A family of polypeptide substrates and inhibitors of insulin receptor kinase
Meyerovitch, Kahn, and Shechter. 1990. “A Family of Polypeptide Substrates and Inhibitors of Insulin Receptor Kinase”. Biochemistry 29 (15): 3654-60.
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Alterations in the hepatic insulin receptor kinase in genetic and acquired obesity in rats
Hurrell, Pedersen, and Kahn. 1989. “Alterations in the Hepatic Insulin Receptor Kinase in Genetic and Acquired Obesity in Rats”. Endocrinology 125 (5): 2454-62.
Hepatic phosphotyrosine phosphatase activity and its alterations in diabetic rats
Meyerovitch, Backer, and Kahn. 1989. “Hepatic Phosphotyrosine Phosphatase Activity and Its Alterations in Diabetic Rats”. J Clin Invest 84 (3): 976-83.
Molecular defects in insulin action
Kahn, and Goldstein. 1989. “Molecular Defects in Insulin Action”. Science 245 (4913): 13.
Conformational changes in the alpha- and beta-subunits of the insulin receptor identified by anti-peptide antibodies
Perlman, Bottaro, White, and Kahn. 1989. “Conformational Changes in the Alpha- and Beta-Subunits of the Insulin Receptor Identified by Anti-Peptide Antibodies”. J Biol Chem 264 (15): 8946-50.
Tyrosine phosphorylation of the insulin receptor during insulin-stimulated internalization in rat hepatoma cells
Backer, Kahn, and White. 1989. “Tyrosine Phosphorylation of the Insulin Receptor During Insulin-Stimulated Internalization in Rat Hepatoma Cells”. J Biol Chem 264 (3): 1694-701.
Insulin and epidermal growth factor stimulate phosphorylation of a 170-kDa protein in intact hepatocytes immunologically related to lipocortin 1
Karasik, Pepinsky, and Kahn. 1988. “Insulin and Epidermal Growth Factor Stimulate Phosphorylation of a 170-KDa Protein in Intact Hepatocytes Immunologically Related to Lipocortin 1”. J Biol Chem 263 (34): 18558-62.
The insulin receptor gene and its expression in insulin-resistant mice
Ludwig, Müller-Wieland, Goldstein, and Kahn. 1988. “The Insulin Receptor Gene and Its Expression in Insulin-Resistant Mice”. Endocrinology 123 (1): 594-600.
Tryptic activation of the insulin receptor. Proteolytic truncation of the alpha-subunit releases the beta-subunit from inhibitory control
Shoelson, White, and Kahn. 1988. “Tryptic Activation of the Insulin Receptor. Proteolytic Truncation of the Alpha-Subunit Releases the Beta-Subunit from Inhibitory Control”. J Biol Chem 263 (10): 4852-60.
Phorbol ester-induced serine phosphorylation of the insulin receptor decreases its tyrosine kinase activity
Takayama, White, and Kahn. 1988. “Phorbol Ester-Induced Serine Phosphorylation of the Insulin Receptor Decreases Its Tyrosine Kinase Activity”. J Biol Chem 263 (7): 3440-7.