Structure-function analysis of epidermal growth factor: site directed mutagenesis and nuclear magnetic resonance
โ Scribed by T.J. Dudgeon; R.M. Cooke; M. Baron; I.D. Campbell; R.M. Edwards; A. Fallon
- Book ID
- 115923414
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 604 KB
- Volume
- 261
- Category
- Article
- ISSN
- 0014-5793
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
The heparin-binding or fibroblast growth factors (HBGFs) modulate cell growth and migration, angiogenesis, wound repair, neurite extension, and mesoderm induction. Relatively little is known regarding the precise mechanism of action of these growth factors or the structural basis for their action. A
Four residues in the carboxy-terminal domain of human epidermal growth factor (hEGF), glutamate 40, glutamine 43, arginine 45, and aspartate 46 were targeted for site-directed mutagenesis to evaluate their potential role in epidermal growth factor (EGF) receptor-ligand interaction. One or more mutat