Interaction between the extracellular matrix protein tenascin-R and the neuronal adhesion molecule F3 might be involved in the formation of neuronal networks. In this study, the fragment of tenascin-R comprising epithelial growth factor (EGF)-like repeats and the cysteine-rich NH2 terminal stretch (
✦ LIBER ✦
Characterization of TonB Interactions with the FepA Cork Domain and FecA N-terminal Signaling Domain
✍ Scribed by R. Sean Peacock; Valery V. Andrushchenko; A. Ross Demcoe; Matt Gehmlich; Lily Sia Lu; Alicia Garcia Herrero; Hans J. Vogel
- Publisher
- Springer Netherlands
- Year
- 2006
- Tongue
- English
- Weight
- 578 KB
- Volume
- 19
- Category
- Article
- ISSN
- 1572-8773
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## Abstract Thrombospondin‐1 (TSP‐1) is an extracellular matrix protein that modulates focal adhesion in mammalian cells and exhibits dual roles in angiogenesis. In a previous work, we showed that a recombinant 18 kDa protein encompassing the N‐terminal residues 1‐174 of human TSP‐1 (TSP18) induced
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