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Items: 18


The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system.

Levy JB, Canoll PD, Silvennoinen O, Barnea G, Morse B, Honegger AM, Huang JT, Cannizzaro LA, Park SH, Druck T, et al.

J Biol Chem. 1993 May 15;268(14):10573-81.


Identification of a carbonic anhydrase-like domain in the extracellular region of RPTP gamma defines a new subfamily of receptor tyrosine phosphatases.

Barnea G, Silvennoinen O, Shaanan B, Honegger AM, Canoll PD, D'Eustachio P, Morse B, Levy JB, Laforgia S, Huebner K, et al.

Mol Cell Biol. 1993 Mar;13(3):1497-506.


Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis.

Mohammadi M, Dionne CA, Li W, Li N, Spivak T, Honegger AM, Jaye M, Schlessinger J.

Nature. 1992 Aug 20;358(6388):681-4.


A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1.

Mohammadi M, Honegger AM, Rotin D, Fischer R, Bellot F, Li W, Dionne CA, Jaye M, Rubinstein M, Schlessinger J.

Mol Cell Biol. 1991 Oct;11(10):5068-78.


Separate endocytic pathways of kinase-defective and -active EGF receptor mutants expressed in same cells.

Honegger AM, Schmidt A, Ullrich A, Schlessinger J.

J Cell Biol. 1990 May;110(5):1541-8.


Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor.

Margolis B, Bellot F, Honegger AM, Ullrich A, Schlessinger J, Zilberstein A.

Mol Cell Biol. 1990 Feb;10(2):435-41.


Domain deletion in the extracellular portion of the EGF-receptor reduces ligand binding and impairs cell surface expression.

Lax I, Bellot F, Honegger AM, Schmidt A, Ullrich A, Givol D, Schlessinger J.

Cell Regul. 1990 Jan;1(2):173-88.


All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor.

Margolis BL, Lax I, Kris R, Dombalagian M, Honegger AM, Howk R, Givol D, Ullrich A, Schlessinger J.

J Biol Chem. 1989 Jun 25;264(18):10667-71.


Metabolic effects induced by epidermal growth factor (EGF) in cells expressing EGF receptor mutants.

Scimeca JC, Ballotti R, Alengrin F, Honegger AM, Ullrich A, Schlessinger J, Obberghen EV.

J Biol Chem. 1989 Apr 25;264(12):6831-5.


A point mutation at the ATP-binding site of the EGF-receptor abolishes signal transduction.

Moolenaar WH, Bierman AJ, Tilly BC, Verlaan I, Defize LH, Honegger AM, Ullrich A, Schlessinger J.

EMBO J. 1988 Mar;7(3):707-10.


Signal transduction by epidermal growth factor receptor.

Schlessinger J, Ullrich A, Honegger AM, Moolenaar WH.

Cold Spring Harb Symp Quant Biol. 1988;53 Pt 1:515-9. No abstract available.


A mutant epidermal growth factor receptor with defective protein tyrosine kinase is unable to stimulate proto-oncogene expression and DNA synthesis.

Honegger AM, Szapary D, Schmidt A, Lyall R, Van Obberghen E, Dull TJ, Ullrich A, Schlessinger J.

Mol Cell Biol. 1987 Dec;7(12):4568-71.


Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing.

Honegger AM, Dull TJ, Felder S, Van Obberghen E, Bellot F, Szapary D, Schmidt A, Ullrich A, Schlessinger J.

Cell. 1987 Oct 23;51(2):199-209.


The conformation of insulin-like growth factors: relationships with insulins.

Dafgård E, Bajaj M, Honegger AM, Pitts J, Wood S, Blundell T.

J Cell Sci Suppl. 1985;3:53-64. Review.


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