Linked Life Data

12297674

Source:http://linkedlifedata.com/resource/pubmed/id/12297674

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
151
pubmed:dateCreated
2002-9-25
pubmed:abstractText
Cytokines of the transforming growth factor-beta (TGF-beta) superfamily transduce their signals by activating receptor-regulated Smads (R-Smads). Distinct R-Smads or combinations of R-Smads are activated by TGF-beta, activin, or bone morphogenetic proteins (BMPs). R-Smads activated by BMPs induce expression of Id proteins, which act as inhibitors of differentiation and stimulators of cell growth by inhibiting the function of basic helix-loop-helix transcription factors. In endothelial cells, TGF-beta binds to two distinct type I receptor serine-threonine kinases, ALK-5 and ALK-1; the latter activates the same R-Smads that are activated by BMP and induces synthesis of Id (inhibitor of differentiation or inhibitor of DNA binding) proteins. Growing evidence suggests that Id proteins may play crucial roles in angiogenesis, neurogenesis, and osteogenesis and act as key molecules in regulating biological responses induced by BMPs and TGF-beta.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1525-8882
pubmed:author
pubmed:issnType
Electronic
pubmed:day
24
pubmed:volume
2002
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
pe40
pubmed:dateRevised
2009-10-21
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Id: a target of BMP signaling.
pubmed:affiliation
Department of Molecular Pathology, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. miyazono-ind@umin.ac.jp
pubmed:publicationType
Journal Article, Review