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Journal of Molecular and Cellular Cardiology
|
December 12, 2001
The last frontier in cardiovascular health: a landmark lecture for the XVII World Congress of the International Society for Heart Research
C Lenfant, J K Drugan, C A Roth
The Journal of Biological Chemistry
|
August 24, 2000
The Ras/p120 GTPase-activating protein (GAP) interaction is regulated by the p120 GAP pleckstrin homology domain
J K Drugan, K Rogers-Graham, T Gilmer, et al.
The Journal of Biological Chemistry
|
August 15, 1998
Identification of residues in the cysteine-rich domain of Raf-1 that control Ras binding and Raf-1 activity
D G Winkler, R E Cutler, J K Drugan, et al.
The Journal of Biological Chemistry
|
April 25, 2000
Elucidation of binding determinants and functional consequences of Ras/Raf-cysteine-rich domain interactions
J G Williams, J K Drugan, G S Yi, et al.
Oncogene
|
May 13, 1999
TC21 and Ras share indistinguishable transforming and differentiating activities
S M Graham, S M Oldham, C B Martin, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
February 20, 1996
Peptides containing a consensus Ras binding sequence from Raf-1 and theGTPase activating protein NF1 inhibit Ras function
G J Clark, J K Drugan, R S Terrell, et al.
The Journal of Biological Chemistry
|
April 28, 1995
Two distinct Raf domains mediate interaction with Ras
T R Brtva, J K Drugan, S Ghosh, et al.
The Journal of Biological Chemistry
|
January 5, 1996
Ras interaction with two distinct binding domains in Raf-1 may be required for Ras transformation
J K Drugan, R Khosravi-Far, M A White, et al.
The Journal of Biological Chemistry
|
August 22, 1997
14-3-3 zeta negatively regulates raf-1 activity by interactions with the Raf-1 cysteine-rich domain
G J Clark, J K Drugan, K L Rossman, et al.
The Journal of Biological Chemistry
|
May 10, 1996
Involvement of the switch 2 domain of Ras in its interaction with guanine nucleotide exchange factors
L A Quilliam, M M Hisaka, S Zhong, et al.
Page
of 1
Search research articles
Search
Showing results (1-10 of 10) with videos related to
Sort By:
Page
of 1
Journal of Molecular and Cellular Cardiology
|
December 12, 2001
The last frontier in cardiovascular health: a landmark lecture for the XVII World Congress of the International Society for Heart Research
C Lenfant, J K Drugan, C A Roth
The Journal of Biological Chemistry
|
August 24, 2000
The Ras/p120 GTPase-activating protein (GAP) interaction is regulated by the p120 GAP pleckstrin homology domain
J K Drugan, K Rogers-Graham, T Gilmer, et al.
The Journal of Biological Chemistry
|
August 15, 1998
Identification of residues in the cysteine-rich domain of Raf-1 that control Ras binding and Raf-1 activity
D G Winkler, R E Cutler, J K Drugan, et al.
The Journal of Biological Chemistry
|
April 25, 2000
Elucidation of binding determinants and functional consequences of Ras/Raf-cysteine-rich domain interactions
J G Williams, J K Drugan, G S Yi, et al.
Oncogene
|
May 13, 1999
TC21 and Ras share indistinguishable transforming and differentiating activities
S M Graham, S M Oldham, C B Martin, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
February 20, 1996
Peptides containing a consensus Ras binding sequence from Raf-1 and theGTPase activating protein NF1 inhibit Ras function
G J Clark, J K Drugan, R S Terrell, et al.
The Journal of Biological Chemistry
|
April 28, 1995
Two distinct Raf domains mediate interaction with Ras
T R Brtva, J K Drugan, S Ghosh, et al.
The Journal of Biological Chemistry
|
January 5, 1996
Ras interaction with two distinct binding domains in Raf-1 may be required for Ras transformation
J K Drugan, R Khosravi-Far, M A White, et al.
The Journal of Biological Chemistry
|
August 22, 1997
14-3-3 zeta negatively regulates raf-1 activity by interactions with the Raf-1 cysteine-rich domain
G J Clark, J K Drugan, K L Rossman, et al.
The Journal of Biological Chemistry
|
May 10, 1996
Involvement of the switch 2 domain of Ras in its interaction with guanine nucleotide exchange factors
L A Quilliam, M M Hisaka, S Zhong, et al.
Page
of 1