The E6AP Binding Pocket of the HPV16 E6 Oncoprotein Provides a Docking Site for a Small Inhibitory Peptide Unrelated to E6AP, Indicating Druggability of E6

Structure Based Identification and Characterization of Flavonoids That Disrupt Human Papillomavirus-16 E6 Function

(2013) Jonathan J. Cherry et al.   PLoS One

Using chemical shift perturbation to characterise ligand binding

(2013) Mike P. Williamson   PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Structural Basis for Hijacking of Cellular LxxLL Motifs by Papillomavirus E6 Oncoproteins

(2013) K. Zanier et al.   SCIENCE

Pocket-Based Drug Design: Exploring Pocket Space

(2012) Xiliang Zheng et al.   AAPS Journal

The Future of Peptide-based Drugs

(2012) David J. Craik et al.   Chemical Biology & Drug Design

Solution Structure Analysis of the HPV16 E6 Oncoprotein Reveals a Self-Association Mechanism Required for E6-Mediated Degradation of p53

(2012) Katia Zanier et al.   STRUCTURE

Emerging topics in human tumor virology

(2011) Felix Hoppe-Seyler et al.   INTERNATIONAL JOURNAL OF CANCER

Druggable pockets and binding site centric chemical space: a paradigm shift in drug discovery

(2010) Stéphanie Pérot et al.   DRUG DISCOVERY TODAY

Design and development of peptides and peptide mimetics as antagonists for therapeutic intervention

(2010) Jody M Mason   Future Medicinal Chemistry

The stability of the human papillomavirus E6 oncoprotein is E6AP dependent

(2009) Vjekoslav Tomaić et al.   VIROLOGY

Oncogenic activities of human papillomaviruses

(2009) Margaret E. McLaughlin-Drubin et al.   VIRUS RESEARCH

Oncogene Addiction

(2008) I. B. Weinstein et al.   CANCER RESEARCH

A novel peptide motif binding to and blocking the intracellular activity of the human papillomavirus E6 oncoprotein

(2008) Susanne Dymalla et al.   JOURNAL OF MOLECULAR MEDICINE-JMM