Биологический каталог




Биомембраны - Молекулярная структура и функции

Автор Р.Геннис

Protein into Isolated Mitochondria Requires an Energized Inner Membrane, but No Added ATP, The EMBO Journal, 6, 2449—2456.

1515. Verselis V, White R.L., Spray D.C., Bennett M.V.L. (1986). Gap Junctional Conductance and Permeability Are Linearly Related, Science, 234, 461—464.

1516. Vigo C, Grossman S.H., Drost-Hansen W. (1984). Interaction of Dolichol and Dolichol Phosphate with Phospholipid Bilayers, Biochim. Biophys. Acta, 774, 221—226.

1517. Viitanen P.V., Geiger P.J., Erickson-Viitanen S., Bessman S.P. (1984). Evidence for Functional Hexokinase Compartmentation in Rat Skeletal Muscle Mitochondria, J. Biol. Chem., 259, 9679—9686.

1518. Vilsen В., Andersen J.R, Petersen J, Jorgensen PL. (1987). Occlusion of 22Na+ and MRb+ in Membrane-bound and Soluble Protomeric а/3-Units of Na.K-ATPase, J. Biol. Chem., 262, 10 511—10 517.

1519. Vitala J., Jarnefelt J. (1985). The Red Cell Surface Revisited, TIBS, 10, 392—395.

1520. Voelker D.R. (1985). Lipid Assembly into Cell Membranes, Biochemistry of Lipids and Membranes (D.E. Vance and J.E. Vance, Eds.), pp. 475—502, The Benjamin/Cummings Publishing Company, Inc., Menlo Park, California.

1521. Voelker D.R. (1984). Phosphatidylserine Functions as the Major Precursor of Phosphatidylethanolamine in Cultured BHK-21 Cells, Proc. Natl. Acad. Sci. USA, 81, 2669—2673.

1522. VogelH. (1981). Incorporation of Melittin in Phosphatidylcholine Bilayers, FEBS Lett., 134, 37—42.

1523. Vogel H, Jahnig F. (1986). Models for the Structure of Outer-membrane Proteins of Escherichia coli Derived from Raman Spectroscopy and Prediction Methods, J. Mol. Biol., 190, 191—199.

Литература 593

1524. Vogel H, Jahnig F. (1986). The Structure of Melittin in Membranes, Biophys. J., 50, 573—582.

1525. Vogel H, Wright J.K., Jahnig F. (1985). The Structure of the Lactose Permease Derived from Raman Spectroscopy and Prediction Methods, The EMBO Journal, 4, 3625—3631.

1526. VogelH., Gartner W. (1987). The Secondary Structure of Bacteriorhodopsin Determined by Raman and Circular Dichroism Spectroscopy, J. Biol. Chem., 262, 11 464—11 469.

1527. von Heijne G. (1986). Mitochondrial Targeting Sequences May Form Amphiphilic Helices, The EMBO Journal, 5, 1335—1342.

1528. von Heijne G. (1986). Towards a Comparative Anatomy of N-Terminal Topogenic Protein Sequences, J. Mol. Biol., 189, 239—242.

1529. von Heijne G. (1986). The Distribution of Positively Charged Residues in Bacterial Inner Membrane Proteins Correlates with the Transmembrane Topology, The EMBO Journal, 5, 3021—3027.

1530. von Heijne G. (1986). A New Method for Predicting Signal Sequence Cleavage Sites, Nucleic Acids Research, 14, 4683—4690.

1531. von Heijne G., Segrest J.R (1987). The Leader peptides from Bacteriorhodopsin and Halorhodopsin Are Potential Membrane-spaning Amphipathic Helices, FEBS Lett., 213, 238—240.

1532. von Jagow G., Link T.A., Ohnishi T. (1986). Organisation and Function of Cytochrome b and Ubiquinone in the Cristae Membrane of Beef Heart Mitochondria, J. Bioenerg. and Biomemb., 18, 157—179.

1533. Vos-Scheperkeuter G.H., Witholt R (1984). Assembly Pathway of Newly Synthesized LamB Protein, an Outer Membrane Protein of Escherichia coli K-12, J. Mol. Biol., 175, 511—528.

1534. Waggoner A.S. (1979). Dye Indicators of Membrane Potential, Ann. Rev. Biophys. Bioeng., 8, 47—68.

1535. Waldemann T.A. (1986). The Structure, Function, and Expression of Interleukin-2 Receptors on Normal and Malignant Lymphocytes, Science, 232, 727—732.

1536. Walker J.E., CarneA.F, Schmitt H.W. (1979). The Topography of the Purple Membrane, Nature, 278, 653—654.

1537. Wallace RA. (1986). Structure of Gramicidin A, Biophysical Discussion Abstracts, 277—286.

1538. Wallace RA., Teeters C.L. (1987). Differential Absorption Flattening Optical Effects Are Significant in the Circular Dichroism Spectra of Large Membrane Fragments, Biochemistry, 26, 65—70.

1539. Wallace RA., Mao D. (1984). Circular Dichroism Analysis of Membrane Proteins: An Examination of Differential Light Scattering and Absorption Flattening Effects in Large Membrane Vesicles and Membrane Sheets, Anal. Bioch., 142, 317—328.

1540. Wallace RA., Cascio M., Mielke D.L. (1986). Evaluation of Methods for the Prediction of Membrane Protein Secondary Structures, Proc. Natl. Acad. Sci. USA, 83, 9423—9427.

1541. Wallace RA., Kohl N. (1984). The C-Terminus of Bacteriorhodopsin is a Random Coil., Biochim. Biophys. Acta, 777, 93—98.

1542. Wallace RA., Henderson R. (1982). Location of Carboxyl Terminus of Bacteriorhodopsin in Purple Membrane, Biophys. J., 39, 233—239.

1543. Wallach D.F.H., Zahler PH. (1966). Protein Conformations in Cellular Membranes, Proc. Natl. Acad. Sci. USA, 56, 1552—1559.

1544. Wallach D.F.H., Verma SP, Fookson J. (1979). Application of Lasar Raman and Infrared Spectroscoy to the Analysis of Membrane Structure, Biochim. Biophys. Acta, 559, 153—208.

594 Литература

1545. Walsh J.P., Bell RM. (1986). sn-l,2-Diacylglycerol Kinase of Escherichia coli, J. Biol. Chem., 261, 6239—6247.

1546. Walter A., Gutknecht J. (1986). Permeability of Small Nonelectrolytes through Lipid Bilayer Membranes, J. Membrane Biol., 98, 207—217.

1547. Walter P. (1987). Signal Recognition: Two Receptors Act Sequentially, Nature, 328, 763—764.

1548. Walter P., Blobel G. (1982). Signac Recognition Particle Contains a 7S RNA Essential for Protein Translocation across the Endoplasmic Reticulum, Nature, 299, 691—784.

1549. Wang J.-E, Falke J.J., Chan S.I. (1986). A Proton NMR Study of the Mechanism of the Erythrocyte Glucose Transporter, Proc. Natl. Acad. Sci. USA, 83, 3277—3281.

1550. Ward DM., Kaplan J. (1986). Mitogenic Agents Induce Redistribution of Transferrin Receptors from Internal Pools to the Cell Surface, Biochem. J., 231, 721—728.

1551. Warren G.R, Houslay M.D., Metcalfe J.C., Birdsall N.J.M. (1975). Cholesterol Is Excluded from the Phospholipid Annulus Surrounding an Active Calcium Transport Protein, Nature, 255, 684—687.

1552. Warschel A. (1981). Electrostatic Basis of Structure-Function Correlation in Proteins, Acc. Chem. Res., 14, 284—290.

1553. WarshelA., Russell ST., Churg A.K. (1984). Macroscopic Models for Studies of Electrostatic Interactions in Proteins: Limitations and Applicability. Proc Natl. Acad. Sci. USA, 81, 4785—4789.

1554. Wasmann CC., Reiss В., Bartlett S.G., Bohnert H.J. (1986). The Importance of the Transit Peptide and the Transported Protein for Protein Import into Chloroplasls, Mol. Gen. Genet., 205, 446—453.

1555. Waters M.G., Blobel G. (1986). Secretory Protein Translocation in a Yeast Cell-free System Can Occur Posttranslationally and Requires ATP Hydrolysis, J. Cell Biol., 102, 1543—1550.

1556. Waters M.G., Chirico W.J., Blobel G. (1986). Protein TVanslocation across the Yeast Microsomal Membrane Is Stimulated by a Soluble Factor, J. Cell Biol., 103, 2629—2636.

1557. Wattenberg RW, Silbert D.F. (1983). Sterol Partitioning among Intracellular Membranes, J. Biol. Chem., 258, 2284—2289.

1558. Wattenberg RW., Rothman J.E. (1986). Multiple Cytosolic Components Promote Intra-Golgi Protein Transport: Resolution of a Protein Acting at a Late Stage, Prior to Membrane Fusion, J. Biol. Chem., 261, 2208—2213.

1559. Watts Т.Н., Gaub H.E., McConnell H.M. (1986). T-Cell-Mediated Association of Peptide Antigen and Major Histocompatibility Complex Protein Detected by Energy Transfer in a Evanescent Wave-Field, Nature, 320, 179—181.

1560. Waxman S.G, Ritchie JM. (1986). Organization of Ion Channels in the Myelinated Nerve Fiber, Science, 228, 1502—1507.

1561. Weber K., Johnsson N, Plessmann U, Nguyen Van P., Soling H.-D, Ampe C, Van-dekerckhove J. (1987). The Amino Acid Sequence of Protein II and its Phosphorylation Site for Protein Kinase C; the Domain Structure Ca2 * -modulated Lipid Binding Proteins, The EMBO Journal, 6, 1599—1604.

1562. Weckstrom K. (1985). Aqueous Micellar Systems in Membrane Protein Crystallization, FEBS Lett., 192, 220—224.

1563. Weinberg R.A. (1985). The Action of Oncogenes in the Cytoplasm and Nucleus, Science, 230, 770—776.

1564. Weinstein S, Durkin J.T., Veatch W.R., Blout E.R. (1985). Conformation of the Gramicidin A Channel in Phospholipid Vesicles: A Fluorine-19 Nuclear Magnetic Resonance Study, Biochemistry, 24, 4374—4382.

1565. Weis R.M., McConnell H.M. (1984). Two-dimensional Chiral Crystals of Phospholipid, Nature, 310, 47—49.

Литература 595

1566. Weiss H., Wingfield P. (1979). Enzymology of Ubiquinone-Utilising Electron Transfer Complexes in Nonionic Detergent, Eur. J. Bioch., 99, 151—160.

1567. Weissman A.M., Samelson L.E., Klausner R.D. (1986). Л New Subunit of the Human T-Cell Antigen Receptor Compex, Nature, 324, 480—482.

1568. Welsh EJ., Thorn D, Morris E.R., Rees D.A. (1985) Molecular Organization of Glycophorin A: Implications for Membrane Interactions, Biopolymers, 24, 2301—2332.

1569. Weyer KA., Schafer W., Lottspeich F, Michel H. (1987) The Cytochrome Subunit of the Photosynthetic Reaction Center from Rhodopseudomonas viridis Is a Lipoprotein, Biochemistry, 26, 2909—2914.

1570. White DA. (1973). The Phospholipid Composition of Mammalian Tissues. Form and Function of Phospholipids (G.B. Ansdl, J.N. Hawthorn*, and R.MC Dawson, Eds.), 2nd Edition, pp. 441—482, Elsevier Scientific Publication Company, New York.

1571. White J, Kielian M., Helenius A. (1983). Membrane fusion Proteins of Enveloped Animal Viruses, Quarterly Reviews of Biophysics, 16, 151—195.

1572. Whiting P., Lindstrom J. (1987). Affinity Labelling of Neuronal Acetylcholine Receptors Localizes AcetylchoKne-binding Sites to Their 0-Subunits, FEBS Lett., 213, 55—60.

1573. Whitmarsh J. (1986). Mobile Electron Carriers in Thyltcoids, Encyclopedia of Plant Physiology, New Series, Vol. 1», Photosynthesis Ш, 19. 508—527.

1574. Wickner W. (1976). Asymmetric Orientation of Phage M13 Coat Protein in Escherichia coli Cytoplasmic Membranes and in Synthetic Lipid Vesicles, Proc. Natl. Acad. Sci. USA, 73, 1159—1163.

1575. Wickner W. (1979). The Assembly of Proteins into Biological Membranes: The Membrane Trigger Hypothesis, Ann. Rev. Biochem., 48, 23-—45.

1576. Wickner W.T., Lodish H.F. (1985). Multiple Mechanisms of Protein Insertion Into and Across Membranes, Science, 230, 400—407.

1577. Wiech H, Sagstetter M., Muller G., Zimmermann R. (1987). The ATP Requiring Step in Assembly of M13 Procoat Protein into Microsomes Is Related to Preservation of Transport Competence of the Precursor Protein, The EMBO Journal, 6, 1011—1016.

1578. Wiedmann M., Kurzchalia TV, Hartmen E, Rappoport ТА. (1987). A Signal Sequence Receptor in the Endoplasmic Reticulum Membrane, Ntfure, 328, 830—833.

1579. Wiedmann M., Kurzchalia TV, Bielka H, Rappoport ТА. (1987). Direct Probing of the Interaction between the Signal Sequence of Nascent Preprolactin and the Signal Recognition Particle by Specific Cross-linking, J. Cell Biol., 104, 201—208.

1580. WielandET., Gleason M.L., Serafini ТА., Rothman J.E. (1987). The Rate of Bulk Flow from the Endoplasmic Reticulum to the Cell Surface, Cell, 50, 289—300.

1581 Weiner J.R., Pal R., Barenholz Y, WagnerR.R. (1985). Effect of the Vesicular Stomatitis Virus Matrix Protein on the Lateral Organization of Lipid Bilayers Containing Phos-phalidy(glycerol: Use of Fluorescent Phospholipid Analogues, Biochemistry, 24, 7651—7658.

1582. Wieslander A., Rilfors L, Lindblom G. (1986). Metabolic Changes of Membrane Lipid Composition in Acholeplasma laidlawii by Hydrocarbons, Alcohols, and Detergents: Arguments for Effects on Lipid Packing, Biochemistry, 25, 7511—7517.

1583. Wilcox C.A., Olson E.N. (1987). The Majority of Cellular Fatty Acid Acylated Proteins Are Localized to the Cytoplasmic Surface of the Plasma Membrane, Biochemistry, 26, 1029—1036.

1584. Wileman Т., Harding C, Stahl P. (1985). Receptor-mediated Endocytosis, Biochem. )., 232, 1—14.

1585. Wiley D.C, Skehel J.J. (1987). The Structure and Function of the Hemagglutinin Membrane Glucoprotein of Influenza Virus, Ann. Rev. Biochem., 56, 365—394.

1586. Wilkens M.H.F., Blaurock A.E, Engelman DM. (1971). Bilayer Structure in Membranes, Nature New Biology, 230, 72—76.

596 Литература

1587. Wilkinson D.A., Nagle J.E (1979). Dilatometric Study of Binary Mixtures of Phosphatidylcholines, Biochemistry, 18, 4244—4249.

1588. Wilkinson W.O., Walsh J.R, Corless J.M., Bell R.M. (1986). Crystalline Arrays of the Escherichia coli sn-Glycerol-3-phosphate Acyltransferase, an Integral Membrane Protein, J. Biol. Chem., 1986, 9951—9958.

1589. Williams M.A., Lamb R.A. (1986). Determination of the Orientation of an Integral Membrane Protein and Sites of Glycosylation by Oligonucleotide-Directed Mutagenesis: Influenza В Virus NB Glycoprotein Lacks a Cleavable Signal Sequence and Has an Extracellular NH2-Terminal Region, Mol. Cell. Biol., 6, 4317—4328.

1590. Williams R.W. (1983). Estimation of Protein Secondary Structure from the Laser Raman Amide I Spectrum, J. Mol. Biol., 166, 581—603.

1591. Williamson P., Antia R., Schlegel R.A. (1987). Maintenance of Membrane Phospholipid Asymmetry, FEBS Lett., 219, 316—320.

1592. Wills N.K., Zweifach A. (1987). Recent Advances in the Characterization of Epithelal Ionic Channels, Biochim. Biophys. Acta, 906, 1—31.

1593. Wilschut J., Hoekstra D. (1984). Membrane Fusion: From Liposomes to Biological Membranes, TIBS, 9, 479—483.

1594. Wilschut J, Hoekstra D. (1986). Membrane Fusion: Lipid Vesicles as a Model System, Chem. Phys. Lipids, 40, 145—166.

1595. Wilson I.A., Skehel J.J., Wiley DC (1981). Structure of the Haemagglutinin Membrane Glycoprotein of Influenza Virus at 3 A Resolution, Nature, 289, 366—373.

15%. Winiski A.P, McLaughlin AC, McDaniel R.V., Eisenberg M., McLaughlin S. (1986). An Experimental Test of the Discreteness-of-Charge Effect in Positive and Negative Lipid Bilayers, Biochemistry, 25, 8206—8214.

1597. WitzkeN.M., Bittman R. (1984). Dissociation Kinetics and Equilibrium Binding Properties of Polyene Antibiotic Complexes with Phosphatidylcholine/Sterol Vesicles, Biochemistry, 23, 1668—1674.

1598. Wolf DE. (1985). Determination of the Sidedness of Carbocyanine Dye Labeling of Membranes, Biochemistry, 24, 582—586.

1599. Wolf DE, Scott RK, Millette CF. (1986). The Development of Regionalized Lipid Diffusibility in the Germ Cell Plasma Membrane during Spermatogenesis in the Mouse, J. Cell Biol., 103, 1745—1750.

1600. Wolfe PR, Rice M., Wickner W. (1985). Effects of Two sec Genes on Protein Assembly into the Plasma Membrane of Escherichia coli, J. Biol. Chem., 260, 1836—1841.

1601. Wolfe P.B., Wickner W. (1984). Bacterial Leader Peptidase, a Membrane Protein without a Leader Peptide, Uses the Same Export Pathway as Pre-secretory Proteins, Cell, 36, 1067—1072.

1602. Wolfenden R., Andersson L., Cullis P.M., Southgate CCR (1981). Affinities of Amino Acid Side Chains for Solvent Water, Biochemistry, 20, 849—855.

1603. Wolf man A., Macara LG. (1987). Ele

страница 92
< К СПИСКУ КНИГ > 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 66 67 68 69 70 71 72 73 74 75 76 77 78 79 80 81 82 83 84 85 86 87 88 89 90 91 92 93 94 95 96 97

Скачать книгу "Биомембраны - Молекулярная структура и функции" (4.40Mb)


[каталог]  [статьи]  [доска объявлений]  [обратная связь]

п»ї
Химический каталог

Copyright © 2009
(22.05.2022)