Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation
- 1 December 1994
- Vol. 79 (6), 1015-1024
- https://doi.org/10.1016/0092-8674(94)90032-9
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativityBiochemistry, 1994
- Structural studies of the binding of the anti-ulcer drug sucrose octasulfate to acidic fibroblast growth factorStructure, 1993
- Real-time measurements of kinetics of EGF binding to soluble EGF receptor monomers and dimers support the dimerization model for receptor activationBiochemistry, 1993
- Nature of the interaction of heparin with acidic fibroblast growth factorBiochemistry, 1993
- Growth factor signaling by receptor tyrosine kinasesNeuron, 1992
- Three-Dimensional Structures of the Ligand-Binding Domain of the Bacterial Aspartate Receptor with and Without a LigandScience, 1991
- Dimerization of the Extracellular Domain of the Human Growth Hormone Receptor by a Single Hormone MoleculeScience, 1991
- A dual receptor system is required for basic fibroblast growth factor activityCell, 1991
- Fibroblast Growth Factor Receptors from Liver Vary in Three Structural DomainsScience, 1991
- Transformation of mammalian cells with genes from procaryotes and eucaryotesCell, 1979