Ultrastructure of the intact skeleton of the human erythrocyte membrane
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[1] G. Ralston. The influence of salt on the aggregation state of spectrin from bovine erythrocyte membranes. , 1976, Biochimica et biophysica acta.
[2] D. Branton,et al. Partial purification and characterization of an actin-bundling protein, band 4.9, from human erythrocytes , 1985, The Journal of cell biology.
[3] V. Fowler,et al. Erythrocyte membrane tropomyosin. Purification and properties. , 1984, The Journal of biological chemistry.
[4] G. Ralston,et al. Physico-chemical characterization of the spectrin tetramer from bovine erythrocyte membranes. , 1976, Biochimica et biophysica acta.
[5] E. Ungewickell,et al. Self-association of human spectrin. A thermodynamic and kinetic study. , 1978, European journal of biochemistry.
[6] Vincent T. Marchesi,et al. Erythrocyte spectrin is comprised of many homologous triple helical segments , 1984, Nature.
[7] M. Sheetz. Integral membrane protein interaction with Triton cytoskeletons of erythrocytes. , 1979, Biochimica et biophysica acta.
[8] D. Branton,et al. Interaction of cytoskeletal proteins on the human erythrocyte membrane , 1981, Cell.
[9] D. DeRosier,et al. F-actin is a helix with a random variable twist , 1982, Nature.
[10] T. Steck. THE ORGANIZATION OF PROTEINS IN THE HUMAN RED BLOOD CELL MEMBRANE , 1974, The Journal of cell biology.
[11] S. Brenner,et al. Spectrin/actin complex isolated from sheep erythrocytes accelerates actin polymerization by simple nucleation. Evidence for oligomeric actin in the erythrocyte cytoskeleton. , 1980, The Journal of biological chemistry.
[12] F. Matsumura,et al. Isolation and characterization of tropomyosin-containing microfilaments from cultured cells. , 1983, The Journal of biological chemistry.
[13] M. Nermut. Visualization of the "membrane skeleton" in human erythrocytes by freeze-etching. , 1981, European journal of cell biology.
[14] E. Korn,et al. Actin polymerization and its regulation by proteins from nonmuscle cells. , 1982, Physiological reviews.
[15] C. M. Cohen,et al. Functional characterization of human erythrocyte spectrin alpha and beta chains: association with actin and erythrocyte protein 4.1. , 1984, Biochemistry.
[16] T. Steck,et al. Isolation and characterization of band 3, the predominant polypeptide of the human erythrocyte membrane. , 1975, The Journal of biological chemistry.
[17] D. C. Lin,et al. High affinity binding of [3H]dihydrocytochalasin B to peripheral membrane proteins related to the control of cell shape in the human red cell. , 1978, The Journal of biological chemistry.
[18] W. Gratzer,et al. Interaction of divalent cations with human red cell cytoskeletons. , 1980, Biochimica et biophysica acta.
[19] V. Ohanian,et al. Analysis of the ternary interaction of the red cell membrane skeletal proteins spectrin, actin, and 4.1. , 1984, Biochemistry.
[20] D. Branton,et al. Visualization of the protein associations in the erythrocyte membrane skeleton. , 1985, Proceedings of the National Academy of Sciences of the United States of America.
[21] C. M. Cohen. The molecular organization of the red cell membrane skeleton. , 1983, Seminars in hematology.
[22] R. Johnson,et al. Shape and volume changes in erythrocyte ghosts and spectrin-actin networks , 1980, The Journal of cell biology.
[23] D. Branton,et al. Spectrin-actin associations studied by electron microscopy of shadowed preparations , 1980, Cell.
[24] J. Dunbar,et al. The temperature-dependent dissociation of spectrin. , 1977, Biochimica et biophysica acta.
[25] R. Waugh,et al. Thermoelasticity of red blood cell membrane. , 1979, Biophysical journal.
[26] D. Wallach,et al. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. , 1971, Biochemistry.
[27] Richard A. Anderson,et al. Glycophorin is linked by band 4.1 protein to the human erythrocyte membrane skeleton , 1984, Nature.
[28] S. Goodman,et al. The spectrin membrane skeleton of normal and abnormal human erythrocytes: a review. , 1983, The American journal of physiology.
[29] A. Mikkelsen,et al. Human erythrocyte spectrin dimer intrinsic viscosity: temperature dependence and implications for the molecular basis of the erythrocyte membrane free energy. , 1985, Biochimica et biophysica acta.
[30] T. Steck,et al. Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergents. , 1973, Journal of supramolecular structure.
[31] A. Timme. The ultrastructure of the erythrocyte cytoskeleton at neutral and reduced pH. , 1981, Journal of ultrastructure research.
[32] Shih-Chun Liu,et al. Oligomeric states of spectrin in normal erythrocyte membranes: Biochemical and electron microscopic studies , 1984, Cell.
[33] T. Mueller,et al. Glycoconnectin (PAS 2), a membrane attachment site for the human erythrocyte cytoskeleton. , 1981, Progress in clinical and biological research.
[34] G. Ralston. Physical-chemical studies of spectrin. , 1978, Journal of supramolecular structure.
[35] E. Ungewickell,et al. An examination of the soluble oligomeric complexes extracted from the red cell membrane and their relation to the membrane cytoskeleton. , 1985, European journal of cell biology.
[36] V. Bennett. The membrane skeleton of human erythrocytes and its implications for more complex cells. , 1985, Annual review of biochemistry.
[37] D M Shotton,et al. The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies. , 1979, Journal of molecular biology.
[38] R. Josephs,et al. Ultrastructure of unit fragments of the skeleton of the human erythrocyte membrane , 1984, The Journal of cell biology.
[39] R. Shelton,et al. Quantitation of the major proteins of the human erythrocyte membrane by amino acid analysis. , 1984, Analytical biochemistry.
[40] V. Marchesi,et al. Spectrin: structure, function, and abnormalities. , 1983, Seminars in hematology.
[41] P. Canham. The minimum energy of bending as a possible explanation of the biconcave shape of the human red blood cell. , 1970, Journal of theoretical biology.
[42] H. Ishikawa,et al. Cytoskeletal network underlying the human erythrocyte membrane. Thin- section electron microscopy , 1980, The Journal of cell biology.
[43] R. Josephs,et al. Structural study of spectrin from human erythrocyte membranes. , 1977, Biochemistry.
[44] W. Gratzer,et al. Structural and dynamic states of actin in the erythrocyte , 1983, The Journal of cell biology.
[45] Nermut Mv. Visualization of the "membrane skeleton" in human erythrocytes by freeze-etching. , 1981 .
[46] Shih-Chun Liu,et al. Spectrin tetramer–dimer equilibrium and the stability of erythrocyte membrane skeletons , 1980, Nature.
[47] P. Detmers,et al. Actin in erythrocyte ghosts and its association with spectrin. Evidence for a nonfilamentous form of these two molecules in situ , 1975, The Journal of cell biology.
[48] Y. Lange,et al. Role of the reticulum in the stability and shape of the isolated human erythrocyte membrane , 1982, The Journal of cell biology.
[49] V. Bennett. The Molecular Basis for Membrane – Cytoskeleton Association in Human Erythrocytes , 1982, Journal of cellular biochemistry.