 Follistatin-Related Proteins
"Follistatin-Related Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Broadly distributed glycoproteins that are homologous to the activin-binding protein, FOLLISTATIN. These follistatin-related proteins are encoded by a number of genes.
| Descriptor ID |
D038702
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| MeSH Number(s) |
D12.776.157.286
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| Concept/Terms |
Follistatin-Like Protein 1- Follistatin-Like Protein 1
- Follistatin Like Protein 1
- Follistatin-Related Protein 1
- Follistatin Related Protein 1
- FSTL1 Gene Product
Follistatin-Like Protein 3- Follistatin-Like Protein 3
- Follistatin Like Protein 3
- FLRG Protein
- Follistatin Secreted Related Protein
- FSTL3 Gene Product
- Follistatin-Like Secreted Glycoprotein
- Follistatin Like Secreted Glycoprotein
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Below are MeSH descriptors whose meaning is more general than "Follistatin-Related Proteins".
Below are MeSH descriptors whose meaning is more specific than "Follistatin-Related Proteins".
This graph shows the total number of publications written about "Follistatin-Related Proteins" by people in this website by year, and whether "Follistatin-Related Proteins" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2002 | 0 | 1 | 1 | | 2003 | 1 | 0 | 1 | | 2004 | 3 | 0 | 3 | | 2005 | 1 | 0 | 1 | | 2006 | 1 | 0 | 1 | | 2007 | 1 | 0 | 1 | | 2008 | 1 | 0 | 1 | | 2009 | 1 | 0 | 1 | | 2011 | 1 | 1 | 2 | | 2012 | 0 | 1 | 1 | | 2013 | 1 | 1 | 2 | | 2016 | 1 | 0 | 1 |
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Below are the most recent publications written about "Follistatin-Related Proteins" by people in Profiles.
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Brown ML, Andrzejewski D, Burnside A, Schneyer AL. Activin Enhances a- to ß-Cell Transdifferentiation as a Source For ß-Cells In Male FSTL3 Knockout Mice. Endocrinology. 2016 Mar; 157(3):1043-54.
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Ungerleider NA, Bonomi LM, Brown ML, Schneyer AL. Increased activin bioavailability enhances hepatic insulin sensitivity while inducing hepatic steatosis in male mice. Endocrinology. 2013 Jun; 154(6):2025-33.
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Oldknow KJ, Seebacher J, Goswami T, Villen J, Pitsillides AA, O'Shaughnessy PJ, Gygi SP, Schneyer AL, Mukherjee A. Follistatin-like 3 (FSTL3) mediated silencing of transforming growth factor ß (TGFß) signaling is essential for testicular aging and regulating testis size. Endocrinology. 2013 Mar; 154(3):1310-20.
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Matzelle MM, Gallant MA, Condon KW, Walsh NC, Manning CA, Stein GS, Lian JB, Burr DB, Gravallese EM. Resolution of inflammation induces osteoblast function and regulates the Wnt signaling pathway. Arthritis Rheum. 2012 May; 64(5):1540-50.
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Brown ML, Kimura F, Bonomi LM, Ungerleider NA, Schneyer AL. Differential synthesis and action of TGFß superfamily ligands in mouse and rat islets. Islets. 2011 Nov-Dec; 3(6):367-75.
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Brown ML, Bonomi L, Ungerleider N, Zina J, Kimura F, Mukherjee A, Sidis Y, Schneyer A. Follistatin and follistatin like-3 differentially regulate adiposity and glucose homeostasis. Obesity (Silver Spring). 2011 Oct; 19(10):1940-9.
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Thadhani R, Powe CE, Tjoa ML, Khankin E, Ye J, Ecker J, Schneyer A, Karumanchi SA. First-trimester follistatin-like-3 levels in pregnancies complicated by subsequent gestational diabetes mellitus. Diabetes Care. 2010 Mar; 33(3):664-9.
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Stamler R, Keutmann HT, Sidis Y, Kattamuri C, Schneyer A, Thompson TB. The structure of FSTL3.activin A complex. Differential binding of N-terminal domains influences follistatin-type antagonist specificity. J Biol Chem. 2008 Nov 21; 283(47):32831-8.
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Mukherjee A, Sidis Y, Mahan A, Raher MJ, Xia Y, Rosen ED, Bloch KD, Thomas MK, Schneyer AL. FSTL3 deletion reveals roles for TGF-beta family ligands in glucose and fat homeostasis in adults. Proc Natl Acad Sci U S A. 2007 Jan 23; 104(4):1348-53.
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Sidis Y, Mukherjee A, Keutmann H, Delbaere A, Sadatsuki M, Schneyer A. 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. Endocrinology. 2006 Jul; 147(7):3586-97.
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