๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells

โœ Scribed by White, Morris F.; Maron, Ruth; Kahn, C. Ronald


Book ID
109741847
Publisher
Nature Publishing Group
Year
1985
Tongue
English
Weight
485 KB
Volume
318
Category
Article
ISSN
0028-0836

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Insulin-stimulated tyrosine phosphorylat
โœ Ulysses Klee; Toolsee J. Singh ๐Ÿ“‚ Article ๐Ÿ“… 1991 ๐Ÿ› Springer ๐ŸŒ English โš– 649 KB

The insulin receptor (IR) tyrosine kinase is essential for the regulation of different cellular functions by insulin. This may occur by a direct phosphorylation of membrane and/or cytoplasmic proteins by the IR tyrosine kinase. Hence it is important to identify putative physiological substrates for

Stimulation of a Mr 80,000 protein phosp
โœ Masamichi Hirai; Nobuyoshi Shimizu ๐Ÿ“‚ Article ๐Ÿ“… 1989 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 1005 KB

NA and Ca9-22 cells derived from squamous cell carcinomas of the tongue possess a large number of epidermal growth factor (EGF) receptors (2.0 x 10" and 1.3 x l o 6 receptorsicell, respectively). In these cell lines, EGF stimulated receptor autophosphorylation and phosphatidylinositol (PI) turnover.

Identification of tyrosine-phosphorylate
โœ Richard D. Huhn; Mary Elizabeth Cicione; A. Raymond Frackelton Jr. ๐Ÿ“‚ Article ๐Ÿ“… 1989 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 599 KB

Colony-stimulating factor 1 (CSF-1) selectively supports the survival, proliferation, and maturation of hemopoietic cells of the monocytehacrophage lineage. Although the cellular receptor for CSF-1, (the c-fms protein) is a protein-tyrosine kinase activated by the binding of CFS-I, the role of phosp