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S D Briggs

Showing results (1-10 of 20) with videos related to

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The Journal of Biological Chemistry|September 3, 1999
SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in Rat-2 fibroblastsS D Briggs, T E Smithgall
Psychology and Aging|October 6, 1999
Age-related deficits in generation and manipulation of mental images: I. The role of sensorimotor speed and working memoryS D Briggs, N Raz, W Marks
Biochemistry|January 21, 2000
Affinity of Src family kinase SH3 domains for HIV Nef in vitro does not predict kinase activation by Nef in vivoS D Briggs, E C Lerner, T E Smithgall
Current Opinion in Cell Biology|May 10, 2000
Acetylation and chromosomal functionsW L Cheung, S D Briggs, C D Allis
Biochemistry|October 5, 1993
Phosphorylation of the ras GTPase-activating protein (GAP) by the p93c-fes protein-tyrosine kinase in vitro and formation of GAP-fes complexes via an SH2 domain-dependent mechanismS J Hjermstad, S D Briggs, T E Smithgall
Professional Psychology, Research and Practice|February 1, 1993
Sexual misconduct in psychotherapy: reactions to a consumer-oriented brochureB E Thorn, R C Shealy, S D Briggs
The Journal of Biological Chemistry|July 18, 1997
SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1S D Briggs, M Sharkey, M Stevenson, et al.
AJNR. American Journal of Neuroradiology|February 12, 1998
Differential effects of age and sex on the cerebellar hemispheres and the vermis: a prospective MR studyN Raz, J H Dupuis, S D Briggs, et al.
The Journal of Biological Chemistry|June 16, 1995
The Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, HckS D Briggs, S S Bryant, R Jove, et al.
Oncogene|August 1, 1993
Regulation of the human c-fes protein tyrosine kinase (p93c-fes) by its src homology 2 domain and major autophosphorylation site (Tyr-713)S J Hjermstad, K L Peters, S D Briggs, et al.
Pageof 2

Showing results (1-10 of 20) with videos related to

Sort By:
Pageof 2
The Journal of Biological Chemistry|September 3, 1999
SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in Rat-2 fibroblastsS D Briggs, T E Smithgall
Psychology and Aging|October 6, 1999
Age-related deficits in generation and manipulation of mental images: I. The role of sensorimotor speed and working memoryS D Briggs, N Raz, W Marks
Biochemistry|January 21, 2000
Affinity of Src family kinase SH3 domains for HIV Nef in vitro does not predict kinase activation by Nef in vivoS D Briggs, E C Lerner, T E Smithgall
Current Opinion in Cell Biology|May 10, 2000
Acetylation and chromosomal functionsW L Cheung, S D Briggs, C D Allis
Biochemistry|October 5, 1993
Phosphorylation of the ras GTPase-activating protein (GAP) by the p93c-fes protein-tyrosine kinase in vitro and formation of GAP-fes complexes via an SH2 domain-dependent mechanismS J Hjermstad, S D Briggs, T E Smithgall
Professional Psychology, Research and Practice|February 1, 1993
Sexual misconduct in psychotherapy: reactions to a consumer-oriented brochureB E Thorn, R C Shealy, S D Briggs
The Journal of Biological Chemistry|July 18, 1997
SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1S D Briggs, M Sharkey, M Stevenson, et al.
AJNR. American Journal of Neuroradiology|February 12, 1998
Differential effects of age and sex on the cerebellar hemispheres and the vermis: a prospective MR studyN Raz, J H Dupuis, S D Briggs, et al.
The Journal of Biological Chemistry|June 16, 1995
The Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, HckS D Briggs, S S Bryant, R Jove, et al.
Oncogene|August 1, 1993
Regulation of the human c-fes protein tyrosine kinase (p93c-fes) by its src homology 2 domain and major autophosphorylation site (Tyr-713)S J Hjermstad, K L Peters, S D Briggs, et al.
Pageof 2