By Lisette Leyton Ph.D., James S. Hagood M.D. (auth.), Vladimir Berezin, Peter S. Walmod (eds.)
Cell Adhesion Molecules: Implications in Neurological ailments includes overview articles on contemporary advancements within the box of neural mobile adhesion molecules (CAMs). the focus is at the function of cellphone adhesion molecules in quite a few neurological and neurodegenerative ailments. this attitude has been basically ignored in lately released books on neural CAMs. additionally, the members disguise many newly pointed out mobilephone adhesion molecules and a few that experience now not got a lot awareness lately. This books fills an enormous hole within the at present on hand literature.
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Exp Cell Res 295(2):488–496 Barker TH, Pallero MA, MacEwen MW, Tilden SG, Woods A, Murphy-Ullrich JE, Hagood JS (2004b) Thrombospondin-1-induced focal adhesion disassembly in fibroblasts requires Thy-1 surface expression, lipid raft integrity, and Src activation. J Biol Chem 279(22):23510–23516 Beech JN, Morris RJ, Raisman G (1983) Density of Thy-1 on axonal membrane of different rat nerves. J Neurochem 41(2):411–417 Beissert S, He HT, Hueber AO, Lellouch AC, Metze D, Mehling A, Luger TA, Schwarz T, Grabbe S (1998) Impaired cutaneous immune responses in Thy-1-deficient mice.
The AB loop contributes over 50 % of interfacial protein– protein interactions, including the three hydrogen bonds involving conserved atoms in Ad12, Ad2, Ad5, and Ad9 knob and thus may be the key anchor for the complex (Law and Davidson 2005). The cryo-electron microscopic reconstruction of CVB3 complexes with CAR showed that the D1 domain of CAR binds within the canyon of CVB3. The interface between the virus and CAR consists of the BC and FG loops of D1 binding to the north rim and the floor of the canyon, as well as the A and G β-strands interacting with the south rim of the canyon (He et al.
2002; Patzke et al. 2010). Furthermore, in non-polarized cells and in neurons CAR is diffusely localized over the entire cell surface but accumulates at cell–cell contact sites. Crystallographic studies on the single D1 and the complete extracellular region of CAR suggested that CAR homophilic binding is mediated by interactions of D1 (van Raaij et al. 2000; Verdino et al. 2010; Patzke et al. 2010). However, a detailed analysis of binding activities of single extracellular domains of CAR, combined with adhesion assays, indicated that homophilic interactions of CAR are also mediated by D1–D2 binding (Patzke et al.
Cell Adhesion Molecules: Implications in Neurological Diseases by Lisette Leyton Ph.D., James S. Hagood M.D. (auth.), Vladimir Berezin, Peter S. Walmod (eds.)