Article
Follistatin: essential role for the N-terminal domain in activin binding and neutralization.
The Journal of biological chemistry - 25 May 2001
Sidis Y, Schneyer A L, Sluss P M, Johnson L N, Keutmann H T
Abstract excerpt
Follistatin is recognized to be an important regulator of cellular differentiation and secretion through its potent ability to bind and bioneutralize activin with which it is colocalized in many tissue systems. The 288-residue follistatin molecule is comprised of a 63-residue N-terminal segment followed by three repeating 10-cysteine "follistatin domains" also represented in several extracellular matrix proteins....
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