Substitution of arginine for histidine at position 209 in the alpha-subunit of the human insulin receptor. A mutation that impairs receptor dimerization and transport of receptors to the cell surface.-Reference-Cited by-同舟云学术

Substitution of arginine for histidine at position 209 in the alpha-subunit of the human insulin receptor. A mutation that impairs receptor dimerization and transport of receptors to the cell surface.

Published:1991-11 Issue:31 Volume:266 Page:21224-21231
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Kadowaki T.,Kadowaki H.,Accili D.,Yazaki Y.,Taylor S.I.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference43 articles.

1. A mutation in the insulin receptor gene that impairs transport of the receptor to the plasma membrane and causes insulin-resistant diabetes.

2. A mutation in the extracellular domain of the insulin receptor impairs the ability of insulin to stimulate receptor autophosphorylation.

3. Tyrosine phosphorylation of the insulin receptor is not required for receptor internalization: studies in 2,4-dinitrophenol-treated cells.

4. On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors

5. The neu oncogene encodes an epidermal growth factor receptor-related protein

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