Substitution of glutamic acid for alanine 1135 in the putative “catalytic loop” of the tyrosine kinase domain of the human insulin receptor. A mutation that impairs proteolytic processing into subunits and inhibits receptor tyrosine kinase activity.-Reference-Cited by-同舟云学术

Substitution of glutamic acid for alanine 1135 in the putative “catalytic loop” of the tyrosine kinase domain of the human insulin receptor. A mutation that impairs proteolytic processing into subunits and inhibits receptor tyrosine kinase activity.

Published:1993-04 Issue:11 Volume:268 Page:8060-8069
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cama A.,de la Luz Sierra M.,Quon M.J.,Ottini L.,Gorden P.,Taylor S.I.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference54 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. Immunoglobulin heavy chain-binding protein binds to misfolded mutant insulin receptors with mutations in the extracellular domain.

4. Insulin Resistance, Acanthosis Nigricans, and Normal Insulin Receptors in a Young Woman: Evidence for a Postreceptor Defect

5. Characterization of insulin receptors in patients with the syndromes of insulin resistance and acanthosis nigricans

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