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September 1, 1988Journal of Biological ChemistryOpen Access

Insulin receptors with defective tyrosine kinase inhibit normal receptor function at the level of substrate phosphorylation.

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Authors

HMHiroshi MaegawaShiga University of Medical Science
Jerrold M. Olefsky
Jerrold M. OlefskyPreventive CardiologySTStephanie ThiesHelmholtz Centre for Infection Research

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Maegawa et al. (1988) studied this question.

synapsesocial.com/papers/6a2102a4064f8ffe09330539https://doi.org/10.1016/s0021-9258(18)37800-1
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin.1987 · 648 citations
  2. 2Metabolism of photoaffinity-labeled insulin receptors by adipocytes. Role of internalization, degradation, and recycling.1984 · 44 citations
  3. 3Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity.1987 · 398 citations
  4. 4Linking functional domains of the human insulin receptor with the bacterial aspartate receptor.1986 · 26 citations