Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1998-9-8
pubmed:abstractText
In early development of Xenopus laevis, it is known that activities of polypeptide growth factors are negatively regulated by their binding proteins. In this study, follistatin, originally known as an activin-binding protein, was shown to inhibit all aspects of bone morphogenetic protein (BMP) activity in early Xenopus embryos. Furthermore, using a surface plasmon resonance biosensor, we demonstrated that follistatin can directly interact with multiple BMPs at significantly high affinities. Interestingly, follistatin was found to be noncompetitive with the BMP receptor for ligand binding and to form a trimeric complex with BMP and its receptor. The results suggest that follistatin acts as an organizer factor in early amphibian embryogenesis by inhibiting BMP activities by a different mechanism from that used by chordin and noggin.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-1339313, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-1425340, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-1425343, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-1457128, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-1510675, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-1724720, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-1906804, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-2106159, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-2113615, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-7498789, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-7522972, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-7554498, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-7630398, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-7630399, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-7774578, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-7790373, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-7937936, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-8001117, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-8168135, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-8299934, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-8313998, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-8318252, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-8348610, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-8365557, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-8422980, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-8752213, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-8752214, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-9108472, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-9111068, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-9118212, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-9125121, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-9178255, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-9196324, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-9241429, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-9281341, http://linkedlifedata.com/resource/pubmed/commentcorrection/9689081-9299160
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9337-42
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo.
pubmed:affiliation
Department of Developmental Biology, National Institute for Basic Biology, 38 Nishigonaka, Myodaiji, Okazaki, 444-8585 Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't