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Volumn 11, Issue 9, 2004, Pages 812-815

Combinatorial control of gene expression

Author keywords

[No Author keywords available]

Indexed keywords

DNA; TRANSCRIPTION FACTOR;

EID: 4344595718     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb820     Document Type: Review
Times cited : (202)

References (29)
  • 1
    • 0028332036 scopus 로고
    • Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers
    • Glass, C.K. Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers. Endocr. Rev. 15, 391-407 (1994).
    • (1994) Endocr. Rev. , vol.15 , pp. 391-407
    • Glass, C.K.1
  • 2
    • 0028934434 scopus 로고
    • The MADS-box family of transcription factors
    • Shore, P. & Sharrocks, A.D. The MADS-box family of transcription factors. Eur. J. Biochem. 229, 1-13 (1995).
    • (1995) Eur. J. Biochem. , vol.229 , pp. 1-13
    • Shore, P.1    Sharrocks, A.D.2
  • 3
    • 0033559518 scopus 로고    scopus 로고
    • From head to toes: The multiple facets of Sox proteins
    • Wegner, M. From head to toes: the multiple facets of Sox proteins. Nucleic Acids Res. 27, 1409-1420 (1999).
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1409-1420
    • Wegner, M.1
  • 4
    • 0029124988 scopus 로고
    • The POU domain: Versatility in transcriptional regulation by a flexible two-in-one DNA-binding domain
    • Herr, W. & Cleary, M.A. The POU domain: versatility in transcriptional regulation by a flexible two-in-one DNA-binding domain. Genes Dev. 9, 1679-1693 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 1679-1693
    • Herr, W.1    Cleary, M.A.2
  • 5
    • 0345849436 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Ptashne, M. & Gann, A. Genes & Signals (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 2002).
    • (2002) Genes & Signals
    • Ptashne, M.1    Gann, A.2
  • 6
    • 0028337542 scopus 로고
    • Transcriptional activation: A complex puzzle with few easy pieces
    • Tjian, R. & Maniatis, T. Transcriptional activation: a complex puzzle with few easy pieces. Cell 77, 5-8 (1994).
    • (1994) Cell , vol.77 , pp. 5-8
    • Tjian, R.1    Maniatis, T.2
  • 7
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin, J.A. & Yamamoto, K.R. Allosteric effects of DNA on transcriptional regulators. Nature 392, 885-888 (1998).
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 8
    • 0029044997 scopus 로고
    • Structural determinants of nuclear receptor assembly on DNA direct repeats
    • Rastinejad, F., Perlmann, T., Evans, R.M. & Sigler, P.B. Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature 375, 203-211 (1995).
    • (1995) Nature , vol.375 , pp. 203-211
    • Rastinejad, F.1    Perlmann, T.2    Evans, R.M.3    Sigler, P.B.4
  • 9
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf, D.J. & Evans, R.M. The RXR heterodimers and orphan receptors. Cell 83, 841-850 (1995).
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 10
    • 0029102041 scopus 로고
    • Structure of serum response factor core bound to DNA
    • Pellegrini, L., Tan, S. & Richmond, T.J. Structure of serum response factor core bound to DNA. Nature 376, 490-498 (1995).
    • (1995) Nature , vol.376 , pp. 490-498
    • Pellegrini, L.1    Tan, S.2    Richmond, T.J.3
  • 11
    • 0035875907 scopus 로고    scopus 로고
    • The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex
    • Hassler, M. & Richmond, T.J. The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex. EMBO J. 20, 3018-3028 (2001).
    • (2001) EMBO J. , vol.20 , pp. 3018-3028
    • Hassler, M.1    Richmond, T.J.2
  • 12
    • 0032509980 scopus 로고    scopus 로고
    • Crystal structure of the yeast MATα2/MCM1/DNA ternary complex
    • Tan, S. & Richmond, T.J. Crystal structure of the yeast MATα2/MCM1/DNA ternary complex. Nature 391, 660-666 (1998).
    • (1998) Nature , vol.391 , pp. 660-666
    • Tan, S.1    Richmond, T.J.2
  • 13
    • 0030918673 scopus 로고    scopus 로고
    • POU domain family values: Flexibility, partnerships, and developmental codes
    • Ryan, A.K. & Rosenfeld, M.G. POU domain family values: flexibility, partnerships, and developmental codes. Genes Dev. 11, 1207-1225 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 1207-1225
    • Ryan, A.K.1    Rosenfeld, M.G.2
  • 14
    • 0034175998 scopus 로고    scopus 로고
    • Pairing SOX off: With partners in the regulation of embryonic development
    • Kamachi, Y., Uchikawa, M. & Kondoh, H. Pairing SOX off: with partners in the regulation of embryonic development. Trends Genet. 16, 182-187 (2000).
    • (2000) Trends Genet. , vol.16 , pp. 182-187
    • Kamachi, Y.1    Uchikawa, M.2    Kondoh, H.3
  • 15
    • 0035125506 scopus 로고    scopus 로고
    • Coevolution of HMG domains and homeodomains and the generation of transcriptional regulation by Sox/POU complexes
    • Dailey, L. & Basilico, C. Coevolution of HMG domains and homeodomains and the generation of transcriptional regulation by Sox/POU complexes. J. Cell Physiol. 186, 315-328 (2001).
    • (2001) J. Cell Physiol. , vol.186 , pp. 315-328
    • Dailey, L.1    Basilico, C.2
  • 16
    • 0030820931 scopus 로고    scopus 로고
    • Synergistic activation of the fibroblast growth factor 4 enhancer by Sox2 and Oct-3 depends on protein-protein interactions facilitated by a specific spatial arrangement of factor binding sites
    • Ambrosetti, D.C., Basilico, C. & Dailey, L. Synergistic activation of the fibroblast growth factor 4 enhancer by Sox2 and Oct-3 depends on protein-protein interactions facilitated by a specific spatial arrangement of factor binding sites. Mol. Cell. Biol. 17, 6321-6329 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6321-6329
    • Ambrosetti, D.C.1    Basilico, C.2    Dailey, L.3
  • 17
    • 0037227099 scopus 로고    scopus 로고
    • Multipotent cell lineages in early mouse development depend on SOX2 function
    • Avilion, A.A. et al. Multipotent cell lineages in early mouse development depend on SOX2 function. Genes Dev. 17, 126-140 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 126-140
    • Avilion, A.A.1
  • 18
    • 0042161878 scopus 로고    scopus 로고
    • Crystal structure of a POU/HMG/DNA ternary complex suggests differential assembly of Oct4 and Sox2 on two enhancers
    • Remenyi, A. et al. Crystal structure of a POU/HMG/DNA ternary complex suggests differential assembly of Oct4 and Sox2 on two enhancers. Genes Dev. 17, 2048-2059 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 2048-2059
    • Remenyi, A.1
  • 19
    • 0035827568 scopus 로고    scopus 로고
    • The recruitment of SOX/OCT complexes and the differential activity of HOXA1 and HOXB1 modulate the Hoxb1 auto-regulatory enhancer function
    • Di Rocco, G. et al. The recruitment of SOX/OCT complexes and the differential activity of HOXA1 and HOXB1 modulate the Hoxb1 auto-regulatory enhancer function. J. Biol. Chem. 276, 20506-20515 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 20506-20515
    • Di Rocco, G.1
  • 20
    • 0346462991 scopus 로고    scopus 로고
    • Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1.Sox2.Hoxb1-DNA ternary transcription factor complex
    • Williams, D.C. Jr., Cai, M. & Clore, G.M. Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1.Sox2.Hoxb1-DNA ternary transcription factor complex. J. Biol. Chem. 279, 1449-1457 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 1449-1457
    • Williams Jr., D.C.1    Cai, M.2    Clore, G.M.3
  • 21
    • 0035873448 scopus 로고    scopus 로고
    • Pax6 and SOX2 form a co-DNA-binding partner complex that regulates initiation of lens development
    • Kamachi, Y., Uchikawa, M., Tanouchi, A., Sekido, R. & Kondoh, H. Pax6 and SOX2 form a co-DNA-binding partner complex that regulates initiation of lens development. Genes Dev. 15, 1272-1286 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 1272-1286
    • Kamachi, Y.1    Uchikawa, M.2    Tanouchi, A.3    Sekido, R.4    Kondoh, H.5
  • 22
    • 0028200262 scopus 로고
    • Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules
    • Klemm, J.D., Rould, M.A., Aurora, R., Herr, W. & Pabo, C.O. Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell 77, 21-32 (1994).
    • (1994) Cell , vol.77 , pp. 21-32
    • Klemm, J.D.1    Rould, M.A.2    Aurora, R.3    Herr, W.4    Pabo, C.O.5
  • 23
    • 0033639075 scopus 로고    scopus 로고
    • Synergism with the coactivator OBF-1 (OCA-B, BOB-1) is mediated by a specific POU dimer configuration
    • Tomilin, A. et al. Synergism with the coactivator OBF-1 (OCA-B, BOB-1) is mediated by a specific POU dimer configuration. Cell 103, 853-864 (2000).
    • (2000) Cell , vol.103 , pp. 853-864
    • Tomilin, A.1
  • 24
    • 0034791092 scopus 로고    scopus 로고
    • Differential dimer activities of the transcription factor Oct-1 by DNA-induced interface swapping
    • Remenyi, A. et al. Differential dimer activities of the transcription factor Oct-1 by DNA-induced interface swapping. Mol. Cell 8, 569-580 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 569-580
    • Remenyi, A.1
  • 25
    • 0033569643 scopus 로고    scopus 로고
    • Crystal structure of an OCAB peptide bound to an Oct-1 POU domain/octamer DNA complex: Specific recognition of a protein-DNA interface
    • Chasman, D., Cepek, K., Sharp, P.A. & Pabo, C.O. Crystal structure of an OCAB peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface. Genes Dev. 13, 2650-2657 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2650-2657
    • Chasman, D.1    Cepek, K.2    Sharp, P.A.3    Pabo, C.O.4
  • 26
    • 0344629668 scopus 로고    scopus 로고
    • STAT5 and Oct-1 form a stable complex that modulates cyclin D1 expression
    • Magne, S., Caron, S., Charon, M., Rouyez, M.C. & Dusanter-Fourt, I. STAT5 and Oct-1 form a stable complex that modulates cyclin D1 expression. Mol. Cell. Biol. 23, 8934-8945 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8934-8945
    • Magne, S.1    Caron, S.2    Charon, M.3    Rouyez, M.C.4    Dusanter-Fourt, I.5
  • 27
    • 0034634340 scopus 로고    scopus 로고
    • Allosteric effects of Pit-1 DNA sites on long-term repression in cell type specification
    • Scully, K.M. et al. Allosteric effects of Pit-1 DNA sites on long-term repression in cell type specification. Science 290, 1127-1131 (2000).
    • (2000) Science , vol.290 , pp. 1127-1131
    • Scully, K.M.1
  • 28
    • 0742306815 scopus 로고    scopus 로고
    • Computational prediction of transcription-factor binding site locations
    • Bulyk, M.L. Computational prediction of transcription-factor binding site locations. Genome Biol. 5, 201 (2003).
    • (2003) Genome Biol. , vol.5 , pp. 201
    • Bulyk, M.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.