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. 1969 Sep 1;42(3):613–646. doi: 10.1083/jcb.42.3.613

CURRENT MODELS FOR THE STRUCTURE OF BIOLOGICAL MEMBRANES

Walther Stoeckenius 1, Donald M Engelman 1
PMCID: PMC2107701  PMID: 4895596

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Selected References

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  1. Acheson N. H., Tamm I. Replication of Semliki Forest virus: an electron microscopic study. Virology. 1967 May;32(1):128–143. doi: 10.1016/0042-6822(67)90261-9. [DOI] [PubMed] [Google Scholar]
  2. Adelman W. J., Jr, Senft J. P. Dynamic asymmetries in the squid axon membrane. J Gen Physiol. 1968 May;51(5 Suppl):102S+–102S+. [PubMed] [Google Scholar]
  3. Andreoli T. E., Bangham J. A., Tosteson D. C. The formation and properties of thin lipid membranes from HK and LK sheep red cell lipids. J Gen Physiol. 1967 Jul;50(6):1729–1749. doi: 10.1085/jgp.50.6.1729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Andrews D. M., Haydon D. A. Electron microscope studies of lipid bilayer membranes. J Mol Biol. 1968 Feb 28;32(1):149–150. doi: 10.1016/0022-2836(68)90152-6. [DOI] [PubMed] [Google Scholar]
  5. Ashworth L. A., Green C. Plasma membranes: phospholipid and sterol content. Science. 1966 Jan 14;151(3707):210–211. doi: 10.1126/science.151.3707.210. [DOI] [PubMed] [Google Scholar]
  6. BROWN A. D. THE PERIPHERAL STRUCTURES OF GRAM-NEGATIVE BACTERIA.IV. THE CATION-SENSITIVE DISSOLUTION OF THE CELL MEMBRANE OF THE HALOPHILIC BACTERIUM, HALOBACTERIUM HALOBIUM. Biochim Biophys Acta. 1963 Nov 29;75:425–435. doi: 10.1016/0006-3002(63)90630-9. [DOI] [PubMed] [Google Scholar]
  7. Bancroft J. B., Hills G. J., Markham R. A study of the self-assembly process in a small spherical virus. Formation of organized structures from protein subunits in vitro. Virology. 1967 Feb;31(2):354–379. doi: 10.1016/0042-6822(67)90180-8. [DOI] [PubMed] [Google Scholar]
  8. Bangham A. D., Standish M. M., Miller N. Cation permeability of phospholipid model membranes: effect of narcotics. Nature. 1965 Dec 25;208(5017):1295–1297. doi: 10.1038/2081295a0. [DOI] [PubMed] [Google Scholar]
  9. Bangham A. D., Standish M. M., Watkins J. C. Diffusion of univalent ions across the lamellae of swollen phospholipids. J Mol Biol. 1965 Aug;13(1):238–252. doi: 10.1016/s0022-2836(65)80093-6. [DOI] [PubMed] [Google Scholar]
  10. Bangham A. D., Standish M. M., Weissmann G. The action of steroids and streptolysin S on the permeability of phospholipid structures to cations. J Mol Biol. 1965 Aug;13(1):253–259. doi: 10.1016/s0022-2836(65)80094-8. [DOI] [PubMed] [Google Scholar]
  11. Bar R. S., Deamer D. W., Cornwell D. G. Surface area of human erythrocyte lipids: reinvestigation of experiments on plasma membrane. Science. 1966 Aug 26;153(3739):1010–1012. doi: 10.1126/science.153.3739.1010. [DOI] [PubMed] [Google Scholar]
  12. Bayer M. E. Adsorption of bacteriophages to adhesions between wall and membrane of Escherichia coli. J Virol. 1968 Apr;2(4):346–356. doi: 10.1128/jvi.2.4.346-356.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Bean R. C., Shepherd W. C., Chan H. Permeability of lipid bilayer membranes to organic solutes. J Gen Physiol. 1968 Sep;52(3):495–508. doi: 10.1085/jgp.52.3.495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Benedetti E. L., Emmelot P. Hexagonal array of subunits in tight junctions separated from isolated rat liver plasma membranes. J Cell Biol. 1968 Jul;38(1):15–24. doi: 10.1083/jcb.38.1.15. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Benson A. A. On the orientation of lipids in chloroplast and cell membranes. J Am Oil Chem Soc. 1966 May;43(5):265–270. doi: 10.1007/BF02609671. [DOI] [PubMed] [Google Scholar]
  16. Blasie J. K., Dewey M. M., Blaurock A. E., Worthington C. R. Electron microscope and low-angle x-ray diffraction studies on outer segment membranes from the retina of the frog. J Mol Biol. 1965 Nov;14(1):143–152. doi: 10.1016/s0022-2836(65)80236-4. [DOI] [PubMed] [Google Scholar]
  17. Brandt P. W., Freeman A. R. Plasma membrane: substructural changes correlated with electrical resistance and pinocytosis. Science. 1967 Feb 3;155(3762):582–585. doi: 10.1126/science.155.3762.582. [DOI] [PubMed] [Google Scholar]
  18. Branton D. Fracture faces of frozen membranes. Proc Natl Acad Sci U S A. 1966 May;55(5):1048–1056. doi: 10.1073/pnas.55.5.1048. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Branton D., Park R. B. Subunits in chloroplast lamellae. J Ultrastruct Res. 1967 Aug;19(3):283–303. doi: 10.1016/s0022-5320(67)80222-3. [DOI] [PubMed] [Google Scholar]
  20. Bullivant S., Loewenstein W. R. Structure of coupled and uncoupled cell junctions. J Cell Biol. 1968 Jun;37(3):621–632. doi: 10.1083/jcb.37.3.621. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Burge R. E., Draper J. C. Structure of the cell wall of the Gram-negative bacterium Proteus vulgaris. II. Distribution of electron density across the wall. J Mol Biol. 1967 Sep 14;28(2):189–204. doi: 10.1016/s0022-2836(67)80002-0. [DOI] [PubMed] [Google Scholar]
  22. Burge R. E., Draper J. C. The structure of the cell wall of the Gram-negative bacterium Proteus vulgaris. 3. A lipopolysaccharide "unit membrane". J Mol Biol. 1967 Sep 14;28(2):205–210. doi: 10.1016/s0022-2836(67)80003-2. [DOI] [PubMed] [Google Scholar]
  23. Burge R. E., Draper J. C. The structure of the cell wall of the Gram-negative bacterium Proteus vulgaris. I. An electron microscope and x-ray study. J Mol Biol. 1967 Sep 14;28(2):173–187. doi: 10.1016/s0022-2836(67)80001-9. [DOI] [PubMed] [Google Scholar]
  24. CLEMENTS J. A. Surface phenomena in relation to pulmonary function. Physiologist. 1962 Feb;5:11–28. [PubMed] [Google Scholar]
  25. CRIDDLE R. S., BOCK R. M., GREEN D. E., TISDALE H. Physical characteristics of proteins of the electron transfer system and interpretation of the structure of the mitochondrion. Biochemistry. 1962 Sep;1:827–842. doi: 10.1021/bi00911a015. [DOI] [PubMed] [Google Scholar]
  26. Capek A., Hanc O., Tadra M. Spaltung von 11-substituierten Steroiden durch den Stamm Proactinomyces ruber. Naturwissenschaften. 1967 Feb;54(3):70–70. doi: 10.1007/BF00592759. [DOI] [PubMed] [Google Scholar]
  27. Caspar D. L. Surface lattices and membrane design. Protoplasma. 1967;63(1):197–201. [PubMed] [Google Scholar]
  28. Cass A., Finkelstein A. Water permeability of thin lipid membranes. J Gen Physiol. 1967 Jul;50(6):1765–1784. doi: 10.1085/jgp.50.6.1765. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Chapman D., Kamat V. B., Levene R. J. Infrared spectra and the chain organization of erythrocyte membranes. Science. 1968 Apr 19;160(3825):314–316. doi: 10.1126/science.160.3825.314. [DOI] [PubMed] [Google Scholar]
  30. Chapman D., Kamat V. B., de Gier J., Penkett S. A. Nuclear magnetic resonance studies of erythrocyte membranes. J Mol Biol. 1968 Jan 14;31(1):101–114. doi: 10.1016/0022-2836(68)90058-2. [DOI] [PubMed] [Google Scholar]
  31. Cohen L. B., Keynes R. D., Hille B. Light scattering and birefringence changes during nerve activity. Nature. 1968 May 4;218(5140):438–441. doi: 10.1038/218438a0. [DOI] [PubMed] [Google Scholar]
  32. Criddle R. S., Edwards D. L., Petersen T. G. Chemical studies on the homogeneity of the structural protein from mitochondria. Biochemistry. 1966 Feb;5(2):578–582. doi: 10.1021/bi00866a025. [DOI] [PubMed] [Google Scholar]
  33. Dales S., Mosbach E. H. Vaccinia as a model for membrane biogenesis. Virology. 1968 Aug;35(4):564–583. doi: 10.1016/0042-6822(68)90286-9. [DOI] [PubMed] [Google Scholar]
  34. Dallner G., Siekevitz P., Palade G. E. Biogenesis of endoplasmic reticulum membranes. I. Structural and chemical differentiation in developing rat hepatocyte. J Cell Biol. 1966 Jul;30(1):73–96. doi: 10.1083/jcb.30.1.73. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Dallner G., Siekevitz P., Palade G. E. Biogenesis of endoplasmic reticulum membranes. II. Synthesis of constitutive microsomal enzymes in developing rat hepatocyte. J Cell Biol. 1966 Jul;30(1):97–117. doi: 10.1083/jcb.30.1.97. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Deamer D. W., Branton D. Fracture planes in an ice-bilayer model membrane system. Science. 1967 Nov 3;158(3801):655–657. doi: 10.1126/science.158.3801.655. [DOI] [PubMed] [Google Scholar]
  37. Dermer G. B. Ultrastructural changes in the microvillus plasma membrane during lipid absorption and the form of absorbed lipid: an in vitro study 1t 37 degrees C. J Ultrastruct Res. 1967 Oct 31;20(5):311–320. doi: 10.1016/s0022-5320(67)80101-1. [DOI] [PubMed] [Google Scholar]
  38. Dixon K. E., Mercer E. H. The formation of the cyst wall of the metacercaria of Fasciola hepatica L. Z Zellforsch Mikrosk Anat. 1967;77(3):345–360. doi: 10.1007/BF00339240. [DOI] [PubMed] [Google Scholar]
  39. Ebashi S., Lipmann F. ADENOSINE TRIPHOSPHATE-LINKED CONCENTRATION OF CALCIUM IONS IN A PARTICULATE FRACTION OF RABBIT MUSCLE. J Cell Biol. 1962 Sep 1;14(3):389–400. doi: 10.1083/jcb.14.3.389. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Eisenman G., Ciani S. M., Szabo G. Some theoretically expected and experimentally observed properties of lipid bilayer membranes containing neutral molecular carriers of ions. Fed Proc. 1968 Nov-Dec;27(6):1289–1304. [PubMed] [Google Scholar]
  41. Ellory J. C., Keynes R. D. Binding of tritiated digoxin to human red cell ghosts. Nature. 1969 Feb 22;221(5182):776–776. doi: 10.1038/221776a0. [DOI] [PubMed] [Google Scholar]
  42. Engelman D. M., Morowitz H. J. Characterization of the plasma membrane of Mycoplasma laidlawii. 3. The formation and aggregation of small lipoprotein structures derived from sodium dodecyl sulfate-solubilized membrane components. Biochim Biophys Acta. 1968 Apr 29;150(3):376–384. doi: 10.1016/0005-2736(68)90136-3. [DOI] [PubMed] [Google Scholar]
  43. Engelman D. M., Terry T. M., Morowitz H. J. Characterization of the plasma membrane of Mycoplasma laidlawii. I. Sodium dodecyl sulfate solubilization. Biochim Biophys Acta. 1967 Jul 3;135(3):381–390. doi: 10.1016/0005-2736(67)90028-4. [DOI] [PubMed] [Google Scholar]
  44. FERNANDEZ-MORAN H. Cell-membrane ultrastructure. Low-temperature electron microsopy and x-ray diffraction studies of lipoprotein components in lamellar systems. Circulation. 1962 Nov;26:1039–1065. doi: 10.1161/01.cir.26.5.1039. [DOI] [PubMed] [Google Scholar]
  45. FERNANDEZ-MORAN H., FINEAN J. B. Electron microscope and low-angle x-ray diffraction studies of the nerve myelin sheath. J Biophys Biochem Cytol. 1957 Sep 25;3(5):725–748. doi: 10.1083/jcb.3.5.725. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. FINEAN J. B., BURGE R. E. THE DETERMINATION OF THE FOURIER TRANSFORM OF THE MYELIN LAYER FROM A STUDY OF SWELLING PHENOMENA. J Mol Biol. 1963 Dec;7:672–682. doi: 10.1016/s0022-2836(63)80115-1. [DOI] [PubMed] [Google Scholar]
  47. FLEISCHER S., BRIERLEY G., KLOUWEN H., SLAUTTERBACK D. B. Studies of the electron transfer system. 47. The role of phospholipids in electron transfer. J Biol Chem. 1962 Oct;237:3264–3272. [PubMed] [Google Scholar]
  48. FLEISCHER S., ROUSER G. LIPIDS OF SUBCELLULAR PARTICLES. J Am Oil Chem Soc. 1965 Jul;42:588–607. doi: 10.1007/BF02541295. [DOI] [PubMed] [Google Scholar]
  49. FRASER M. J. Behaviour of proteins at interfaces. J Pharm Pharmacol. 1957 Aug;9(8):497–521. doi: 10.1111/j.2042-7158.1957.tb12304.x. [DOI] [PubMed] [Google Scholar]
  50. Finch J. T., Bancroft J. B. Structure of the reaggregted protein shells of 2 spherical viruses. Nature. 1968 Nov 23;220(5169):815–816. doi: 10.1038/220815a0. [DOI] [PubMed] [Google Scholar]
  51. Finean J. B., Coleman R., Green W. G., Limbrick A. R. Low-angle x-ray diffraction and electron-microscope studies of isolated cell membranes. J Cell Sci. 1966 Sep;1(3):287–296. doi: 10.1242/jcs.1.3.287. [DOI] [PubMed] [Google Scholar]
  52. Finean J. B. The molecular organization of cell membranes. Prog Biophys Mol Biol. 1966;16:143–170. doi: 10.1016/0079-6107(66)90005-8. [DOI] [PubMed] [Google Scholar]
  53. Fleischer S., Zahler W. L., Ozawa H. The extraction of structural protein from submitochondrial vesicles. Biochem Biophys Res Commun. 1968 Sep 30;32(6):1031–1038. doi: 10.1016/0006-291x(68)90133-2. [DOI] [PubMed] [Google Scholar]
  54. Fricke H. THE ELECTRIC CAPACITY OF SUSPENSIONS WITH SPECIAL REFERENCE TO BLOOD. J Gen Physiol. 1925 Nov 20;9(2):137–152. doi: 10.1085/jgp.9.2.137. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. GHOSH S., BULL H. B. Adsorption and enzymic activity of chymotrypsin at an n-octadecane--water interface. Arch Biochem Biophys. 1962 Oct;99:121–125. doi: 10.1016/0003-9861(62)90253-9. [DOI] [PubMed] [Google Scholar]
  56. GLYNN I. M. The action of cardiac glycosides on sodium and potassium movements in human red cells. J Physiol. 1957 Apr 3;136(1):148–173. doi: 10.1113/jphysiol.1957.sp005749. [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. GREEN D. E., LESTER R. L. Role of lipides in the mitochondrial electron transport system. Fed Proc. 1959 Dec;18:987–1000. [PubMed] [Google Scholar]
  58. GREEN D. E., ODA T. On the unit of mitochondrial structure and function. J Biochem. 1961 Jun;49:742–757. doi: 10.1093/oxfordjournals.jbchem.a127366. [DOI] [PubMed] [Google Scholar]
  59. Gorter E., Grendel F. ON BIMOLECULAR LAYERS OF LIPOIDS ON THE CHROMOCYTES OF THE BLOOD. J Exp Med. 1925 Mar 31;41(4):439–443. doi: 10.1084/jem.41.4.439. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Got K., Polya G. M., Polya J. B., Cockerill L. M. Water-insoluble proteins from subfractions of sheep brain microsomes. Biochim Biophys Acta. 1967 May 2;135(2):225–235. doi: 10.1016/0005-2736(67)90117-4. [DOI] [PubMed] [Google Scholar]
  61. Green D. E., Allmann D. W., Bachmann E., Baum H., Kopaczyk K., Korman E. F., Lipton S., MacLennan D. H., McConnell D. G., Perdue J. F. Formation of membranes by repeating units. Arch Biochem Biophys. 1967 Mar;119(1):312–335. doi: 10.1016/0003-9861(67)90461-4. [DOI] [PubMed] [Google Scholar]
  62. Gulik-Krzywicki T., Rivas E., Luzzati V. Structure et polymorphisme des lipides: étude par diffraction des rayons X du systéme formé de lipides de mitochondries de coeur de boeuf et d'eau. J Mol Biol. 1967 Jul 28;27(2):303–322. doi: 10.1016/0022-2836(67)90022-8. [DOI] [PubMed] [Google Scholar]
  63. HASSELBACH W., MAKINOSE M. [The calcium pump of the "relaxing granules" of muscle and its dependence on ATP-splitting]. Biochem Z. 1961;333:518–528. [PubMed] [Google Scholar]
  64. Haldar D., Freeman K., Work T. S. Biogenesis ommitochondria. Nature. 1966 Jul 2;211(5044):9–12. doi: 10.1038/211009a0. [DOI] [PubMed] [Google Scholar]
  65. Hanai T., Haydon D. A., Taylor J. Polar group orientation and the electrical properties of lecithin bimolecular leaflets. J Theor Biol. 1965 Sep;9(2):278–296. doi: 10.1016/0022-5193(65)90113-x. [DOI] [PubMed] [Google Scholar]
  66. Hasselbach W., Elfvin L. G. Structural and chemical asymmetry of the calcium-transporting membranes of the sarcotubular system as revealed by electron microscopy. J Ultrastruct Res. 1967 Mar;17(5):598–622. doi: 10.1016/s0022-5320(67)80143-6. [DOI] [PubMed] [Google Scholar]
  67. Haydon D. A. Properties of lipid bilayers at a water-water interface. J Am Oil Chem Soc. 1968 Apr;45(4):230–240. doi: 10.1007/BF02652418. [DOI] [PubMed] [Google Scholar]
  68. Haydon D. A., Taylor J. The stability and properties of bimolecular lipid leaflets in aqueous solutions. J Theor Biol. 1963 May;4(3):281–296. doi: 10.1016/0022-5193(63)90007-9. [DOI] [PubMed] [Google Scholar]
  69. Henn F. A., Thompson T. E. Properties of lipid bilayer membranes separating two aqueous phases: composition studies. J Mol Biol. 1968 Jan 28;31(2):227–235. doi: 10.1016/0022-2836(68)90441-5. [DOI] [PubMed] [Google Scholar]
  70. Holt S. C., Trüper H. G., Takács B. J. Fine structure of Ectothiorhodospira mobilis strain 8113 thylakoids: chemical fixation and freeze-etching studies. Arch Mikrobiol. 1968;62(2):111–128. doi: 10.1007/BF00410398. [DOI] [PubMed] [Google Scholar]
  71. Hosemann R., Kreutz W. On the tertiary structure of the protein layers of chloroplasts. Naturwissenschaften. 1966 Jun;53(12):298–304. doi: 10.1007/BF00712212. [DOI] [PubMed] [Google Scholar]
  72. Hubbell W. L., McConnell H. M. Spin-label studies of the excitable membranes of nerve and muscle. Proc Natl Acad Sci U S A. 1968 Sep;61(1):12–16. doi: 10.1073/pnas.61.1.12. [DOI] [PMC free article] [PubMed] [Google Scholar]
  73. Inesi G., Asai H. Trypsin digestion of fragmented sarcoplasmic reticulum. Arch Biochem Biophys. 1968 Aug;126(2):469–477. doi: 10.1016/0003-9861(68)90431-1. [DOI] [PubMed] [Google Scholar]
  74. Ji T. H., Urry D. W. Correlation of light scattering and absorption flattening effects with distortions in the circular dichroism patterns of mitochondrial membrane fragments. Biochem Biophys Res Commun. 1969 Feb 21;34(4):404–411. doi: 10.1016/0006-291x(69)90396-9. [DOI] [PubMed] [Google Scholar]
  75. Johnson C. F. Disaccharidase: localization in hamster intestine brush borders. Science. 1967 Mar 31;155(3770):1670–1672. doi: 10.1126/science.155.3770.1670. [DOI] [PubMed] [Google Scholar]
  76. Kagawa Y., Racker E. Partial resolution of the enzymes catalyzing oxidative phosphorylation. X. Correlation of morphology and function in submitochondrial particles. J Biol Chem. 1966 May 25;241(10):2475–2482. [PubMed] [Google Scholar]
  77. Keith A. D., Waggoner A. S., Griffith O. H. Spin-labeled mitochondrial lipids in Neurospora crassa. Proc Natl Acad Sci U S A. 1968 Nov;61(3):819–826. doi: 10.1073/pnas.61.3.819. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. Korn E. D. A chromatographic and spectrophotometric study of the products of the reaction of osmium tetroxide with unsaturated lipids. J Cell Biol. 1967 Aug;34(2):627–638. doi: 10.1083/jcb.34.2.627. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Korn E. D. Structure of biological membranes. Science. 1966 Sep 23;153(3743):1491–1498. doi: 10.1126/science.153.3743.1491. [DOI] [PubMed] [Google Scholar]
  80. Kreutz W. Sub-structure of quantasomes. Nature. 1965 Jun 26;206(991):1358–1359. doi: 10.1038/2061358b0. [DOI] [PubMed] [Google Scholar]
  81. LANGRIDGE R., BARRON P. D., SISTROM W. R. STRUCTURE OF A CHROMATOPHORE FRACTION OF RHODOPSEUDOMONAS SPHEROIDES. Nature. 1964 Oct 3;204:97–98. doi: 10.1038/204097a0. [DOI] [PubMed] [Google Scholar]
  82. LUCY J. A. GLOBULAR LIPID MICELLES AND CELL MEMBRANES. J Theor Biol. 1964 Sep;7:360–373. doi: 10.1016/0022-5193(64)90080-3. [DOI] [PubMed] [Google Scholar]
  83. Landgraf W. C., Inesi G. ATP dependent conformational change in "spin labelled" sarcoplasmic reticulum. Arch Biochem Biophys. 1969 Mar;130(1):111–118. doi: 10.1016/0003-9861(69)90016-2. [DOI] [PubMed] [Google Scholar]
  84. Lenard J., Singer S. J. Protein conformation in cell membrane preparations as studied by optical rotatory dispersion and circular dichroism. Proc Natl Acad Sci U S A. 1966 Dec;56(6):1828–1835. doi: 10.1073/pnas.56.6.1828. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Lenard J., Singer S. J. Structure of membranes: reaction of red blood cell membranes with phospholipase C. Science. 1968 Feb 16;159(3816):738–739. doi: 10.1126/science.159.3816.738-a. [DOI] [PubMed] [Google Scholar]
  86. Lenaz G., Haard N. F., Lauwers A., Allmann D. W., Green D. E. Mitochondrial structural protein I. Methods of preparation and purification: characterization by gel electrophoresis. Arch Biochem Biophys. 1968 Sep 10;126(3):746–772. doi: 10.1016/0003-9861(68)90466-9. [DOI] [PubMed] [Google Scholar]
  87. Lennarz W. J. Lipid metabolism in the bacteria. Adv Lipid Res. 1966;4:175–225. doi: 10.1016/b978-1-4831-9940-5.50012-0. [DOI] [PubMed] [Google Scholar]
  88. Loewenstein W. R. Permeability of membrane junctions. Ann N Y Acad Sci. 1966 Jul 14;137(2):441–472. doi: 10.1111/j.1749-6632.1966.tb50175.x. [DOI] [PubMed] [Google Scholar]
  89. MADDY A. H. A FLUORESCENT LABEL FOR THE OUTER COMPONENTS OF THE PLASMA MEMBRANE. Biochim Biophys Acta. 1964 Sep 25;88:390–399. doi: 10.1016/0926-6577(64)90194-9. [DOI] [PubMed] [Google Scholar]
  90. MARTONOSI A. ROLE OF PHOSPHOLIPIDS IN ATPASE ACTIVITY AND CA TRANSPORT OF FRAGMENTED SARCOPLASMIC RETICULUM. Fed Proc. 1964 Sep-Oct;23:913–921. [PubMed] [Google Scholar]
  91. MOODY M. F. X-RAY DIFFRACTION PATTERN OF NERVE MYELIN: A METHOD FOR DETERMINING THE PHASES. Science. 1963 Nov 29;142(3596):1173–1174. doi: 10.1126/science.142.3596.1173. [DOI] [PubMed] [Google Scholar]
  92. Maddy A. H., Malcolm B. R. Protein conformations in the plasma membrane. Science. 1965 Dec 17;150(3703):1616–1618. doi: 10.1126/science.150.3703.1616. [DOI] [PubMed] [Google Scholar]
  93. Maddy A. H. The chemical organization of the plasma membrane of animal cells. Int Rev Cytol. 1966;20:1–65. doi: 10.1016/s0074-7696(08)60796-2. [DOI] [PubMed] [Google Scholar]
  94. Martonosi A. Sarcoplasmic reticulum. IV. Solubilization of microsomal adenosine triphosphatase. J Biol Chem. 1968 Jan 10;243(1):71–81. [PubMed] [Google Scholar]
  95. Martonosi A. Sarcoplasmic reticulum. V. The structure of sarcoplasmic reticulum membranes. Biochim Biophys Acta. 1968 Jun 11;150(4):694–704. doi: 10.1016/0005-2736(68)90059-x. [DOI] [PubMed] [Google Scholar]
  96. McElhaney R. N., Tourtellotte M. E. Mycoplasma membrane lipids: variations in fatty acid composition. Science. 1969 Apr 25;164(3878):433–434. doi: 10.1126/science.164.3878.433. [DOI] [PubMed] [Google Scholar]
  97. Menke W. The molecular structure of photosynthetic lamellar systems. Brookhaven Symp Biol. 1966;19:328–340. [PubMed] [Google Scholar]
  98. Menke W., Weichan C. Uber die Struktur der Thylakoide von Rhodopseudomonas spheroides. Arch Mikrobiol. 1968;60(1):1–23. [PubMed] [Google Scholar]
  99. Mercer E. H., Dixon K. E. The fine structure of the cystogenic cells of the cercaria of Fasciola hepatica L. Z Zellforsch Mikrosk Anat. 1967;77(3):331–344. doi: 10.1007/BF00339239. [DOI] [PubMed] [Google Scholar]
  100. Mitchell P. Translocations through natural membranes. Adv Enzymol Relat Areas Mol Biol. 1967;29:33–87. doi: 10.1002/9780470122747.ch2. [DOI] [PubMed] [Google Scholar]
  101. Moor H. Use of freeze-etching in the study of biological ultrastructure. Int Rev Exp Pathol. 1966;5:179–216. [PubMed] [Google Scholar]
  102. Moore J. W., Narahashi T., Shaw T. I. An upper limit to the number of sodium channels in nerve membrane? J Physiol. 1967 Jan;188(1):99–105. doi: 10.1113/jphysiol.1967.sp008126. [DOI] [PMC free article] [PubMed] [Google Scholar]
  103. Moudrianakis E. N. Structural and functional aspects of photosynthetic lamellae. Fed Proc. 1968 Sep-Oct;27(5):1180–1185. [PubMed] [Google Scholar]
  104. NILSSON S. E. A GLOBULAR SUBSTRUCTURE OF THE RETINAL RECEPTOR OUTER SEGMENT MEMBRANES AND SOME OTHER CELL MEMBRANES IN THE TADPOLE. Nature. 1964 May 2;202:509–510. doi: 10.1038/202509a0. [DOI] [PubMed] [Google Scholar]
  105. NILSSON S. E. THE ULTRASTRUCTURE OF THE RECEPTOR OUTER SEGMENTS IN THE RETINA OF THE LEOPARD FROG (RANA PIPIENS). J Ultrastruct Res. 1965 Feb;12:207–231. doi: 10.1016/s0022-5320(65)80016-8. [DOI] [PubMed] [Google Scholar]
  106. Napolitano L., Lebaron F., Scaletti J. Preservation of myelin lamellar structure in the absence of lipid. A correlated chemical and morphological study. J Cell Biol. 1967 Sep;34(3):817–826. doi: 10.1083/jcb.34.3.817. [DOI] [PMC free article] [PubMed] [Google Scholar]
  107. Nomura M. Colicins and related bacteriocins. Annu Rev Microbiol. 1967;21:257–284. doi: 10.1146/annurev.mi.21.100167.001353. [DOI] [PubMed] [Google Scholar]
  108. O'BRIEN J. S. STABILITY OF THE MYELIN MEMBRANE. Science. 1965 Mar 5;147(3662):1099–1107. doi: 10.1126/science.147.3662.1099. [DOI] [PubMed] [Google Scholar]
  109. Omura T., Siekevitz P., Palade G. E. Turnover of constituents of the endoplasmic reticulum membranes of rat hepatocytes. J Biol Chem. 1967 May 25;242(10):2389–2396. [PubMed] [Google Scholar]
  110. PAGANELLI C. V., SOLOMON A. K. The rate of exchange of tritiated water across the human red cell membrane. J Gen Physiol. 1957 Nov 20;41(2):259–277. doi: 10.1085/jgp.41.2.259. [DOI] [PMC free article] [PubMed] [Google Scholar]
  111. PARK R. B., PON N. G. Chemical composition and the substructure of lamellae isolated from Spinacea oleracea chloroplasts. J Mol Biol. 1963 Feb;6:105–114. doi: 10.1016/s0022-2836(63)80126-6. [DOI] [PubMed] [Google Scholar]
  112. PARK R. B., PON N. G. Correlation of structure with function in Spinacea oleracea chloroplasts. J Mol Biol. 1961 Feb;3:1–10. doi: 10.1016/s0022-2836(61)80002-8. [DOI] [PubMed] [Google Scholar]
  113. PAULY H., PACKER L., SCHWAN H. P. Electrical properties of mitochondrial membranes. J Biophys Biochem Cytol. 1960 Jul;7:589–601. doi: 10.1083/jcb.7.4.589. [DOI] [PMC free article] [PubMed] [Google Scholar]
  114. PAULY H., PACKER L. The relationship of internal conductance and membrane capacity to mitochondrial volume. J Biophys Biochem Cytol. 1960 Jul;7:603–612. doi: 10.1083/jcb.7.4.603. [DOI] [PMC free article] [PubMed] [Google Scholar]
  115. PFEFFERKORN E. R., CLIFFORD R. L. THE ORIGIN OF THE PROTEIN OF SINDBIS VIRUS. Virology. 1964 Jun;23:217–223. doi: 10.1016/0042-6822(64)90285-5. [DOI] [PubMed] [Google Scholar]
  116. PFEFFERKORN E. R., HUNTER H. S. THE SOURCE OF THE RIBONUCLEIC ACID AND PHOSPHOLIPID OF SINDBIS VIRUS. Virology. 1963 Jul;20:446–456. doi: 10.1016/0042-6822(63)90093-x. [DOI] [PubMed] [Google Scholar]
  117. Papahadjopoulos D., Miller N. Phospholipid model membranes. I. Structural characteristics of hydrated liquid crystals. Biochim Biophys Acta. 1967 Sep 9;135(4):624–638. doi: 10.1016/0005-2736(67)90094-6. [DOI] [PubMed] [Google Scholar]
  118. Papahadjopoulos D., Watkins J. C. Phospholipid model membranes. II. Permeability properties of hydrated liquid crystals. Biochim Biophys Acta. 1967 Sep 9;135(4):639–652. doi: 10.1016/0005-2736(67)90095-8. [DOI] [PubMed] [Google Scholar]
  119. Pardee A. B. Membrane transport proteins. Proteins that appear to be parts of membrane transport systems are being isolated and characterized. Science. 1968 Nov 8;162(3854):632–637. doi: 10.1126/science.162.3854.632. [DOI] [PubMed] [Google Scholar]
  120. Parsegian V. A. Forces between lecithin bimolecular leaflets are due to a disordered surface layer. Science. 1967 May 19;156(3777):939–942. doi: 10.1126/science.156.3777.939. [DOI] [PubMed] [Google Scholar]
  121. RICHARDSON S. H., HULTIN H. O., FLEISCHER S. INTERACTIONS OF MITOCHONDRIAL STRUCTURAL PROTEIN WITH PHOSPHOLIPIDS. Arch Biochem Biophys. 1964 May;105:254–260. doi: 10.1016/0003-9861(64)90006-2. [DOI] [PubMed] [Google Scholar]
  122. Rand R. P., Luzzati V. X-ray diffraction study in water of lipids extracted from human erythrocytes: the position of cholesterol in the lipid lamellae. Biophys J. 1968 Jan;8(1):125–137. doi: 10.1016/S0006-3495(68)86479-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  123. Razin S., Cosenza B. J., Tourtellotte M. E. Variations in Mycoplasma morphology induced by long-chain fatty acids. J Gen Microbiol. 1966 Jan;42(1):139–145. doi: 10.1099/00221287-42-1-139. [DOI] [PubMed] [Google Scholar]
  124. Razin S., Morowitz H. J., Terry T. M. Membrane subunits of Mycoplasma laidlawii and their assembly to membranelike structures. Proc Natl Acad Sci U S A. 1965 Jul;54(1):219–225. doi: 10.1073/pnas.54.1.219. [DOI] [PMC free article] [PubMed] [Google Scholar]
  125. Reiss-Husson F. Structure des phases liquide-cristallines de différents phospholipides, monoglycérides, sphingolipides, anhydres ou en présence d'eau. J Mol Biol. 1967 May 14;25(3):363–382. doi: 10.1016/0022-2836(67)90192-1. [DOI] [PubMed] [Google Scholar]
  126. Robertson J. D. Origin of the unit membrane concept. Protoplasma. 1967;63(1):218–245. [PubMed] [Google Scholar]
  127. Rosenberg S. A., Guidotti G. The protein of human erythrocyte membranes. I. Preparation, solubilization, and partial characterization. J Biol Chem. 1968 Apr 25;243(8):1985–1992. [PubMed] [Google Scholar]
  128. Rosenberg S. A., McIntosh J. R. Erythrocyte membranes: effects on sonication. Biochim Biophys Acta. 1968 Nov 5;163(3):285–289. doi: 10.1016/0005-2736(68)90113-2. [DOI] [PubMed] [Google Scholar]
  129. Rothfield L., Finkelstein A. Membrane biochemistry. Annu Rev Biochem. 1968;37:463–496. doi: 10.1146/annurev.bi.37.070168.002335. [DOI] [PubMed] [Google Scholar]
  130. SCHWAN H. P. Electrical properties of tissue and cell suspensions. Adv Biol Med Phys. 1957;5:147–209. doi: 10.1016/b978-1-4832-3111-2.50008-0. [DOI] [PubMed] [Google Scholar]
  131. STEINMANN E. Contribution to the structure of granular chloroplasts. Experientia. 1952 Aug 15;8(8):300–301. doi: 10.1007/BF02153299. [DOI] [PubMed] [Google Scholar]
  132. STOECKENIUS W. An electron microscope study of myelin figures. J Biophys Biochem Cytol. 1959 May 25;5(3):491–500. doi: 10.1083/jcb.5.3.491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  133. STOECKENIUS W., MAHR S. C. STUDIES ON THE REACTION OF OSMIUM TETROXIDE WITH LIPIDS AND RELATED COMPOUNDS. Lab Invest. 1965 Jun;14:1196–1207. [PubMed] [Google Scholar]
  134. STOECKENIUS W. Some electron microscopical observations on liquid-crystalline phases in lipid-water systems. J Cell Biol. 1962 Feb;12:221–229. doi: 10.1083/jcb.12.2.221. [DOI] [PMC free article] [PubMed] [Google Scholar]
  135. Salton M. R. Isolation and characterization of bacterial membranes. Trans N Y Acad Sci. 1967 Apr;29(6):764–781. doi: 10.1111/j.2164-0947.1967.tb02300.x. [DOI] [PubMed] [Google Scholar]
  136. Salton M. R., Schmitt M. D. Separation of lipids from proteins and cell membranes by disc electrophoresis. Biochem Biophys Res Commun. 1967 Jun 9;27(5):529–534. doi: 10.1016/s0006-291x(67)80019-6. [DOI] [PubMed] [Google Scholar]
  137. Salton M. R. Structure and function of bacterial cell membranes. Annu Rev Microbiol. 1967;21:417–442. doi: 10.1146/annurev.mi.21.100167.002221. [DOI] [PubMed] [Google Scholar]
  138. Schneiderman L. J., Junga I. G. Isolation and partial characterization of structural protein derived from human red cell membranes. Biochemistry. 1968 Jun;7(6):2281–2286. doi: 10.1021/bi00846a034. [DOI] [PubMed] [Google Scholar]
  139. Shemyakin M. M., Ovchinnikov Y. A., Ivanov V. T., Antonov V. K., Shkrob A. M., Mikhaleva I. I., Evstratov A. V., Malenkov G. G. The physicochemical basis of the functioning of biological membranes: conformational specificity of the interaction of cyclodepsipeptides with membranes and of their complexation with alkali metal ions. Biochem Biophys Res Commun. 1967 Dec 29;29(6):834–841. doi: 10.1016/0006-291x(67)90295-1. [DOI] [PubMed] [Google Scholar]
  140. Small D. M. A classification of biologic lipids based upon their interaction in aqeous systems. J Am Oil Chem Soc. 1968 Mar;45(3):108–119. doi: 10.1007/BF02915334. [DOI] [PubMed] [Google Scholar]
  141. Small D. M. Phase equilibria and structure of dry and hydrated egg lecithin. J Lipid Res. 1967 Nov;8(6):551–557. [PubMed] [Google Scholar]
  142. Staehelin L. A. The interpretation of freeze-etched artificial and bilogical membranes. J Ultrastruct Res. 1968 Feb;22(3):326–347. doi: 10.1016/s0022-5320(68)90025-7. [DOI] [PubMed] [Google Scholar]
  143. Steim J. M., Fleischer S. Aggregation-induced red shift of the Cotton effect of mitochondrial structural protein. Proc Natl Acad Sci U S A. 1967 Oct;58(4):1292–1298. doi: 10.1073/pnas.58.4.1292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  144. Stoeckenius W. Electron microscopy of fixed lipids. Protoplasma. 1967;63(1):214–217. [PubMed] [Google Scholar]
  145. Stoeckenius W., Rowen R. A morphological study of Halobacterium halobium and its lysis in media of low salt concentration. J Cell Biol. 1967 Jul;34(1):365–393. doi: 10.1083/jcb.34.1.365. [DOI] [PMC free article] [PubMed] [Google Scholar]
  146. Strauss J. H., Jr, Burge B. W., Darnell J. E. Sindbis virus infection of chick and hamster cells: synthesis of virus-specific proteins. Virology. 1969 Mar;37(3):367–376. doi: 10.1016/0042-6822(69)90220-7. [DOI] [PubMed] [Google Scholar]
  147. Strauss J. H., Jr, Burge B. W., Pfefferkorn E. R., Darnell J. E., Jr Identification of the membrane protein and "core" protein of Sindbis virus. Proc Natl Acad Sci U S A. 1968 Feb;59(2):533–537. doi: 10.1073/pnas.59.2.533. [DOI] [PMC free article] [PubMed] [Google Scholar]
  148. TASAKI I., TAKENAKA T. EFFECTS OF VARIOUS POTASSIUM SALTS AND PROTEASES UPON EXCITABILITY OF INTRACELLULARLY PERFUSED SQUID GIANT AXONS. Proc Natl Acad Sci U S A. 1964 Sep;52:804–810. doi: 10.1073/pnas.52.3.804. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Tien H. T., Diana A. L. Bimolecular lipid membranes: a review and a summary of some recent studies. Chem Phys Lipids. 1968 Feb;2(1):55–101. doi: 10.1016/0009-3084(68)90035-2. [DOI] [PubMed] [Google Scholar]
  150. Toeckenius W., Kunau W. H. Further characterization of particulate fractions from lysed cell envelopes of Halobacterium halobium and isolation of gas vacuole membranes. J Cell Biol. 1968 Aug;38(2):337–357. doi: 10.1083/jcb.38.2.337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  151. Urry D. W., Ji T. H. Distortions in circular dichroism patterns of particulate (or membranous) systems. Arch Biochem Biophys. 1968 Dec;128(3):802–807. doi: 10.1016/0003-9861(68)90088-x. [DOI] [PubMed] [Google Scholar]
  152. Urry D. W., Mednieks M., Bejnarowicz E. Optical rotation of mitochondrial membranes. Proc Natl Acad Sci U S A. 1967 Apr;57(4):1043–1049. doi: 10.1073/pnas.57.4.1043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  153. VANDENHEUVEL F. A. STUDY OF BIOLOGICAL STRUCTURE AT THE MOLECULAR LEVEL WITH STEREOMODEL PROJECTIONS. II. THE STRUCTURE OF MYELIN IN RELATION TO OTHER MEMBRANE SYSTEMS. J Am Oil Chem Soc. 1965 Jun;42:481–492. doi: 10.1007/BF02540089. [DOI] [PubMed] [Google Scholar]
  154. Vandenheuvel F. A. Lipid-protein interactions and cohesional forces in the lipoproteins systems of membranes. J Am Oil Chem Soc. 1966 May;43(5):258–264. doi: 10.1007/BF02609670. [DOI] [PubMed] [Google Scholar]
  155. Wallach D. F., Gordon A. Lipid protein interactions in cellular membranes. Fed Proc. 1968 Nov-Dec;27(6):1263–1268. [PubMed] [Google Scholar]
  156. Wallach D. F., Zahler P. H. Protein conformations in cellular membranes. Proc Natl Acad Sci U S A. 1966 Nov;56(5):1552–1559. doi: 10.1073/pnas.56.5.1552. [DOI] [PMC free article] [PubMed] [Google Scholar]
  157. Wasemiller G., Abrams A., Bakerman S. Fluorescence studies on components of human erythrocyte membrane. Biochem Biophys Res Commun. 1968 Jan 25;30(2):178–184. doi: 10.1016/0006-291x(68)90467-1. [DOI] [PubMed] [Google Scholar]
  158. Woodward D. O. Functional and organizational properties of Neurospora mitochondrial structural protein. Fed Proc. 1968 Sep-Oct;27(5):1167–1173. [PubMed] [Google Scholar]
  159. Worthington C. R., Blaurock A. E. Electron density model for nerve myelin. Nature. 1968 Apr 6;218(5136):87–88. doi: 10.1038/218087a0. [DOI] [PubMed] [Google Scholar]
  160. van Iterson W. Die Feinstruktur der Bakterienzelle. Mikroskopie. 1967 Mar;21(5):107–121. [PubMed] [Google Scholar]

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