The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding (Q24337354)

GOA release 2020-03-11

peptide hormone binding

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GOA release 2020-03-11

Thomas B Thompson

1

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Teresa K. Woodruff

object named as

Teresa K Woodruff

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Theodore Jardetzky

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object named as

Theodore S Jardetzky

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author name string

Thomas F Lerch

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Robert W Cook

Potent ectopic bone-inducing activity of bone morphogenetic protein-4/7 heterodimer

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language of work or name

English

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publication date

October 2005

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published in

Developmental Cell

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volume

9

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page(s)

535-43

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issue

4

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cites work

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Follistatin inhibits the function of the oocyte-derived factor BMP-15

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Follistatin regulates bone morphogenetic protein-7 (BMP-7) activity to stimulate embryonic muscle growth.

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Follistatins neutralize activin bioactivity by inhibition of activin binding to its type II receptors

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Facilitated transport of a Dpp/Scw heterodimer by Sog/Tsg leads to robust patterning of the Drosophila blastoderm embryo.

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Depletion of three BMP antagonists from Spemann's organizer leads to a catastrophic loss of dorsal structures

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Solution Structure of the Third TB Domain from LTBP1 Provides Insight into Assembly of the Large Latent Complex that Sequesters Latent TGF-β

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Autocrine/paracrine regulation of pituitary function by activin, inhibin and follistatin

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A flexible activin explains the membrane-dependent cooperative assembly of TGF-beta family receptors

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Structure of the integrin binding fragment from fibrillin-1 gives new insights into microfibril organization

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Follistatin complexes Myostatin and antagonises Myostatin-mediated inhibition of myogenesis.

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

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Difference between follistatin isoforms in the inhibition of activin signalling: activin neutralizing activity of follistatin isoforms is dependent on their affinity for activin

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Ventral mesoderm induction and patterning by bone morphogenetic protein heterodimers in Xenopus embryos.

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Activin signal transduction pathways

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The other side of TGF-beta superfamily signal regulation: thinking outside the cell.

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The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly

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Multiple defects and perinatal death in mice deficient in follistatin

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Crystal structure of the BMP-2-BRIA ectodomain complex

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Structural basis of BMP signalling inhibition by the cystine knot protein Noggin

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Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo

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Crystal structures of the heparan sulfate-binding domain of follistatin. Insights into ligand binding

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An activin mutant with disrupted ALK4 binding blocks signaling via type II receptors

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Latent transforming growth factor-beta (TGF-beta) binding proteins: orchestrators of TGF-beta availability

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Activin receptor signaling.

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Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin

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Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions

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Differential Binding and Neutralization of Activins A and B by Follistatin and Follistatin Like-3 (FSTL-3/FSRP/FLRG)

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Differential distribution of follistatin isoforms: application of a new FS315-specific immunoassay

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The Role of Follistatin Domains in Follistatin Biological Action

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TGFbeta/activin/nodal signaling is necessary for the maintenance of pluripotency in human embryonic stem cells

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Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction

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Regulation of ovarian function by the TGF-beta superfamily and follistatin

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Bone morphogenetic protein (BMP) ligands and receptors in bovine ovarian follicle cells: actions of BMP-4, -6 and -7 on granulosa cells and differential modulation of Smad-1 phosphorylation by follistatin.

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Activin A maintains pluripotency of human embryonic stem cells in the absence of feeder layers

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Residues in the C-terminal region of activin A determine specificity for follistatin and type II receptor binding

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Activins, myostatin and related TGF-beta family members as novel therapeutic targets for endocrine, metabolic and immune disorders.

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

274489

274489

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference