Journal
VIROLOGY
Volume 445, Issue 1-2, Pages 115-137Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2013.04.026
Keywords
Papillomavirus; Viral oncogenes; Transformation; Cervical cancer; Notch; Telomerase; P53; Ubiquitin
Categories
Funding
- NIH [CA120352, CA08093, AG027388, DE019953)]
- University of Iowa Microbiology Developmental Grant
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Papillomaviruses induce benign and malignant epithelial tumors, and the viral E6 oncoprotein is essential for full transformation. E6 contributes to transformation by associating with cellular proteins, docking on specific acidic LXXLL peptide motifs found on these proteins. This review examines insights from recent studies of human and animal E6 proteins that determine the three-dimensional structure of E6 when bound to acidic LXXLL peptides. The structure of E6 is related to recent advances in the purification and identification of E6 associated protein complexes. These E6 protein-complexes, together with other proteins that bind to E6, alter a broad array of biological outcomes including modulation of cell survival, cellular transcription, host cell differentiation, growth factor dependence, DNA damage responses, and cell cycle progression. (C) 2013 Elsevier Inc. All rights reserved.
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