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Volumn 287, Issue 27, 2012, Pages 23035-23045

Endoplasmic reticulum stress-responsive transcription factor ATF6α directs recruitment of the mediator of RNA polymerase II transcription and multiple histone acetyltransferase complexes

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL TRANSFERASE; BINDING SEQUENCE; BIOCHEMICAL MECHANISMS; COREGULATORS; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM STRESS RESPONSE; ER STRESS; HISTONE ACETYLTRANSFERASES; LEUCINE-ZIPPER TRANSCRIPTION FACTORS; MASTER REGULATORS; MECHANISM OF ACTION; MULTIDIMENSIONAL PROTEINS; REGULATORY ELEMENTS; RNA POLYMERASE II; STRAIGHTFORWARD STRATEGY; TECHNOLOGY-BASED;

EID: 84863329769     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.369504     Document Type: Article
Times cited : (18)

References (51)
  • 1
    • 47949099916 scopus 로고    scopus 로고
    • From endoplasmic reticulum stress to the inflammatory response
    • Zhang, K., and Kaufman, R. J. (2008) From endoplasmic reticulum stress to the inflammatory response. Nature 454, 455-462
    • (2008) Nature , vol.454 , pp. 455-462
    • Zhang, K.1    Kaufman, R.J.2
  • 2
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • DOI 10.1038/nrm2199, PII NRM2199
    • Ron, D., and Walter, P. (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519-529 (Pubitemid 46985379)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 3
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • DOI 10.1146/annurev.biochem.73.011303.074134
    • Schröder, M., and Kaufman, R. J. (2005) The mammalian unfolded protein response. Annu. Rev. Biochem. 74, 739-789 (Pubitemid 40995523)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 4
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze, K., Yoshida, H., Yanagi, H., Yura, T., and Mori, K. (1999) Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol. Biol. Cell 10, 3787-3799 (Pubitemid 29534025)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.11 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 5
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • DOI 10.1016/S1097-2765(00)00133-7
    • Ye, J., Rawson, R. B., Komuro, R., Chen, X., Davé, U. P., Prywes, R., Brown, M. S., and Goldstein, J. L. (2000) ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol. Cell 6, 1355-1364 (Pubitemid 32045928)
    • (2000) Molecular Cell , vol.6 , Issue.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3    Chen, X.4    Dave, U.P.5    Prywes, R.6    Brown, M.S.7    Goldstein, J.L.8
  • 6
    • 0037066741 scopus 로고    scopus 로고
    • The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the er to the Golgi
    • DOI 10.1074/jbc.M110636200
    • Chen, X., Shen, J., and Prywes, R. (2002) The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi. J. Biol. Chem. 277, 13045-13052 (Pubitemid 34952673)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 13045-13052
    • Chen, X.1    Shen, J.2    Prywes, R.3
  • 7
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of golgi localization signals
    • DOI 10.1016/S1534-5807(02)00203-4
    • Shen, J., Chen, X., Hendershot, L., and Prywes, R. (2002) ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3, 99-111 (Pubitemid 34778399)
    • (2002) Developmental Cell , vol.3 , Issue.1 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 8
    • 5644244829 scopus 로고    scopus 로고
    • Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6
    • DOI 10.1074/jbc.M408466200
    • Shen, J., and Prywes, R. (2004) Dependence of site 2 protease cleavage of ATF6 on prior site 1 protease digestion is determined by the size of the luminal domain of ATF6. J. Biol. Chem. 279, 43046-43051 (Pubitemid 39372199)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 43046-43051
    • Shen, J.1    Prywes, R.2
  • 9
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins: Involvement of basic leucine zipper transcription factors
    • Yoshida, H., Haze, K., Yanagi, H., Yura, T., and Mori, K. (1998) Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins: involvement of basic leucine zipper transcription factors. J. Biol. Chem. 273, 33741-33749
    • (1998) J. Biol. Chem. , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 10
    • 18944390015 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induction of the Grp78/BiP promoter: Activating mechanisms mediated by YY1 and its interactive chromatin modifiers
    • DOI 10.1128/MCB.25.11.4529-4540.2005
    • Baumeister, P., Luo, S., Skarnes, W. C., Sui, G., Seto, E., Shi, Y., and Lee, A. S. (2005) Endoplasmic reticulum stress induction of the Grp78/BiP promoter: activating mechanisms mediated by YY1 and its interactive chromatin modifiers. Mol. Cell Biol. 25, 4529-4540 (Pubitemid 40705758)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.11 , pp. 4529-4540
    • Baumeister, P.1    Luo, S.2    Skarnes, W.C.3    Sui, G.4    Seto, E.5    Shi, Y.6    Lee, A.S.7
  • 11
    • 50249159442 scopus 로고    scopus 로고
    • CBF/NF-Y controls endoplasmic reticulum stress-induced transcription through recruitment of both ATF6(N) and TBP
    • Luo, R., Lu, J. F., Hu, Q., and Maity, S. N. (2008) CBF/NF-Y controls endoplasmic reticulum stress-induced transcription through recruitment of both ATF6(N) and TBP. J. Cell Biochem. 104, 1708-1723
    • (2008) J. Cell Biochem. , vol.104 , pp. 1708-1723
    • Luo, R.1    Lu, J.F.2    Hu, Q.3    Maity, S.N.4
  • 12
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • Yoshida, H., Okada, T., Haze, K., Yanagi, H., Yura, T., Negishi, M., and Mori, K. (2000) ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol. Cell Biol. 20, 6755-6767
    • (2000) Mol. Cell Biol. , vol.20 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6    Mori, K.7
  • 13
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional Induction of Mammalian ER Quality Control Proteins Is Mediated by Single or Combined Action of ATF6α and XBP1
    • DOI 10.1016/j.devcel.2007.07.018, PII S1534580707003000
    • Yamamoto, K., Sato, T., Matsui, T., Sato, M., Okada, T., Yoshida, H., Harada, A., and Mori, K. (2007) Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6α and XBP1. Dev. Cell 13, 365-376 (Pubitemid 47308680)
    • (2007) Developmental Cell , vol.13 , Issue.3 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 14
    • 0032493662 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase mediates the transcriptional induction of the atrial natriuretic factor gene through a serum response element: A potential role for the transcription factor ATF6
    • DOI 10.1074/jbc.273.32.20636
    • Thuerauf, D. J., Arnold, N. D., Zechner, D., Hanford, D. S., DeMartin, K. M., McDonough, P. M., Prywes, R., and Glembotski, C. C. (1998) p38 mitogen-activated protein kinase mediates the transcriptional induction of the atrial natriuretic factor gene through a serum response element: a potential role for the transcription factor ATF6. J. Biol. Chem. 273, 20636-20643 (Pubitemid 28377635)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 20636-20643
    • Thuerauf, D.J.1    Arnold, N.D.2    Zechner, D.3    Hanford, D.S.4    DeMartin, K.M.5    McDonough, P.M.6    Prywes, R.7    Glembotski, C.C.8
  • 15
    • 0037036412 scopus 로고    scopus 로고
    • Coordination of ATF6-mediated transcription and ATF6 degradation by a domain that is shared with the viral transcription factor, VP16
    • DOI 10.1074/jbc.M201749200
    • Thuerauf, D. J., Morrison, L. E., Hoover, H., and Glembotski, C. C. (2002) Coordination of ATF6-mediated transcription and ATF6 degradation by a domain that is shared with the viral transcription factor, VP16. J. Biol. Chem. 277, 20734-20739 (Pubitemid 34967378)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.23 , pp. 20734-20739
    • Thuerauf, D.J.1    Morrison, L.E.2    Hoover, H.3    Glembotski, C.C.4
  • 16
    • 33745135117 scopus 로고    scopus 로고
    • Dynamic recruitment of transcription factors and epigenetic changes on the ER stress response gene promoters
    • DOI 10.1093/nar/gkl304
    • Donati, G., Imbriano, C., and Mantovani, R. (2006) Dynamic recruitment of transcription factors and epigenetic changes on the ER stress response gene promoters. Nucleic Acids Res. 34, 3116-3127 (Pubitemid 44540437)
    • (2006) Nucleic Acids Research , vol.34 , Issue.10 , pp. 3116-3127
    • Donati, G.1    Imbriano, C.2    Mantovani, R.3
  • 18
    • 62849096067 scopus 로고    scopus 로고
    • The human SPT20-containing SAGA complex plays a direct role in the regulation of endoplasmic reticulum stress-induced genes
    • Nagy, Z., Riss, A., Romier, C., le Guezennec, X., Dongre, A. R., Orpinell, M., Han, J., Stunnenberg, H., and Tora, L. (2009) The human SPT20-containing SAGA complex plays a direct role in the regulation of endoplasmic reticulum stress-induced genes. Mol. Cell Biol. 29, 1649-1660
    • (2009) Mol. Cell Biol. , vol.29 , pp. 1649-1660
    • Nagy, Z.1    Riss, A.2    Romier, C.3    Le Guezennec, X.4    Dongre, A.R.5    Orpinell, M.6    Han, J.7    Stunnenberg, H.8    Tora, L.9
  • 19
    • 0037099312 scopus 로고    scopus 로고
    • TFIID and human mediator coactivator complexes assemble cooperatively on promoter DNA
    • DOI 10.1101/gad.995702
    • Johnson, K. M., Wang, J., Smallwood, A., Arayata, C., and Carey, M. (2002) TFIID and human mediator coactivator complexes assemble cooperatively on promoter DNA. Genes Dev. 16, 1852-1863 (Pubitemid 34803900)
    • (2002) Genes and Development , vol.16 , Issue.14 , pp. 1852-1863
    • Johnson, K.M.1    Wang, J.2    Smallwood, A.3    Arayata, C.4    Carey, M.5
  • 20
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., Lebovitz, R. M., and Roeder, R. G. (1983) Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11, 1475-1489
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 22
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • Washburn, M. P., Wolters, D., and Yates, J. R., 3rd (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242-247 (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 23
    • 33746500659 scopus 로고    scopus 로고
    • Proteomic analysis by multidimensional protein identification technology
    • Florens, L., and Washburn, M. P. (2006) Proteomic analysis by multidimensional protein identification technology. Methods Mol. Biol. 328, 159-175
    • (2006) Methods Mol. Biol. , vol.328 , pp. 159-175
    • Florens, L.1    Washburn, M.P.2
  • 25
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K., McCormack, A. L., and Yates, J. R., 3rd (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass. Spec. 5, 976-989
    • (1994) J. Am. Soc. Mass. Spec. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 26
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L., McDonald, W. H., and Yates, J. R., 3rd (2002) DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 1, 21-26
    • (2002) J. Proteome Res. , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 27
    • 77949795829 scopus 로고    scopus 로고
    • Refinements to label free proteome quantitation: How to deal with peptides shared by multiple proteins
    • Zhang, Y., Wen, Z., Washburn, M. P., and Florens, L. (2010) Refinements to label free proteome quantitation: how to deal with peptides shared by multiple proteins. Anal. Chem. 82, 2272-2281
    • (2010) Anal. Chem. , vol.82 , pp. 2272-2281
    • Zhang, Y.1    Wen, Z.2    Washburn, M.P.3    Florens, L.4
  • 28
    • 33750699996 scopus 로고    scopus 로고
    • Analyzing chromatin remodeling complexes using shotgun proteomics and normalized spectral abundance factors
    • DOI 10.1016/j.ymeth.2006.07.028, PII S1046202306002076
    • Florens, L., Carozza, M. J., Swanson, S. K., Fournier, M., Coleman, M. K., Workman, J. L., and Washburn, M. P. (2006) Analyzing chromatin remodeling complexes using shotgun proteomics and normalized spectral abundance factors. Methods 40, 303-311 (Pubitemid 44709624)
    • (2006) Methods , vol.40 , Issue.4 , pp. 303-311
    • Florens, L.1    Carozza, M.J.2    Swanson, S.K.3    Fournier, M.4    Coleman, M.K.5    Workman, J.L.6    Washburn, M.P.7
  • 30
    • 33748319353 scopus 로고    scopus 로고
    • Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae
    • DOI 10.1021/pr060161n
    • Zybailov, B., Mosley, A. L., Sardiu, M. E., Coleman, M. K., Florens, L., and Washburn, M. P. (2006) Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae. J. Proteome Res. 5, 2339-2347 (Pubitemid 44330827)
    • (2006) Journal of Proteome Research , vol.5 , Issue.9 , pp. 2339-2347
    • Zybailov, B.1    Mosley, A.L.2    Sardiu, M.E.3    Coleman, M.K.4    Florens, L.5    Washburn, M.P.6
  • 32
    • 79953162883 scopus 로고    scopus 로고
    • Function and regulation of the Mediator complex
    • Conaway, R. C., and Conaway, J. W. (2011) Function and regulation of the Mediator complex. Curr. Opin. Genet. Dev. 21, 225-230
    • (2011) Curr. Opin. Genet. Dev. , vol.21 , pp. 225-230
    • Conaway, R.C.1    Conaway, J.W.2
  • 33
    • 77954759030 scopus 로고    scopus 로고
    • The human Mediator complex: A versatile, genomewide regulator of transcription
    • Taatjes, D. J. (2010) The human Mediator complex: a versatile, genomewide regulator of transcription. Trends Biochem. Sci. 35, 315-322
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 315-322
    • Taatjes, D.J.1
  • 34
    • 77958111633 scopus 로고    scopus 로고
    • The metazoan Mediator co-activator complex as an integrative hub for transcriptional regulation
    • Malik, S., and Roeder, R. G. (2010) The metazoan Mediator co-activator complex as an integrative hub for transcriptional regulation. Nat. Rev. Genet. 11, 761-772
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 761-772
    • Malik, S.1    Roeder, R.G.2
  • 35
    • 68249129270 scopus 로고    scopus 로고
    • Insights into SAGA function during gene expression
    • Rodríguez-Navarro, S. (2009) Insights into SAGA function during gene expression. EMBO Rep. 10, 843-850
    • (2009) EMBO Rep. , vol.10 , pp. 843-850
    • Rodríguez-Navarro, S.1
  • 36
    • 77952569347 scopus 로고    scopus 로고
    • Inducible gene expression: Diverse regulatory mechanisms
    • Weake, V. M., and Workman, J. L. (2010) Inducible gene expression: diverse regulatory mechanisms. Nat. Rev. Genet. 11, 426-437
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 426-437
    • Weake, V.M.1    Workman, J.L.2
  • 37
    • 38749108891 scopus 로고    scopus 로고
    • Dubbing SAGA Unveils New Epigenetic Crosstalk
    • DOI 10.1016/j.molcel.2008.01.007, PII S1097276508000427
    • Pijnappel, W. W., and Timmers, H. T. (2008) Dubbing SAGA unveils new epigenetic crosstalk. Mol. Cell 29, 152-154 (Pubitemid 351181281)
    • (2008) Molecular Cell , vol.29 , Issue.2 , pp. 152-154
    • Pijnappel, W.W.M.P.1    Timmers, H.Th.M.2
  • 38
    • 84858329099 scopus 로고    scopus 로고
    • ATAC-king the complexity of SAGA during evolution
    • Spedale, G., Timmers, H. T., and Pijnappel, W. W. (2012) ATAC-king the complexity of SAGA during evolution. Genes Dev. 26, 527-541
    • (2012) Genes Dev. , vol.26 , pp. 527-541
    • Spedale, G.1    Timmers, H.T.2    Pijnappel, W.W.3
  • 39
    • 0242322038 scopus 로고    scopus 로고
    • Identification of New Subunits of the Multiprotein Mammalian TRRAP/TIP60-containing Histone Acetyltransferase Complex
    • DOI 10.1074/jbc.C300389200
    • Cai, Y., Jin, J., Tomomori-Sato, C., Sato, S., Sorokina, I., Parmely, T. J., Conaway, R. C., and Conaway, J. W. (2003) Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex. J. Biol. Chem. 278, 42733-42736 (Pubitemid 37345881)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.44 , pp. 42733-42736
    • Cai, Y.1    Jin, J.2    Tomomori-Sato, C.3    Sato, S.4    Sorokina, I.5    Parmely, T.J.6    Conaway, R.C.7    Conaway, J.W.8
  • 40
    • 1342346531 scopus 로고    scopus 로고
    • Structural and Functional Conservation of the NuA4 Histone Acetyltransferase Complex from Yeast to Humans
    • DOI 10.1128/MCB.24.5.1884-1896.2004
    • Doyon, Y., Selleck, W., Lane, W. S., Tan, S., and Côté, J. (2004) Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. Mol. Cell Biol. 24, 1884-1896 (Pubitemid 38248930)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.5 , pp. 1884-1896
    • Doyon, Y.1    Selleck, W.2    Lane, W.S.3    Tan, S.4    Cote, J.5
  • 42
    • 0036838096 scopus 로고    scopus 로고
    • Differential requirement of SAGA components for recruitment of TATA-box-binding protein to promoters in vivo
    • Bhaumik, S. R., and Green, M. R. (2002) Differential requirement of SAGA components for recruitment of TATA-box-binding protein to promoters in vivo. Mol. Cell Biol. 22, 7365-7371
    • (2002) Mol. Cell Biol. , vol.22 , pp. 7365-7371
    • Bhaumik, S.R.1    Green, M.R.2
  • 43
    • 0032710459 scopus 로고    scopus 로고
    • The Spt components of SAGA facilitate TBP binding to a promoter at a post-activator-binding step in vivo
    • Dudley, A. M., Rougeulle, C., and Winston, F. (1999) The Spt components of SAGA facilitate TBP binding to a promoter at a post-activator-binding step in vivo. Genes Dev. 13, 2940-2945
    • (1999) Genes Dev. , vol.13 , pp. 2940-2945
    • Dudley, A.M.1    Rougeulle, C.2    Winston, F.3
  • 44
    • 0033571527 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of transcriptional activators correlates with activation domain potency in vivo
    • DOI 10.1093/emboj/18.22.6439
    • Molinari, E., Gilman, M., and Natesan, S. (1999) Proteasome-mediated degradation of transcriptional activators correlates with activation domain potency in vivo. EMBO J. 18, 6439-6447 (Pubitemid 29533247)
    • (1999) EMBO Journal , vol.18 , Issue.22 , pp. 6439-6447
    • Molinari, E.1    Gilman, M.2    Natesan, S.3
  • 45
    • 0036158808 scopus 로고    scopus 로고
    • The H1 and H2 regions of the activation domain of herpes simplex virion protein 16 stimulate transcription through distinct molecular mechanisms
    • DOI 10.1046/j.1356-9597.2001.00492.x
    • Ikeda, K., Stuehler, T., and Meisterernst, M. (2002) The H1 and H2 regions of the activation domain of herpes simplex virion protein 16 stimulate transcription through distinct molecular mechanisms. Genes Cells 7, 49-58 (Pubitemid 34121305)
    • (2002) Genes to Cells , vol.7 , Issue.1 , pp. 49-58
    • Ikeda, K.1    Stuehler, T.2    Meisterernst, M.3
  • 46
    • 0346993714 scopus 로고    scopus 로고
    • A novel docking site on Mediator is critical for activation by VP16 in mammalian cells
    • DOI 10.1093/emboj/cdg619
    • Mittler, G., Stühler, T., Santolin, L., Uhlmann, T., Kremmer, E., Lottspeich, F., Berti, L., and Meisterernst, M. (2003) A novel docking site on Mediator is critical for activation by VP16 in mammalian cells. EMBO J. 22, 6494-6504 (Pubitemid 38009597)
    • (2003) EMBO Journal , vol.22 , Issue.24 , pp. 6494-6504
    • Mittler, G.1    Stuhler, T.2    Santolin, L.3    Uhlmann, T.4    Kremmer, E.5    Lottspeich, F.6    Berti, L.7    Meisterernst, M.8
  • 47
    • 1442354965 scopus 로고    scopus 로고
    • The activator-recruited cofactor/Mediator coactivation subunit ARC92 is a functionally important target of the VP16 transcriptional activator
    • DOI 10.1073/pnas.0308676100
    • Yang, F., DeBeaumont, R., Zhou, S., and Näär, A. M. (2004) The activator-recruited cofactor/Mediator coactivator subunit ARC92 is a functionally important target of the VP16 transcriptional activator. Proc. Natl. Acad. Sci. U.S.A. 101, 2339-2344 (Pubitemid 38269313)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.8 , pp. 2339-2344
    • Yang, F.1    DeBeaumont, R.2    Zhou, S.3    Naar, A.M.4
  • 51
    • 80054864019 scopus 로고    scopus 로고
    • Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25
    • Eletsky, A., Ruyechan, W. T., Xiao, R., Acton, T. B., Montelione, G. T., and Szyperski, T. (2011) Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25. J. Struct. Funct. Genomics 12, 159-166
    • (2011) J. Struct. Funct. Genomics , vol.12 , pp. 159-166
    • Eletsky, A.1    Ruyechan, W.T.2    Xiao, R.3    Acton, T.B.4    Montelione, G.T.5    Szyperski, T.6


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