Heparan sulfate is required for interaction and activation of the epithelial cell fibroblast growth factor receptor-2IIIb with stromal-derived fibroblast growth factor-7
in press
Jang, J.-H.; Wang, F.; Kan, M. Heparan sulfate is required for interaction and activation of the epithelial cell fibroblast growth factor receptor-2IIIb with stromal-derived fibroblast growth factor-7. In Vitro Cell. Dev. Biol. Animal (in press); 1997.
High and low affinity binding of heparin-binding growth factor to a 130-kDa receptor correlates with stimulation and inhibition of growth of a differentiated human hepatoma cell
PID: 2457020, COI: 1:CAS:528:DyaL1cXltVGitrY%3D
Kan, M.; DiSorbo, D.; Hou, J., et al. High and low affinity binding of heparin-binding growth factor to a 130-kDa receptor correlates with stimulation and inhibition of growth of a differentiated human hepatoma cell. J. Biol. Chem. 263:11306–11313; 1988.
Identification and assay of heparin-binding (fibroblast) growth factor receptors
PID: 1713285, COI: 1:CAS:528:DyaK3MXlsFCns7o%3D
Kan, M.; Shi, E.; McKeehan, W. L. Identification and assay of heparin-binding (fibroblast) growth factor receptors. Methods Enzymol. 198:158–171; 1991. DOI: 10.1016/0076-6879(91)98017-Z
Divalent cations and heparan sulfate cooperate to control assembly and activity of the fibroblast growth factor receptor complex
PID: 8824259, COI: 1:CAS:528:DyaK28XmsVCgsbw%3D
Kan, M.; Wang, F.; Kan, M., et al. Divalent cations and heparan sulfate cooperate to control assembly and activity of the fibroblast growth factor receptor complex. J. Biol. Chem. 271:26143–26148; 1996. DOI: 10.1074/jbc.271.42.26143
An essential heparin-binding domain in the fibroblast growth factor receptor kinase
PID: 8456318, COI: 1:CAS:528:DyaK3sXks1Kntrk%3D
Kan, M.; Wang, F.; Xu, J., et al. An essential heparin-binding domain in the fibroblast growth factor receptor kinase. Science 259:1918–1921; 1993. DOI: 10.1126/science.8456318
The heparan sulfate-fibroblast growth factor family: Diversity of structure and function
in press
McKeehan, W. L.; Wang, F.; Kan, M. The heparan sulfate-fibroblast growth factor family: diversity of structure and function. Prog. Nucleic Acid Res. Mol. Biol. (in press); 1997.
High and low affinity binding sites for basic fibroblast growth factor on cultured cells: absence of a role for low affinity binding in the stimulation of plasminogen activator production by bovine capillary endothelial cells
PID: 3032990, COI: 1:CAS:528:DyaL2sXktVWmtro%3D
Moscatelli, D. High and low affinity binding sites for basic fibroblast growth factor on cultured cells: absence of a role for low affinity binding in the stimulation of plasminogen activator production by bovine capillary endothelial cells. J. Cell. Physiol. 131:123–130; 1987. DOI: 10.1002/jcp.1041310118
Fibroblast-growth-factor receptor mutations in human skeletal disorders
PID: 8585128, COI: 1:CAS:528:DyaK2MXnsVOhs7o%3D
Muenke, M.; Schell, U. Fibroblast-growth-factor receptor mutations in human skeletal disorders. Trends Genet. 11:308–313; 1995. DOI: 10.1016/S0168-9525(00)89088-5
Heparin increases the affinity of basic fibroblast growth factor for its receptor but is not required for binding
PID: 8307953, COI: 1:CAS:528:DyaK2cXhsFCrsLo%3D
Roghani, M.; Mansukhani, A.; Dell’Era, P., et al. Heparin increases the affinity of basic fibroblast growth factor for its receptor but is not required for binding. J. Biol. Chem. 269:3976–3984; 1994.
The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase and heparanases
PID: 8626565, COI: 1:CAS:528:DyaK28XisFGqu78%3D
Whitelock, J. M.; Murdock, A. D.; Iozzo, R. V., et al. The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase and heparanases. J. Biol. Chem. 271:10079–10086; 1996. DOI: 10.1074/jbc.271.17.10079
