Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1999-1-11
pubmed:abstractText
Fibroblast growth factors (FGFs) are members of a protein family with a broad range of biological activities. The best characterized FGFs interact with two distinct extracellular receptors--a transmembrane tyrosine kinase FGF receptor (FGFR) and a heparan f1p4ate-related proteoglycan of the extracellular matrix. These components form a FGF-FGFR-proteoglycan complex that activates the FGF-mediated signal transduction process through FGFR dimerization. Recent crystal structure determinations of FGF-heparin complexes have provided insights into both the interactions between these components and the role of heparin-like proteoglycans in FGF function. Future advances in this field will benefit enormously from an ability to specifically prepare homogeneous heparin-based oligosaccharides of defined sequence for use in biochemical and structural studies of FGF and many other systems.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0959-440X
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
578-86
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Diversity does make a difference: fibroblast growth factor-heparin interactions.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of California, Los Angeles 90095-1570, USA. salem@ewald.mbi.ucla.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't