1. LuzuriagaK, SullivanJL (2010) Infectious mononucleosis. N Engl J Med 362: 1993–2000.
2. NiedermanJC, MillerG, PearsonHA, PaganoJS, DowalibyJM (1976) Infectious mononucleosis. Epstein-Barr-virus shedding in saliva and the oropharynx. N Engl J Med 294: 1355–1359.
3. Shannon-LoweC, AdlandE, BellAI, DelecluseHJ, RickinsonAB, et al. (2009) Features distinguishing Epstein-Barr virus infections of epithelial cells and B cells: viral genome expression, genome maintenance, and genome amplification. J Virol 83: 7749–7760.
4. CordierM, CalenderA, BillaudM, ZimberU, RousseletG, et al. (1990) Stable transfection of Epstein-Barr virus (EBV) nuclear antigen 2 in lymphoma cells containing the EBV P3HR1 genome induces expression of B-cell activation molecules CD21 and CD23. J Virol 64: 1002–1013.
5. BabcockGJ, DeckerLL, VolkM, Thorley-LawsonDA (1998) EBV persistence in memory B cells in vivo. Immunity 9: 395–404.
6. HerbstH, DallenbachF, HummelM, NiedobitekG, PileriS, et al. (1991) Epstein-Barr virus latent membrane protein expression in Hodgkin and Reed-Sternberg cells. Proc Natl Acad Sci U S A 88: 4766–4770.
7. JohanssonB, KleinG, HenleW, HenleG (1970) Epstein-Barr virus (EBV)-associated antibody patterns in malignant lymphoma and leukemia. I. Hodgkin's disease. Int J Cancer 6: 450–462.
8. RoweDT, RoweM, EvanGI, WallaceLE, FarrellPJ, et al. (1986) Restricted expression of EBV latent genes and T-lymphocyte-detected membrane antigen in Burkitt's lymphoma cells. EMBO J 5: 2599–2607.
9. EpsteinMA, AchongBG, BarrYM (1964) Virsu particles in cultured lymphoblasts from Burkitt's lymphoma. Lancet 1: 702–703.
10. FahraeusR, FuHL, ErnbergI, FinkeJ, RoweM, et al. (1988) Expression of Epstein-Barr virus-encoded proteins in nasopharyngeal carcinoma. Int J Cancer 42: 329–338.
11. YoungLS, DawsonCW, ClarkD, RupaniH, BussonP, et al. (1988) Epstein-Barr virus gene expression in nasopharyngeal carcinoma. J Gen Virol 69(Pt 5): 1051–1065.
12. BabcockGJ, DeckerLL, FreemanRB, Thorley-LawsonDA (1999) Epstein-barr virus-infected resting memory B cells, not proliferating lymphoblasts, accumulate in the peripheral blood of immunosuppressed patients. J Exp Med 190: 567–576.
13. HoM, MillerG, AtchisonRW, BreinigMK, DummerJS, et al. (1985) Epstein-Barr virus infections and DNA hybridization studies in posttransplantation lymphoma and lymphoproliferative lesions: the role of primary infection. J Infect Dis 152: 876–886.
14. KutokJL, WangF (2006) Spectrum of Epstein-Barr virus-associated diseases. Annu Rev Pathol 1: 375–404.
15. WangF, GregoryC, SampleC, RoweM, LiebowitzD, et al. (1990) Epstein-Barr virus latent membrane protein (LMP1) and nuclear proteins 2 and 3C are effectors of phenotypic changes in B lymphocytes: EBNA-2 and LMP1 cooperatively induce CD23. J Virol 64: 2309–2318.
16. CohenJI, WangF, MannickJ, KieffE (1989) Epstein-Barr virus nuclear protein 2 is a key determinant of lymphocyte transformation. Proc Natl Acad Sci U S A 86: 9558–9562.
17. TomkinsonB, RobertsonE, KieffE (1993) Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation. J Virol 67: 2014–2025.
18. KayeKM, IzumiKM, KieffE (1993) Epstein-Barr virus latent membrane protein 1 is essential for B-lymphocyte growth transformation. Proc Natl Acad Sci U S A 90: 9150–9154.
19. MannickJB, CohenJI, BirkenbachM, MarchiniA, KieffE (1991) The Epstein-Barr virus nuclear protein encoded by the leader of the EBNA RNAs is important in B-lymphocyte transformation. J Virol 65: 6826–6837.
20. AbbotSD, RoweM, CadwalladerK, RickstenA, GordonJ, et al. (1990) Epstein-Barr virus nuclear antigen 2 induces expression of the virus-encoded latent membrane protein. J Virol 64: 2126–2134.
21. FahraeusR, JanssonA, RickstenA, SjoblomA, RymoL (1990) Epstein-Barr virus-encoded nuclear antigen 2 activates the viral latent membrane protein promoter by modulating the activity of a negative regulatory element. Proc Natl Acad Sci U S A 87: 7390–7394.
22. WangF, TsangSF, KurillaMG, CohenJI, KieffE (1990) Epstein-Barr virus nuclear antigen 2 transactivates latent membrane protein LMP1. J Virol 64: 3407–3416.
23. WoisetschlaegerM, JinXW, YandavaCN, FurmanskiLA, StromingerJL, et al. (1991) Role for the Epstein-Barr virus nuclear antigen 2 in viral promoter switching during initial stages of infection. Proc Natl Acad Sci U S A 88: 3942–3946.
24. HammerschmidtW, SugdenB (1989) Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes. Nature 340: 393–397.
25. LingPD, RawlinsDR, HaywardSD (1993) The Epstein-Barr virus immortalizing protein EBNA-2 is targeted to DNA by a cellular enhancer-binding protein. Proc Natl Acad Sci U S A 90: 9237–9241.
26. GrossmanSR, JohannsenE, TongX, YalamanchiliR, KieffE (1994) The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J kappa recombination signal binding protein. Proc Natl Acad Sci U S A 91: 7568–7572.
27. HenkelT, LingPD, HaywardSD, PetersonMG (1994) Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa. Science 265: 92–95.
28. WaltzerL, LogeatF, BrouC, IsraelA, SergeantA, et al. (1994) The human J kappa recombination signal sequence binding protein (RBP-J kappa) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements. EMBO J 13: 5633–5638.
29. Zimber-StroblU, StroblLJ, MeitingerC, HinrichsR, SakaiT, et al. (1994) Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-J kappa, the homologue of Drosophila Suppressor of Hairless. EMBO J 13: 4973–4982.
30. SungNS, KenneyS, GutschD, PaganoJS (1991) EBNA-2 transactivates a lymphoid-specific enhancer in the BamHI C promoter of Epstein-Barr virus. J Virol 65: 2164–2169.
31. FahraeusR, JanssonA, SjoblomA, NilssonT, KleinG, et al. (1993) Cell phenotype-dependent control of Epstein-Barr virus latent membrane protein 1 gene regulatory sequences. Virology 195: 71–80.
32. TsangSF, WangF, IzumiKM, KieffE (1991) Delineation of the cis-acting element mediating EBNA-2 transactivation of latent infection membrane protein expression. J Virol 65: 6765–6771.
33. TongX, DrapkinR, ReinbergD, KieffE (1995) The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2. Proc Natl Acad Sci U S A 92: 3259–3263.
34. TongX, DrapkinR, YalamanchiliR, MosialosG, KieffE (1995) The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE. Mol Cell Biol 15: 4735–4744.
35. TongX, WangF, ThutCJ, KieffE (1995) The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein. J Virol 69: 585–588.
36. CohenJI, KieffE (1991) An Epstein-Barr virus nuclear protein 2 domain essential for transformation is a direct transcriptional activator. J Virol 65: 5880–5885.
37. CohenJI, WangF, KieffE (1991) Epstein-Barr virus nuclear protein 2 mutations define essential domains for transformation and transactivation. J Virol 65: 2545–2554.
38. WangL, GrossmanSR, KieffE (2000) Epstein-Barr virus nuclear protein 2 interacts with p300, CBP, and PCAF histone acetyltransferases in activation of the LMP1 promoter. Proc Natl Acad Sci U S A 97: 430–435.
39. Di LelloP, NguyenBD, JonesTN, PotempaK, KoborMS, et al. (2005) NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites. Biochemistry 44: 7678–7686.
40. Di LelloP, JenkinsLM, JonesTN, NguyenBD, HaraT, et al. (2006) Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53. Mol Cell 22: 731–740.
41. LangloisC, MasC, Di LelloP, JenkinsLM, LegaultP, et al. (2008) NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. J Am Chem Soc 130: 10596–10604.
42. Di LelloP, Miller JenkinsLM, MasC, LangloisC, MalitskayaE, et al. (2008) p53 and TFIIEalpha share a common binding site on the Tfb1/p62 subunit of TFIIH. Proc Natl Acad Sci U S A 105: 106–111.
43. FerreonJC, LeeCW, AraiM, Martinez-YamoutMA, DysonHJ, et al. (2009) Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2. Proc Natl Acad Sci U S A 106: 6591–6596.
44. TeufelDP, FreundSM, BycroftM, FershtAR (2007) Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53. Proc Natl Acad Sci U S A 104: 7009–7014.
45. CohenJI (1992) A region of herpes simplex virus VP16 can substitute for a transforming domain of Epstein-Barr virus nuclear protein 2. Proc Natl Acad Sci U S A 89: 8030–8034.
46. XiaoH, PearsonA, CoulombeB, TruantR, ZhangS, et al. (1994) Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53. Mol Cell Biol 14: 7013–7024.
47. PearsonA, GreenblattJ (1997) Modular organization of the E2F1 activation domain and its interaction with general transcription factors TBP and TFIIH. Oncogene 15: 2643–2658.
48. MahantaSK, SchollT, YangFC, StromingerJL (1997) Transactivation by CIITA, the type II bare lymphocyte syndrome-associated factor, requires participation of multiple regions of the TATA box binding protein. Proc Natl Acad Sci U S A 94: 6324–6329.
49. KimYK, BourgeoisCF, PearsonR, TyagiM, WestMJ, et al. (2006) Recruitment of TFIIH to the HIV LTR is a rate-limiting step in the emergence of HIV from latency. EMBO J 25: 3596–3604.
50. RegierJL, ShenF, TriezenbergSJ (1993) Pattern of aromatic and hydrophobic amino acids critical for one of two subdomains of the VP16 transcriptional activator. Proc Natl Acad Sci U S A 90: 883–887.
51. BlairWS, BogerdHP, MadoreSJ, CullenBR (1994) Mutational analysis of the transcription activation domain of RelA: identification of a highly synergistic minimal acidic activation module. Mol Cell Biol 14: 7226–7234.
52. Huyghues-DespointesBM, ScholtzJM, BaldwinRL (1993) Effect of a single aspartate on helix stability at different positions in a neutral alanine-based peptide. Protein Sci 2: 1604–1611.
53. ScholtzJM, QianH, RobbinsVH, BaldwinRL (1993) The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry 32: 9668–9676.
54. Ausubel FM BR, Kingston RE, Moore DD, Smith JA, Struhl K (1997) Current Protocols in Molecular Biology (Wiley, New York).
55. LangloisC, Del GattoA, ArseneaultG, Lafrance-VanasseJ, De SimoneM, et al. (2012) Structure-based design of a potent artificial transactivation domain based on p53. J Am Chem Soc 134: 1715–1723.
56. HoutmanJC, HigashimotoY, DimasiN, ChoS, YamaguchiH, et al. (2004) Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preferences. Biochemistry 43: 4170–4178.
57. NguyenBD, Di LelloP, LegaultP, OmichinskiJG (2005) 1H, 15N, and 13C resonance assignment of the amino-terminal domain of the Tfb1 subunit of yeast TFIIH. J Biomol NMR 31: 173–174.
58. PascalSM, MuhandiramDR, YamazakiT, Forman-KayJD, KayLE (1994) Simultaneous acquisition of 15N- and 13C-edited NOE spectra of proteins dissolved in H2O. J Magn Reson A 197–201.
59. ZhangO, KayLE, OlivierJP, Forman-KayJD (1994) Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 4: 845–858.
60. DelaglioF, GrzesiekS, VuisterGW, ZhuG, PfeiferJ, et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277–293.
61. VrankenWF, BoucherW, StevensTJ, FoghRH, PajonA, et al. (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59: 687–696.
62. FletcherCM, JonesDN, DiamondR, NeuhausD (1996) Treatment of NOE constraints involving equivalent or nonstereoassigned protons in calculations of biomacromolecular structures. J Biomol NMR 8: 292–310.
63. ShenY, BaxA (2013) Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks. J Biomol NMR 56: 227–241.
64. BrungerAT, AdamsPD, CloreGM, DeLanoWL, GrosP, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54: 905–921.
65. LaskowskiRA, RullmannnJA, MacArthurMW, KapteinR, ThorntonJM (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8: 477–486.
66. KoradiR, BilleterM, WuthrichK (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14: 51–55, 29–32.
67. The PyMOL Molecular Graphics System. Version 18.104.22.168. Schrödinger. LLC.