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
โฆ LIBER โฆ
Regulation by protein tyrosine phosphorylation of stress responses in the brain
โ 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
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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