The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Replacement 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.
Open accessAbstract
To test whether the tyrosine kinase activity of the insulin receptor is crucial for insulin action, we have constructed mutations of the human insulin receptor at Lys-1030, which is in the presumed ATP-binding region. By using oligonucleotide-directed mutagenesis, this lysine residue was replaced with either methionine, arginine, or alanine. Chinese hamster ovary cells were transfected by mutant cDNAs and the expressed insulin receptors were characterized. We show here that none of these mutants exhibited insulin-activated autophosphorylation and kinase activity in vitro. They also do not mediate insulin- and antibody-stimulated uptake of 2-deoxyglucose. The tyrosine kinase activity is thus required for a key physiological response of insulin.
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CRC Handbook of Chemistry and Physics
(2014) · doi:10.1201/b17118 · Cited by 57,706
Ellis, L., Clauser, E., Morgan, D. O., Edery, M., Roth, R. A., & Rutter, W. J. (1986) · Cell · doi:10.1016/0092-8674(86)90786-5 · Cited by 1,070
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Cited by
The insulin receptor and the molecular mechanism of insulin action.
Kahn, C. R., & White, M. F. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113711 · Cited by 432
Chiu, S.-L., Chen, C.-M., & Cline, H. T. (2008) · Neuron · doi:10.1016/j.neuron.2008.04.014 · Cited by 425
Ray, L. B., & Sturgill, T. W. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.3753 · Cited by 398
Saad, M. J., Folli, F., Kahn, J. A., & Kahn, C. R. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116803 · Cited by 349
Expression and characterization of a functional human insulin-like growth factor I receptor.
Steele-Perkins, G., Turner, J., Edman, J. C., Hari, J., Pierce, S. B., Stover, C., Rutter, W. J., & Roth, R. A. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37983-3 · Cited by 314
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Metadata
- Authors
- Ebina, Y., Araki, E., Taira, M., Shimada, F., Mori, M., Craik, C. S., Siddle, K., Pierce, S. B., Roth, R. A., & Rutter, W. J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1987-02
- Volume
- 84
- Issue
- 3
- Pages
- 704-708
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2016910304
- Cited by
- 390
- References
- 2
- FWCI
- 21.93
- Type
- journal article
- Language
- en
- Open access
- green
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- Ebina, Y., Araki, E., Taira, M., Shimada, F., Mori, M., Craik, C. S., Siddle, K., Pierce, S. B., Roth, R. A., & Rutter, W. J. (1987). Replacement 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. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.84.3.704
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