메뉴 건너뛰기




Volumn 10, Issue 3, 2014, Pages

Structural and Functional Characterization of a Complex between the Acidic Transactivation Domain of EBNA2 and the Tfb1/p62 Subunit of TFIIH

Author keywords

[No Author keywords available]

Indexed keywords

EPSTEIN BARR VIRUS ANTIGEN 2; PROTEIN P53; PROTEIN P62; PROTEIN TFB1; REGULATOR PROTEIN; TRANSCRIPTION FACTOR IIH; UNCLASSIFIED DRUG;

EID: 84897434052     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004042     Document Type: Article
Times cited : (29)

References (67)
  • 1
  • 2
    • 0017197974 scopus 로고
    • Infectious mononucleosis. Epstein-Barr-virus shedding in saliva and the oropharynx
    • Niederman JC, Miller G, Pearson HA, Pagano JS, Dowaliby JM, (1976) Infectious mononucleosis. Epstein-Barr-virus shedding in saliva and the oropharynx. N Engl J Med 294: 1355-1359.
    • (1976) N Engl J Med , vol.294 , pp. 1355-1359
    • Niederman, J.C.1    Miller, G.2    Pearson, H.A.3    Pagano, J.S.4    Dowaliby, J.M.5
  • 3
    • 67650882553 scopus 로고    scopus 로고
    • Features distinguishing Epstein-Barr virus infections of epithelial cells and B cells: viral genome expression, genome maintenance, and genome amplification
    • Shannon-Lowe C, Adland E, Bell AI, Delecluse HJ, Rickinson AB, 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.
    • (2009) J Virol , vol.83 , pp. 7749-7760
    • Shannon-Lowe, C.1    Adland, E.2    Bell, A.I.3    Delecluse, H.J.4    Rickinson, A.B.5
  • 4
    • 0025237712 scopus 로고
    • 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
    • Cordier M, Calender A, Billaud M, Zimber U, Rousselet G, 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.
    • (1990) J Virol , vol.64 , pp. 1002-1013
    • Cordier, M.1    Calender, A.2    Billaud, M.3    Zimber, U.4    Rousselet, G.5
  • 6
    • 0025819202 scopus 로고
    • Epstein-Barr virus latent membrane protein expression in Hodgkin and Reed-Sternberg cells
    • Herbst H, Dallenbach F, Hummel M, Niedobitek G, Pileri S, 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.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 4766-4770
    • Herbst, H.1    Dallenbach, F.2    Hummel, M.3    Niedobitek, G.4    Pileri, S.5
  • 7
    • 0014950290 scopus 로고
    • Epstein-Barr virus (EBV)-associated antibody patterns in malignant lymphoma and leukemia. I. Hodgkin's disease
    • Johansson B, Klein G, Henle W, Henle G, (1970) Epstein-Barr virus (EBV)-associated antibody patterns in malignant lymphoma and leukemia. I. Hodgkin's disease. Int J Cancer 6: 450-462.
    • (1970) Int J Cancer , vol.6 , pp. 450-462
    • Johansson, B.1    Klein, G.2    Henle, W.3    Henle, G.4
  • 8
    • 0022798705 scopus 로고
    • Restricted expression of EBV latent genes and T-lymphocyte-detected membrane antigen in Burkitt's lymphoma cells
    • Rowe DT, Rowe M, Evan GI, Wallace LE, Farrell PJ, 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.
    • (1986) EMBO J , vol.5 , pp. 2599-2607
    • Rowe, D.T.1    Rowe, M.2    Evan, G.I.3    Wallace, L.E.4    Farrell, P.J.5
  • 9
    • 49749222804 scopus 로고
    • Virsu particles in cultured lymphoblasts from Burkitt's lymphoma
    • Epstein MA, Achong BG, Barr YM, (1964) Virsu particles in cultured lymphoblasts from Burkitt's lymphoma. Lancet 1: 702-703.
    • (1964) Lancet , vol.1 , pp. 702-703
    • Epstein, M.A.1    Achong, B.G.2    Barr, Y.M.3
  • 10
    • 0023802718 scopus 로고
    • Expression of Epstein-Barr virus-encoded proteins in nasopharyngeal carcinoma
    • Fahraeus R, Fu HL, Ernberg I, Finke J, Rowe M, et al. (1988) Expression of Epstein-Barr virus-encoded proteins in nasopharyngeal carcinoma. Int J Cancer 42: 329-338.
    • (1988) Int J Cancer , vol.42 , pp. 329-338
    • Fahraeus, R.1    Fu, H.L.2    Ernberg, I.3    Finke, J.4    Rowe, M.5
  • 11
    • 0023881404 scopus 로고
    • Epstein-Barr virus gene expression in nasopharyngeal carcinoma
    • Young LS, Dawson CW, Clark D, Rupani H, Busson P, et al. (1988) Epstein-Barr virus gene expression in nasopharyngeal carcinoma. J Gen Virol 69 (Pt 5):: 1051-1065.
    • (1988) J Gen Virol , vol.69 , Issue.Pt 5 , pp. 1051-1065
    • Young, L.S.1    Dawson, C.W.2    Clark, D.3    Rupani, H.4    Busson, P.5
  • 12
    • 0033575762 scopus 로고    scopus 로고
    • Epstein-barr virus-infected resting memory B cells, not proliferating lymphoblasts, accumulate in the peripheral blood of immunosuppressed patients
    • Babcock GJ, Decker LL, Freeman RB, Thorley-Lawson DA, (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.
    • (1999) J Exp Med , vol.190 , pp. 567-576
    • Babcock, G.J.1    Decker, L.L.2    Freeman, R.B.3    Thorley-Lawson, D.A.4
  • 13
    • 0022394678 scopus 로고
    • Epstein-Barr virus infections and DNA hybridization studies in posttransplantation lymphoma and lymphoproliferative lesions: the role of primary infection
    • Ho M, Miller G, Atchison RW, Breinig MK, Dummer JS, 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.
    • (1985) J Infect Dis , vol.152 , pp. 876-886
    • Ho, M.1    Miller, G.2    Atchison, R.W.3    Breinig, M.K.4    Dummer, J.S.5
  • 14
    • 33645745240 scopus 로고    scopus 로고
    • Spectrum of Epstein-Barr virus-associated diseases
    • Kutok JL, Wang F, (2006) Spectrum of Epstein-Barr virus-associated diseases. Annu Rev Pathol 1: 375-404.
    • (2006) Annu Rev Pathol , vol.1 , pp. 375-404
    • Kutok, J.L.1    Wang, F.2
  • 15
    • 0025342480 scopus 로고
    • 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
    • Wang F, Gregory C, Sample C, Rowe M, Liebowitz D, 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.
    • (1990) J Virol , vol.64 , pp. 2309-2318
    • Wang, F.1    Gregory, C.2    Sample, C.3    Rowe, M.4    Liebowitz, D.5
  • 16
    • 0024317091 scopus 로고
    • Epstein-Barr virus nuclear protein 2 is a key determinant of lymphocyte transformation
    • Cohen JI, Wang F, Mannick J, Kieff E, (1989) Epstein-Barr virus nuclear protein 2 is a key determinant of lymphocyte transformation. Proc Natl Acad Sci U S A 86: 9558-9562.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 9558-9562
    • Cohen, J.I.1    Wang, F.2    Mannick, J.3    Kieff, E.4
  • 17
    • 0027479649 scopus 로고
    • Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation
    • Tomkinson B, Robertson E, Kieff E, (1993) Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation. J Virol 67: 2014-2025.
    • (1993) J Virol , vol.67 , pp. 2014-2025
    • Tomkinson, B.1    Robertson, E.2    Kieff, E.3
  • 18
    • 0027449255 scopus 로고
    • Epstein-Barr virus latent membrane protein 1 is essential for B-lymphocyte growth transformation
    • Kaye KM, Izumi KM, Kieff E, (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.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 9150-9154
    • Kaye, K.M.1    Izumi, K.M.2    Kieff, E.3
  • 19
    • 0025750139 scopus 로고
    • The Epstein-Barr virus nuclear protein encoded by the leader of the EBNA RNAs is important in B-lymphocyte transformation
    • Mannick JB, Cohen JI, Birkenbach M, Marchini A, Kieff E, (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.
    • (1991) J Virol , vol.65 , pp. 6826-6837
    • Mannick, J.B.1    Cohen, J.I.2    Birkenbach, M.3    Marchini, A.4    Kieff, E.5
  • 20
    • 0025274390 scopus 로고
    • Epstein-Barr virus nuclear antigen 2 induces expression of the virus-encoded latent membrane protein
    • Abbot SD, Rowe M, Cadwallader K, Ricksten A, Gordon J, et al. (1990) Epstein-Barr virus nuclear antigen 2 induces expression of the virus-encoded latent membrane protein. J Virol 64: 2126-2134.
    • (1990) J Virol , vol.64 , pp. 2126-2134
    • Abbot, S.D.1    Rowe, M.2    Cadwallader, K.3    Ricksten, A.4    Gordon, J.5
  • 21
    • 0025114515 scopus 로고
    • Epstein-Barr virus-encoded nuclear antigen 2 activates the viral latent membrane protein promoter by modulating the activity of a negative regulatory element
    • Fahraeus R, Jansson A, Ricksten A, Sjoblom A, Rymo L, (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.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 7390-7394
    • Fahraeus, R.1    Jansson, A.2    Ricksten, A.3    Sjoblom, A.4    Rymo, L.5
  • 22
    • 0025285021 scopus 로고
    • Epstein-Barr virus nuclear antigen 2 transactivates latent membrane protein LMP1
    • Wang F, Tsang SF, Kurilla MG, Cohen JI, Kieff E, (1990) Epstein-Barr virus nuclear antigen 2 transactivates latent membrane protein LMP1. J Virol 64: 3407-3416.
    • (1990) J Virol , vol.64 , pp. 3407-3416
    • Wang, F.1    Tsang, S.F.2    Kurilla, M.G.3    Cohen, J.I.4    Kieff, E.5
  • 23
    • 0025892705 scopus 로고
    • Role for the Epstein-Barr virus nuclear antigen 2 in viral promoter switching during initial stages of infection
    • Woisetschlaeger M, Jin XW, Yandava CN, Furmanski LA, Strominger JL, 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.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3942-3946
    • Woisetschlaeger, M.1    Jin, X.W.2    Yandava, C.N.3    Furmanski, L.A.4    Strominger, J.L.5
  • 24
    • 0024375760 scopus 로고
    • Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes
    • Hammerschmidt W, Sugden B, (1989) Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes. Nature 340: 393-397.
    • (1989) Nature , vol.340 , pp. 393-397
    • Hammerschmidt, W.1    Sugden, B.2
  • 25
    • 0027358873 scopus 로고
    • The Epstein-Barr virus immortalizing protein EBNA-2 is targeted to DNA by a cellular enhancer-binding protein
    • Ling PD, Rawlins DR, Hayward SD, (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.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 9237-9241
    • Ling, P.D.1    Rawlins, D.R.2    Hayward, S.D.3
  • 26
    • 0028124316 scopus 로고
    • The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J kappa recombination signal binding protein
    • Grossman SR, Johannsen E, Tong X, Yalamanchili R, Kieff E, (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.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 7568-7572
    • Grossman, S.R.1    Johannsen, E.2    Tong, X.3    Yalamanchili, R.4    Kieff, E.5
  • 27
    • 0028133036 scopus 로고
    • Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa
    • Henkel T, Ling PD, Hayward SD, Peterson MG, (1994) Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa. Science 265: 92-95.
    • (1994) Science , vol.265 , pp. 92-95
    • Henkel, T.1    Ling, P.D.2    Hayward, S.D.3    Peterson, M.G.4
  • 28
    • 0028171081 scopus 로고
    • The human J kappa recombination signal sequence binding protein (RBP-J kappa) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements
    • Waltzer L, Logeat F, Brou C, Israel A, Sergeant A, 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.
    • (1994) EMBO J , vol.13 , pp. 5633-5638
    • Waltzer, L.1    Logeat, F.2    Brou, C.3    Israel, A.4    Sergeant, A.5
  • 29
    • 0028063483 scopus 로고
    • 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
    • Zimber-Strobl U, Strobl LJ, Meitinger C, Hinrichs R, Sakai T, 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.
    • (1994) EMBO J , vol.13 , pp. 4973-4982
    • Zimber-Strobl, U.1    Strobl, L.J.2    Meitinger, C.3    Hinrichs, R.4    Sakai, T.5
  • 30
    • 0025739303 scopus 로고
    • EBNA-2 transactivates a lymphoid-specific enhancer in the BamHI C promoter of Epstein-Barr virus
    • Sung NS, Kenney S, Gutsch D, Pagano JS, (1991) EBNA-2 transactivates a lymphoid-specific enhancer in the BamHI C promoter of Epstein-Barr virus. J Virol 65: 2164-2169.
    • (1991) J Virol , vol.65 , pp. 2164-2169
    • Sung, N.S.1    Kenney, S.2    Gutsch, D.3    Pagano, J.S.4
  • 31
    • 0027290634 scopus 로고
    • Cell phenotype-dependent control of Epstein-Barr virus latent membrane protein 1 gene regulatory sequences
    • Fahraeus R, Jansson A, Sjoblom A, Nilsson T, Klein G, et al. (1993) Cell phenotype-dependent control of Epstein-Barr virus latent membrane protein 1 gene regulatory sequences. Virology 195: 71-80.
    • (1993) Virology , vol.195 , pp. 71-80
    • Fahraeus, R.1    Jansson, A.2    Sjoblom, A.3    Nilsson, T.4    Klein, G.5
  • 32
    • 0025719718 scopus 로고
    • Delineation of the cis-acting element mediating EBNA-2 transactivation of latent infection membrane protein expression
    • Tsang SF, Wang F, Izumi KM, Kieff E, (1991) Delineation of the cis-acting element mediating EBNA-2 transactivation of latent infection membrane protein expression. J Virol 65: 6765-6771.
    • (1991) J Virol , vol.65 , pp. 6765-6771
    • Tsang, S.F.1    Wang, F.2    Izumi, K.M.3    Kieff, E.4
  • 33
    • 0028897411 scopus 로고
    • The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2
    • Tong X, Drapkin R, Reinberg D, Kieff E, (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.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3259-3263
    • Tong, X.1    Drapkin, R.2    Reinberg, D.3    Kieff, E.4
  • 34
    • 0029131021 scopus 로고
    • The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE
    • Tong X, Drapkin R, Yalamanchili R, Mosialos G, Kieff E, (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.
    • (1995) Mol Cell Biol , vol.15 , pp. 4735-4744
    • Tong, X.1    Drapkin, R.2    Yalamanchili, R.3    Mosialos, G.4    Kieff, E.5
  • 35
    • 0028924735 scopus 로고
    • The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein
    • Tong X, Wang F, Thut CJ, Kieff E, (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.
    • (1995) J Virol , vol.69 , pp. 585-588
    • Tong, X.1    Wang, F.2    Thut, C.J.3    Kieff, E.4
  • 36
    • 0026086344 scopus 로고
    • An Epstein-Barr virus nuclear protein 2 domain essential for transformation is a direct transcriptional activator
    • Cohen JI, Kieff E, (1991) An Epstein-Barr virus nuclear protein 2 domain essential for transformation is a direct transcriptional activator. J Virol 65: 5880-5885.
    • (1991) J Virol , vol.65 , pp. 5880-5885
    • Cohen, J.I.1    Kieff, E.2
  • 37
    • 0025834279 scopus 로고
    • Epstein-Barr virus nuclear protein 2 mutations define essential domains for transformation and transactivation
    • Cohen JI, Wang F, Kieff E, (1991) Epstein-Barr virus nuclear protein 2 mutations define essential domains for transformation and transactivation. J Virol 65: 2545-2554.
    • (1991) J Virol , vol.65 , pp. 2545-2554
    • Cohen, J.I.1    Wang, F.2    Kieff, E.3
  • 38
    • 0034602777 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear protein 2 interacts with p300, CBP, and PCAF histone acetyltransferases in activation of the LMP1 promoter
    • Wang L, Grossman SR, Kieff E, (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.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 430-435
    • Wang, L.1    Grossman, S.R.2    Kieff, E.3
  • 39
    • 19644388865 scopus 로고    scopus 로고
    • NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites
    • Di Lello P, Nguyen BD, Jones TN, Potempa K, Kobor MS, 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.
    • (2005) Biochemistry , vol.44 , pp. 7678-7686
    • Di Lello, P.1    Nguyen, B.D.2    Jones, T.N.3    Potempa, K.4    Kobor, M.S.5
  • 40
    • 33745214419 scopus 로고    scopus 로고
    • Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53
    • Di Lello P, Jenkins LM, Jones TN, Nguyen BD, Hara T, 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.
    • (2006) Mol Cell , vol.22 , pp. 731-740
    • Di Lello, P.1    Jenkins, L.M.2    Jones, T.N.3    Nguyen, B.D.4    Hara, T.5
  • 41
    • 49449118629 scopus 로고    scopus 로고
    • NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53
    • Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, 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.
    • (2008) J Am Chem Soc , vol.130 , pp. 10596-10604
    • Langlois, C.1    Mas, C.2    Di Lello, P.3    Jenkins, L.M.4    Legault, P.5
  • 43
    • 66149124079 scopus 로고    scopus 로고
    • Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2
    • Ferreon JC, Lee CW, Arai M, Martinez-Yamout MA, Dyson HJ, 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.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 6591-6596
    • Ferreon, J.C.1    Lee, C.W.2    Arai, M.3    Martinez-Yamout, M.A.4    Dyson, H.J.5
  • 44
    • 34249863018 scopus 로고    scopus 로고
    • Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53
    • Teufel DP, Freund SM, Bycroft M, Fersht AR, (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.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7009-7014
    • Teufel, D.P.1    Freund, S.M.2    Bycroft, M.3    Fersht, A.R.4
  • 45
    • 0026645980 scopus 로고
    • A region of herpes simplex virus VP16 can substitute for a transforming domain of Epstein-Barr virus nuclear protein 2
    • Cohen JI, (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.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 8030-8034
    • Cohen, J.I.1
  • 46
    • 0027983521 scopus 로고
    • Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53
    • Xiao H, Pearson A, Coulombe B, Truant R, Zhang S, et al. (1994) Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53. Mol Cell Biol 14: 7013-7024.
    • (1994) Mol Cell Biol , vol.14 , pp. 7013-7024
    • Xiao, H.1    Pearson, A.2    Coulombe, B.3    Truant, R.4    Zhang, S.5
  • 47
    • 0030690423 scopus 로고    scopus 로고
    • Modular organization of the E2F1 activation domain and its interaction with general transcription factors TBP and TFIIH
    • Pearson A, Greenblatt J, (1997) Modular organization of the E2F1 activation domain and its interaction with general transcription factors TBP and TFIIH. Oncogene 15: 2643-2658.
    • (1997) Oncogene , vol.15 , pp. 2643-2658
    • Pearson, A.1    Greenblatt, J.2
  • 48
    • 0030987367 scopus 로고    scopus 로고
    • Transactivation by CIITA, the type II bare lymphocyte syndrome-associated factor, requires participation of multiple regions of the TATA box binding protein
    • Mahanta SK, Scholl T, Yang FC, Strominger JL, (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.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 6324-6329
    • Mahanta, S.K.1    Scholl, T.2    Yang, F.C.3    Strominger, J.L.4
  • 49
    • 33747605357 scopus 로고    scopus 로고
    • Recruitment of TFIIH to the HIV LTR is a rate-limiting step in the emergence of HIV from latency
    • Kim YK, Bourgeois CF, Pearson R, Tyagi M, West MJ, 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.
    • (2006) EMBO J , vol.25 , pp. 3596-3604
    • Kim, Y.K.1    Bourgeois, C.F.2    Pearson, R.3    Tyagi, M.4    West, M.J.5
  • 50
    • 0027402497 scopus 로고
    • Pattern of aromatic and hydrophobic amino acids critical for one of two subdomains of the VP16 transcriptional activator
    • Regier JL, Shen F, Triezenberg SJ, (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.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 883-887
    • Regier, J.L.1    Shen, F.2    Triezenberg, S.J.3
  • 51
    • 0027945048 scopus 로고
    • Mutational analysis of the transcription activation domain of RelA: identification of a highly synergistic minimal acidic activation module
    • Blair WS, Bogerd HP, Madore SJ, Cullen BR, (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.
    • (1994) Mol Cell Biol , vol.14 , pp. 7226-7234
    • Blair, W.S.1    Bogerd, H.P.2    Madore, S.J.3    Cullen, B.R.4
  • 52
    • 0027359429 scopus 로고
    • Effect of a single aspartate on helix stability at different positions in a neutral alanine-based peptide
    • Huyghues-Despointes BM, Scholtz JM, Baldwin RL, (1993) Effect of a single aspartate on helix stability at different positions in a neutral alanine-based peptide. Protein Sci 2: 1604-1611.
    • (1993) Protein Sci , vol.2 , pp. 1604-1611
    • Huyghues-Despointes, B.M.1    Scholtz, J.M.2    Baldwin, R.L.3
  • 53
    • 0027497118 scopus 로고
    • The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
    • Scholtz JM, Qian H, Robbins VH, Baldwin RL, (1993) The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry 32: 9668-9676.
    • (1993) Biochemistry , vol.32 , pp. 9668-9676
    • Scholtz, J.M.1    Qian, H.2    Robbins, V.H.3    Baldwin, R.L.4
  • 56
    • 11144358282 scopus 로고    scopus 로고
    • Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preferences
    • Houtman JC, Higashimoto Y, Dimasi N, Cho S, Yamaguchi H, et al. (2004) Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preferences. Biochemistry 43: 4170-4178.
    • (2004) Biochemistry , vol.43 , pp. 4170-4178
    • Houtman, J.C.1    Higashimoto, Y.2    Dimasi, N.3    Cho, S.4    Yamaguchi, H.5
  • 57
    • 15844398113 scopus 로고    scopus 로고
    • 1H, 15N, and 13C resonance assignment of the amino-terminal domain of the Tfb1 subunit of yeast TFIIH
    • Nguyen BD, Di Lello P, Legault P, Omichinski JG, (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.
    • (2005) J Biomol NMR , vol.31 , pp. 173-174
    • Nguyen, B.D.1    Di Lello, P.2    Legault, P.3    Omichinski, J.G.4
  • 59
    • 0028541866 scopus 로고
    • 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
    • Zhang O, Kay LE, Olivier JP, Forman-Kay JD, (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.
    • (1994) J Biomol NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 60
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 61
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: development of a software pipeline
    • Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, et al. (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59: 687-696.
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1    Boucher, W.2    Stevens, T.J.3    Fogh, R.H.4    Pajon, A.5
  • 62
    • 0001083043 scopus 로고    scopus 로고
    • Treatment of NOE constraints involving equivalent or nonstereoassigned protons in calculations of biomacromolecular structures
    • Fletcher CM, Jones DN, Diamond R, Neuhaus D, (1996) Treatment of NOE constraints involving equivalent or nonstereoassigned protons in calculations of biomacromolecular structures. J Biomol NMR 8: 292-310.
    • (1996) J Biomol NMR , vol.8 , pp. 292-310
    • Fletcher, C.M.1    Jones, D.N.2    Diamond, R.3    Neuhaus, D.4
  • 63
    • 84880132018 scopus 로고    scopus 로고
    • Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks
    • Shen Y, Bax A, (2013) Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks. J Biomol NMR 56: 227-241.
    • (2013) J Biomol NMR , vol.56 , pp. 227-241
    • Shen, Y.1    Bax, A.2
  • 65
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM, (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8: 477-486.
    • (1996) J Biomol NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 66
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K, (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14: 51-55, 29-32.
    • (1996) J Mol Graph , vol.14
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 67
    • 84897430225 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System. Version 1.5.0.4. Schrödinger. LLC
    • The PyMOL Molecular Graphics System. Version 1.5.0.4. Schrödinger. LLC.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.