HPV-16 E7 is one of the key proteins that, by interfering with the host metabolism through many protein-protein interactions, hijacks cell regulation and contributes to malignancy. Here we report the high resolution investigation of the CR3 region of HPV-16 E7, both as an isolated domain and in the full-length protein. This opens the way to the atomic level study of the many interactions in which HPV-16 E7 is involved. Along these lines we show here the effect of one of the key post-translational modifications of HPV-16 E7, the phosphorylation by casein kinase II.

Monitoring HPV-16 E7 phosphorylation events / Marcela Oliveira, Nogueira; Hosek, Tomas; Eduardo O., Calçada; Castiglia, Francesca; Massimi, Paola; Banks, Lawrence; Felli, Isabella C.; Pierattelli, Roberta. - In: VIROLOGY. - ISSN 0042-6822. - STAMPA. - 503:(2017), pp. 70-75. [10.1016/j.virol.2016.12.030]

Monitoring HPV-16 E7 phosphorylation events

Nogueira, Marcela Oliveira;Hosek, Tomas;Calçada, Eduardo O.;Felli, Isabella C.
;
Pierattelli, Roberta
2017

Abstract

HPV-16 E7 is one of the key proteins that, by interfering with the host metabolism through many protein-protein interactions, hijacks cell regulation and contributes to malignancy. Here we report the high resolution investigation of the CR3 region of HPV-16 E7, both as an isolated domain and in the full-length protein. This opens the way to the atomic level study of the many interactions in which HPV-16 E7 is involved. Along these lines we show here the effect of one of the key post-translational modifications of HPV-16 E7, the phosphorylation by casein kinase II.
2017
503
70
75
Marcela Oliveira, Nogueira; Hosek, Tomas; Eduardo O., Calçada; Castiglia, Francesca; Massimi, Paola; Banks, Lawrence; Felli, Isabella C.; Pierattelli, Roberta
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1078349
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