Analysis of Human Follistatin Structure: Identification of Two Discontinuous N-Terminal Sequences Coding for Activin A Binding and Structural Consequences of Activin Binding to Native Proteins*
Author:
Affiliation:
1. National Cooperative Program for Infertility Research, Reproductive Endocrine Unit, Massachusetts General Hospital, Boston, Massachusetts 02114
Publisher
The Endocrine Society
Subject
Endocrinology
Link
http://academic.oup.com/endo/article-pdf/141/9/3183/10361979/endo3183.pdf
Reference45 articles.
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2. Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone.;Ueno;Proc Natl Acad Sci USA,1987
3. The isolation of polypeptides with FSH suppressing activity from bovine follicular fluid which are structurally different to inhibin.;Robertson;Biochem Biophys Res Commun,1987
4. Activin-binding protein from rat ovary is follistatin.;Nakamura;Science,1990
5. Activin-binding protein is present in pituitary.;Kogawa;Endocrinology,1991
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