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B J Mayer

Showing results (31-40 of 63) with videos related to

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Science (New York, N.Y.)|June 22, 1990
Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteinsM Matsuda, B J Mayer, Y Fukui, et al.
Advances in Second Messenger and Phosphoprotein Research|January 1, 1990
Cell transformation by an oncogene that regulates protein kinasesH Hanafusa, B J Mayer, C Reichman, et al.
Cell|May 21, 1993
A putative modular domain present in diverse signaling proteinsB J Mayer, R Ren, K L Clark, et al.
Cell Growth & Differentiation : the Molecular Biology Journal of the American Association for Cancer Research|July 1, 1992
The product of the cellular crk gene consists primarily of SH2 and SH3 regionsC T Reichman, B J Mayer, S Keshav, et al.
Journal of Virology|February 1, 1987
Analysis of p60v-src mutants carrying lesions involved in temperature sensitivityE A Garber, B J Mayer, R Jove, et al.
The Journal of Biological Chemistry|May 25, 1992
Tyrosine-phosphorylated epidermal growth factor receptor and cellular p130 provide high affinity binding substrates to analyze Crk-phosphotyrosine-dependent interactions in vitroR B Birge, J E Fajardo, B J Mayer, et al.
The Journal of Biological Chemistry|January 25, 1993
Direct analysis of the binding of the abl Src homology 2 domain to the activated epidermal growth factor receptorG Zhu, S J Decker, B J Mayer, et al.
Molecular and Cellular Biology|February 1, 1992
Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivoB J Mayer, P K Jackson, R A Van Etten, et al.
Molecular and Cellular Biology|August 1, 1997
p21CIP1 and Cdc25A: competition between an inhibitor and an activator of cyclin-dependent kinasesP Saha, Q Eichbaum, E D Silberman, et al.
Structure (London, England : 1993)|October 15, 1995
The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) constructY Q Gosser, J Zheng, M Overduin, et al.
Pageof 7

Showing results (31-40 of 63) with videos related to

Sort By:
Pageof 7
Science (New York, N.Y.)|June 22, 1990
Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteinsM Matsuda, B J Mayer, Y Fukui, et al.
Advances in Second Messenger and Phosphoprotein Research|January 1, 1990
Cell transformation by an oncogene that regulates protein kinasesH Hanafusa, B J Mayer, C Reichman, et al.
Cell|May 21, 1993
A putative modular domain present in diverse signaling proteinsB J Mayer, R Ren, K L Clark, et al.
Cell Growth & Differentiation : the Molecular Biology Journal of the American Association for Cancer Research|July 1, 1992
The product of the cellular crk gene consists primarily of SH2 and SH3 regionsC T Reichman, B J Mayer, S Keshav, et al.
Journal of Virology|February 1, 1987
Analysis of p60v-src mutants carrying lesions involved in temperature sensitivityE A Garber, B J Mayer, R Jove, et al.
The Journal of Biological Chemistry|May 25, 1992
Tyrosine-phosphorylated epidermal growth factor receptor and cellular p130 provide high affinity binding substrates to analyze Crk-phosphotyrosine-dependent interactions in vitroR B Birge, J E Fajardo, B J Mayer, et al.
The Journal of Biological Chemistry|January 25, 1993
Direct analysis of the binding of the abl Src homology 2 domain to the activated epidermal growth factor receptorG Zhu, S J Decker, B J Mayer, et al.
Molecular and Cellular Biology|February 1, 1992
Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivoB J Mayer, P K Jackson, R A Van Etten, et al.
Molecular and Cellular Biology|August 1, 1997
p21CIP1 and Cdc25A: competition between an inhibitor and an activator of cyclin-dependent kinasesP Saha, Q Eichbaum, E D Silberman, et al.
Structure (London, England : 1993)|October 15, 1995
The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) constructY Q Gosser, J Zheng, M Overduin, et al.
Pageof 7