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I Suzuki-Takahashi

Showing results (1-10 of 13) with videos related to

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Biochemical and Biophysical Research Communications|May 19, 1997
Effects of exogenous p16INK4a on growth of cells with various status of cell-cycle regulatorsI Suzuki-Takahashi, H Higashi, E Yoshida, et al.
Biochemical and Biophysical Research Communications|February 24, 1997
Expression of p16INK4a suppresses the unbounded and anchorage-independent growth of a glioblastoma cell line that lacks p16INK4aH Higashi, I Suzuki-Takahashi, E Yoshida, et al.
Biochemical and Biophysical Research Communications|November 13, 1995
Differences in substrate specificity between Cdk2-cyclin A and Cdk2-cyclin E in vitroH Higashi, I Suzuki-Takahashi, Y Taya, et al.
European Journal of Biochemistry|April 15, 1996
Cyclin-dependent kinase-2 (Cdk2) forms an inactive complex with cyclin D1 since Cdk2 associated with cyclin D1 is not phosphorylated by Cdk7-cyclin-HH Higashi, I Suzuki-Takahashi, S Saitoh, et al.
Oncogene|January 19, 1995
Phosphorylation of E2F-1 by cyclin A-cdk2M Kitagawa, H Higashi, I Suzuki-Takahashi, et al.
The Journal of Biological Chemistry|May 4, 2001
Crystallographic approach to identification of cyclin-dependent kinase 4 (CDK4)-specific inhibitors by using CDK4 mimic CDK2 proteinM Ikuta, K Kamata, K Fukasawa, et al.
Oncogene|May 4, 1995
The interactions of E2F with pRB and with p107 are regulated via the phosphorylation of pRB and p107 by a cyclin-dependent kinaseI Suzuki-Takahashi, M Kitagawa, M Saijo, et al.
Oncogene|September 1, 1993
Butyrolactone I, a selective inhibitor of cdk2 and cdc2 kinaseM Kitagawa, T Okabe, H Ogino, et al.
The EMBO Journal|December 16, 1996
The consensus motif for phosphorylation by cyclin D1-Cdk4 is different from that for phosphorylation by cyclin A/E-Cdk2M Kitagawa, H Higashi, H K Jung, et al.
Molecular Pharmacology|July 11, 1998
J-104,871, a novel farnesyltransferase inhibitor, blocks Ras farnesylation in vivo in a farnesyl pyrophosphate-competitive mannerM Yonemoto, T Satoh, H Arakawa, et al.
Pageof 2

Showing results (1-10 of 13) with videos related to

Sort By:
Pageof 2
Biochemical and Biophysical Research Communications|May 19, 1997
Effects of exogenous p16INK4a on growth of cells with various status of cell-cycle regulatorsI Suzuki-Takahashi, H Higashi, E Yoshida, et al.
Biochemical and Biophysical Research Communications|February 24, 1997
Expression of p16INK4a suppresses the unbounded and anchorage-independent growth of a glioblastoma cell line that lacks p16INK4aH Higashi, I Suzuki-Takahashi, E Yoshida, et al.
Biochemical and Biophysical Research Communications|November 13, 1995
Differences in substrate specificity between Cdk2-cyclin A and Cdk2-cyclin E in vitroH Higashi, I Suzuki-Takahashi, Y Taya, et al.
European Journal of Biochemistry|April 15, 1996
Cyclin-dependent kinase-2 (Cdk2) forms an inactive complex with cyclin D1 since Cdk2 associated with cyclin D1 is not phosphorylated by Cdk7-cyclin-HH Higashi, I Suzuki-Takahashi, S Saitoh, et al.
Oncogene|January 19, 1995
Phosphorylation of E2F-1 by cyclin A-cdk2M Kitagawa, H Higashi, I Suzuki-Takahashi, et al.
The Journal of Biological Chemistry|May 4, 2001
Crystallographic approach to identification of cyclin-dependent kinase 4 (CDK4)-specific inhibitors by using CDK4 mimic CDK2 proteinM Ikuta, K Kamata, K Fukasawa, et al.
Oncogene|May 4, 1995
The interactions of E2F with pRB and with p107 are regulated via the phosphorylation of pRB and p107 by a cyclin-dependent kinaseI Suzuki-Takahashi, M Kitagawa, M Saijo, et al.
Oncogene|September 1, 1993
Butyrolactone I, a selective inhibitor of cdk2 and cdc2 kinaseM Kitagawa, T Okabe, H Ogino, et al.
The EMBO Journal|December 16, 1996
The consensus motif for phosphorylation by cyclin D1-Cdk4 is different from that for phosphorylation by cyclin A/E-Cdk2M Kitagawa, H Higashi, H K Jung, et al.
Molecular Pharmacology|July 11, 1998
J-104,871, a novel farnesyltransferase inhibitor, blocks Ras farnesylation in vivo in a farnesyl pyrophosphate-competitive mannerM Yonemoto, T Satoh, H Arakawa, et al.
Pageof 2