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Volumn 85, Issue 11, 2011, Pages 5287-5300

A conserved amphipathic helix in the N-terminal regulatory region of the papillomavirus E1 helicase is required for efficient viral DNA replication

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; HELICASE; HUMAN PAPILLOMAVIRUS E1 HELICASE; HUMAN PAPILLOMAVIRUS E2 HELICASE; PROTEIN P53; PROTEIN P62; PROTEIN TFB1; PROTEIN VP16; PROTEIN VP16C; TRANSCRIPTION FACTOR IIH; UNCLASSIFIED DRUG; VIRUS DNA;

EID: 79956103105     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01829-10     Document Type: Article
Times cited : (21)

References (64)
  • 1
    • 0030872645 scopus 로고    scopus 로고
    • Interaction between replication protein A and p53 is disrupted after UV damage in a DNA repair-dependent manner
    • Abramova, N., J. Russell, M. Botchan, and R. Li. 1997. Interaction between replication protein A and p53 is disrupted after UV damage in a DNA repair-dependent manner. Proc. Natl. Acad. Sci. U. S. A. 94:7186-7191.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 7186-7191
    • Abramova, N.1    Russell, J.2    Botchan, M.3    Li, R.4
  • 2
    • 0034691115 scopus 로고    scopus 로고
    • Identification of domains of the HPV11 E1 protein required for DNA replication in vitro
    • Amin, A. A., et al. 2000. Identification of domains of the HPV11 E1 protein required for DNA replication in vitro. Virology 272:137-150.
    • (2000) Virology , vol.272 , pp. 137-150
    • Amin, A.A.1
  • 3
    • 34547879583 scopus 로고    scopus 로고
    • The SAGA continues: expanding the cellular role of a transcriptional co-activator complex
    • Baker, S. P., and P. A. Grant. 2007. The SAGA continues: expanding the cellular role of a transcriptional co-activator complex. Oncogene 26:5329-5340.
    • (2007) Oncogene , vol.26 , pp. 5329-5340
    • Baker, S.P.1    Grant, P.A.2
  • 4
    • 0035814797 scopus 로고    scopus 로고
    • Solution structure determination and mutational analysis of the papillomavirus E6 interacting peptide of E6AP
    • Be, X., et al. 2001. Solution structure determination and mutational analysis of the papillomavirus E6 interacting peptide of E6AP. Biochemistry 40: 1293-1299.
    • (2001) Biochemistry , vol.40 , pp. 1293-1299
    • Be, X.1
  • 5
    • 27344449049 scopus 로고    scopus 로고
    • Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A
    • Bochkareva, E., et al. 2005. Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A. Proc. Natl. Acad. Sci. U. S. A. 102:15412-15417.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15412-15417
    • Bochkareva, E.1
  • 6
    • 0033485261 scopus 로고    scopus 로고
    • Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation
    • Bulavin, D. V., et al. 1999. Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation. EMBO J. 18:6845-6854.
    • (1999) EMBO J , vol.18 , pp. 6845-6854
    • Bulavin, D.V.1
  • 7
    • 0030864137 scopus 로고    scopus 로고
    • Two tandem and independent sub-activation domains in the amino terminus of p53 require the adaptor complex for activity
    • Candau, R., et al. 1997. Two tandem and independent sub-activation domains in the amino terminus of p53 require the adaptor complex for activity. Oncogene 15:807-816.
    • (1997) Oncogene , vol.15 , pp. 807-816
    • Candau, R.1
  • 8
    • 79956082348 scopus 로고    scopus 로고
    • Clontech Laboratories, Inc. Clontech Laboratories, Inc., Mountain View, CA
    • a. Clontech Laboratories, Inc. 2009. Yeast protocols handbook: user manual. Clontech Laboratories, Inc., Mountain View, CA.
    • (2009) Yeast protocols handbook: user manual
  • 9
    • 38349090826 scopus 로고    scopus 로고
    • Human papillomavirus E1 helicase interacts with theWDrepeat protein p80 to promote maintenance of the viral genome in keratinocytes
    • Cote-Martin, A., et al. 2008. Human papillomavirus E1 helicase interacts with theWDrepeat protein p80 to promote maintenance of the viral genome in keratinocytes. J. Virol. 82:1271-1283.
    • (2008) J. Virol. , vol.82 , pp. 1271-1283
    • Cote-Martin, A.1
  • 10
    • 0024436944 scopus 로고
    • The C-terminal 79 amino acids of the herpes simplex virus regulatory protein, Vmw65, efficiently activate transcription in yeast and mammalian cells in chimeric DNAbinding proteins
    • Cousens, D., R. Greaves, C. Goding, and P. O'Hare. 1989. The C-terminal 79 amino acids of the herpes simplex virus regulatory protein, Vmw65, efficiently activate transcription in yeast and mammalian cells in chimeric DNAbinding proteins. EMBO J. 8:2337-2342.
    • (1989) EMBO J , vol.8 , pp. 2337-2342
    • Cousens, D.1    Greaves, R.2    Goding, C.3    O'Hare, P.4
  • 11
    • 0032520529 scopus 로고    scopus 로고
    • The human papillomavirus type 18 (HPV18) replication protein E1 is a transcriptional activator when interacting with HPV18 E2
    • Demeret, C., S. Goyat, M. Yaniv, and F. Thierry. 1998. The human papillomavirus type 18 (HPV18) replication protein E1 is a transcriptional activator when interacting with HPV18 E2. Virology 242:378-386.
    • (1998) Virology , vol.242 , pp. 378-386
    • Demeret, C.1    Goyat, S.2    Yaniv, M.3    Thierry, F.4
  • 12
    • 10044284508 scopus 로고    scopus 로고
    • Cyclin/CDK regulates the nucleocytoplasmic localization of the human papillomavirus E1 DNA helicase
    • Deng, W., et al. 2004. Cyclin/CDK regulates the nucleocytoplasmic localization of the human papillomavirus E1 DNA helicase. J. Virol. 78:13954-13965.
    • (2004) J. Virol. , vol.78 , pp. 13954-13965
    • Deng, W.1
  • 13
    • 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., 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
  • 14
    • 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., 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
  • 15
    • 14744285753 scopus 로고    scopus 로고
    • The papillomavirus life cycle
    • Doorbar, J. 2005. The papillomavirus life cycle. J. Clin. Virol. 32(Suppl. 1):S7-S15.
    • (2005) J. Clin. Virol. , vol.32 , Issue.SUPPL. 1
    • Doorbar, J.1
  • 16
    • 0027358857 scopus 로고
    • Inhibition of DNA replication factor RPA by p53
    • Dutta, A., J. M. Ruppert, J. C. Aster, and E. Winchester. 1993. Inhibition of DNA replication factor RPA by p53. Nature 365:79-82.
    • (1993) Nature , vol.365 , pp. 79-82
    • Dutta, A.1    Ruppert, J.M.2    Aster, J.C.3    Winchester, E.4
  • 17
    • 0017646950 scopus 로고
    • Chromatin-like structures obtained after alkaline disruption of bovine and human papillomaviruses
    • Favre, M., F. Breitburd, O. Croissant, and G. Orth. 1977. Chromatin-like structures obtained after alkaline disruption of bovine and human papillomaviruses. J. Virol. 21:1205-1209.
    • (1977) J. Virol. , vol.21 , pp. 1205-1209
    • Favre, M.1    Breitburd, F.2    Croissant, O.3    Orth, G.4
  • 18
    • 0025024469 scopus 로고
    • Presence of a potent transcription activating sequence in the p53 protein
    • Fields, S., and S. Jang. 1990. Presence of a potent transcription activating sequence in the p53 protein. Science 249:1046-1049.
    • (1990) Science , vol.249 , pp. 1046-1049
    • Fields, S.1    Jang, S.2
  • 19
    • 78049519078 scopus 로고    scopus 로고
    • Nuclear export of human papillomavirus type 31 E1 is regulated by Cdk2 phosphorylation and required for viral genome maintenance
    • Fradet-Turcotte, A., C. Moody, L. A. Laimins, and J. Archambault. 2010. Nuclear export of human papillomavirus type 31 E1 is regulated by Cdk2 phosphorylation and required for viral genome maintenance. J. Virol. 84: 11747-11760.
    • (2010) J. Virol. , vol.84 , pp. 11747-11760
    • Fradet-Turcotte, A.1    Moody, C.2    Laimins, L.A.3    Archambault, J.4
  • 20
    • 77049089459 scopus 로고    scopus 로고
    • Development of quantitative and high-throughput assays of polyomavirus and papillomavirus DNA replication
    • Fradet-Turcotte, A., G. Morin, M. Lehoux, P. A. Bullock, and J. Archambault. 2010. Development of quantitative and high-throughput assays of polyomavirus and papillomavirus DNA replication. Virology 399:65-76.
    • (2010) Virology , vol.399 , pp. 65-76
    • Fradet-Turcotte, A.1    Morin, G.2    Lehoux, M.3    Bullock, P.A.4    Archambault, J.5
  • 21
    • 34548151496 scopus 로고    scopus 로고
    • Quantitative analysis of the binding of simian virus 40 large T antigen to DNA
    • Fradet-Turcotte, A., C. Vincent, S. Joubert, P. A. Bullock, and J. Archambault. 2007. Quantitative analysis of the binding of simian virus 40 large T antigen to DNA. J. Virol. 81:9162-9174.
    • (2007) J. Virol. , vol.81 , pp. 9162-9174
    • Fradet-Turcotte, A.1    Vincent, C.2    Joubert, S.3    Bullock, P.A.4    Archambault, J.5
  • 22
    • 58249105355 scopus 로고    scopus 로고
    • Role of intrinsically disordered protein regions/domains in transcriptional regulation
    • Garza, A. S., N. Ahmad, and R. Kumar. 2009. Role of intrinsically disordered protein regions/domains in transcriptional regulation. Life Sci. 84:189-193.
    • (2009) Life Sci , vol.84 , pp. 189-193
    • Garza, A.S.1    Ahmad, N.2    Kumar, R.3
  • 23
    • 0037173615 scopus 로고    scopus 로고
    • Functional profiling of the Saccharomyces cerevisiae genome
    • Giaever, G., et al. 2002. Functional profiling of the Saccharomyces cerevisiae genome. Nature 418:387-391.
    • (2002) Nature , vol.418 , pp. 387-391
    • Giaever, G.1
  • 24
    • 0033060916 scopus 로고    scopus 로고
    • Interactions of the papovavirus DNA replication initiator proteins, bovine papillomavirus type 1 E1 and simian virus 40 large T antigen, with human replication protein A
    • Han, Y., Y. M. Loo, K. T. Militello, and T. Melendy. 1999. Interactions of the papovavirus DNA replication initiator proteins, bovine papillomavirus type 1 E1 and simian virus 40 large T antigen, with human replication protein A. J. Virol. 73:4899-4907.
    • (1999) J. Virol. , vol.73 , pp. 4899-4907
    • Han, Y.1    Loo, Y.M.2    Militello, K.T.3    Melendy, T.4
  • 25
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery, D. M., E. Kalkhoven, S. Hoare, and M. G. Parker. 1997. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387:733-736.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 26
    • 11144358282 scopus 로고    scopus 로고
    • Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preferences
    • Houtman, J. C., 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
  • 27
    • 0035821734 scopus 로고    scopus 로고
    • Novel human p53 mutations that are toxic to yeast can enhance transactivation of specific promoters and reactivate tumor p53 mutants
    • Inga, A., and M. A. Resnick. 2001. Novel human p53 mutations that are toxic to yeast can enhance transactivation of specific promoters and reactivate tumor p53 mutants. Oncogene 20:3409-3419.
    • (2001) Oncogene , vol.20 , pp. 3409-3419
    • Inga, A.1    Resnick, M.A.2
  • 28
    • 44349192171 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins based on the meta approach
    • Ishida, T., and K. Kinoshita. 2008. Prediction of disordered regions in proteins based on the meta approach. Bioinformatics 24:1344-1348.
    • (2008) Bioinformatics , vol.24 , pp. 1344-1348
    • Ishida, T.1    Kinoshita, K.2
  • 30
    • 0043123216 scopus 로고    scopus 로고
    • GeneSilico protein structure prediction meta-server
    • Kurowski, M. A., and J. M. Bujnicki. 2003. GeneSilico protein structure prediction meta-server. Nucleic Acids Res. 31:3305-3307.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3305-3307
    • Kurowski, M.A.1    Bujnicki, J.M.2
  • 31
    • 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., 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
  • 32
    • 0029841744 scopus 로고    scopus 로고
    • A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors
    • Le Douarin, B., et al. 1996. A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors. EMBO J. 15:6701-6715.
    • (1996) EMBO J , vol.15 , pp. 6701-6715
    • Le Douarin, B.1
  • 33
    • 0027394518 scopus 로고
    • The E1 replication protein of bovine papillomavirus type 1 contains an extended nuclear localization signal that includes a p34cdc2 phosphorylation site
    • Lentz, M. R., D. Pak, I. Mohr, and M. R. Botchan. 1993. The E1 replication protein of bovine papillomavirus type 1 contains an extended nuclear localization signal that includes a p34cdc2 phosphorylation site. J. Virol. 67:1414-1423.
    • (1993) J. Virol. , vol.67 , pp. 1414-1423
    • Lentz, M.R.1    Pak, D.2    Mohr, I.3    Botchan, M.R.4
  • 34
    • 0028226007 scopus 로고
    • Acidic transcription factors alleviate nucleosome-mediated repression of DNA replication of bovine papillomavirus type 1
    • Li, R., and M. R. Botchan. 1994. Acidic transcription factors alleviate nucleosome-mediated repression of DNA replication of bovine papillomavirus type 1. Proc. Natl. Acad. Sci. U. S. A. 91:7051-7055.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 7051-7055
    • Li, R.1    Botchan, M.R.2
  • 35
    • 0842304459 scopus 로고    scopus 로고
    • Recruitment of replication protein A by the papillomavirus E1 protein and modulation by single-stranded DNA
    • Loo, Y. M., and T. Melendy. 2004. Recruitment of replication protein A by the papillomavirus E1 protein and modulation by single-stranded DNA. J. Virol. 78:1605-1615.
    • (2004) J. Virol. , vol.78 , pp. 1605-1615
    • Loo, Y.M.1    Melendy, T.2
  • 36
    • 0023649184 scopus 로고
    • A new class of yeast transcriptional activators
    • Ma, J., and M. Ptashne. 1987. A new class of yeast transcriptional activators. Cell 51:113-119.
    • (1987) Cell , vol.51 , pp. 113-119
    • Ma, J.1    Ptashne, M.2
  • 37
    • 0031818287 scopus 로고    scopus 로고
    • A C-terminal helicase domain of the human papillomavirus E1 protein binds E2 and the DNA polymerase alpha-primase p68 subunit
    • Masterson, P. J., M. A. Stanley, A. P. Lewis, and M. A. Romanos. 1998. A C-terminal helicase domain of the human papillomavirus E1 protein binds E2 and the DNA polymerase alpha-primase p68 subunit. J. Virol. 72:7407-7419.
    • (1998) J. Virol. , vol.72 , pp. 7407-7419
    • Masterson, P.J.1    Stanley, M.A.2    Lewis, A.P.3    Romanos, M.A.4
  • 38
    • 37649012742 scopus 로고    scopus 로고
    • Human papillomaviruses activate caspases upon epithelial differentiation to induce viral genome amplification
    • Moody, C. A., A. Fradet-Turcotte, J. Archambault, and L. A. Laimins. 2007. Human papillomaviruses activate caspases upon epithelial differentiation to induce viral genome amplification. Proc. Natl. Acad. Sci. U. S. A. 104:19541-19546.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 19541-19546
    • Moody, C.A.1    Fradet-Turcotte, A.2    Archambault, J.3    Laimins, L.A.4
  • 39
    • 73349125474 scopus 로고    scopus 로고
    • Human papillomaviruses activate the ATM DNA damage pathway for viral genome amplification upon differentiation
    • Moody, C. A., and L. A. Laimins. 2009. Human papillomaviruses activate the ATM DNA damage pathway for viral genome amplification upon differentiation. PLoS Pathog. 5:e1000605.
    • (2009) PLoS Pathog , vol.5
    • Moody, C.A.1    Laimins, L.A.2
  • 40
    • 0342420551 scopus 로고    scopus 로고
    • Domains of the E1 protein of human papillomavirus type 33 involved in binding to the E2 protein
    • Muller, F., and M. Sapp. 1996. Domains of the E1 protein of human papillomavirus type 33 involved in binding to the E2 protein. Virology 219:247-256.
    • (1996) Virology , vol.219 , pp. 247-256
    • Muller, F.1    Sapp, M.2
  • 41
    • 0026600972 scopus 로고
    • Human p53 and CDC2Hs genes combine to inhibit the proliferation of Saccharomyces cerevisiae
    • Nigro, J. M., R. Sikorski, S. I. Reed, and B. Vogelstein. 1992. Human p53 and CDC2Hs genes combine to inhibit the proliferation of Saccharomyces cerevisiae. Mol. Cell. Biol. 12:1357-1365.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1357-1365
    • Nigro, J.M.1    Sikorski, R.2    Reed, S.I.3    Vogelstein, B.4
  • 42
    • 0034664733 scopus 로고    scopus 로고
    • p53AIP1, a potential mediator of p53-dependent apoptosis, and its regulation by Ser-46-phosphorylated p53
    • Oda, K., et al. 2000. p53AIP1, a potential mediator of p53-dependent apoptosis, and its regulation by Ser-46-phosphorylated p53. Cell 102:849-862.
    • (2000) Cell , vol.102 , pp. 849-862
    • Oda, K.1
  • 44
    • 47749130885 scopus 로고    scopus 로고
    • Intrinsic structural disorder in adenovirus E1A: a viral molecular hub linking multiple diverse processes
    • Pelka, P., J. N. Ablack, G. J. Fonseca, A. F. Yousef, and J. S. Mymryk. 2008. Intrinsic structural disorder in adenovirus E1A: a viral molecular hub linking multiple diverse processes. J. Virol. 82:7252-7263.
    • (2008) J. Virol. , vol.82 , pp. 7252-7263
    • Pelka, P.1    Ablack, J.N.2    Fonseca, G.J.3    Yousef, A.F.4    Mymryk, J.S.5
  • 45
    • 17444397116 scopus 로고    scopus 로고
    • Porter: a new, accurate server for protein secondary structure prediction
    • Pollastri, G., and A. McLysaght. 2005. Porter: a new, accurate server for protein secondary structure prediction. Bioinformatics 21:1719-1720.
    • (2005) Bioinformatics , vol.21 , pp. 1719-1720
    • Pollastri, G.1    McLysaght, A.2
  • 46
    • 69249116137 scopus 로고    scopus 로고
    • Interaction between the transactivation domain of p53 and PC4 exemplifies acidic activation domains as single-stranded DNA mimics
    • Rajagopalan, S., A. Andreeva, D. P. Teufel, S. M. Freund, and A. R. Fersht. 2009. Interaction between the transactivation domain of p53 and PC4 exemplifies acidic activation domains as single-stranded DNA mimics. J. Biol. Chem. 284:21728-21737.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21728-21737
    • Rajagopalan, S.1    Andreeva, A.2    Teufel, D.P.3    Freund, S.M.4    Fersht, A.R.5
  • 47
    • 0026429185 scopus 로고
    • Generating yeast transcriptional activators containing no yeast protein sequences
    • Ruden, D. M., J. Ma, Y. Li, K. Wood, and M. Ptashne. 1991. Generating yeast transcriptional activators containing no yeast protein sequences. Nature 350:250-252.
    • (1991) Nature , vol.350 , pp. 250-252
    • Ruden, D.M.1    Ma, J.2    Li, Y.3    Wood, K.4    Ptashne, M.5
  • 48
    • 33846027417 scopus 로고    scopus 로고
    • Amino acid substitutions that specifically impair the transcriptional activity of papillomavirus E2 affect binding to the long isoform of Brd4
    • Senechal, H., G. G. Poirier, B. Coulombe, L. A. Laimins, and J. Archambault. 2007. Amino acid substitutions that specifically impair the transcriptional activity of papillomavirus E2 affect binding to the long isoform of Brd4. Virology 358:10-17.
    • (2007) Virology , vol.358 , pp. 10-17
    • Senechal, H.1    Poirier, G.G.2    Coulombe, B.3    Laimins, L.A.4    Archambault, J.5
  • 49
    • 37149020787 scopus 로고    scopus 로고
    • The contribution of transactivation subdomains 1 and 2 to p53-induced gene expression is heterogeneous but not subdomain-specific
    • Smith, J. M., L. J. Stubbert, J. D. Hamill, and B. C. McKay. 2007. The contribution of transactivation subdomains 1 and 2 to p53-induced gene expression is heterogeneous but not subdomain-specific. Neoplasia 9:1057-1065.
    • (2007) Neoplasia , vol.9 , pp. 1057-1065
    • Smith, J.M.1    Stubbert, L.J.2    Hamill, J.D.3    McKay, B.C.4
  • 50
    • 0141891451 scopus 로고    scopus 로고
    • Initiation of DNA replication: lessons from viral initiator proteins
    • Stenlund, A. 2003. Initiation of DNA replication: lessons from viral initiator proteins. Nat. Rev. Mol. Cell Biol. 4:777-785.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 777-785
    • Stenlund, A.1
  • 51
    • 0345390067 scopus 로고    scopus 로고
    • The chromatin structure of the long control region of human papillomavirus type 16 represses viral oncoprotein expression
    • Stunkel, W., and H. U. Bernard. 1999. The chromatin structure of the long control region of human papillomavirus type 16 represses viral oncoprotein expression. J. Virol. 73:1918-1930.
    • (1999) J. Virol. , vol.73 , pp. 1918-1930
    • Stunkel, W.1    Bernard, H.U.2
  • 52
    • 0031848539 scopus 로고    scopus 로고
    • Active domains of human papillomavirus type 11 E1 protein for origin replication
    • Sun, Y., H. Han, and D. J. McCance. 1998. Active domains of human papillomavirus type 11 E1 protein for origin replication. J. Gen. Virol. 79:1651-1658.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1651-1658
    • Sun, Y.1    Han, H.2    McCance, D.J.3
  • 53
    • 0037405823 scopus 로고    scopus 로고
    • Characterization of the minimal DNA binding domain of the human papillomavirus E1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant protein
    • Titolo, S., K. Brault, J. Majewski, P. W. White, and J. Archambault. 2003. Characterization of the minimal DNA binding domain of the human papillomavirus E1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant protein. J. Virol. 77:5178-5191.
    • (2003) J. Virol. , vol.77 , pp. 5178-5191
    • Titolo, S.1    Brault, K.2    Majewski, J.3    White, P.W.4    Archambault, J.5
  • 54
    • 0033852428 scopus 로고    scopus 로고
    • Identification of domains of the human papillomavirus type 11 E1 helicase involved in oligomerization and binding to the viral origin
    • Titolo, S., et al. 2000. Identification of domains of the human papillomavirus type 11 E1 helicase involved in oligomerization and binding to the viral origin. J. Virol. 74:7349-7361.
    • (2000) J. Virol. , vol.74 , pp. 7349-7361
    • Titolo, S.1
  • 55
    • 0033064136 scopus 로고    scopus 로고
    • Role of the ATP-binding domain of the human papillomavirus type 11 E1 helicase in E2-dependent binding to the origin
    • Titolo, S., et al. 1999. Role of the ATP-binding domain of the human papillomavirus type 11 E1 helicase in E2-dependent binding to the origin. J. Virol. 73:5282-5293.
    • (1999) J. Virol. , vol.73 , pp. 5282-5293
    • Titolo, S.1
  • 56
    • 0030912539 scopus 로고    scopus 로고
    • The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function
    • Torchia, J., et al. 1997. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387:677-684.
    • (1997) Nature , vol.387 , pp. 677-684
    • Torchia, J.1
  • 57
    • 0030756675 scopus 로고    scopus 로고
    • Induced alpha helix in the VP16 activation domain upon binding to a human TAF
    • Uesugi, M., O. Nyanguile, H. Lu, A. J. Levine, and G. L. Verdine. 1997. Induced alpha helix in the VP16 activation domain upon binding to a human TAF. Science 277:1310-1313.
    • (1997) Science , vol.277 , pp. 1310-1313
    • Uesugi, M.1    Nyanguile, O.2    Lu, H.3    Levine, A.J.4    Verdine, G.L.5
  • 58
    • 44449116120 scopus 로고    scopus 로고
    • Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
    • Wells, M., et al. 2008. Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain. Proc. Natl. Acad. Sci. U. S. A. 105:5762-5767.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 5762-5767
    • Wells, M.1
  • 59
    • 0035933838 scopus 로고    scopus 로고
    • Characterization of recombinant HPV6 and 11 E1 helicases: effect of ATP on the interaction of E1 with E2 and mapping of a minimal helicase domain
    • White, P. W., et al. 2001. Characterization of recombinant HPV6 and 11 E1 helicases: effect of ATP on the interaction of E1 with E2 and mapping of a minimal helicase domain. J. Biol. Chem. 276:22426-22438.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22426-22438
    • White, P.W.1
  • 60
    • 0027983521 scopus 로고
    • Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53
    • Xiao, H., 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
  • 61
    • 0036840610 scopus 로고    scopus 로고
    • Stimulation of DNA replication from the polyomavirus origin by PCAF and GCN5 acetyltransferases: acetylation of large T antigen
    • Xie, A. Y., V. P. Bermudez, and W. R. Folk. 2002. Stimulation of DNA replication from the polyomavirus origin by PCAF and GCN5 acetyltransferases: acetylation of large T antigen. Mol. Cell. Biol. 22:7907-7918.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7907-7918
    • Xie, A.Y.1    Bermudez, V.P.2    Folk, W.R.3
  • 62
    • 0031016642 scopus 로고    scopus 로고
    • Mapping and characterization of the interaction domains of human papillomavirus type 16 E1 and E2 proteins
    • Yasugi, T., J. D. Benson, H. Sakai, M. Vidal, and P. M. Howley. 1997. Mapping and characterization of the interaction domains of human papillomavirus type 16 E1 and E2 proteins. J. Virol. 71:891-899.
    • (1997) J. Virol. , vol.71 , pp. 891-899
    • Yasugi, T.1    Benson, J.D.2    Sakai, H.3    Vidal, M.4    Howley, P.M.5
  • 63
    • 38349048247 scopus 로고    scopus 로고
    • Coactivator requirements for p53-dependent transcription in the yeast Saccharomyces cerevisiae
    • Yousef, A. F., G. W. Xu, M. Mendez, C. J. Brandl, and J. S. Mymryk. 2008. Coactivator requirements for p53-dependent transcription in the yeast Saccharomyces cerevisiae. Int. J. Cancer 122:942-946.
    • (2008) Int. J. Cancer. , vol.122 , pp. 942-946
    • Yousef, A.F.1    Xu, G.W.2    Mendez, M.3    Brandl, C.J.4    Mymryk, J.S.5
  • 64
    • 34248380889 scopus 로고    scopus 로고
    • Mitogenactivated protein kinases activate the nuclear localization sequence of human papillomavirus type 11 E1 DNA helicase to promote efficient nuclear import
    • Yu, J.-H., B. Y. Lin, W. Deng, T. R. Broker, and L. T. Chow. 2007. Mitogenactivated protein kinases activate the nuclear localization sequence of human papillomavirus type 11 E1 DNA helicase to promote efficient nuclear import. J. Virol. 81:5066-5078.
    • (2007) J. Virol. , vol.81 , pp. 5066-5078
    • Yu, J.-H.1    Lin, B.Y.2    Deng, W.3    Broker, T.R.4    Chow, L.T.5


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