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- W1991002945 endingPage "12" @default.
- W1991002945 startingPage "2" @default.
- W1991002945 abstract "Like other members of the transforming growth factor-β (TGF-β) superfamily, activins are synthesised as precursor molecules comprising an N-terminal prodomain and C-terminal mature region. During synthesis, the prodomain interacts non-covalently with mature activin, maintaining the molecule in a conformation competent for dimerisation. Dimeric precursors are cleaved by proprotein convertases and activin is secreted from the cell non-covalently associated with its propeptide. Extracellularly, the propeptide interacts with heparan sulfate proteoglycans to regulate activin localization within tissues. The mature activin dimer exhibits the classic 'open-hand' structure of TGF-β ligands with 'finger-like' domains projecting outward from the cysteine knot core of the molecule. These finger domains form the binding epitopes for type I and II serine/threonine kinase receptors. Activins ability to access its signalling receptors is regulated by the extracellular binding proteins, follistatin, follistatin-like-3, and by inhibins, which, in the presence of betaglycan, sequester type II receptors." @default.
- W1991002945 created "2016-06-24" @default.
- W1991002945 creator A5072084225 @default.
- W1991002945 creator A5079892976 @default.
- W1991002945 creator A5082722215 @default.
- W1991002945 date "2012-08-01" @default.
- W1991002945 modified "2023-09-26" @default.
- W1991002945 title "New insights into the mechanisms of activin action and inhibition" @default.
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