๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Src Homology 2 Domains of Protein Tyrosine Phosphatase Are Phosphorylated by Insulin Receptor Kinase and Bind to the COOH-Terminus of Insulin Receptors in Vitro

โœ Scribed by H. Maegawa; S. Ugi; O. Ishibashi; R. Tachikawaide; N. Takahara; Y. Tanaka; Y. Takagi; R. Kikkawa; Y. Shigeta; A. Kashiwagi


Book ID
115573189
Publisher
Elsevier Science
Year
1993
Tongue
English
Weight
379 KB
Volume
194
Category
Article
ISSN
0006-291X

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Ligation of the T cell antigen receptor
โœ Hiroko Kanda; Toshihide Mimura; Noritsugu Morino; Ken Hamasaki; Tetsuya Nakamoto ๐Ÿ“‚ Article ๐Ÿ“… 1997 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 728 KB

p105CasL (CasL) is a recently identified signaling molecule closely related to the p130Cas (Crk-associated substrate) docking protein. CasL has a single Src homology (SH) 3 domain in its N-terminal portion followed by multiple consensus motifs for binding to SH2 domains. Like original p130Cas, CasL