๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Key Role of Succinate Dehydrogenase in Insulin-Induced Inactivation of Protein Tyrosine Phosphatases

โœ Scribed by I. A. Pomytkin; O. E. Kolesova


Book ID
110393669
Publisher
Springer US
Year
2002
Tongue
English
Weight
371 KB
Volume
133
Category
Article
ISSN
0007-4888

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Approaches to the molecular cloning of p
โœ Barry J. Goldstein; Wei-Ren Zhang; Naotake Hashimoto; C. Ronald Kahn ๐Ÿ“‚ Article ๐Ÿ“… 1992 ๐Ÿ› Springer ๐ŸŒ English โš– 576 KB

The intrinsic tyrosyl kinase activity of the insulin receptor is regulated by a balance between insulin-induced receptor autophosphorylation, which stimulates the receptor kinase, and enzymatic dephosphorylation of the receptor, which deactivates its kinase activity. The cellular protein-tyrosine ph

Cell density-dependent changes in the in
โœ Pei-Ming Li; Barry J. Goldstein ๐Ÿ“‚ Article ๐Ÿ“… 1996 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 789 KB

In order to examine alterations in the phosphorylation state of proteins involved in insulin action that might accompany the reduced growth state of density-arrested cells, we measured the insulin-stimulated phosphorylation of the receptor and high M, cellular substrates of the receptor kinase in ra