Fibrillin, calcium binding

Fibrillin, calcium binding, 46 473, 474, 477 Fibulin-I, calcium binding, 46 473 Field desorption mass spectroscopy, 28 6, 21 Field effects, of astatophenols, 31 66 Fine structure, 13 193-204 Fingerprinting of polymetalates, 19 246-248 Finite perturbation theory, 22 211, 212 First transition series, substitution, transferrins, 41 423 26... 

Cardy, C. M., and Handford, P. A. (1998). Metal ion dependency of microfibrils supports a rod-like conformation for fibrillin-1 calcium-binding epidermal growth factor-like domains. J. Mol. Biol. 276, 855-860. 

Reinhardt, D. P., Ono, R. N., Notbohm, H., Muller, P. K., Bachinger, H. P., and Sakai, L. Y. (2000a). Mutations in calcium-binding epidermal growth factor modules render fibrillin-1 susceptible to proteolysis. A potential disease-causing mechanism in Marfan syndrome. / Biol. Chem. 275, 12339-12345. 

Smallridge, R. S., Whiteman, P., Werner, J. M., Campbell, I. D., Handford, P. A., and Downing, A. K. (2003). Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1./. Biol. Chem. 278, 12199-12206. 

Many cells secrete at least one of the three immature forms of TGF-P, and essentially all cells have receptors that respond to the presence of mature TGF-P in the stroma. In the periodontium, TGF-P stimulates fibroblast and osteoblast proliferation during connective tissue or bone remodeling (Sect. 10.1.3), and maintains the proliferation of dentally attached epithelial cells (Sect. 5.2.3). The linker domains that connect calcium binding domains in fibrillin are identical to the sequence of protein receptors that bind to TGF-P (Sect. 6.1.1). 

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