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activin binding

Interacting selectively and non-covalently with activin, a dimer of inhibin-beta subunits. [GOC:jid, GOC:mah]
National Institutes of Health

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Highly Cited
2004
Highly Cited
2004
Overexpression of follistatin-like 3 in gonads causes defects in gonadal development and function in transgenic mice.
Activin has numerous biological activities including regulation of follicular development, spermatogenesis, and steroidogenesis… 
Review
2001
Review
2001
The contribution of inhibins and activins to malignant prostate disease
2001
2001
The activin binding proteins follistatin and follistatin-related protein are differentially regulated in vitro and during cutaneous wound repair.
Follistatin is a secreted protein that binds activin in vitro and in vivo and thereby inhibits its biological functions. Recently… 
2000
2000
BMP‐2 induces the expression of activin βA and follistatin in vitro
Activins are members of the transforming growth factor β (TGF‐β) superfamily and have been shown to be multifunctional regulators… 
2000
2000
Regulation of inhibin/activin subunits and follistatin mRNA expression in the rat pituitary at early estrus.
Highly Cited
1999
Highly Cited
1999
Is gonadotrope expression of the gonadotropin releasing hormone receptor gene mediated by autocrine/paracrine stimulation of an activin response element?
Expression of the FSHbeta subunit and GnRH receptor (GnRHR) genes in gonadotropes is stimulated by activin. We sought to identify… 
1998
1998
Differential expression of activin subunits, activin receptors and follistatin genes in bovine oocytes and preimplantation embryos.
The presence of inhibin subunits (alpha, betaA and betaB), activin binding protein follistatin and activin receptors (ActR-I… 
1998
1998
Expression of activin and follistatin in the rat hypothalamus
The central role of activin in the regulation of the reproductive axis remains largely unexplored. Evidence suggests that activin… 
1997
1997
A novel activin binding protein in ovine allantoic fluid
1996
1996
Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors.
Truncated activin type II receptors have been reported to inhibit activin receptor signaling in Xenopus embryos, although the… 
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