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The Journal of Biological Chemistry|February 25, 1993
Insulin receptor autophosphorylation occurs asymmetricallyJ Lee, T O'Hare, P F Pilch, et al.The Journal of Biological Chemistry|December 29, 1995
Intermolecular phosphorylation between insulin holoreceptors does not stimulate substrate kinase activityJ Lee, S E Shoelson, P F PilchBiochemistry|March 4, 1997
Conformational changes of the insulin receptor upon insulin binding and activation as monitored by fluorescence spectroscopyJ Lee, P F Pilch, S E Shoelson, et al.The International Journal of Biochemistry|January 1, 1990
Intrinsic kinase activity of the insulin receptorT O'Hare, P F PilchThe Journal of Biological Chemistry|January 5, 1989
Intrinsic kinase activity of the insulin receptor. The intact (alpha 2 beta 2) insulin receptor from rat liver contains a kinase domain with greater intrinsic activity than the intact insulin receptor from human placentaT O'Hare, P F PilchBiochemistry|July 26, 1988
Separation and characterization of three insulin receptor species that differ in subunit compositionT O'Hare, P F PilchThe Journal of Biological Chemistry|February 25, 1993
BpaB25 insulins. Photoactivatable analogues that quantitatively cross-link, radiolabel, and activate the insulin receptorS E Shoelson, J Lee, C S Lynch, et al.Biochemistry|August 6, 1991
Autophosphorylation within insulin receptor beta-subunits can occur as an intramolecular processS E Shoelson, M Boni-Schnetzler, P F Pilch, et al.Biochemical and Biophysical Research Communications|April 14, 1986
The ligand binding subunit of the insulin-like growth factor 1 receptor has properties of a peripheral membrane proteinP F Pilch, T O'Hare, J Rubin, et al.The Biochemical Journal|December 1, 1988
Protein phosphotyrosine phosphatase purified from the particulate fraction of human placenta dephosphorylates insulin and growth-factor receptorsJ Roome, T O'Hare, P F Pilch, et al.Pageof 1,969