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Oncogene
|
May 1, 1991
TPA inhibits the tyrosine kinase activity of the neu protein in vivo and in vitro
H Cao, S Decker, D F Stern
Journal of Virology
|
April 1, 1982
Structural analysis of virion proteins of the avian coronavirus infectious bronchitis virus
D F Stern, L Burgess, B M Sefton
Current Genetics
|
February 1, 1997
Mutations in SPK1/RAD53 that specifically abolish checkpoint but not growth-related functions
D S Fay, Z Sun, D F Stern
Molecular and Cellular Biology
|
September 1, 1988
Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo
D F Stern, M P Kamps, H Cao
Molecular and Cellular Biology
|
March 1, 1990
Tyrosine phosphorylation is an early and specific event involved in primary keratinocyte differentiation
E Filvaroff, D F Stern, G P Dotto
Molecular and Cellular Biology
|
May 1, 1986
p185, a product of the neu proto-oncogene, is a receptorlike protein associated with tyrosine kinase activity
D F Stern, P A Heffernan, R A Weinberg
Current Protocols in Molecular Biology
|
February 12, 2008
Production of antibodies that recognize specific tyrosine-phosphorylated peptides
M P Digiovanna, R R Roussel, D F Stern
Science (New York, N.Y.)
|
July 10, 1998
Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint
Z Sun, J Hsiao, D S Fay, et al.
The EMBO Journal
|
March 1, 1992
A subdomain in the transmembrane domain is necessary for p185neu* activation
H Cao, L Bangalore, B J Bormann, et al.
Molecular and Cellular Biology
|
February 1, 1991
Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine
D F Stern, P Zheng, D R Beidler, et al.
Page
of 7
Search research articles
Search
Showing results (21-30 of 64) with videos related to
Sort By:
Page
of 7
Oncogene
|
May 1, 1991
TPA inhibits the tyrosine kinase activity of the neu protein in vivo and in vitro
H Cao, S Decker, D F Stern
Journal of Virology
|
April 1, 1982
Structural analysis of virion proteins of the avian coronavirus infectious bronchitis virus
D F Stern, L Burgess, B M Sefton
Current Genetics
|
February 1, 1997
Mutations in SPK1/RAD53 that specifically abolish checkpoint but not growth-related functions
D S Fay, Z Sun, D F Stern
Molecular and Cellular Biology
|
September 1, 1988
Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo
D F Stern, M P Kamps, H Cao
Molecular and Cellular Biology
|
March 1, 1990
Tyrosine phosphorylation is an early and specific event involved in primary keratinocyte differentiation
E Filvaroff, D F Stern, G P Dotto
Molecular and Cellular Biology
|
May 1, 1986
p185, a product of the neu proto-oncogene, is a receptorlike protein associated with tyrosine kinase activity
D F Stern, P A Heffernan, R A Weinberg
Current Protocols in Molecular Biology
|
February 12, 2008
Production of antibodies that recognize specific tyrosine-phosphorylated peptides
M P Digiovanna, R R Roussel, D F Stern
Science (New York, N.Y.)
|
July 10, 1998
Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint
Z Sun, J Hsiao, D S Fay, et al.
The EMBO Journal
|
March 1, 1992
A subdomain in the transmembrane domain is necessary for p185neu* activation
H Cao, L Bangalore, B J Bormann, et al.
Molecular and Cellular Biology
|
February 1, 1991
Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine
D F Stern, P Zheng, D R Beidler, et al.
Page
of 7