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Pilch, P. F., Thompson, P. A., Czech, M. P. (1980) Coordinate modulation of D-glucose transport activity and bilayer fluidity in plasma membranes derived from control and insulin-treated adipocytes. Proceedings of the National Academy of Sciences, 77 (2) 915-918 doi:10.1073/pnas.77.2.915

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Reference TypeJournal (article/letter/editorial)
TitleCoordinate modulation of D-glucose transport activity and bilayer fluidity in plasma membranes derived from control and insulin-treated adipocytes.
JournalProceedings of the National Academy of Sciences
AuthorsPilch, P. F.Author
Thompson, P. A.Author
Czech, M. P.Author
Year1980 (February 1)Volume77
Issue2
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.77.2.915Search in ResearchGate
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Mindat Ref. ID1409595Long-form Identifiermindat:1:5:1409595:7
GUID0
Full ReferencePilch, P. F., Thompson, P. A., Czech, M. P. (1980) Coordinate modulation of D-glucose transport activity and bilayer fluidity in plasma membranes derived from control and insulin-treated adipocytes. Proceedings of the National Academy of Sciences, 77 (2) 915-918 doi:10.1073/pnas.77.2.915
Plain TextPilch, P. F., Thompson, P. A., Czech, M. P. (1980) Coordinate modulation of D-glucose transport activity and bilayer fluidity in plasma membranes derived from control and insulin-treated adipocytes. Proceedings of the National Academy of Sciences, 77 (2) 915-918 doi:10.1073/pnas.77.2.915
In(1980, February) Proceedings of the National Academy of Sciences Vol. 77 (2) Proceedings of the National Academy of Sciences

See Also

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Massague, J., Pilch, P. F., Czech, M. P. (1980) Electrophoretic resolution of three major insulin receptor structures with unique subunit stoichiometries. Proceedings of the National Academy of Sciences, 77 (12) 7137-7141 doi:10.1073/pnas.77.12.7137
Harrison, S. A., Buxton, J. M., Czech, M. P. (1991) Suppressed intrinsic catalytic activity of GLUT1 glucose transporters in insulin-sensitive 3T3-L1 adipocytes. Proceedings of the National Academy of Sciences, 88 (17) 7839-7843 doi:10.1073/pnas.88.17.7839
Kandror, K. V., Pilch, P. F. (1994) gp160, a tissue-specific marker for insulin-activated glucose transport. Proceedings of the National Academy of Sciences, 91 (17) 8017-8021 doi:10.1073/pnas.91.17.8017
Smith, C. J., Rubin, C. S., Rosen, O. M. (1980) Insulin-treated 3T3-L1 adipocytes and cell-free extracts derived from them incorporate 32P into ribosomal protein S6. Proceedings of the National Academy of Sciences, 77 (5) 2641-2645 doi:10.1073/pnas.77.5.2641
Suzuki, K., Kono, T. (1980) Evidence that insulin causes translocation of glucose transport activity to the plasma membrane from an intracellular storage site. Proceedings of the National Academy of Sciences, 77 (5) 2542-2545 doi:10.1073/pnas.77.5.2542
Pilch, Paul F., Czech, Michael P. (1980) HEXOSE TRANSPORT IN ADIPOCYTES: STIMULATION BY INSULIN IN THE ABSENCE OF INTACT RECEPTOR. Annals of the New York Academy of Sciences, 358 (1) 356 doi:10.1111/j.1749-6632.1980.tb15418.x
Virji, M. A., Vassalli, J. D., Estensen, R. D., Reich, E. (1980) Plasminogen activator of islets of Langerhans: modulation by glucose and correlation with insulin production. Proceedings of the National Academy of Sciences, 77 (2) 875-879 doi:10.1073/pnas.77.2.875
Dill, K. A., Flory, P. J. (1980) Interphases of chain molecules: Monolayers and lipid bilayer membranes. Proceedings of the National Academy of Sciences, 77 (6) 3115-3119 doi:10.1073/pnas.77.6.3115
Saltiel, A. R., Cuatrecasas, P. (1986) Insulin stimulates the generation from hepatic plasma membranes of modulators derived from an inositol glycolipid. Proceedings of the National Academy of Sciences, 83 (16) 5793-5797 doi:10.1073/pnas.83.16.5793
Berhanu, P., Olefsky, J. M., Tsai, P., Thamm, P., Saunders, D., Brandenburg, D. (1982) Internalization and molecular processing of insulin receptors in isolated rat adipocytes. Proceedings of the National Academy of Sciences, 79 (13) 4069-4073 doi:10.1073/pnas.79.13.4069
Epstein, D. A., Torrence, P. F., Friedman, R. M. (1980) Double-stranded RNA inhibits a phosphoprotein phosphatase present in interferon-treated cells. Proceedings of the National Academy of Sciences, 77 (1) 107-111 doi:10.1073/pnas.77.1.107
 
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