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Volumn 2, Issue 2, 1998, Pages 201-212

Structures of SAP-1 bound to DNA targets from the E74 and c-fos promoters: Insights into DNA sequence discrimination by Ets proteins

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA BINDING PROTEIN; E74 PROTEIN, DROSOPHILA; ELK4 PROTEIN, HUMAN; ELK4 PROTEIN, MOUSE; ONCOPROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ELK 4; TRANSCRIPTION FACTOR ETS;

EID: 0032135105     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80130-6     Document Type: Article
Times cited : (97)

References (68)
  • 1
    • 44949289693 scopus 로고
    • Crystallization of DNA binding proteins with oligonucleotides
    • Aggarwal, A.K. (1990). Crystallization of DNA binding proteins with oligonucleotides. Methods 1, 83-90.
    • (1990) Methods , vol.1 , pp. 83-90
    • Aggarwal, A.K.1
  • 2
    • 0030966101 scopus 로고    scopus 로고
    • The roles of ets transcription factors in the development and function of the mammalian immune system
    • Bassuk, A.G., and Leiden, J.M. (1997). The roles of Ets transcription factors in the development and function of the mammalian immune system. Adv. Immunol. 64, 65-104.
    • (1997) Adv. Immunol. , vol.64 , pp. 65-104
    • Bassuk, A.G.1    Leiden, J.M.2
  • 3
    • 0032512459 scopus 로고    scopus 로고
    • The structure of GABPα/β: An ETS domain-ankyrin repeat heterodimer bound to DNA
    • Batchelor, A.H., Piper, D.E., de la Brousse, F.C., McKnight, S.L., and Wolberger, C. (1998). The structure of GABPα/β: an ETS domain-ankyrin repeat heterodimer bound to DNA. Science 279, 1037-1041.
    • (1998) Science , vol.279 , pp. 1037-1041
    • Batchelor, A.H.1    Piper, D.E.2    De La Brousse, F.C.3    McKnight, S.L.4    Wolberger, C.5
  • 5
    • 0027275485 scopus 로고
    • The winged-helix DNA-binding motif: Another helix-turn-helix takeoff
    • Brennan, R.G. (1993). The winged-helix DNA-binding motif: another helix-turn-helix takeoff. Cell 74, 773-776.
    • (1993) Cell , vol.74 , pp. 773-776
    • Brennan, R.G.1
  • 6
    • 0027083526 scopus 로고
    • Specificities of protein-protein and protein-DNA interaction of GABPα and two newly defined ETS-related proteins
    • Brown, T.A., and McKnight, S.L. (1992). Specificities of protein-protein and protein-DNA interaction of GABPα and two newly defined ETS-related proteins. Genes Dev. 6, 2502-2512.
    • (1992) Genes Dev. , vol.6 , pp. 2502-2512
    • Brown, T.A.1    McKnight, S.L.2
  • 9
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity assessing the accuracy of crystal structures
    • Brünger, A.T. (1992b). The free R value: a novel statistical quantity assessing the accuracy of crystal structures. Nature 335, 472-474.
    • (1992) Nature , vol.335 , pp. 472-474
    • Brünger, A.T.1
  • 10
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brünger, A.T., and Krukowski, A. (1990). Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr. A 46, 585-593.
    • (1990) Acta Crystallogr. A , vol.46 , pp. 585-593
    • Brünger, A.T.1    Krukowski, A.2
  • 11
    • 0023140814 scopus 로고
    • Crystallographic r factor refinement by molecular dynamics
    • Brünger, AT., Kuriyan, J., and Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 12
    • 0029680611 scopus 로고    scopus 로고
    • Signalling pathways: Jack of all cascades
    • Cahill, M.A., Janknecht, R., and Nordheim, A. (1996). Signalling pathways: jack of all cascades. Curr. Biol. 6, 16-19.
    • (1996) Curr. Biol. , vol.6 , pp. 16-19
    • Cahill, M.A.1    Janknecht, R.2    Nordheim, A.3
  • 13
    • 0027270989 scopus 로고
    • Cocrystal structure of the HNF-3/forkhead DNA-recognition motif resembles histone H5
    • Clark, K.L., Halay, E.D., Lai, E., and Burley, S.K. (1993). Cocrystal structure of the HNF-3/forkhead DNA-recognition motif resembles histone H5. Nature 364, 412-420.
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 14
    • 0026556859 scopus 로고
    • Characterization of sap-1, a protein recruited by serum response factor to the c-fos serum response element
    • Dalton, S., and Treisman, R. (1992). Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element. Cell 68, 597-612.
    • (1992) Cell , vol.68 , pp. 597-612
    • Dalton, S.1    Treisman, R.2
  • 15
    • 0026702486 scopus 로고
    • Dnastructurefrom A to Z
    • Dickerson, R.E. (1992). DNAstructurefrom A to Z. Methods Enzymol. 211, 67-111.
    • (1992) Methods Enzymol. , vol.211 , pp. 67-111
    • Dickerson, R.E.1
  • 16
    • 0030841590 scopus 로고    scopus 로고
    • Collaborative computational project, number 4: Providing programs for X-ray crystallography
    • Dodson, E.J., Winn, M., and Ralph, A. (1997). Collaborative Computational Project, Number 4: providing programs for X-ray crystallography. Methods Enzymol. 277, 620-633.
    • (1997) Methods Enzymol. , vol.277 , pp. 620-633
    • Dodson, E.J.1    Winn, M.2    Ralph, A.3
  • 17
    • 0030044420 scopus 로고    scopus 로고
    • Solution structure of the ETS domain from murine Ets-1: A winged helix-turn-helix DNA binding motif
    • Donaldson, L.W., Petersen, J.M., Graves, B.J., and McIntosh, L.P. (1996). Solution structure of the ETS domain from murine Ets-1: a winged helix-turn-helix DNA binding motif. EMBO J. 15, 125-134.
    • (1996) EMBO J. , vol.15 , pp. 125-134
    • Donaldson, L.W.1    Petersen, J.M.2    Graves, B.J.3    McIntosh, L.P.4
  • 18
    • 0027049805 scopus 로고
    • The gCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted a helices: Crystal structure of the protein-DNA complex
    • Ellenberger, T.E., Brandi, C.J., Struhl, K., and Harrison, S.C. (1992). The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted a helices: crystal structure of the protein-DNA complex. Cell 71, 1223-1237.
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandi, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 19
    • 0031933646 scopus 로고    scopus 로고
    • Structure of IRF-1 with bound DNA reveals determinants of interferon regulation
    • Escalante, C.R., Yie, J., Thanos, D., and Aggarwal, A.K. (1998). Structure of IRF-1 with bound DNA reveals determinants of interferon regulation. Nature 391, 103-106.
    • (1998) Nature , vol.391 , pp. 103-106
    • Escalante, C.R.1    Yie, J.2    Thanos, D.3    Aggarwal, A.K.4
  • 20
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representation of macromolecules
    • Evans, S.V. (1993). SETOR: hardware lighted three-dimensional solid model representation of macromolecules. J. Mol. Graph. 11, 134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 21
    • 0026630148 scopus 로고
    • Human ets-1-oncoprotein - Purification, isoforms, SH modification, and DNA sequence-specific binding
    • Fisher, R.J., Koizumi, S., Kondoh, A., Mariano, J.M., Mavrothalassitis, G., Bhat, N.K., and Papas, T.S. (1992). Human Ets-1-oncoprotein - purification, isoforms, SH modification, and DNA sequence-specific binding. Biol. Chem. 267, 17957-17965.
    • (1992) Biol. Chem. , vol.267 , pp. 17957-17965
    • Fisher, R.J.1    Koizumi, S.2    Kondoh, A.3    Mariano, J.M.4    Mavrothalassitis, G.5    Bhat, N.K.6    Papas, T.S.7
  • 22
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program package for the processing and analysis of diffraction data from macromolecules
    • C.W. Carter and R.M. Sweet, eds. (Orlando, FL: Academic Press)
    • Furey, W., and Swaminathan, S. (1997). PHASES-95: a program package for the processing and analysis of diffraction data from macromolecules. In Methods in Enzymology, C.W. Carter and R.M. Sweet, eds. (Orlando, FL: Academic Press), pp. 590-620.
    • (1997) Methods in Enzymology , pp. 590-620
    • Furey, W.1    Swaminathan, S.2
  • 24
    • 0025310356 scopus 로고
    • DNA recognition by proteins with the helix-turn-helix motif
    • Harrison, S.C., and Aggarwal, A.K. (1990). DNA recognition by proteins with the helix-turn-helix motif. Annu. Rev. Biochem. 59, 933-969.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 933-969
    • Harrison, S.C.1    Aggarwal, A.K.2
  • 25
    • 0027958045 scopus 로고
    • Crystal structure of the DNA binding domain of the heat shock transcription factor
    • Harrison, C.J., Bohm, A.A., and Nelson, H.C.M. (1994). Crystal structure of the DNA binding domain of the heat shock transcription factor. Science 364, 224-227.
    • (1994) Science , vol.364 , pp. 224-227
    • Harrison, C.J.1    Bohm, A.A.2    Nelson, H.C.M.3
  • 26
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson, E.G., and Thornton, J.M. (1996). PROMOTIF - a program to identify and analyze structural motifs in proteins. Protein Sci. 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 27
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsin and neuraminidase crystal structures
    • Jiang, J.S., and Brünger, A.T. (1994). Protein hydration observed by X-ray diffraction: solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243, 100-115.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brünger, A.T.2
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., and Cowen, S.W. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowen, S.W.3
  • 29
    • 85027632383 scopus 로고
    • Automatic indexing of rotation diffraction patterns
    • Kabsch, W. (1988a). Automatic indexing of rotation diffraction patterns. J. Appl. Crystallogr. 21, 67-71.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 67-71
    • Kabsch, W.1
  • 30
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. (1988b). Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 21, 916-924.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 31
    • 0030497978 scopus 로고    scopus 로고
    • Efficient rebuilding of protein structures
    • Kleywegt, G.J., and Jones, T.A. (1996a). Efficient rebuilding of protein structures. Acta Crystallogr. D 52, 829-832.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 829-832
    • Kleywegt, G.J.1    Jones, T.A.2
  • 32
    • 0030589514 scopus 로고    scopus 로고
    • Phi/Psi-chology: Ramachandran revisted
    • Kleywegt, G.J., and Jones, T.A. (1996b). Phi/Psi-chology: Ramachandran revisted. Curr. Biol. 4, 1395-1400.
    • (1996) Curr. Biol. , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 33
    • 0029670530 scopus 로고    scopus 로고
    • A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex
    • Kodandapani, R., Rio, F., Ni, C.-Z., Piccialli, G., Klemsz, M., McKercher, S., Maki, R.A., and Ely, K.R. (1996). A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex. Nature 380, 456-460.
    • (1996) Nature , vol.380 , pp. 456-460
    • Kodandapani, R.1    Rio, F.2    Ni, C.-Z.3    Piccialli, G.4    Klemsz, M.5    McKercher, S.6    Maki, R.A.7    Ely, K.R.8
  • 34
    • 0032499208 scopus 로고    scopus 로고
    • Erratum: A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex
    • Kodandapani, R., Pio, F., Ni, C.-Z., Piccialli, G., Klemsz, M., McKercher, S., Maki, R.A., and Ely, K.R. (1998). Erratum: A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex. Nature 392 (6676).
    • (1998) Nature , vol.392 , pp. 6676
    • Kodandapani, R.1    Pio, F.2    Ni, C.-Z.3    Piccialli, G.4    Klemsz, M.5    McKercher, S.6    Maki, R.A.7    Ely, K.R.8
  • 35
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 36
    • 0024539180 scopus 로고
    • Defining the structure of irregular nucleic acids: Conventions and principles
    • Lavery, R., and Sklenar, H. (1989). Defining the structure of irregular nucleic acids: conventions and principles. J. Biomol. Struct. Dyn. 6, 655-667.
    • (1989) J. Biomol. Struct. Dyn. , vol.6 , pp. 655-667
    • Lavery, R.1    Sklenar, H.2
  • 38
    • 0030921505 scopus 로고    scopus 로고
    • Molecular characterization of the B-box protein-protein interaction motif of the ETS-domain transcription factor Elk-1
    • Ling, Y., Lakey, J.H., Roberts, C.E., and Sharrocks, A.D. (1997). Molecular characterization of the B-box protein-protein interaction motif of the ETS-domain transcription factor Elk-1. EMBO J. 16, 2431-2440.
    • (1997) EMBO J. , vol.16 , pp. 2431-2440
    • Ling, Y.1    Lakey, J.H.2    Roberts, C.E.3    Sharrocks, A.D.4
  • 39
    • 0028345890 scopus 로고
    • ERP, a new member of the ETS transcription factor oncoprotein family - Cloning, characterization, and differential expression during B-lymphocyte development
    • Lopez, M., Oettgen, P., Akbarali, Y., Dendorfer, U., and Libermann, T.A. (1994). ERP, a new member of the ETS transcription factor oncoprotein family - cloning, characterization, and differential expression during B-lymphocyte development. Mol. Cell. Biol. 14, 3292-3309.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3292-3309
    • Lopez, M.1    Oettgen, P.2    Akbarali, Y.3    Dendorfer, U.4    Libermann, T.A.5
  • 40
    • 0028277788 scopus 로고
    • The Fli-1 chimeric Ews-Fli-1 oncoproteins display similar DNA-binding specificities
    • Mao, X.H., Miesfeldt, S., Yang, H.D., Leiden, J.M., and Thompson, C.B. (1994). The Fli-1 chimeric Ews-Fli-1 oncoproteins display similar DNA-binding specificities. J. Biol. Chem. 268, 18216-18222.
    • (1994) J. Biol. Chem. , vol.268 , pp. 18216-18222
    • Mao, X.H.1    Miesfeldt, S.2    Yang, H.D.3    Leiden, J.M.4    Thompson, C.B.5
  • 41
    • 0026547747 scopus 로고
    • DNA recognition by GAL4: Structure of a protein-DNA complex
    • Marmorstein, R., Carey, M., Ptashne, M., and Harrison, S.C. (1992). DNA recognition by GAL4: structure of a protein-DNA complex. Nature 356, 408-414.
    • (1992) Nature , vol.356 , pp. 408-414
    • Marmorstein, R.1    Carey, M.2    Ptashne, M.3    Harrison, S.C.4
  • 42
    • 0028057108 scopus 로고
    • RASTER3D version 2.0: A program for photorealistic molecular graphics
    • Merritt, E.A., and Murphy, M.E.P. (1994). RASTER3D version 2.0: a program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 43
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta. Crystallogr. A 50, 157-163.
    • (1994) Acta. Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 44
    • 0028241531 scopus 로고
    • Distinctive DNA conformation with enlarged major groove is found in Zn-finger DNA and other protein-DNA complexes
    • Nekludova, L., and Pabo, C.O. (1994). Distinctive DNA conformation with enlarged major groove is found in Zn-finger DNA and other protein-DNA complexes. Proc. Natl. Acad. Sci. USA 91, 6948-6952.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6948-6952
    • Nekludova, L.1    Pabo, C.O.2
  • 45
    • 0028921122 scopus 로고
    • Structure and function of DNA binding proteins
    • Nelson, H.C. (1995). Structure and function of DNA binding proteins. Curr. Opin. Genet. Dev. 5, 180-189.
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 180-189
    • Nelson, H.C.1
  • 46
    • 0026729269 scopus 로고
    • Interaction of murine ETS-1 with GGA-binding sites establishes the ets domain as a new DNA-binding motif
    • Nye, J.A., Petersen, J.M., Gunther, C.V., Jonsen, M.D., and Graves, B.J. (1992). Interaction of murine ETS-1 with GGA-binding sites establishes the ets domain as a new DNA-binding motif. Genes Dev. 6, 975-990.
    • (1992) Genes Dev. , vol.6 , pp. 975-990
    • Nye, J.A.1    Petersen, J.M.2    Gunther, C.V.3    Jonsen, M.D.4    Graves, B.J.5
  • 47
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, and S. Bailey, eds. (Warrington, UK: SERC Daresbury Laboratory)
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing., L. Sawyer, N. Isaacs, and S. Bailey, eds. (Warrington, UK: SERC Daresbury Laboratory), pp. 56-62.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 48
    • 0029102041 scopus 로고
    • Structure of serum response factor core bound to DNA
    • Pellegrini, L., Tan, S., and Richmond, T.J. (1995). Structure of serum response factor core bound to DNA. Nature 376, 490-498.
    • (1995) Nature , vol.376 , pp. 490-498
    • Pellegrini, L.1    Tan, S.2    Richmond, T.J.3
  • 49
    • 10144255103 scopus 로고    scopus 로고
    • New insights on dna recognition by ets proteins from the crystal structure of the PU.1 ETS domain-DNA complex
    • Pio, F., Kodandapani, R., Ni, C.-Z., Shepard, W., Klemsz, M., McKercher, S.R., Maki, R.A., and Ely, K.R. (1996). New insights on DNA recognition by ets proteins from the crystal structure of the PU.1 ETS domain-DNA complex. J. Biol. Chem. 271, 23329-23337.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23329-23337
    • Pio, F.1    Kodandapani, R.2    Ni, C.-Z.3    Shepard, W.4    Klemsz, M.5    McKercher, S.R.6    Maki, R.A.7    Ely, K.R.8
  • 50
    • 0029005240 scopus 로고
    • Comparative analysis of the ternary complex factors Elk-1. SAP-1a and SAP-2 (ERP/NET)
    • Price, M.A., Rogers, A.E., and Treisman, R. (1995). Comparative analysis of the ternary complex factors Elk-1. SAP-1a and SAP-2 (ERP/NET). EMBO J. 14, 2589-2601.
    • (1995) EMBO J. , vol.14 , pp. 2589-2601
    • Price, M.A.1    Rogers, A.E.2    Treisman, R.3
  • 51
    • 0027402969 scopus 로고
    • Crystal structure of the globular domain of histone H5 and its implications for nucleosomal binding
    • Ramakrishnan, V., Finch, J.T., Graviano, V., Lee, P.L., and Sweet, R.M. (1993). Crystal structure of the globular domain of histone H5 and its implications for nucleosomal binding. Nature 362, 219-223.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graviano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 52
    • 0024536716 scopus 로고
    • Elk-1, tissue-specific ets related genes on chromosome X and 14 near translocation breakpoints
    • Rao, U.N., Huebner, K., Isobe, M., Ar-Rushdi, A., Croce, C.M., and Reddy, E.S. (1989). Elk-1, tissue-specific ets related genes on chromosome X and 14 near translocation breakpoints. Science 244, 66-70.
    • (1989) Science , vol.244 , pp. 66-70
    • Rao, U.N.1    Huebner, K.2    Isobe, M.3    Ar-Rushdi, A.4    Croce, C.M.5    Reddy, E.S.6
  • 53
    • 0029125443 scopus 로고
    • DNA binding specificities of spi-1/PU.1 and Spi-B transcription factors and identification of a Spi-1/Spi-B binding site in the c-fes/ c-fps promoter
    • Ray-Gallet, D., Mao, C., Tavitian, A., and Moreau-Gachelin, F. (1995). DNA binding specificities of Spi-1/PU.1 and Spi-B transcription factors and identification of a Spi-1/Spi-B binding site in the c-fes/ c-fps promoter. Oncogene 11, 303-313.
    • (1995) Oncogene , vol.11 , pp. 303-313
    • Ray-Gallet, D.1    Mao, C.2    Tavitian, A.3    Moreau-Gachelin, F.4
  • 54
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • Rice, L.M., and Brünger, A.T. (1994). Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement. Proteins 19, 277-290.
    • (1994) Proteins , vol.19 , pp. 277-290
    • Rice, L.M.1    Brünger, A.T.2
  • 56
    • 0028211125 scopus 로고
    • The transcription factors Elk-1 and serum response factor interact by direct protein-protein contacts mediated by a short region of Elk-1
    • Shore, P., and Sharrocks, A.D. (1994). The transcription factors Elk-1 and serum response factor interact by direct protein-protein contacts mediated by a short region of Elk-1. Mol. Cell. Biol. 14, 3283-3291.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3283-3291
    • Shore, P.1    Sharrocks, A.D.2
  • 57
    • 0028934434 scopus 로고
    • The MADS-box family of transcription factors
    • Shore, P., and Sharrocks, A.D. (1995a). The MADS-box family of transcription factors. Eur. J. Biochem. 229, 1-13.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 1-13
    • Shore, P.1    Sharrocks, A.D.2
  • 58
    • 0028801386 scopus 로고
    • The ETS-domain transcription factors ELK-1 and SAP-1 exhibit differential DNA binding specificities
    • Shore, P., and Sharrocks, A.D. (1995b). The ETS-domain transcription factors ELK-1 and SAP-1 exhibit differential DNA binding specificities. Nucleic Acids Res. 23, 4698-4706.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4698-4706
    • Shore, P.1    Sharrocks, A.D.2
  • 62
    • 0028084337 scopus 로고
    • Ternary complex factors: Growth factor regulated transcriptional activators
    • Treisman, R. (1994). Ternary complex factors: growth factor regulated transcriptional activators. Curr. Opin. Genet. Dev. 4, 96-101.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 96-101
    • Treisman, R.1
  • 63
    • 0025134378 scopus 로고
    • Molecular interactions within the ecdysone regulatory hierarchy - DNA-binding properties of the Drosophilia ecdysone-inducible E74A protein
    • Urness, L.D., and Thummel, C.S. (1990). Molecular interactions within the ecdysone regulatory hierarchy - DNA-binding properties of the Drosophilia ecdysone-inducible E74A protein. Cell 63, 47-61.
    • (1990) Cell , vol.63 , pp. 47-61
    • Urness, L.D.1    Thummel, C.S.2
  • 64
    • 0043203406 scopus 로고    scopus 로고
    • Crystal structures of A-DNA duplexes
    • Wahl, M.C., and Sundaralingam, M. (1997). Crystal structures of A-DNA duplexes. Biopolymers 44, 45-63.
    • (1997) Biopolymers , vol.44 , pp. 45-63
    • Wahl, M.C.1    Sundaralingam, M.2
  • 65
    • 0028785254 scopus 로고
    • The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation
    • Werner, M.H., Clore, G.M., Fisher, C.L., Fisher, R.J., Trinh, L., Shiloach, J., and Gronenborn, A.M. (1995). The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation. Cell 83, 761-771.
    • (1995) Cell , vol.83 , pp. 761-771
    • Werner, M.H.1    Clore, G.M.2    Fisher, C.L.3    Fisher, R.J.4    Trinh, L.5    Shiloach, J.6    Gronenborn, A.M.7
  • 66
    • 16044369184 scopus 로고    scopus 로고
    • Erratum: The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation
    • Werner, M.H., Clore, G.M., Fisher, C.L., Fisher, R.J., Trinh, L., Shiloach, J., and Gronenborn, A.M. (1996). Erratum: The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation. Cell 87 (2).
    • (1996) Cell , vol.87 , pp. 2
    • Werner, M.H.1    Clore, G.M.2    Fisher, C.L.3    Fisher, R.J.4    Trinh, L.5    Shiloach, J.6    Gronenborn, A.M.7
  • 68
    • 0026531907 scopus 로고
    • Identification of nucleotide preferences in DNA-sequences recognized specifically by c-Ets-1 protein
    • Woods, D.B., Ghysdeal, J., and Owen, M.J. (1992). Identification of nucleotide preferences in DNA-sequences recognized specifically by c-Ets-1 protein. Nucleic Acids Res. 20, 699-704.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 699-704
    • Woods, D.B.1    Ghysdeal, J.2    Owen, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.