๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Regulation by protein tyrosine phosphorylation of stress responses in the brain

โœ Scribed by Hiroshi Ohnishi; Shinya Kusakari; Takaaki Murata; Toshi Maruyama; Yuriko Hayashi; Keizo Takao; Tsuyoshi Miyakawa; Yukio Ago; Ken Koda; Toshio Matsuda; Katsuya Okawa; Yasuyuki Saito; Yoji Murata; Takashi Matozaki


Book ID
116777273
Publisher
Elsevier Science
Year
2010
Tongue
English
Weight
60 KB
Volume
68
Category
Article
ISSN
0168-0102

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Developmental regulation of protein tyro
โœ M. Aubry; Dr. P. F. Maness ๐Ÿ“‚ Article ๐Ÿ“… 1988 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 805 KB

Proteins phosphorylated at tyrosine residues in the developing rat brain have been identified with a focus on the nerve growth cone and synaptic terminal. Endogenous protein phosphorylation in membranes from a subcellular growth cone fraction of fetal rat brain revealed prominent 55-60 kD phosphotyr

Role of protein tyrosine phosphorylation
โœ P. A. Maher ๐Ÿ“‚ Article ๐Ÿ“… 1989 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 953 KB

The role of protein tyrosine phosphorylation in the response of PC12 cells to NGF was investigated by using a variety of agents which affect NGF-induced neurite outgrowth. K-252a, a kinase inhibitor, was previously found to selectively inhibit many of the actions of NGF on PC12 cells. In the present