Characterization of follistatin-type domains and their contribution to myostatin and activin A antagonism. (Q36065507)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22593183%20AND%20SRC:MED&resulttype=core&format=json

1 February 2020

title

Characterization of follistatin-type domains and their contribution to myostatin and activin A antagonism (English)

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1 February 2020

4

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1 February 2020

author name string

Jennifer N Cash

series ordinal

1

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1 February 2020

Elizabeth B Angerman

series ordinal

2

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1 February 2020

Henry T Keutmann

series ordinal

3

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1 February 2020

publication date

16 May 2012

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1 February 2020

published in

Molecular Endocrinology

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1 February 2020

volume

26

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1 February 2020

issue

7

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1 February 2020

page(s)

1167-1178

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Structure of Myostatin·Follistatin-like 3

1 February 2020

cites work

1 reference

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Latent TGF-β structure and activation

2 October 2017

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Follistatin and follistatin like-3 differentially regulate adiposity and glucose homeostasis

2 October 2017

1 reference

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TGF-β signalling is mediated by two autonomously functioning TβRI:TβRII pairs

2 October 2017

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Bone morphogenetic protein-2 and -6 heterodimer illustrates the nature of ligand-receptor assembly

2 October 2017

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The structure of myostatin:follistatin 288: insights into receptor utilization and heparin binding

2 October 2017

1 reference

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The biology of activin: recent advances in structure, regulation and function

2 October 2017

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Crystal structure analysis reveals a spring-loaded latch as molecular mechanism for GDF-5-type I receptor specificity

2 October 2017

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The Structure of FSTL3·Activin A Complex DIFFERENTIAL BINDING OF N-TERMINAL DOMAINS INFLUENCES FOLLISTATIN-TYPE ANTAGONIST SPECIFICITY

2 October 2017

1 reference

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Differential antagonism of activin, myostatin and growth and differentiation factor 11 by wild-type and mutant follistatin

2 October 2017

1 reference

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Crystal structure analysis reveals how the Chordin family member crossveinless 2 blocks BMP-2 receptor binding

2 October 2017

1 reference

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Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding

2 October 2017

1 reference

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Transgenic expression of a myostatin inhibitor derived from follistatin increases skeletal muscle mass and ameliorates dystrophic pathology in mdx mice

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Characterization of follistatin-related gene as a negative regulatory factor for activin family members during mouse heart development

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Structural and biophysical coupling of heparin and activin binding to follistatin isoform functions

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

A silent H-bond can be mutationally activated for high-affinity interaction of BMP-2 and activin type IIB receptor

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

FSTL3 deletion reveals roles for TGF-beta family ligands in glucose and fat homeostasis in adults

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Structure of the ternary signaling complex of a TGF-beta superfamily member

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Biological activity of follistatin isoforms and follistatin-like-3 is dependent on differential cell surface binding and specificity for activin, myostatin, and bone morphogenetic proteins

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Activin-A binds follistatin and type II receptors through overlapping binding sites: generation of mutants with isolated binding activities

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Structural basis for the inhibition of activin signalling by follistatin.

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Regulation of muscle mass by myostatin

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Heparin and activin-binding determinants in follistatin and FSTL3.

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Molecular recognition of BMP-2 and BMP receptor IA

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

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

2 October 2017

1 reference

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

2 October 2017

1 reference

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Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex

2 October 2017

1 reference

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Evolutionary trace analysis of TGF-beta and related growth factors: implications for site-directed mutagenesis.

2 October 2017

1 reference

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Crystal structure of the BMP-2-BRIA ectodomain complex

2 October 2017

1 reference

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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

2 October 2017

1 reference

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FLRG (follistatin-related gene), a new target of chromosomal rearrangement in malignant blood disorders

2 October 2017

1 reference

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Direct binding of Smad3 and Smad4 to critical TGF beta-inducible elements in the promoter of human plasminogen activator inhibitor-type 1 gene

2 October 2017

1 reference

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Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Multiple defects and perinatal death in mice deficient in follistatin

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Different phenotypes for mice deficient in either activins or activin receptor type II

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

A novel role of follistatin, an activin-binding protein, in the inhibition of activin action in rat pituitary cells. Endocytotic degradation of activin and its acceleration by follistatin associated with cell-surface heparan sulfate

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Characterization of unique binding kinetics of follistatin and activin or inhibin in serum.

11 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Activin-binding protein from rat ovary is follistatin.

11 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Follistatin-derived peptide expression in muscle decreases adipose tissue mass and prevents hepatic steatosis.

11 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

The Role of Follistatin Domains in Follistatin Biological Action

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Cooperativity of binding epitopes and receptor chains in the BMP/TGFbeta superfamily

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

Follistatin: essential role for the N-terminal domain in activin binding and neutralization

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3385792

23 September 2018

Identifiers

DOI

10.1210/ME.2012-1061

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22593183%20AND%20SRC:MED&resulttype=core&format=json

1 February 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22593183%20AND%20SRC:MED&resulttype=core&format=json

1 February 2020

1 reference