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
Protein tyrosine phosphorylation in normal rat tissues
โ Scribed by Lise Tremblay; Richard Beliveau
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 627 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0020-711X
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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