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Volumn 49, Issue 9, 2010, Pages 1985-1997

Identification of bZIP interaction partners of viral proteins HBZ, MEQ, BZLF1, and K-bZIP using coiled-coil arrays

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DICHROISM; COILED COIL; COMPUTATIONAL DESIGN; DNA-BINDING SPECIFICITY; HETERODIMERS; HUMAN INTERACTIONS; HUMAN PROTEINS; INTERACTION PROFILES; LEUCINE ZIPPERS; LEUCINE-ZIPPER TRANSCRIPTION FACTORS; SELF-ASSOCIATIONS; VIRAL PROTEINS;

EID: 77749289862     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi902065k     Document Type: Article
Times cited : (55)

References (71)
  • 1
    • 0037276564 scopus 로고    scopus 로고
    • Viral versuscellular BCL-2 proteins
    • Hardwick, J. M., and Bellows, D. S. (2003) Viral versuscellular BCL-2 proteins. Cell. Death Differ. 10 (Suppl. 1), S68-S76.
    • (2003) Cell. Death Differ. , vol.10 , Issue.SUPPL. 1
    • Hardwick, J.M.1    Bellows, D.S.2
  • 2
    • 52149113769 scopus 로고    scopus 로고
    • Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domainswapped dimer that binds a highly selective subset of BH3-containing death ligands
    • Kvansakul, M., Yang, H., Fairlie, W. D., Czabotar, P. E., Fischer, S. F., Perugini, M. A., Huang, D. C., and Colman, P. M. (2008) Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domainswapped dimer that binds a highly selective subset of BH3-containing death ligands. Cell. Death Differ. 15, 1564-1571.
    • (2008) Cell. Death Differ. , vol.15 , pp. 1564-1571
    • Kvansakul, M.1    Yang, H.2    Fairlie, W.D.3    Czabotar, P.E.4    Fischer, S.F.5    Perugini, M.A.6    Huang, D.C.7    Colman, P.M.8
  • 3
    • 85047698710 scopus 로고    scopus 로고
    • Opposing functions of ATF2 and Fos-like transcription factors in c-Jun-mediated myogenin expression and terminal differentiation of avian myoblasts
    • Daury, L., Busson, M., Tourkine, N., Casas, F., Cassar-Malek, I., Wrutniak-Cabello, C., Castellazzi, M., and Cabello, G. (2001) Opposing functions of ATF2 and Fos-like transcription factors in c-Jun-mediated myogenin expression and terminal differentiation of avian myoblasts. Oncogene 20, 7998-8008.
    • (2001) Oncogene , vol.20 , pp. 7998-8008
    • Daury, L.1    Busson, M.2    Tourkine, N.3    Casas, F.4    Cassar-Malek, I.5    Wrutniak-Cabello, C.6    Castellazzi, M.7    Cabello, G.8
  • 4
    • 0025878233 scopus 로고
    • Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity
    • Hai, T., and Curran, T. (1.991) Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity, Proc. Natl. Acad. Sci. U.S.A. 88, 3720-3724.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 3720-3724
    • Hai, T.1    Curran, T.2
  • 5
    • 65249171530 scopus 로고    scopus 로고
    • Design of protein-interaction specificity gives selective bZIP-binding peptides
    • Grigoryan, G., Reinke, A. W., and Keating, A. E. (2009) Design of protein-interaction specificity gives selective bZIP-binding peptides. Nature 458, 859-864.
    • (2009) Nature , vol.458 , pp. 859-864
    • Grigoryan, G.1    Reinke, A.W.2    Keating, A.E.3
  • 6
    • 0037595546 scopus 로고    scopus 로고
    • Comprehensive identification of human bZIP interactions with coiled-coil arrays
    • Newman, J. R. S., and Keating, A. E. (2003) Comprehensive identification of human bZIP interactions with coiled-coil arrays. Science 300, 2097-2101.
    • (2003) Science , vol.300 , pp. 2097-2101
    • Newman, J.R.S.1    Keating, A.E.2
  • 7
    • 0006622640 scopus 로고
    • Complete nucleotide sequence of a human c-onc gene: Deduced amino acid sequence of the human c-fos protein
    • van Straaten, F., Muller, R., Curran, T., Van Beveren, C., and Verma, I. M. (1983) Complete nucleotide sequence of a human c-onc gene: deduced amino acid sequence of the human c-fos protein. Proc. Natl. Acad. Sci. U.S.A. 80, 3183-3187.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 3183-3187
    • Van Straaten, F.1    Muller, R.2    Curran, T.3    Van Beveren, C.4    Verma, I.M.5
  • 8
    • 0024580645 scopus 로고
    • The carboxy terminus of the viral Jun oncoprotein is required for complex formation with the cellular Fos protein
    • Bos, T. J., Rauscher, F. J., III, Curran, T., and Vogt, P. K. (1989) The carboxy terminus of the viral Jun oncoprotein is required for complex formation with the cellular Fos protein. Oncogene 4, 123-126.
    • (1989) Oncogene , vol.4 , pp. 123-126
    • Bos, T.J.1    Rauscher III, F.J.2    Curran, T.3    Vogt, P.K.4
  • 9
    • 0027532371 scopus 로고
    • Structure-function analysis of the maf oncogene product, a member of the b-Zip protein family
    • Kataoka, K., Nishizawa, M.,andKawai, S. (1993)Structure-function analysis of the maf oncogene product, a member of the b-Zip protein family. J. Virol. 67, 2133-2141.
    • (1993) J. Virol. , vol.67 , pp. 2133-2141
    • Kataoka, K.1    Nishizawa, M.2    Kawai, S.3
  • 10
    • 33845484007 scopus 로고    scopus 로고
    • HBZ, a new important player in the mystery of adult T-cell leukemia
    • DOI 10.1182/blood-2006-03-007732
    • Mesnard, J. M., Barbeau, B., and Devaux, C. (2006) HBZ, a new important player in the mystery of adult-T-cell leukemia, Blood 108, 3979-3982. (Pubitemid 44913265)
    • (2006) Blood , vol.108 , Issue.13 , pp. 3979-3982
    • Mesnard, J.-M.1    Barbeau, B.2    Devaux, C.3
  • 11
    • 31444442856 scopus 로고    scopus 로고
    • HTLV-I basic leucine zipper factor gene mRNA supports proliferation of adult T cell leukemia cells
    • Satou, Y., Yasunaga, J.-i., Yoshida, M., and Matsuoka, M. (2006) HTLV-I basic leucine zipper factor gene mRNA supports proliferation of adult T cell leukemia cells. Proc. Natl. Acad. Sci. U.S.A. 103, 720-725.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 720-725
    • Satou, Y.1    Yasunaga, J.-I.2    Yoshida, M.3    Matsuoka, M.4
  • 12
    • 33846846713 scopus 로고    scopus 로고
    • Human T-Cell leukemia virus type 1 (HTLV-1) bZIP protein interacts with the cellular transcription factor CREB to inhibit HTLV-1 transcription
    • DOI 10.1128/JVI.00480-06
    • Lemasson, I., Lewis, M. R., Polakowski, N., Hivin, P., Cavanagh, M.-H., Thebault, S., Barbeau, B., Nyborg, J. K., and Mesnard, J.-M. (2007) Human T-cell leukemia virus type 1 (HTLV-1) bZIP protein interacts with the cellular transcription factor CREB to inhibit HTLV-1 transcription. J. Virol. 81, 1543-1553. (Pubitemid 46214429)
    • (2007) Journal of Virology , vol.81 , Issue.4 , pp. 1543-1553
    • Lemasson, I.1    Lewis, M.R.2    Polakowski, N.3    Hivin, P.4    Cavanagh, M.-H.5    Thebault, S.6    Barbeau, B.7    Nyborg, J.K.8    Mesnard, J.-M.9
  • 13
    • 1642324261 scopus 로고    scopus 로고
    • HBZ interacts with JunD and stimulates its transcriptional activity
    • DOI 10.1016/S0014-5793(04)00225-X, PII S001457930400225X
    • Thebault, S., Basbous, J., Hivin, P., Devaux, C., and Mesnard, J.-M. (2004) HBZ interacts with JunD and stimulates its transcriptional activity. FEBS Lett. 562, 165-170. (Pubitemid 38388465)
    • (2004) FEBS Letters , vol.562 , Issue.1-3 , pp. 165-170
    • Thebault, S.1    Basbous, J.2    Hivin, P.3    Devaux, C.4    Mesnard, J.-M.5
  • 14
    • 0242321897 scopus 로고    scopus 로고
    • The HBZ Factor of Human T-cell Leukemia Virus Type i Dimerizes with Transcription Factors JunB and c-Jun and Modulates Their Transcriptional Activity
    • DOI 10.1074/jbc.M307275200
    • Basbous, J., Arpin, C., Gaudray, G., Piechaczyk, M., Devaux, C., and Mesnard, J.-M. (2003) The HBZ factor of human T-cell leukemia virus type I dimerizes with transcription factors JunB and c-Jun and modulates their transcriptional activity. J. Biol. Chem. 278, 43620-43627. (Pubitemid 37345988)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.44 , pp. 43620-43627
    • Basbous, J.1    Arpin, C.2    Gaudray, G.3    Piechaczyk, M.4    Devaux, C.5    Mesnard, J.-M.6
  • 15
    • 0036891865 scopus 로고    scopus 로고
    • The complementary strand of the human T-cell leukemia virus type 1 RNA genome encodes a bZIP transcription factor that down-regulates viral transcription
    • DOI 10.1128/JVI.76.24.12813-12822.2002
    • Gaudray, G., Gachon, F., Basbous, J., Biard-Piechaczyk, M., Devaux, C., and Mesnard, J.-M. (2002) The complementary strand of the human T-cell leukemia virus type 1 RNA genome encodes a bZIP transcription factor that down-regulates viral transcription. J. Virol. 76, 12813-12822. (Pubitemid 35386965)
    • (2002) Journal of Virology , vol.76 , Issue.24 , pp. 12813-12822
    • Gaudray, G.1    Gachon, F.2    Basbous, J.3    Biard-Piechaczyk, M.4    Devaux, C.5    Mesnard, J.-M.6
  • 16
    • 14744269942 scopus 로고    scopus 로고
    • Evolution ofMarek's disease - Aparadigmfor incessant race between the pathogen and the host
    • Nair, V. (2005) Evolution ofMarek's disease - Aparadigmfor incessant race between the pathogen and the host. Vet. J. 170, 175-183.
    • (2005) Vet. J. , vol.170 , pp. 175-183
    • Nair, V.1
  • 17
    • 58149502549 scopus 로고    scopus 로고
    • Homodimerization of Marek's disease virus-encoded Meq protein is not sufficient for transformation of lymphocytes in chickens
    • Suchodolski, P. F., Izumiya, Y., Lupiani, B., Ajithdoss, D. K., Gilad, O., Lee, L. F., Kung, H.-J., and Reddy, S. M. (2009) Homodimerization of Marek's disease virus-encoded Meq protein is not sufficient for transformation of lymphocytes in chickens. J. Virol. 83, 859-869.
    • (2009) J. Virol. , vol.83 , pp. 859-869
    • Suchodolski, P.F.1    Izumiya, Y.2    Lupiani, B.3    Ajithdoss, D.K.4    Gilad, O.5    Lee, L.F.6    Kung, H.-J.7    Reddy, S.M.8
  • 19
    • 70350309789 scopus 로고    scopus 로고
    • Homodimerization of the Meq viral oncoprotein is necessary for induction of T-cell lymphoma by Marek's disease virus
    • Brown, A. C., Smith, L. P., Kgosana, L., Baigent, S. J., Nair, V., and Allday, M. J. (2009) Homodimerization of the Meq viral oncoprotein is necessary for induction of T-cell lymphoma by Marek's disease virus. J. Virol. 83, 11142-11151.
    • (2009) J. Virol. , vol.83 , pp. 11142-11151
    • Brown, A.C.1    Smith, L.P.2    Kgosana, L.3    Baigent, S.J.4    Nair, V.5    Allday, M.J.6
  • 20
    • 0242576765 scopus 로고    scopus 로고
    • Characterization of the chromosomal binding sites and dimerization partners of the viral oncoprotein meq in marek's disease virus-transformed t cells
    • DOI 10.1128/JVI.77.23.12841-12851.2003
    • Levy, A. M., Izumiya, Y., Brunovskis, P., Xia, L., Parcells, M. S., Reddy, S. M., Lee, L., Chen, H.-W., and Kung, H.-J. (2003) Characterization of the chromosomal binding sites and dimerization partners of the viral oncoprotein Meq in Marek's disease virus-transformed T cells. J. Virol. 77, 12841-12851. (Pubitemid 37430678)
    • (2003) Journal of Virology , vol.77 , Issue.23 , pp. 12841-12851
    • Levy, A.M.1    Izumiya, Y.2    Brunovskis, P.3    Xia, L.4    Parcells, M.S.5    Reddy, S.M.6    Lee, L.7    Chen, H.-W.8    Kung, H.-J.9
  • 21
    • 0029814869 scopus 로고    scopus 로고
    • Novel DNA binding specificities of a putative herpesvirus bZIP oncoprotein
    • Qian, Z., Brunovskis, P., Lee, L., Vogt, P. K., and Kung, H. J. (1996) Novel DNA binding specificities of a putative herpesvirus bZIP oncoprotein. J. Virol. 70, 7161-7170. (Pubitemid 26307433)
    • (1996) Journal of Virology , vol.70 , Issue.10 , pp. 7161-7170
    • Qian, Z.1    Brunovskis, P.2    Lee, L.3    Vogt, P.K.4    Kung, H.-J.5
  • 22
    • 0029046226 scopus 로고
    • Transactivation activity of Meq, a Marek's disease herpesvirus bZIP protein persistently expressed in latently infected transformed T cells
    • Qian, Z., Brunovskis, P., Rauscher, F., III, Lee, L., and Kung, H. J. (1995) Transactivation activity of Meq, a Marek's disease herpesvirus bZIP protein persistently expressed in latently infected transformed T cells. J. Virol. 69, 4037-4044.
    • (1995) J. Virol. , vol.69 , pp. 4037-4044
    • Qian, Z.1    Brunovskis, P.2    Rauscher, F.3    Lee III, L.4    Kung, H.J.5
  • 23
    • 31144433632 scopus 로고    scopus 로고
    • The pleiotropic effects of Kaposi's sarcoma herpesvirus
    • Thomas, F. S. (2006) The pleiotropic effects of Kaposi's sarcoma herpesvirus. J. Pathol. 208, 187-198.
    • (2006) J. Pathol. , vol.208 , pp. 187-198
    • Thomas, F.S.1
  • 24
    • 33645745240 scopus 로고    scopus 로고
    • Spectrum of Epstein-Barr virusassociated diseases
    • Kutok, J. L., and Wang, F. (2006) Spectrum of Epstein-Barr virusassociated diseases. Annu. Rev. Pathol: Mech. Dis. 1, 375-404.
    • (2006) Annu. Rev. Pathol: Mech. Dis. , vol.1 , pp. 375-404
    • Kutok, J.L.1    Wang, F.2
  • 25
    • 0032978479 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus encodes a bZIP protein with homology to BZLF1 of Epstein-Barr virus
    • Lin, S.-F., Robinson, D. R., Miller, G., and Kung, H.-J. (1999) Kaposi's sarcoma-associated herpesvirus encodes a bZIP protein with homology to BZLF1 of Epstein-Barr virus. J. Virol. 73, 1909-1917. (Pubitemid 29098092)
    • (1999) Journal of Virology , vol.73 , Issue.3 , pp. 1909-1917
    • Lin, S.-F.1    Robinson, D.R.2    Miller, G.3    Kung, H.-J.4
  • 26
    • 0023503201 scopus 로고
    • Polymorphic proteins encoded within BZLF1 of defective and standard Epstein-Barr viruses disrupt latency
    • Countryman, J., Jenson, H., Seibl, R., Wolf, H., and Miller, G. (1987) Polymorphic proteins encoded within BZLF1 of defective and standard Epstein-Barr viruses disrupt latency. J. Virol. 61, 3672-3679. (Pubitemid 18011461)
    • (1987) Journal of Virology , vol.61 , Issue.12 , pp. 3672-3679
    • Countryman, J.1    Jenson, H.2    Seibl, R.3    Wolf, H.4    Miller, G.5
  • 27
    • 0029944992 scopus 로고    scopus 로고
    • Activation of oriLyt, the lytic origin of DNA replication of Epstein-Barr virus, by BZLF1
    • DOI 10.1006/viro.1996.0325
    • Schepers, A., Pich, D., and Hammerschmidt, W. (1996) Activation of oriLyt, the lytic origin of DNA replication of Epstein-Barr virus, by BZLF1. Virology 220, 367-376. (Pubitemid 26201693)
    • (1996) Virology , vol.220 , Issue.2 , pp. 367-376
    • Schepers, A.1    Pich, D.2    Hammerschmid, W.3
  • 28
    • 69249208678 scopus 로고    scopus 로고
    • Kaposi's sarcomaassociated herpesvirus/human herpesvirus 8 K-bZIP modulates LANA mediated suppression of lytic origin-dependent DNA synthesis
    • JVI.00922-00909.
    • Rossetto, C., Yamboliev, I., and Pari, G. S. (2009) Kaposi's sarcomaassociated herpesvirus/human herpesvirus 8 K-bZIP modulates LANA mediated suppression of lytic origin-dependent DNA synthesis, J. Virol., JVI.00922-00909.
    • (2009) J. Virol.
    • Rossetto, C.1    Yamboliev, I.2    Pari, G.S.3
  • 29
    • 63549108515 scopus 로고    scopus 로고
    • A comprehensive analysis of recruitment and transactivation potential of K-Rta and K-bZIP during reactivation of Kaposi's sarcoma-associated herpesvirus
    • Ellison, T. J., Izumiya, Y., Izumiya, C., Luciw, P. A., and Kung, H.-J. (2009) A comprehensive analysis of recruitment and transactivation potential of K-Rta and K-bZIP during reactivation of Kaposi's sarcoma-associated herpesvirus. Virology 387, 76-88.
    • (2009) Virology , vol.387 , pp. 76-88
    • Ellison, T.J.1    Izumiya, Y.2    Izumiya, C.3    Luciw, P.A.4    Kung, H.-J.5
  • 30
    • 0043169617 scopus 로고    scopus 로고
    • BZIP proteins of human gammaherpesviruses
    • Sinclair, A. J. (2003) bZIP proteins of human gammaherpesviruses. J. Gen. Virol. 84, 1941-1949.
    • (2003) J. Gen. Virol. , vol.84 , pp. 1941-1949
    • Sinclair, A.J.1
  • 31
    • 4344575045 scopus 로고    scopus 로고
    • CCAAT/enhancer binding protein {alpha} binds to the Epstein-Barr virus (EBV) ZTA protein through oligomeric interactions and contributes to cooperative transcriptional activation of the ZTA promoter through direct binding to the ZII and ZIIIB motifs during induction of the EBV lytic cycle
    • Wu, F. Y., Wang, S. E., Chen, H., Wang, L., Hayward, S. D., and Hayward, G. S. (2004) CCAAT/enhancer binding protein {alpha} binds to the Epstein-Barr virus (EBV) ZTA protein through oligomeric interactions and contributes to cooperative transcriptional activation of the ZTA promoter through direct binding to the ZII and ZIIIB motifs during induction of the EBV lytic cycle. J. Virol. 78, 4847-4865.
    • (2004) J. Virol. , vol.78 , pp. 4847-4865
    • Wu, F.Y.1    Wang, S.E.2    Chen, H.3    Wang, L.4    Hayward, S.D.5    Hayward, G.S.6
  • 32
    • 0041488861 scopus 로고    scopus 로고
    • Cell cycle arrest by Kaposi's sarcoma-associated herpesvirus replication-associated protein is mediated at both the transcriptional and posttranslational levels by binding to CCAAT/enhancer-binding protein {alpha} and p21CIP-1
    • Wu, F. Y., Wang, S. E., Tang, Q.-Q., Fujimuro, M., Chiou, C.-J., Zheng, Q., Chen,H., Hayward, S. D., Lane, M. D., and Hayward, G. S. (2003) Cell cycle arrest by Kaposi's sarcoma-associated herpesvirus replication-associated protein is mediated at both the transcriptional and posttranslational levels by binding to CCAAT/enhancer-binding protein {alpha} and p21CIP-1. J. Virol. 77, 8893-8914.
    • (2003) J. Virol. , vol.77 , pp. 8893-8914
    • Wu, F.Y.1    Wang, S.E.2    Tang, Q.-Q.3    Fujimuro, M.4    Chiou, C.-J.5    Zheng, Q.6    Chen, H.7    Hayward, S.D.8    Lane, M.D.9    Hayward, G.S.10
  • 33
    • 32444448106 scopus 로고    scopus 로고
    • Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein
    • DOI 10.1016/j.molcel.2006.01.006, PII S1097276506000074
    • Petosa, C., Morand, P., Baudin, F., Moulin, M., Artero, J.-B., and Muller, C. W. (2006) Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein. Mol. Cell 21, 565-572. (Pubitemid 43228011)
    • (2006) Molecular Cell , vol.21 , Issue.4 , pp. 565-572
    • Petosa, C.1    Morand, P.2    Baudin, F.3    Moulin, M.4    Artero, J.-B.5    Muller, C.W.6
  • 34
    • 0038420735 scopus 로고    scopus 로고
    • The zipper region of Epstein-Barr virus bZIP transcription factor Zta is necessary but not sufficient to directDNAbinding
    • Hicks, M. R., Al-Mehairi, S. S., and Sinclair, A. J. (2003) The zipper region of Epstein-Barr virus bZIP transcription factor Zta is necessary but not sufficient to directDNAbinding. J. Virol. 77, 8173-8177.
    • (2003) J. Virol. , vol.77 , pp. 8173-8177
    • Hicks, M.R.1    Al-Mehairi, S.S.2    Sinclair, A.J.3
  • 35
    • 0037095730 scopus 로고    scopus 로고
    • DNAWorks: An automated method for designing oligonucleotides for PCR-based gene synthesis
    • Hoover, D. M., and Lubkowski, J. (2002)DNAWorks: an automated method for designing oligonucleotides for PCR-based gene synthesis. Nucleic Acids Res. 30, e43.
    • (2002) Nucleic Acids Res. , vol.30
    • Hoover, D.M.1    Lubkowski, J.2
  • 40
    • 0028072795 scopus 로고
    • MafB, a new Maf family transcription activator that can associate with Maf and Fos but not with Jun
    • Kataoka, K., Fujiwara, K. T., Noda, M., and Nishizawa, M. (1994) MafB, a new Maf family transcription activator that can associate with Maf and Fos but not with Jun. Mol. Cell. Biol. 14, 7581-7591.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7581-7591
    • Kataoka, K.1    Fujiwara, K.T.2    Noda, M.3    Nishizawa, M.4
  • 41
    • 33747786692 scopus 로고    scopus 로고
    • Experimental identification of homodimerizing B-ZIP families in Homo sapiens
    • Acharya, A., Rishi, V., Moll, J., and Vinson, C. (2006) Experimental identification of homodimerizing B-ZIP families in Homo sapiens. J. Struct. Biol. 155, 130-139.
    • (2006) J. Struct. Biol. , vol.155 , pp. 130-139
    • Acharya, A.1    Rishi, V.2    Moll, J.3    Vinson, C.4
  • 43
    • 0028303982 scopus 로고
    • Expansion of CREB's DNA recognition specificity by Tax results from interaction with Ala-Ala-Arg at positions 282-284 near the conserved DNA-binding domain of CREB
    • Adya, N., Zhao, L. J., Huang, W., Boros, I., and Giam, C. Z. (1994) Expansion of CREB's DNA recognition specificity by Tax results from interaction with Ala-Ala-Arg at positions 282-284 near the conserved DNA-binding domain of CREB. Proc. Natl. Acad. Sci. U.S.A. 91, 5642-5646.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5642-5646
    • Adya, N.1    Zhao, L.J.2    Huang, W.3    Boros, I.4    Giam, C.Z.5
  • 44
    • 29044441963 scopus 로고    scopus 로고
    • Cooperative interaction of Zhangfei and ATF4 in transactivation of the cyclic AMP response element
    • Hogan, M., R., Cockram, G., P., and Lu, R. (2006) Cooperative interaction of Zhangfei and ATF4 in transactivation of the cyclic AMP response element. FEBS Lett. 580, 58-62.
    • (2006) FEBS Lett. , vol.580 , pp. 58-62
    • Hogan, M.R.1    Cockram, G.P.2    Lu, R.3
  • 45
    • 0029928173 scopus 로고    scopus 로고
    • Stress-induced binding of the transcriptional factor CHOP to a novel DNA control element
    • Ubeda, M., Wang, X. Z., Zinszner, H., Wu, I., Habener, J. F., and Ron, D. (1996) Stress-induced binding of the transcriptional factor CHOP to a novel DNA control element. Mol. Cell. Biol. 16, 1479-1489.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1479-1489
    • Ubeda, M.1    Wang, X.Z.2    Zinszner, H.3    Wu, I.4    Habener, J.F.5    Ron, D.6
  • 46
    • 33744802934 scopus 로고    scopus 로고
    • A modified version of a Fos-associated cluster in HBZ affects Jun transcriptional potency
    • DOI 10.1093/nar/gkl375
    • Hivin, P., Arpin-Andre, C., Clerc, I., Barbeau, B., and Mesnard, J.-M. (2006) A modified version of a Fos-associated cluster in HBZ affects Jun transcriptional potency. Nucleic Acids Res. 34, 2761-2772. (Pubitemid 43985637)
    • (2006) Nucleic Acids Research , vol.34 , Issue.9 , pp. 2761-2772
    • Hivin, P.1    Arpin-Andre, C.2    Clerc, I.3    Barbeau, B.4    Mesnard, J.-M.5
  • 47
    • 35148863054 scopus 로고    scopus 로고
    • Binding of Kaposi's sarcoma-associated herpesvirus K-bZIP to interferon-responsive factor 3 elements modulates antiviral gene expression
    • DOI 10.1128/JVI.00183-07
    • Lefort, S., Soucy-Faulkner, A., Grandvaux, N., and Flamand, L. (2007) Binding of Kaposi's sarcoma-associated herpesvirus K-bZIP to interferon-responsive factor 3 elements modulates antiviral gene expression. J. Virol. 81, 10950-10960. (Pubitemid 47536069)
    • (2007) Journal of Virology , vol.81 , Issue.20 , pp. 10950-10960
    • Lefort, S.1    Soucy-Faulkner, A.2    Grandvaux, N.3    Flamand, L.4
  • 48
    • 0025290086 scopus 로고
    • The Epstein-Barr virus Zta transactivator: A member of the bZIP family with unique DNA-binding specificity and a dimerization domain that lacks the characteristic heptad leucine zipper motif
    • Chang, Y. N., Dong, D. L., Hayward, G. S., and Hayward, S. D. (1990) The Epstein-Barr virus Zta transactivator: a member of the bZIP family with unique DNA-binding specificity and a dimerization domain that lacks the characteristic heptad leucine zipper motif. J. Virol. 64, 3358-3369.
    • (1990) J. Virol. , vol.64 , pp. 3358-3369
    • Chang, Y.N.1    Dong, D.L.2    Hayward, G.S.3    Hayward, S.D.4
  • 49
    • 13944265035 scopus 로고    scopus 로고
    • HTLV-1 HBZ suppresses AP-1 activity by impairing both the DNA-binding ability and the stability of c-Jun protein
    • DOI 10.1038/sj.onc.1208297
    • Matsumoto, J., Ohshima, T., Isono, O., and Shimotohno, K. (2005) HTLV-1 HBZ suppresses AP-1 activity by impairing both the DNAbinding ability and the stability of c-Jun protein. Oncogene 24, 1001-1010. (Pubitemid 40313877)
    • (2005) Oncogene , vol.24 , Issue.6 , pp. 1001-1010
    • Matsumoto, J.1    Ohshima, T.2    Isono, O.3    Shimotohno, K.4
  • 50
    • 0035038931 scopus 로고    scopus 로고
    • Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1
    • Hicks, M. R., Balesaria, S., Medina-Palazon, C., Pandya, M. J., Woolfson, D. N., and Sinclair, A. J. (2001) Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1. J. Virol. 75, 5381-5384.
    • (2001) J. Virol. , vol.75 , pp. 5381-5384
    • Hicks, M.R.1    Balesaria, S.2    Medina-Palazon, C.3    Pandya, M.J.4    Woolfson, D.N.5    Sinclair, A.J.6
  • 51
    • 0028053782 scopus 로고
    • A conserved region adjacent to the basic domain is required for recognition of an extended DNA binding site by Maf/Nrl family proteins
    • Kerppola, T. K., and Curran, T. (1994) A conserved region adjacent to the basic domain is required for recognition of an extended DNA binding site by Maf/Nrl family proteins. Oncogene 9, 3149-3158.
    • (1994) Oncogene , vol.9 , pp. 3149-3158
    • Kerppola, T.K.1    Curran, T.2
  • 52
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen, Y. H., Yang, J. T., and Chau, K. H. (1974) Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 53
    • 0024284824 scopus 로고
    • Common DNA binding site for Fos protein complexes and transcription factor AP-1
    • Rauscher, F. J., III, Sambucetti, L. C., Curran, T., Distel, R. J., and Spiegelman, B. M. (1988) Common DNA binding site for Fos protein complexes and transcription factor AP-1. Cell 52, 471-480.
    • (1988) Cell , vol.52 , pp. 471-480
    • Rauscher III, F.J.1    Sambucetti, L.C.2    Curran, T.3    Distel, R.J.4    Spiegelman, B.M.5
  • 54
    • 0023655765 scopus 로고
    • Separate binding sites for nuclear factor 1 and a CCAAT DNA binding factor in the mouse alpha 2(I) collagen promoter
    • Oikarinen, J., Hatamochi, A., and de Crombrugghe, B. (1987) Separate binding sites for nuclear factor 1 and a CCAAT DNA binding factor in the mouse alpha 2(I) collagen promoter. J. Biol. Chem. 262, 11064-11070.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11064-11070
    • Oikarinen, J.1    Hatamochi, A.2    De Crombrugghe, B.3
  • 55
    • 0027176792 scopus 로고
    • Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding: Prediction and rational design
    • Vinson, C. R., Hai, T., and Boyd, S. M. (1993) Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding: prediction and rational design. Genes Dev. 7, 1047-1058.
    • (1993) Genes Dev. , vol.7 , pp. 1047-1058
    • Vinson, C.R.1    Hai, T.2    Boyd, S.M.3
  • 56
    • 0026772417 scopus 로고
    • Transcriptional repression by a novel member of the bZIP family of transcription factors
    • Cowell, I. G., Skinner, A., and Hurst, H. C. (1992) Transcriptional repression by a novel member of the bZIP family of transcription factors. Mol. Cell. Biol. 12, 3070-3077.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3070-3077
    • Cowell, I.G.1    Skinner, A.2    Hurst, H.C.3
  • 57
    • 0030804094 scopus 로고    scopus 로고
    • Leucine is the most stabilizing aliphatic amino acid in the d position of a dimeric leucine zipper coiled coil
    • Moitra, J., Szilak, L., Krylov, D., and Vinson, C. (1997) Leucine is the most stabilizing aliphatic amino acid in the d position of a dimeric leucine zipper coiled coil. Biochemistry 36, 12567-12573.
    • (1997) Biochemistry , vol.36 , pp. 12567-12573
    • Moitra, J.1    Szilak, L.2    Krylov, D.3    Vinson, C.4
  • 58
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury, P. B., Zhang, T., Kim, P. S., and Alber, T. (1993) A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262, 1401-1407. (Pubitemid 23983059)
    • (1993) Science , vol.262 , Issue.5138 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 59
    • 0037117698 scopus 로고    scopus 로고
    • Contribution of buried lysine residues to the oligomerization specificity and stability of the Fos coiled coil
    • Campbell, K. M., Sholders, A. J., and Lumb, K. J. (2002) Contribution of buried lysine residues to the oligomerization specificity and stability of the Fos coiled coil. Biochemistry 41, 4866-4871.
    • (2002) Biochemistry , vol.41 , pp. 4866-4871
    • Campbell, K.M.1    Sholders, A.J.2    Lumb, K.J.3
  • 60
    • 39049166620 scopus 로고    scopus 로고
    • HTLV-1 HBZ cooperates with JunD to enhance transcription of the human telomerase reverse transcriptase gene (hTERT)
    • Kuhlmann, A.-S., Villaudy, J., Gazzolo, L., Castellazzi, M., Mesnard, J.-M., and Duc Dodon, M. (2007) HTLV-1 HBZ cooperates with JunD to enhance transcription of the human telomerase reverse transcriptase gene (hTERT). Retrovirology 4, 92.
    • (2007) Retrovirology , vol.4 , pp. 92
    • Kuhlmann, A.-S.1    Villaudy, J.2    Gazzolo, L.3    Castellazzi, M.4    Mesnard, J.-M.5    Duc Dodon, M.6
  • 61
    • 0025829599 scopus 로고
    • C-JUN, JUN B, and JUNDdiffer in their binding affinities to AP-1 and CRE consensus sequences: Effect of FOS proteins
    • Ryseck, R. P., and Bravo,R. (1991) c-JUN, JUN B, and JUNDdiffer in their binding affinities to AP-1 and CRE consensus sequences: effect of FOS proteins. Oncogene 6, 533-542.
    • (1991) Oncogene , vol.6 , pp. 533-542
    • Ryseck, R.P.1    Bravo, R.2
  • 62
    • 24344479164 scopus 로고    scopus 로고
    • Genetic evidence that small maf proteins are essential for the activation of antioxidant response elementdependent genes
    • Katsuoka, F., Motohashi, H., Ishii, T., Aburatani, H., Engel, J. D., and Yamamoto, M. (2005) Genetic evidence that small maf proteins are essential for the activation of antioxidant response elementdependent genes. Mol. Cell. Biol. 25, 8044-8051.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8044-8051
    • Katsuoka, F.1    Motohashi, H.2    Ishii, T.3    Aburatani, H.4    Engel, J.D.5    Yamamoto, M.6
  • 63
    • 0035971506 scopus 로고    scopus 로고
    • Jun, the oncoprotein
    • Vogt, P. K. (2001) Jun, the oncoprotein. Oncogene 20, 2365-2377.
    • (2001) Oncogene , vol.20 , pp. 2365-2377
    • Vogt, P.K.1
  • 65
    • 0035965302 scopus 로고    scopus 로고
    • Maf and Jun nuclear oncoproteins share downstream target genes for inducing cell transformation
    • Kataoka, K., Shioda, S., Yoshitomo-Nakagawa, K., Handa, H., and Nishizawa, M. (2001) Maf and Jun nuclear oncoproteins share downstream target genes for inducing cell transformation. J. Biol. Chem. 276, 36849-36856.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36849-36856
    • Kataoka, K.1    Shioda, S.2    Yoshitomo-Nakagawa, K.3    Handa, H.4    Nishizawa, M.5
  • 66
    • 0037189579 scopus 로고    scopus 로고
    • Regulation of CCAAT/enhancer-binding protein (C/EBP) activator proteins by heterodimerization with C/EBPγ (Ig/EBP)
    • DOI 10.1074/jbc.M202184200
    • Parkin, S. E., Baer, M., Copeland, T. D., Schwartz, R. C., and Johnson, P. F. (2002) Regulation of CCAAT/enhancer-binding protein (C/EBP) activator proteins by heterodimerization with C/EBPgamma (Ig/EBP). J. Biol. Chem. 277, 23563-23572. (Pubitemid 34952192)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23563-23572
    • Parkin, S.E.1    Baer, M.2    Copeland, T.D.3    Schwartz, R.C.4    Johnson, P.F.5
  • 67
    • 0031723586 scopus 로고    scopus 로고
    • Transcription factor ATF2 cooperates with v-Jun to promote growth factor-independent proliferation in vitro and tumor formation in vivo
    • Huguier, S., Baguet, J., Perez, S., van Dam, H., and Castellazzi, M. (1998) Transcription factor ATF2 cooperates with v-Jun to promote growth factor-independent proliferation in vitro and tumor formation in vivo. Mol. Cell. Biol. 18, 7020-7029.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7020-7029
    • Huguier, S.1    Baguet, J.2    Perez, S.3    Van Dam, H.4    Castellazzi, M.5
  • 68
    • 0342424185 scopus 로고    scopus 로고
    • Zhangfei: A second cellular protein interacts with herpes simplex virus accessory factor HCF in a manner similar to Luman and VP16
    • Lu, R., and Misra, V. (2000) Zhangfei: a second cellular protein interacts with herpes simplex virus accessory factor HCF in a manner similar to Luman and VP16. Nucleic Acids Res. 28, 2446-2454.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2446-2454
    • Lu, R.1    Misra, V.2
  • 69
    • 0030992167 scopus 로고    scopus 로고
    • Pivotal role for the NFIL3/E4BP4 transcription factor in interleukin 3-mediated survival of pro-B lymphocytes
    • Ikushima, S., Inukai, T., Inaba, T., Nimer, S. D., Cleveland, J. L., and Look, A. T. (1997) Pivotal role for the NFIL3/E4BP4 transcription factor in interleukin 3-mediated survival of pro-B lymphocytes. Proc. Natl. Acad. Sci. U.S.A. 94, 2609-2614.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2609-2614
    • Ikushima, S.1    Inukai, T.2    Inaba, T.3    Nimer, S.D.4    Cleveland, J.L.5    Look, A.T.6
  • 70
    • 0034940767 scopus 로고    scopus 로고
    • Lightinduced phase-delay of the chicken pineal circadian clock is associated with the induction of cE4bp4, a potential transcriptional repressor of cPer2 gene
    • Doi, M., Nakajima, Y., Okano, T., and Fukada, Y. (2001) Lightinduced phase-delay of the chicken pineal circadian clock is associated with the induction of cE4bp4, a potential transcriptional repressor of cPer2 gene. Proc. Natl. Acad. Sci. U.S.A. 98, 8089-8094.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8089-8094
    • Doi, M.1    Nakajima, Y.2    Okano, T.3    Fukada, Y.4
  • 71
    • 0032978728 scopus 로고    scopus 로고
    • Transcriptional repression of human hepatitis B virus genes by a bZIP family member, E4BP4
    • Lai, C.-K., and Ting, L.-P. (1999) Transcriptional repression of human hepatitis B virus genes by a bZIP family member, E4BP4. J. Virol. 73, 3197-3209.
    • (1999) J. Virol. , vol.73 , pp. 3197-3209
    • Lai, C.-K.1    Ting, L.-P.2


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