Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1993-5-24
pubmed:abstractText
We have purified biologically active recombinant human fibroblast growth factor 5 (FGF-5) from Escherichia coli. In the presence of heparin, recombinant FGF-5 is as active as native growth factor, demonstrating that glycosylation does not significantly potentiate FGF-5 activity. FGF-5 can bind and induce autophosphorylation of human FGF receptors (FGFR) 1 and 2. Competition binding studies show that the KD for FGF-5-FGFR-1 and FGF-5-FGFR-2 interactions are both between 0.5 and 1.5 x 10(-9) M.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/FGF5 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/FGFR1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Fgf5 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Fgfr1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 5, http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factors, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Fibroblast Growth..., http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fibroblast Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1311-6
pubmed:dateRevised
2010-5-26
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Activation of fibroblast growth factor (FGF) receptors by recombinant human FGF-5.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, New York, New York 10032.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.