A
A Schmidt
Publications - 10
Citations - 1105
A Schmidt is an academic researcher. The author has contributed to research in topics: Epidermal growth factor & Receptor. The author has an hindex of 7, co-authored 10 publications receiving 1095 citations.
Papers
More filters
Journal ArticleDOI
Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing.
Annemarie Honegger,Thomas J. Dull,S. Felder,E Van Obberghen,F Bellot,D. Szapary,A Schmidt,Axel Ullrich,Joseph Schlessinger +8 more
TL;DR: A single amino acid substitution rendered a "down-regulated" receptor into a receptor that can recycle from cytoplasmic compartment back to the cell surface, suggesting that degradation of normal EGF receptors after endocytosis is due to the kinase activity endogenous to this receptor.
Journal ArticleDOI
A mutant epidermal growth factor receptor with defective protein tyrosine kinase is unable to stimulate proto-oncogene expression and DNA synthesis.
Annemarie Honegger,D. Szapary,A Schmidt,R M Lyall,E Van Obberghen,Thomas J. Dull,Axel Ullrich,Joseph Schlessinger +7 more
TL;DR: EGF was unable to stimulate the stimulation of various responses, including enhanced expression of proto-oncogenes c-fos and c-myc, morphological changes, and stimulation of DNA synthesis, suggesting that the tyrosine kinase activity is essential for EGF receptor signal transduction.
Journal ArticleDOI
Evidence for epidermal growth factor (EGF)-induced intermolecular autophosphorylation of the EGF receptors in living cells.
TL;DR: It appears, therefore, that crucial events of signal transduction occur before K721A and active EGF receptors are separated by their different endocytic itineraries.
Journal ArticleDOI
Biological activities of EGF-receptor mutants with individually altered autophosphorylation sites.
Annemarie Honegger,Thomas J. Dull,F Bellot,E Van Obberghen,D. Szapary,A Schmidt,Axel Ullrich,Joseph Schlessinger +7 more
TL;DR: In vitro site‐directed mutagenesis was used to replace individually the three known autophosphorylation sites of the epidermal growth factor (EGF)‐receptors by phenylalanine, indicating that none of the vital functions of the EGF‐receptor were critically impaired by the loss of individual autoph phosphate acceptor sites.
Journal ArticleDOI
Separate endocytic pathways of kinase-defective and -active EGF receptor mutants expressed in same cells.
TL;DR: Intracellular trafficking of EGF receptors must be determined by a sorting mechanism that specifically recognizes EGF receptor molecules according to their intrinsic kinase activity.