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Volumn 373, Issue 4, 2007, Pages 820-826

A Beta-Sheet Interaction Interface Directs the Tetramerisation of the Miz-1 POZ Domain

Author keywords

BCL6; BTB domain; c Myc

Indexed keywords

DIMER; MYC INTERACTING ZINC FINGER PROTEIN 1; PROTEIN SUBUNIT; TETRAMER; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN;

EID: 34848916670     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.08.026     Document Type: Article
Times cited : (34)

References (29)
  • 2
    • 33750333540 scopus 로고    scopus 로고
    • POZ for effect-POZ-ZF transcription factors in cancer and development
    • Kelly K.F., and Daniel J.M. POZ for effect-POZ-ZF transcription factors in cancer and development. Trends Cell Biol. 16 (2006) 578-587
    • (2006) Trends Cell Biol. , vol.16 , pp. 578-587
    • Kelly, K.F.1    Daniel, J.M.2
  • 3
    • 11144277489 scopus 로고    scopus 로고
    • Specific peptide interference reveals BCL6 transcriptional and oncogenic mechanisms in B-cell lymphoma cells
    • Polo J.M., Dell'Oso T., Ranuncolo S.M., Cerchietti L., Beck D., Da Silva G.F., et al. Specific peptide interference reveals BCL6 transcriptional and oncogenic mechanisms in B-cell lymphoma cells. Nat. Med. 10 (2004) 1329-1335
    • (2004) Nat. Med. , vol.10 , pp. 1329-1335
    • Polo, J.M.1    Dell'Oso, T.2    Ranuncolo, S.M.3    Cerchietti, L.4    Beck, D.5    Da Silva, G.F.6
  • 5
    • 0032724185 scopus 로고    scopus 로고
    • Structure-function studies of the BTB/POZ transcriptional repression domain from the promyelocytic leukemia zinc finger oncoprotein
    • Li X., Peng H., Schultz D.C., Lopez-Guisa J.M., Rauscher III F.J., and Marmorstein R. Structure-function studies of the BTB/POZ transcriptional repression domain from the promyelocytic leukemia zinc finger oncoprotein. Cancer Res. 59 (1999) 5275-5282
    • (1999) Cancer Res. , vol.59 , pp. 5275-5282
    • Li, X.1    Peng, H.2    Schultz, D.C.3    Lopez-Guisa, J.M.4    Rauscher III, F.J.5    Marmorstein, R.6
  • 7
    • 9144242434 scopus 로고    scopus 로고
    • Mechanism of SMRT corepressor recruitment by the BCL6 BTB domain
    • Ahmad K.F., Melnick A., Lax S., Bouchard D., Liu J., Kiang C.L., et al. Mechanism of SMRT corepressor recruitment by the BCL6 BTB domain. Mol. Cell 12 (2003) 1551-1564
    • (2003) Mol. Cell , vol.12 , pp. 1551-1564
    • Ahmad, K.F.1    Melnick, A.2    Lax, S.3    Bouchard, D.4    Liu, J.5    Kiang, C.L.6
  • 8
    • 33750290236 scopus 로고    scopus 로고
    • Structure of the POZ domain of human LRF, a master regulator of oncogenesis
    • Schubot F.D., Tropea J.E., and Waugh D.S. Structure of the POZ domain of human LRF, a master regulator of oncogenesis. Biochem. Biophys. Res. Commun. 351 (2006) 1-6
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 1-6
    • Schubot, F.D.1    Tropea, J.E.2    Waugh, D.S.3
  • 9
    • 33846505435 scopus 로고    scopus 로고
    • Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulator
    • Stogios P.J., Chen L., and Prive G.G. Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulator. Protein Sci. 16 (2007) 336-342
    • (2007) Protein Sci. , vol.16 , pp. 336-342
    • Stogios, P.J.1    Chen, L.2    Prive, G.G.3
  • 10
    • 18644371442 scopus 로고    scopus 로고
    • Negative regulation of the mammalian UV response by Myc through association with Miz-1
    • Herold S., Wanzel M., Beuger V., Frohme C., Beul D., Hillukkala T., et al. Negative regulation of the mammalian UV response by Myc through association with Miz-1. Mol. Cell 10 (2002) 509-521
    • (2002) Mol. Cell , vol.10 , pp. 509-521
    • Herold, S.1    Wanzel, M.2    Beuger, V.3    Frohme, C.4    Beul, D.5    Hillukkala, T.6
  • 11
    • 27544473311 scopus 로고    scopus 로고
    • The ubiquitin ligase HECTH9 regulates transcriptional activation by Myc and is essential for tumor cell proliferation
    • Adhikary S., Marinoni F., Hock A., Hulleman E., Popov N., Beier R., et al. The ubiquitin ligase HECTH9 regulates transcriptional activation by Myc and is essential for tumor cell proliferation. Cell 123 (2005) 409-421
    • (2005) Cell , vol.123 , pp. 409-421
    • Adhikary, S.1    Marinoni, F.2    Hock, A.3    Hulleman, E.4    Popov, N.5    Beier, R.6
  • 12
    • 0033081466 scopus 로고    scopus 로고
    • Co-operative DNA binding by GAGA transcription factor requires the conserved BTB/POZ domain and reorganizes promoter topology
    • Katsani K.R., Hajibagheri M.A., and Verrijzer C.P. Co-operative DNA binding by GAGA transcription factor requires the conserved BTB/POZ domain and reorganizes promoter topology. EMBO J. 18 (1999) 698-708
    • (1999) EMBO J. , vol.18 , pp. 698-708
    • Katsani, K.R.1    Hajibagheri, M.A.2    Verrijzer, C.P.3
  • 13
    • 0033963808 scopus 로고    scopus 로고
    • A combinatorial code for gene expression generated by transcription factor Bach2 and MAZR (MAZ-related factor) through the BTB/POZ domain
    • Kobayashi A., Yamagiwa H., Hoshino H., Muto A., Sato K., Morita M., et al. A combinatorial code for gene expression generated by transcription factor Bach2 and MAZR (MAZ-related factor) through the BTB/POZ domain. Mol. Cell. Biol. 20 (2000) 1733-1746
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1733-1746
    • Kobayashi, A.1    Yamagiwa, H.2    Hoshino, H.3    Muto, A.4    Sato, K.5    Morita, M.6
  • 14
    • 33646195686 scopus 로고    scopus 로고
    • Detection of protein assemblies in crystals
    • Springer, Berlin
    • Krissinel E., and Henrick K. Detection of protein assemblies in crystals. Lecture Notes in Computer Science vol. 3695 (2005), Springer, Berlin
    • (2005) Lecture Notes in Computer Science , vol.3695
    • Krissinel, E.1    Henrick, K.2
  • 15
    • 0030828003 scopus 로고    scopus 로고
    • Overexpression, purification, characterization, and crystallization of the BTB/POZ domain from the PLZF oncoprotein
    • Li X., Lopez-Guisa J.M., Ninan N., Weiner E.J., Rauscher III F.J., and Marmorstein R. Overexpression, purification, characterization, and crystallization of the BTB/POZ domain from the PLZF oncoprotein. J. Biol. Chem. 272 (1997) 27324-27329
    • (1997) J. Biol. Chem. , vol.272 , pp. 27324-27329
    • Li, X.1    Lopez-Guisa, J.M.2    Ninan, N.3    Weiner, E.J.4    Rauscher III, F.J.5    Marmorstein, R.6
  • 16
    • 0032580205 scopus 로고    scopus 로고
    • Crystal structure of the tetramerization domain of the Shaker potassium channel
    • Kreusch A., Pfaffinger P.J., Stevens C.F., and Choe S. Crystal structure of the tetramerization domain of the Shaker potassium channel. Nature 392 (1998) 945-948
    • (1998) Nature , vol.392 , pp. 945-948
    • Kreusch, A.1    Pfaffinger, P.J.2    Stevens, C.F.3    Choe, S.4
  • 17
    • 33646122452 scopus 로고    scopus 로고
    • An algorithm for predicting protein-protein interaction sites: abnormally exposed amino acid residues and secondary structure elements
    • Hoskins J., Lovell S., and Blundell T.L. An algorithm for predicting protein-protein interaction sites: abnormally exposed amino acid residues and secondary structure elements. Protein Sci. 15 (2006) 1017-1029
    • (2006) Protein Sci. , vol.15 , pp. 1017-1029
    • Hoskins, J.1    Lovell, S.2    Blundell, T.L.3
  • 19
  • 20
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 21
    • 33947523060 scopus 로고    scopus 로고
    • Automated search-model discovery and preparation for structure solution by molecular replacement
    • Keegan R.M., and Winn M.D. Automated search-model discovery and preparation for structure solution by molecular replacement. Acta Crystallogr. sect. D: Biol. Crystallogr. 63 (2007) 447-457
    • (2007) Acta Crystallogr. sect. D: Biol. Crystallogr. , vol.63 , pp. 447-457
    • Keegan, R.M.1    Winn, M.D.2
  • 23
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6 (1999) 458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 28
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78 (2000) 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 29
    • 1642368109 scopus 로고    scopus 로고
    • Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants
    • Stafford W.F., and Sherwood P.J. Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants. Biophys. Chem. 108 (2004) 231-243
    • (2004) Biophys. Chem. , vol.108 , pp. 231-243
    • Stafford, W.F.1    Sherwood, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.