Structure and Function of Concanavalin A
作者： George N. Reeke , Joseph W. Becker , Bruce A. Cunningham , John L. Wang , Ichiro Yahara
DOI: 10.1007/978-1-4684-0949-9_2
关键词: Cell surface receptor 、 Chemistry 、 Cytoplasm 、 Concanavalin A 、 Cell biology 、 Receptor 、 Mitosis 、 Cell 、 Peptide sequence 、 Protein structure
摘要: Lectins have been extensively used to analyze a variety of fundamental processes in cell biology. In conjuntion with our studies on the surface and mitosis, we determined amino acid sequence three-dimensional struction concanavalin A (Con A), mitogenic lectin from jack bean. Knowledge structure has helpful interpreting experiments lymphocyte mitogenesis effects Con receptor mobility.
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sci-hub.se 参考文章(52)
K. D. Hardman, M. K. Wood, M. Schiffer, A. B. Edmundson, C. F. Ainsworth, Structure of Concanavalin A at 4.25-Ångström Resolution Proceedings of the National Academy of Sciences of the United States of America. ,vol. 68, pp. 1393- 1397 ,(1971) , 10.1073/PNAS.68.7.1393
J. Z. Rosenblith, T. E. Ukena, H. H. Yin, R. D. Berlin, M. J. Karnovsky, A Comparative Evaluation of the Distribution of Concanavalin A-Binding Sites on the Surfaces of Normal, Virally-Transformed, and Protease-Treated Fibroblasts Proceedings of the National Academy of Sciences of the United States of America. ,vol. 70, pp. 1625- 1629 ,(1973) , 10.1073/PNAS.70.6.1625
BRAD OZANNE, JOE SAMBROOK, Binding of radioactively labelled concanavalin A and wheat germ agglutinin to normal and virus-transformed cells. Nature. ,vol. 232, pp. 156- 160 ,(1971) , 10.1038/NEWBIO232156A0
Ronald D. Poretz, Irwin J. Goldstein, An examination of the topography of the saccharide binding sites of concanavalin A and of the forces involved in complexation. Biochemistry. ,vol. 9, pp. 2890- 2896 ,(1970) , 10.1021/BI00816A021
Bryan J Fuhr, Brian H Barber, Jeremy P Carver, None, Magnetic resonance studies of concanavalin A: location of the binding site of alpha-methyl-D-mannopyranoside. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 73, pp. 322- 326 ,(1976) , 10.1073/PNAS.73.2.322
A. Joseph Kalb, Ariel Lustig, The molecular weight of concanavalin A Biochimica et Biophysica Acta (BBA) - Protein Structure. ,vol. 168, pp. 366- 367 ,(1968) , 10.1016/0005-2795(68)90161-X
ROGER B. TAYLOR, W. PHILIP H. DUFFUS, MARTIN C. RAFF, STEFANELLO de PETRIS, Redistribution and Pinocytosis of Lymphocyte Surface Immunoglobulin Molecules Induced by Anti-Immunoglobulin Antibody Nature. ,vol. 233, pp. 225- 229 ,(1971) , 10.1038/NEWBIO233225A0
Emil R. Unanue, William D. Perkins, Morris J. Karnovsky, Ligand-induced movement of lymphocyte membrane macromolecules. I. Analysis by immunofluorescence and ultrastructural radioautography. Journal of Experimental Medicine. ,vol. 136, pp. 885- 906 ,(1972) , 10.1084/JEM.136.4.885
F. A. Quiocho, G. N. Reeke, J. W. Becker, W. N. Lipscomb, G. M. Edelman, Structure of Concanavalin A at 4 Å Resolution Proceedings of the National Academy of Sciences of the United States of America. ,vol. 68, pp. 1853- 1857 ,(1971) , 10.1073/PNAS.68.8.1853
T. O. Fox, J. R. Sheppard, M. M. Burger, Cyclic membrane changes in animal cells: transformed cells permanently display a surface architecture detected in normal cells only during mitosis. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 68, pp. 244- 247 ,(1971) , 10.1073/PNAS.68.1.244