References
- Roth J., Kahn C. R., Lesniak M. A., Gordon P., DeMeyts P., Megyesi K., Neville D. M., Jr., Gavin J. R., III, Soll A. H., Freychet P., Goldfine I. D., Bar R. S., Archer J. A. Receptors for insulin, NSILA-s, and growth hormone: application to disease states in man. Rec. Prog. Horm. Res. 1976; 31: 95–139
- Gammeltoft S. Insulin receptors: Binding kinetics and structurefunction relationship of insulin. Physiol. Revs. 1984; 64: 1321–1375
- Olefsky J. M., Chang H. Insulin binding to adipocytes. Evidence for functionally distinct receptors. Diabetes. 1978; 27: 946–958
- Olefsky J. M., Kobayashi M., Chang H. Interactions between insulin and its receptors after the initial binding event. Functional heterogeneity and relationships to insulin degradation. Diabetes. 1979; 28: 460–471
- Kono T., Barham F. W. The relationship between the insulinbinding capacity of fat cells and the cellular response to insulin. Studies with intact and trypsin-treated fat cells. J. Biol. Chem. 1971; 246: 6210–6216
- Boeynaems J. M., Dumont J. E. Quantitative analysis of the binding of ligands to their receptors. J. Cyc. Nucl. Res. 1975; 1: 123–142
- Mikulecky D. C., Thomas S. R. Some network thermodynamic models of coupled, dynamic physiological systems. J. Franklin Institute. 1979; 308: 309–325
- White J. C., Mikulecky D. C. Application of network thermodynamics to the computer modeling of the pharmacology of anticancer agents: A network model for methrotrexate action as a comprehensive example. Pharmacol. Ther. 1982; 15: 251–291
- May J. M., Mikulecky D. C. Glucose utilization in rat adipocytes. The interaction of transport and metabolism as affected by insulin. J. Biol. Chem. 1983; 258: 4771–4777
- Cuatrecasas P. Insulin-receptor interactions in adipose tissue cells: direct measurement and properties. Proc. Natl. Acad. Sci. USA 1971; 68: 1264–1268
- Gammeltoft S., Gliemann J. Binding and degradation of 125I-labelled insulin by isolated rat fat cells. Biochim. Biophys. Acta. 1973; 320: 16–32
- Delisi C. The effect of cell size and receptor density on ligand-receptor reaction rate constants. Molec. Immunol. 1981; 18: 507–511
- Lipkin E. W., Teller D. C., de Haën C. Equilibrium binding of insulin to white fat cells at 15°C. J. Biol. Chem. 1986; 261: 1694–1701
- Lipkin E. W., Teller D. C., de Haën C. Kinetics of insulin binding to white fat cells at 15°C. J. Biol. Chem. 1986; 261: 1702–1711
- Donner D. B., Corin R. E. Formation of a receptor state from which insulin dissociates slowly in hepatic cells and plasma membranes. J. Biol. Chem. 1980; 255: 9005–9008
- Hammond J. M., Jarett L., Mariz I. K., Daughaday W. H. Heterogeneity of insulin receptors of fat cell membranes. Biochem. Biophys. Res. Commun. 1972; 49: 1122–1128
- Jacobs S., Cuatrecasas P. The mobile receptor hypothesis and “cooperativity” of hormone binding, Application to insulin. Biochim. Biophys. Acta. 1976; 433: 482–495
- Boeynaems J. M., Dumont J. E. The two-step model of ligand receptor interaction. Molec. Cell. Endocrinol. 1977; 7: 33–47
- DeMeyts P., Roth J., Neville D. M., Jr., Gavin J. R., III, Lesniak M. A. Insulin interactions with its receptors: experimental evidence for negative cooperativity. Biochem. Biophys. Res. Commun. 1973; 55: 154–161
- Beck J. S., Goren H. J. Simulation of association curves and “Scatchard” plots of binding reactions where ligand and receptor are degraded or internalized. J. Recep. Res. 1984; 3: 745–772
- Ketelslegers J.-M., Pirens G., Maghuin-Rogister G., Hennen G., Frere J.-M. The choice of erroneous models of hormonereceptor interactions: a consequence of illegitimate utilization of Scatchard plots. Biochem. Pharmacol. 1984; 33: 707–710
- Mangnall D., Quayle A. R., Clark R. G. A simple computer model for insulin-receptor interactions and insulin dependent glucose uptake by adipocytes. Int. J. Bio-Medical Computing. 1984; 15: 327–339
- Kasuga M., Karisson F. A., Kahn C. R. Insulin stimulates the phosphorylation of the 95,000 dalton subunit of its own receptor. Science 1982; 215: 185–187
- Rosen O. M., Herrera R., Olowe Y., Petruzzelli L. M., Cobb M. H. Phosphorylation activates the insulin receptor tyrosine protein kinase. Proc. Natl. Acad. Sci., USA 1983; 80: 3237–3240
- Kwok Y. C., Nemenoff R. A., Powers A. C., Avruch J. Kinetic properties of the insulin receptor tyrosine protein kinase: Activation through an insulin-stimulated tyrosine-specific, intramolecular autophosphorylation. Arch Biochem. Biophys. 1986; 244: 102–113