DYRK1A stabilizes HPV16E7 oncoprotein through phosphorylation of the threonine 5 and threonine 7 residues

E7 protein of human papilloma virus-16 induces degradation of retinoblastoma protein through the ubiquitin-proteasome pathway.

S N Boyer, David E. Wazer, Vimla Band · PubMed · 1996 · 931 citations

Life Sciences, Cell Biology, Molecular Biology +17

The region of the HPV E7 oncoprotein homologous to adenovirus E1a and Sv40 large T antigen contains separate domains for Rb binding and casein kinase II phosphorylation.

Miguel Barbosa, Charles G. Edmonds, Cynthia L. Fisher et al. · The EMBO Journal · 1990 · 331 citations · Full text

Life Sciences, Molecular Biology, Oncology +16

Degradation of the Retinoblastoma Tumor Suppressor by the Human Papillomavirus Type 16 E7 Oncoprotein Is Important for Functional Inactivation and Is Separable from Proteasomal Degradation of E7

Sonia L. Gonzalez, Matt Stremlau, Xi He et al. · Journal of Virology · 2001 · 320 citations · Full text

Life Sciences, Molecular Biology, Oncology +17

Human Papillomavirus Type 16 E7 Oncoprotein Associates with the Cullin 2 Ubiquitin Ligase Complex, Which Contributes to Degradation of the Retinoblastoma Tumor Suppressor

Kyung-Won Huh, Xiaobo Zhou, Hiroyuki Hayakawa et al. · Journal of Virology · 2007 · 286 citations · Full text

Medicine, Molecular Biology, Oncology +17

Sequence Characteristics, Subcellular Localization, and Substrate Specificity of DYRK-related Kinases, a Novel Family of Dual Specificity Protein Kinases

Walter Becker, Yvonne Weber, Kristiane Wetzel et al. · Journal of Biological Chemistry · 1998 · 286 citations · Full text

Life Sciences, Cell Biology, Molecular Biology +13