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PMID:8386828

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Citation

Clements, DA, Wang, JK, Dionne, CA and Goldfarb, M (1993) Activation of fibroblast growth factor (FGF) receptors by recombinant human FGF-5. Oncogene 8:1311-6

Abstract

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.

Links

PubMed

Keywords

3T3 Cells; Amino Acid Sequence; Animals; Base Sequence; Fibroblast Growth Factor 5; Fibroblast Growth Factors/isolation & purification; Fibroblast Growth Factors/metabolism; Fibroblast Growth Factors/pharmacology; Humans; Mice; Molecular Sequence Data; Phosphorylation; Receptor Protein-Tyrosine Kinases; Receptor, Fibroblast Growth Factor, Type 1; Receptors, Cell Surface/drug effects; Receptors, Cell Surface/metabolism; Receptors, Fibroblast Growth Factor/drug effects; Receptors, Fibroblast Growth Factor/metabolism; Recombinant Proteins/metabolism; Recombinant Proteins/pharmacology

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:FGFR2

enables

GO:0017134: fibroblast growth factor binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P12034

F

Seeded From UniProt

complete


See also

References

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