T J Dull - JoVE Visualize

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Molecular and Cellular Biology|June 1, 1990

Epidermal growth factor receptor cytoplasmic domain mutations trigger ligand-independent transformationS Massoglia, A Gray, T J Dull, et al.

Nature|February 5, 1987

Transforming potential of the c-fms proto-oncogene (CSF-1 receptor)M F Roussel, T J Dull, C W Rettenmier, et al.

The Journal of Biological Chemistry|February 5, 1987

Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulinC K Chou, T J Dull, D S Russell, et al.

The EMBO Journal|October 1, 1988

Biological activities of EGF-receptor mutants with individually altered autophosphorylation sitesA Honegger, T J Dull, F Bellot, et al.

DNA (Mary Ann Liebert, Inc.)|August 1, 1987

Tissue-specific and developmentally regulated transcription of the insulin-like growth factor 2 geneA Gray, A W Tam, T J Dull, et al.

Cell|August 26, 1988

Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activityM F White, J N Livingston, J M Backer, et al.

The Journal of Biological Chemistry|June 25, 1988

Properties of a human insulin receptor with a COOH-terminal truncation. I. Insulin binding, autophosphorylation, and endocytosisD A McClain, H Maegawa, J Levy, et al.

Molecular and Cellular Biology|December 1, 1987

A mutant epidermal growth factor receptor with defective protein tyrosine kinase is unable to stimulate proto-oncogene expression and DNA synthesisA M Honegger, D Szapary, A Schmidt, et al.

The Journal of Biological Chemistry|June 25, 1988

Properties of a human insulin receptor with a COOH-terminal truncation. II. Truncated receptors have normal kinase activity but are defective in signaling metabolic effectsH Maegawa, D A McClain, G Freidenberg, et al.

Cell|October 23, 1987

Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routingA M Honegger, T J Dull, S Felder, et al.

Pageof 4

Showing results (21-30 of 36) with videos related to

Sort By:

Pageof 4

Molecular and Cellular Biology|June 1, 1990

Epidermal growth factor receptor cytoplasmic domain mutations trigger ligand-independent transformationS Massoglia, A Gray, T J Dull, et al.

Nature|February 5, 1987

Transforming potential of the c-fms proto-oncogene (CSF-1 receptor)M F Roussel, T J Dull, C W Rettenmier, et al.

The Journal of Biological Chemistry|February 5, 1987

Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulinC K Chou, T J Dull, D S Russell, et al.

The EMBO Journal|October 1, 1988

Biological activities of EGF-receptor mutants with individually altered autophosphorylation sitesA Honegger, T J Dull, F Bellot, et al.

DNA (Mary Ann Liebert, Inc.)|August 1, 1987

Tissue-specific and developmentally regulated transcription of the insulin-like growth factor 2 geneA Gray, A W Tam, T J Dull, et al.

Cell|August 26, 1988

Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activityM F White, J N Livingston, J M Backer, et al.

The Journal of Biological Chemistry|June 25, 1988

Properties of a human insulin receptor with a COOH-terminal truncation. I. Insulin binding, autophosphorylation, and endocytosisD A McClain, H Maegawa, J Levy, et al.

Molecular and Cellular Biology|December 1, 1987

A mutant epidermal growth factor receptor with defective protein tyrosine kinase is unable to stimulate proto-oncogene expression and DNA synthesisA M Honegger, D Szapary, A Schmidt, et al.

The Journal of Biological Chemistry|June 25, 1988

Properties of a human insulin receptor with a COOH-terminal truncation. II. Truncated receptors have normal kinase activity but are defective in signaling metabolic effectsH Maegawa, D A McClain, G Freidenberg, et al.

Cell|October 23, 1987

Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routingA M Honegger, T J Dull, S Felder, et al.

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