. Том 1.pdf
ТипДокументы
#5292
страница64 из 79
1   ...   60   61   62   63   64   65   66   67   ...   79
41, 439-443, 1925.
2. Hawthorne J. N., Ansell G. B. Phospholipids. New Comprehensive Biochemistry, Vol. 4. Amsterdam, Elsevier, 1982.
Storch J., Kleinfeld A. M.
The lipid structure of biological membranes. Trends Biochem. Sci., 10., 418-421, 1982.
3. Bangham A. D. Models of cell membranes. In: Cell Membranes: Biochemistry, Cell Biology and Pathology (G. Weissmann, R. Claiborne eds.), pp. 24-34. New York. Hospital Practice, 1975.
Edidin M.
Rotational and lateral diffusion of membrane proteins and lipids: phenomena and function. Curr. Top. Memb. Transp., 29, 91-127,
1987.
Kornberg R. D., McConnell H. M.
Lateral diffusion of phospholipids in a vesicle membrane. Proc. Natl. Acad. Sci. USA, 68, 2564-2568, 1971.

426
4. Chapman D. Lipid dynamics in cell membranes. In: Cell Membranes: Biochemistry, Cell Biology and Pathology (G. Weissmann, R. Claiborne eds.), pp. 13-22. New York, Hospical Practice, 1975.
Chapman D., Benga G.
Biomembrane fluidity - studies of model and natural membranes. In: Biological Membranes (D. Chapman ed.), Vol. 5, pp. 1-56. London, Academic, 1984.
Kates M., Manson L. A. eds.
Membrane Fluidity. Biomembranes, Vol 12. New York, Plenum, 1984.
Kimelberg H. K.
The influence of membrane fluidity on the activity of membrane-bound enzymes. In: Dynamic Aspects of Cell Surface
Organization. Cell Surface Reviews (G. Poste, G. L. Nicolson eds.), Vol. 3, pp. 205-293. Amsterdam. Elsevier,
5. Carruthers A., Melchior D. I. How bilayer lipids affect membrane protein activity. Trends Biochem. Sci., 11, 331-335, 1986.
de Kruiff B. et al.
Lipid polymorphism and membrane function. In: The Enzymes of Biological Membranes, Vol. 1, Membrane Structure and
Dynamics, 2nd ed. (A.N. Martonosi ed.), pp. 131-204. New York, Plenum, 1985.
Kleinfeld A.
Current views of membrane structure. Curr. Top. Memb. Transp., 29, 1-27, 1987.
6. Bretscher M. Membrane structure: some general principles. Science, 181, 622-629, 1973.
Rothman J., Lenard J.
Membrane asymmetry. Science, 195, 743-753, 1977.
7. Hakomori S. Glycosphingolipids. Sci. Am., 254(5), 44-53, 1986.
Weigandt H.
The gangliosides. Adv. Neurochem., 4, 149-223, 1982.
8. Eisenberg D. Three-dimensional structure of membrane and surface proteins. Anna Rev. Biochem., 53, 595-623, 1984.
Engelman D. M., Steitz T. A., Goldman A.
Identifuing nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev.
Biophys. Biophys. Chem., 15, 321-353, 1986.
Henderson R.
The structure of bacteriorhodopsin and its relevance to other membrane proteins. In: Membrane Transduction Mechanisms (R.
A. Cone, J.E. Dowling eds.), pp. 3-15. New York, Raven, 1979.
Sefton B. M., Buss J. E.
The covalent modification of eukaryotic proteins with lipid. J. Cell Biol, 104, 1449-1453, 1987.
Unwin N., Henderson R.
The structure of proteins in biological membranes. Sci. Am., 250(2), 78-94, 1984.
9. Helenius A., Simons K. Solubilization of membranes by detergents. Biocim. Biophys. Acta, 415, 29-79, 1975.
Montal M.
Functional reconstruction of membrane proteins in planar lipid bilayer membranes. In: Techniques of the Analysis of Membrane
Proteins (C. J. Regan, R.J. Cherry eds.), pp. 97-128. London. Chapman and Hall, 1986.
Racker E.
Reconstruction of Transporters, Receptors and Pathological States. Orlando, Academic, 1985.
10. Bretscher M. Membrane structure: some general principles. Science, 181, 622-629, 1973.
Steck T. L.
The organization of proteins in the human red blood cell membrane. J. Cell Biol., 62, 1-19, 1974.
11. Bennet V. The membrane skeleton of human erythrocytes and its implications for more complex cells. Annu. Rev. Biochem., 54, 273-304, 1985.
Branton D., Cohen C.M., Tyler J.
Interaction of cytoskeletal proteins on the human erythrocyte membrane. Cell, 24, 24-32, 1981.
Byers T. J., Branton D.
Visualization of the protein associations in the erythrocyte membrane skeleton. Proc. Natl. Acad. Sci. USA, 82, 6153-
6157, 1985.
Marchesi V. T.
Stabilizing infrastructure of cell membranes. Annu. Rev. Cell Biol., 1, 531-561, 1985.
Shen B. W., Josephs R., Steck T. L.
Ultrastructure of the intact skeleton of the human erythrocyte membrane. J. Cell Biol., 102, 997-1006, 1986.
12. Marchesi V. Т., Furthmayr H., Tomita M. The red cell membrane. Annu. Rev. Biochem., 45, 667-698, 1976.
13. Jay D., Cantley L. Structural aspects of the red cell anion exchange protein. Annu. Rev. Biochem., 55, 511-538, 1986.
Kopito R. R., Lodish H. F.
Primary structure and transmembrane orientation of the murine anion exchange protein. Nature, 316, 234-238, 1985.
14. Henderson R., Unwin P. N. T. Three-dimensional model of purple membrane obtained by electron microscopy. Nature, 257, 28-32, 1975.
Stoeckenius W., Bogomolni R. A.
Bacteriorhodopsin and related pigments of Halobacteria. Annu. Rev. Biochem., 51, 587-616, 1982.
15. Deisenhofer J., Epp. O., Miki K., Huber R., Michel H. The structure of the protein subunits in the photosynthetic reaction centre of
Rhodopseudomonas viridis
at 3 A resolution. Nature, 318, 618-624, 1985.
16. de Petris S., Rqff M.C. Normal distribution patching and capping of lymphocyte

427
surface immunoglobulin studied by electron microscopy. Nature New Biol., 241, 257-259, 1973.
Edidin M.
Rotational and lateral diffusion of membrane proteins and lipids: phenomena and function. Curr. Top. Memb. Transp., 29, 91-127,
1987.
Frye L. D., Edidin M.
The rapid intermixing of cell surface antigens after formation of mouse-human heterokaryons. J. Cell Sci., 7, 319-335,
1970.
MvCloskey M., Poo M.-M. Protein diffusion in cell membranes: some biological implications. Int. Rev. Cytpl., 87, 19-81, 1984.
Poo M., Cone R.A.
Lateral diffusion of rhodopsin in the photoreceptor membrane. Nature, 247, 438-441, 1974.
Wier M., Edidin M.
Constraint of the translational diffusion of a membrane glycoprotein by its' external domains. Science, 242, 412-414, 1988.
17. Gumbiner В., Louvard D. Localized barriers in the plasma membrane: a common way to form domains. Trends Biochem. Sci., 10, 435-438,
1985.
Myles D. G., Primakoff P.
Sperm surface domains. In: Hybridoma Technology in the Biosciences and Medicine. (T. A. Springer ed.), pp. 239-
250. New York, Plenum, 1985.
Simons K., Fuller S. D.
Cell Surface Polarity in Epithelia. Annu. Rev. Cell Biol., 1, 243-288, 1985.
18. Hirano H., Parkhouse В., Nicolson G.L., Lennox E.S., Singer S.J. Distribution of saccharide residues on membrane fragments from a myeloma- cell homogenate: its implications for membrane biogenesis. Proc. Natl. Acad Sci. USA, 69, 2945-2949,1972.
Kornfeld R., Kornfeld S.
Structure of glycoproteins and their oligosaccharide units. In: The Biochemistry of Glycoproteins and Proteoglycans
(W.J. Lennarz ed.), pp. 1-84. New York, Plenum, 1980.
Lis H., Sharon N.
Lectins as molecules and tools. Annu. Rev. Biochem., 55, 35-67, 1986.
Olden K., Bernard B. A., Humphries M. J., Yeo T.-K., Yeo K.T., White S.L., Newton S. A., Bauer H. C., Parent J. B.
Function of glycoprotein glycans. Trends Biochem. Sci., 10, 78-82, 1985.
19. Hille B. Ionic Channels of Excitable Membranes, Sunderland, MA, Sinauer, 1984.
Martonosi A. N. ed.
The Enzymes of Biological Membranes, Vol. 3, Membrane Transport, 2nd ed. New York, Plenum, 1985.
West I. S.
The Biochemistry of Membrane Transport. London, Chapman and Hall, 1983.
Stein W.D.
Transport and Diffusion Across Cell Membranes Orlando, Academic, 1986.
20. Andersen 0. S. Permeability properties of unmodified lipid bilayer membranes. In: Membrane Transport in Biology. Vol. 1 (G. Giebisch, D. C.
Tosteson, H. H. Ussing eds.), pp. 369-446. New York, Springer-Verlag, 1978.
Finkelstein A.
Water movement through membrane channels. Curr. Top. Memb. Trans., 21, 295-308, 1984.
Walter A., Gutknecht J.
Permeability of small nonelectrolytes through lipid bilayer membranes. J. Membr. Biol., 90, 207-217, 1986.
21. Hobbs A.S., Alberts R. W. The structure of proteins involved in active membrane transport. Annu. Biophys. Bioeng., 9, 259-291, 1980.
Kyte J.
Molecular considerations relevant to the mechanism of active transport. Nature, 292, 201-204, 1981.
Stein W. D. ed.
Ion pumps: Structure, function and regulation. New York, Alan Liss, 1988.
Tanford C.
Mechanism of the energy coupling in active transport. Annu. Rev. Biochem., 52, 379-409, 1983.
Wilson D.B.
Cellular transport mechanisms. Annu. Rev. Biochem., 47, 933-965, 1978.
22. Cantley L. C. Structure and mechanisms of the (Na, K) ATPase. Curr. Topics Bioenerget., 11, 201-237, 1981.
Glynn I. M., Ellory C. eds.
The Sodium Pump. Cambridge, U. K. The Company of Biologists, 1985.
Shull G. E., Schwartz A., Lingrel J. B.
Amino acid sequence of the catalytic subunit of the (Na
+
-K
+
) ATPase deduced from a complementary
DNA. Nature, 316, 691-695, 1985.
23. Swecdner K. J., Goldin S. M. Active transport of sodium and potassium ions: mechanism, function and regulation. N. Engl. J. Med., 302, 777-
783, 1980.
Glynn I.M.
The Na
+
-K
+
transporting adenosine triphosphatase. In: The Enzymes of Biological Membranes, 2nd ed. (A. Martonosi ed.), Vol. 3, pp. 34-114. New York, Plenum, 1985.
24. Hassebach W., Oetliker H. Energetics and electrogenicity of the sarcoplasmic reti :ulum calcium pump. Annu. Rev. Physiol., 45, 325-339,
1983.
MacLennan D. H., Brandl C. J., Korezak В., Green N. M.
Amino acid sequence of a Ca
2+
, Mg
2+
-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature, 316, 696-700, 1985.
Schatzman H.J.
The red cell calcium pump. Annu. Rev. Physiol., 45, 303-312, 1983.

428
25. Hinkle P.C., McCarty R.E. How cell make ATP. Sci. Am., 238(3), 104-123, 1978.
Nicholls D. G.
An Introduction to the Chemiosmotic Theory, 2nd ed. New York, Academic, 1987.
26. Scott D. M. Sodium cotransport systems: cellular, molecular and regulatory aspects. Bioessays, 7, 71-78, 1987.
Wright J. K., Seckler R., Overath P.
Molecular aspects of sugar: ion transport. Annu. Rev. Biochem., 55, 225-248, 1986.
27. Grinstein S., Rotnstein A. Mechanisms of regulation of the Na
+
/H
+
exchanger. J. Membrane Biol., 90, 1-12, 1986.
Olsnes S., Tonnessen T. I., Sandvig K.
pH-regulation anion antiport in nucleated mammalian cells. J. Cell Biol., 102, 967-971, 1986.
Pouyssegur J., Franchi A., Kohno M., L'Allemain G., Paris S.
Na
+
-H
+
exchange and growth control in fibroblasts: a genetic approach. Curr.
Top. Memb. Transp., 26, 201-220, 1986.
Rozengunt E., Mendoza S.
Early stimulation of Na
+
-H
+
antiport, Na
+
-K
+
pump activity and Ca
2+
fluxes in fibroblast mitogenesis. Curr. Top.
Membr. Transp., 27, 163-191, 1986.
28. Aimers W., Stirling C. Distribution of transport proteins over animal cell membranes. J. Membrane Biol. 77, 169-186, 1984.
Semenza G.
Anchoring and biosynthesis of stalked brush border membrane proteins: Glycosidases and peptidases of Enterocytes and renal tubuli. Annu. Rev. Cell Biol., 2, 255-313, 1986.
29. Postma P. W., Longeler J. W. Phosphoenolpyruvate: carbohydrate phosphotransferase system of bacteria. Microbiol. Rev., 49, 232-269, 1985.
30. Ames G. F. L. Bacterial periplasmic transport systems: structure, mechanism and evolution. Annu. Rev. Biochem., 55, 397-425, 1986.
31. Hille B. Ionic Channels of Excitable Membranes, Sunderland, MA, Sinauer, 1984.
32. Baker P. F., Hodgkin A. L., Shaw T. L. The effects of changes in internal ionic concentration on the electrical properties of perfused giant axons.
J. Physiol., 164, 355-374, 1962.
Hodgkin A. L., Keynes R. D.
Active transport of cations in giant axons from Sepia and Loligo. J. Physiol., 128, 26-60, 1955.
Kuffler S.W., Nicholls J. G., Martin A. R.
From Neuron to Brain, pp. 111-125, Sunderland MA, Sinauer, 1984.
33. Hodgkin A. L., Huxley A. F. A quantitative description of membrane current and its application to conduction and excitation in nerve. J.
Physiol., 117, 500-544, 1952. Kuffler S.W., Nicholls J. G., Martin A. R. From Neuron to Brain, pp. 125-152. Sunderland MA, Sinauer, 1984.
34. Catterall W.A. Molecular properties of voltage-sensitive sodium channels. Annu. Rev. Biochem., 55, 953-985, 1986.
Noda M. et al.
Primary structure of Electrophorus electricus sodium channel deduced from cDNA sequence. Nature, 312, 121-127, 1984.
Sigworth F. J., Neher E.
Single Na
+
channel currents observed in cultured rat muscle cells. Nature, 287, 447-449, 1980.
Stevens C.F.
Biophysical studies of ion channels. Science, 225, 1346-1350, 1984.
Tanabe T. et al.
Primary structure of the receptor for calcium channel blockers from skeletal muscle. Nature, 328, 313-318, 1987.
35. Grenningloh G. et al. The strychnine-binding subunit of the glycine receptor shows homology with nicotinic acetylcholine receptors. Nature,
328
, 215-220, 1987.
Guy H. R., Hucho F.
The ion channel of the nicotinic acetylcholine receptor Trends Neurosci., 10, 318-321, 1987.
Hille B.
Ionic Channels of Excitable Membranes, pp. 117-138 and 335-360. Sunderland MA, Sinauer, 1984.
Noda M. et al.
Structural homology of Torpedo californica acetylcholine receptor subunits. Nature, 302, 528-532, 1983.
Schoefield P. R. et al.
Sequence and functional expression of the GABA
A
receptor shows a ligand-gated receptor super family. Nature, 328,
221-227, 1987.
36. Stevens C. F. The neuron. Sci. Am., 241(3), 54-65, 1979.
37. Gomperts B. D. The Plasma Membrane: Models for Its Structure and Function, pp. 109-212. New York, Academic Press, 1976.
Pressman B. C.
Biological applications of ionophores. Annu. Rev. Biocem., 45, 501-530, 1976.
38. Burgess T. L., Kelly R. B. Constitutive and regulated secretion of proteins. Annu. Rev. Cell Biol., 3, 243-294, 1987.
39. Lawson D., Fewtrell C., Raff M. Localized mast cell degranulation induced by cpncanavalin A-sepharose beads: implications for the Ca
2+
hypothesis of simulus-secretion coupling. J. Cell Biol., 79, 394-400, 1978.
40. Steinman R. M., Mellman I. S., Mutter W. A., Cohn Z. Endocytosis and recycling of plasma membrane. J. Cell Biol., 96, 1-27, 1983.
41. Goldstein J.L., Anderson R.G.W., Brown M.S. Coated pits, coated vesicles, and receptor-mediated endocytosis. Nature, 279, 679-685, 1979.

429
Roth Т. F., Porter К. R.
Volk protein uptake in the oocyte of the mosquito, Aedes aegypti. L. J. Cell Biol., 30, 313-332, 1964.
42. Pearse B. M. F., Bretscher M. S. Membrane recycling by coated vesicles. Annu. Rev. Biochem., 50, 85-101, 1981.
Pearse B.M.F., Growther R.A.
Structure and assembly of coated vesicles. Ann. Rev. Biophys. Biophys. Chem., 16, 49-68, 1987.
Schmid S. L., Rothman J. E.
Enzymatic dissociation of clathrin in a two-stage process. J. Biol., 260, 10044-10049, 1985.
43. 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.
Simionescu N., Simionescu M., Palade G.E.
Premeability of muscle capillaries to small heme-peptides: evidence for the existence of patent transendothelial channels. J. Cell Biol., 64, 586-607, 1975.
44. Brown M. S., Goldstein J. L. How LDL receptors influence cholesterol and atherosclerosis. Sci., Am., 251(5), 58-66, 1984.
Brown M. S., Goldstein J. L.
A receptor-mediated pathway for cholesterol homeostasis. Science, 232, 34-48, 1986.
45. Brown W.J., Goodhouse J., Farquhar M,G. Mannose-6-phosphate receptors for lysosomal enzymes cycle between the Golgi complex and endosomes. J. Cell Biol., 103, 1235-1247, 1986.
Griffiths G., Hoflack В., Simons K., Mellman I., Kornfleld S.
The mannose-6-phosphate receptor and the biogenesis of lysosomes. Cell, 52,
329-341, 1988.
Helenius A., Mellman I., Wall D., Hubbard A.
Endosomes. Trends Biochem. Sci., 8, 245-250, 1983.
Mellman L, Howe C., Helenius A.
The control of membrane traffic on the endocytis pathway. Curr. Top. Memb. Transp., 29, 255-288, 1987.
46. Carpenter G. Receptors for epidermal growth factor and other polypeptide mitogens. Annu. Rev. Biochem., 56, 881-914, 1987.
Dautry-Varsat A., Ciechanover A., Lodish H.F.
pH and the recycling of transferrin during receptor-mediated endocytosis. Proc. Natl. Acad.
Sci. USA,
1   ...   60   61   62   63   64   65   66   67   ...   79


написать администратору сайта