title: Novel antagonists of heparin binding growth factors.
abstract: Structural and functional studies of ligand-RTK interactions over the last decade highlight the importance of multiple binding events and associated conformational changes in RTK ectodomains that are required for kinase activation. These events vary in strength, and even weak interactions appear to provide necessary increments of increased stability to a signal transduction process whose complexity we are only beginning to appreciate.
authors.forename: Fabiola
authors.initials: F
authors.lastname: Cecchi
authors.forename: Donald P
authors.initials: DP
authors.lastname: Bottaro
mesh_terms: D019812:Heparan Sulfate Proteoglycans / Q000737:chemistry* / Q000378:metabolism; D006493:Heparin / Q000737:chemistry* / Q000378:metabolism; D017228:Hepatocyte Growth Factor / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D042461:Vascular Endothelial Growth Factor A / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism
chemical_list: D019812:Heparan Sulfate Proteoglycans; C467484:VEGFA protein, human; D042461:Vascular Endothelial Growth Factor A; D017228:Hepatocyte Growth Factor; D006493:Heparin