L. R. Krumpe and T. Mori, The Use of Phage-Displayed Peptide Libraries to Develop Tumor-Targeting Drugs, International Journal of Peptide Research and Therapeutics, vol.12, pp.79-91, 2006.

L. Yu, Phage display screening against a set of targets to establish peptide-based sugar mimetics and molecular docking to predict binding site, Bioorganic & medicinal chemistry, vol.17, pp.4825-4832, 2009.

D. Zhang, A CD44 specific peptide developed by phage display for targeting gastric cancer, Biotechnology letters, vol.37, pp.2311-2320, 2015.

C. Zhou, J. Kang, X. Wang, W. Wei, and W. Jiang, Phage display screening identifies a novel peptide to suppress ovarian cancer cells in vitro and in vivo in mouse models, BMC cancer, vol.15, 2015.

C. Ma, Screening of a specific peptide binding to esophageal squamous carcinoma cells from phage displayed peptide library, Molecular and cellular probes, vol.29, pp.182-189, 2015.

P. Busson, C. Keryer, T. Ooka, and M. Corbex, EBV-associated nasopharyngeal carcinomas: from epidemiology to virus-targeting strategies, Trends in microbiology, vol.12, pp.356-360, 2004.
URL : https://hal.archives-ouvertes.fr/hal-00120139

S. W. Tsao, G. Tramoutanis, C. W. Dawson, A. K. Lo, and D. P. Huang, The significance of LMP1 expression in nasopharyngeal carcinoma, Seminars in cancer biology, vol.12, pp.473-487, 2002.

V. Soni, E. Cahir-mcfarland, and E. Kieff, LMP1 TRAFficking activates growth and survival pathways, Advances in experimental medicine and biology, vol.597, pp.173-187, 2007.

A. Kieser and K. R. Sterz, The Latent Membrane Protein 1 (LMP1), Current topics in microbiology and immunology, vol.391, pp.119-149, 2015.

A. G. Eliopoulos and L. S. Young, LMP1 structure and signal transduction, Seminars in cancer biology, vol.11, pp.435-444, 2001.

B. A. Mainou, D. N. Everly, and N. Raab-traub, Unique signaling properties of CTAR1 in LMP1-mediated transformation, Journal of virology, vol.81, pp.9680-9692, 2007.

F. Schneider, The viral oncoprotein LMP1 exploits TRADD for signaling by masking its apoptotic activity, PLoS biology, vol.6, 2008.

Z. X. Lu, Effect of EBV LMP1 targeted DNAzymes on cell proliferation and apoptosis, Cancer gene therapy, vol.12, pp.647-654, 2005.

A. K. Lo, Modulation of LMP1 protein expression by EBV-encoded microRNAs, Proceedings of the National Academy of Sciences of the United States of America, vol.104, pp.16164-16169, 2007.

X. Tang, T cells expressing a LMP1-specific chimeric antigen receptor mediate antitumor effects against LMP1-positive nasopharyngeal carcinoma cells in vitro and in vivo, Journal of biomedical research, vol.28, pp.468-475, 2014.

Y. P. Mei, Silencing of LMP1 induces cell cycle arrest and enhances chemosensitivity through inhibition of AKT signaling pathway in EBV-positive nasopharyngeal carcinoma cells, Cell cycle, vol.6, pp.1379-1385, 2007.

S. H. Hutajulu, J. Kurnianda, I. B. Tan, and J. M. Middeldorp, Therapeutic implications of Epstein-Barr virus infection for the treatment of nasopharyngeal carcinoma, Therapeutics and clinical risk management, vol.10, pp.721-736, 2014.

L. Yang, Targeting EBV-LMP1 DNAzyme enhances radiosensitivity of nasopharyngeal carcinoma cells by inhibiting telomerase activity, Cancer Biology & Therapy, vol.15, pp.61-68, 2014.

S. W. Tsao, The biology of EBV infection in human epithelial cells, Seminars in cancer biology, vol.22, pp.137-143, 2012.

K. H. Shair, C. I. Schnegg, and N. Raab-traub, EBV latent membrane protein 1 effects on plakoglobin, cell growth, and migration, Cancer research, vol.68, pp.6997-7005, 2008.

A. Hannigan and J. B. Wilson, Evaluation of LMP1 of Epstein-Barr virus as a therapeutic target by its inhibition, Mol Cancer, vol.9, 2010.

V. I. Romanov, Phage display selection and evaluation of cancer drug targets, Current cancer drug targets, vol.3, pp.119-129, 2003.

X. Dai, Identification of a novel aFGF-binding peptide with anti-tumor effect on breast cancer from phage display library, Biochemical and biophysical research communications, vol.445, pp.795-801, 2014.

L. Wang, Identification of a peptide specifically targeting ovarian cancer by the screening of a phage display peptide library, Oncology letters, vol.11, pp.4022-4026, 2016.

J. Han, The further characterization of the peptide specifically binding to gastric cancer, Molecular and cellular probes, vol.30, pp.125-131, 2016.

V. Soni, T. Yasui, E. Cahir-mcfarland, and E. Kieff, LMP1 Transmembrane Domain 1 and 2 (TM1-2) FWLY Mediates Intermolecular Interactions with TM3-6 To Activate NF-?B, Journal of virology, vol.80, pp.10787-10793, 2006.

Z. L. Pratt, J. Zhang, and B. Sugden, The latent membrane protein 1 (LMP1) oncogene of Epstein-Barr virus can simultaneously induce and inhibit apoptosis in B cells, Journal of virology, vol.86, pp.4380-4393, 2012.

C. D. Laherty, H. M. Hu, A. W. Opipari, F. Wang, and V. M. Dixit, The Epstein-Barr virus LMP1 gene product induces A20 zinc finger protein expression by activating nuclear factor kappa B, The Journal of biological chemistry, vol.267, pp.24157-24160, 1992.

Y. Tao, Structure of a eukaryotic SWEET transporter in a homotrimeric complex, Nature, vol.527, pp.259-263, 2015.

L. Vogeley, Anabaena Sensory Rhodopsin: A Photochromic Color Sensor at 2.0 Å, Science, vol.306, pp.1390-1393, 2004.

D. Jiang, Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A, Proceedings of the National Academy of Sciences of the United States of America, vol.110, pp.14664-14669, 2013.

R. G. Efremov and L. A. Sazanov, Structure of the membrane domain of respiratory complex I, Nature, vol.476, pp.414-420, 2011.

J. Zhang, J. Yang, R. Jang, Y. Zhang, and . Gpcr-i-tasser, A Hybrid Approach to G Protein-Coupled Receptor Structure Modeling and the Application to the Human Genome. Structure, vol.23, p.7, 1993.

I. W. Davis, MolProbity: all-atom contacts and structure validation for proteins and nucleic acids, Nucleic Acids Research, vol.35, pp.375-383, 2007.

N. Ammous-boukhris, Phage-display screening identifies LMP1-binding peptides targeting the C-terminus region of the EBV oncoprotein, Peptides, vol.85, pp.73-79, 2016.

E. Mashiach, An integrated suite of fast docking algorithms, Proteins, vol.78, pp.3197-3204, 2010.

N. Andrusier, R. Nussinov, and H. J. Wolfson, FireDock: fast interaction refinement in molecular docking, Proteins, vol.69, pp.139-159, 2007.

J. Zhang, Y. Liang, and Y. Zhang, Atomic-level protein structure refinement using fragment guided molecular dynamics conformation sampling, Structure, vol.19, pp.1784-1795, 1993.