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Title: Monitoring HPV-16 E7 phosphorylation events

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.

Authors:
; ;
Publication Date:
OSTI Identifier:
22692244
Resource Type:
Journal Article
Journal Name:
Virology
Additional Journal Information:
Journal Volume: 503; Other Information: Copyright (c) 2017 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0042-6822
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CASEIN; METABOLISM; NEOPLASMS; NUCLEAR MAGNETIC RESONANCE; PHOSPHORYLATION; PHOSPHOTRANSFERASES; SPECTROSCOPY

Citation Formats

Nogueira, Marcela O., Hošek, Tomáš, and Calçada, Eduar. Monitoring HPV-16 E7 phosphorylation events. United States: N. p., 2017. Web. doi:10.1016/J.VIROL.2016.12.030.
Nogueira, Marcela O., Hošek, Tomáš, & Calçada, Eduar. Monitoring HPV-16 E7 phosphorylation events. United States. doi:10.1016/J.VIROL.2016.12.030.
Nogueira, Marcela O., Hošek, Tomáš, and Calçada, Eduar. Wed . "Monitoring HPV-16 E7 phosphorylation events". United States. doi:10.1016/J.VIROL.2016.12.030.
@article{osti_22692244,
title = {Monitoring HPV-16 E7 phosphorylation events},
author = {Nogueira, Marcela O. and Hošek, Tomáš and Calçada, Eduar},
abstractNote = {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.},
doi = {10.1016/J.VIROL.2016.12.030},
journal = {Virology},
issn = {0042-6822},
number = ,
volume = 503,
place = {United States},
year = {2017},
month = {3}
}