메뉴 건너뛰기




Volumn 26, Issue , 1997, Pages 289-325

Eukaryotic transcription factor-DNA complexes

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED RNA POLYMERASE; HELIX LOOP HELIX PROTEIN; MESSENGER RNA; METALLOPROTEIN; RNA POLYMERASE II; TATA BINDING PROTEIN; TRANSCRIPTION FACTOR;

EID: 0030943821     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.26.1.289     Document Type: Review
Times cited : (120)

References (157)
  • 1
    • 0025128557 scopus 로고
    • The UGA3 gene regulating the GABA catabolic pathway in Saccharomyces cerevisiae codes for a putative zinc finger protein acting on RNA levels
    • Andre B. 1990. The UGA3 gene regulating the GABA catabolic pathway in Saccharomyces cerevisiae codes for a putative zinc finger protein acting on RNA levels. Mol. Gen. Genet. 220:269-76
    • (1990) Mol. Gen. Genet. , vol.220 , pp. 269-276
    • Andre, B.1
  • 3
    • 0027465103 scopus 로고
    • The solution structure of the Oct-1 POU-specific domain reveals striking similarity to the bacteriophage λ repressor DNA-binding domain
    • Assa-Munt N, Mortshire-Smith RJ, Aurora R, Herr W, Wright PE. 1993. The solution structure of the Oct-1 POU-specific domain reveals striking similarity to the bacteriophage λ repressor DNA-binding domain. Cell 73:193-205
    • (1993) Cell , vol.73 , pp. 193-205
    • Assa-Munt, N.1    Mortshire-Smith, R.J.2    Aurora, R.3    Herr, W.4    Wright, P.E.5
  • 4
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle PA, Henkel T. 1994. Function and activation of NF-κB in the immune system. Annu. Rev. Immunol. 12:141-79
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 5
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin RL. 1986. Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl. Acad. Sci. USA 83:8069-72
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 6
    • 0029005178 scopus 로고
    • Contact with a component of the polymerase II holoenzyme suffices for gene activation
    • Barberis A, Pearlberg J, Simkovich N, Farrell S, Reinagle P, et al. 1995. Contact with a component of the polymerase II holoenzyme suffices for gene activation. Cell 81:359-68
    • (1995) Cell , vol.81 , pp. 359-368
    • Barberis, A.1    Pearlberg, J.2    Simkovich, N.3    Farrell, S.4    Reinagle, P.5
  • 7
    • 0028181750 scopus 로고
    • Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc finger
    • Barlow PN, Luisi B, Milner A, Elliot M, Everett R. 1994. Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc finger. J. Mol. Biol. 237:201-11
    • (1994) J. Mol. Biol. , vol.237 , pp. 201-211
    • Barlow, P.N.1    Luisi, B.2    Milner, A.3    Elliot, M.4    Everett, R.5
  • 8
    • 0025279242 scopus 로고
    • Zinc finger domains: Hypotheses and current knowledge
    • Berg JM. 1991. Zinc finger domains: hypotheses and current knowledge. Annu. Rev. Biophys. Biophys. Chem. 19:405-21
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 405-421
    • Berg, J.M.1
  • 9
    • 0027787519 scopus 로고
    • Determination of the nuclear magnetic solution structure of an Antennapedia homeodomain-DNA complex
    • Billeter M, Qian YQ, Otting G, Muller M, Gehring W, et al. 1993. Determination of the nuclear magnetic solution structure of an Antennapedia homeodomain-DNA complex. J. Mol. Biol. 234:1084-97
    • (1993) J. Mol. Biol. , vol.234 , pp. 1084-1097
    • Billeter, M.1    Qian, Y.Q.2    Otting, G.3    Muller, M.4    Gehring, W.5
  • 10
    • 0030013203 scopus 로고    scopus 로고
    • Biochemistry and structural biology of transcription factor IID
    • Burley SK, Roeder RG. 1996. Biochemistry and structural biology of transcription factor IID. Annu. Rev. Biochem. 65:769-99
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 769-799
    • Burley, S.K.1    Roeder, R.G.2
  • 11
    • 0029140496 scopus 로고
    • Total chemical synthesis of a unique transcription factor-related protein: cMyc-Max
    • Canne LE, Ferré-D' Amaré AR, Burley SK, Kent SBH. 1995. Total chemical synthesis of a unique transcription factor-related protein: cMyc-Max. J. Am. Chem. Soc. 117:2998-3007
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2998-3007
    • Canne, L.E.1    Ferré-D' Amaré, A.R.2    Burley, S.K.3    Kent, S.B.H.4
  • 12
    • 0028402160 scopus 로고
    • Binding of two distamycin A molecules in the minor groove of an alternating B-DNA duplex
    • Chen X, Ramakrishnan B, Sambhorao T, Sundaralingam M. 1994. Binding of two distamycin A molecules in the minor groove of an alternating B-DNA duplex. Nature Struct. Biol. 1:169-75
    • (1994) Nature Struct. Biol. , vol.1 , pp. 169-175
    • Chen, X.1    Ramakrishnan, B.2    Sambhorao, T.3    Sundaralingam, M.4
  • 13
    • 0029045553 scopus 로고
    • A general mechanism for transcriptional synergy by eukaryotic activators
    • Chi T, Lieberman P, Ellwood K, Carey M. 1995. A general mechanism for transcriptional synergy by eukaryotic activators. Nature 377:254-57
    • (1995) Nature , vol.377 , pp. 254-257
    • Chi, T.1    Lieberman, P.2    Ellwood, K.3    Carey, M.4
  • 14
    • 0028206145 scopus 로고
    • Effects of minor groove binding drugs on the interaction of TATA box binding protein and TFIIA with DNA
    • Chiang S-Y, Welch J, Rauscher F, Beerman T. 1994. Effects of minor groove binding drugs on the interaction of TATA box binding protein and TFIIA with DNA. Biochemistry 33:7033-40
    • (1994) Biochemistry , vol.33 , pp. 7033-7040
    • Chiang, S.-Y.1    Welch, J.2    Rauscher, F.3    Beerman, T.4
  • 15
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho Y, Gorina S, Jeffrey PD, Pavletich NP. 1994. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 265:346-55
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 16
    • 0027772890 scopus 로고
    • Eukaryotic activators function during multiple steps of preinitiation complex assembly
    • Choy B, Green MR. 1993. Eukaryotic activators function during multiple steps of preinitiation complex assembly. Nature 366:531-36
    • (1993) Nature , vol.366 , pp. 531-536
    • Choy, B.1    Green, M.R.2
  • 17
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
    • Clark KL, Halay ED, Lai E, Burley SK. 1993. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature 364:412-20
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 18
    • 0028293441 scopus 로고
    • Alpha-helical coiled coils: More facts and better predictions
    • Cohen C, Parry DA. 1994. Alpha-helical coiled coils: more facts and better predictions. Science 263:488-89
    • (1994) Science , vol.263 , pp. 488-489
    • Cohen, C.1    Parry, D.A.2
  • 19
    • 0024495831 scopus 로고
    • Molecular structure of the netropsin-d(CGCGATATCGCG) complex: DNA conformation in an alternating AT segment
    • Coll M, Aymami J, Marel G, Boom J, Wang AH-J. 1989. Molecular structure of the netropsin-d(CGCGATATCGCG) complex: DNA conformation in an alternating AT segment. Biochemistry 28:310-20
    • (1989) Biochemistry , vol.28 , pp. 310-320
    • Coll, M.1    Aymami, J.2    Marel, G.3    Boom, J.4    Wang, A.H.-J.5
  • 20
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick FHC. 1953. The packing of α-helices: simple coiled-coils. Acta Crystallogr. 6:689-97
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 21
    • 0029619217 scopus 로고
    • Refined solution structure and dynamics of the DNA-binding domain of the heat shock factor from Kluyveromyces lactis
    • Damberger FF, Pelton JG, Liu C, Cho H, Harrison CJ, et al. 1995. Refined solution structure and dynamics of the DNA-binding domain of the heat shock factor from Kluyveromyces lactis. J. Mol. Biol. 254:704-19
    • (1995) J. Mol. Biol. , vol.254 , pp. 704-719
    • Damberger, F.F.1    Pelton, J.G.2    Liu, C.3    Cho, H.4    Harrison, C.J.5
  • 23
    • 0030044420 scopus 로고    scopus 로고
    • Solution structure of the ETS domain from murine Ets-1: A winged helix-turn-helix DNA binding motif
    • Donaldson LW, Petersen JM, Graves BJ, McIntosh LP. 1996. Solution structure of the ETS domain from murine Ets-1: a winged helix-turn-helix DNA binding motif. EMBO J. 15:125-34
    • (1996) EMBO J. , vol.15 , pp. 125-134
    • Donaldson, L.W.1    Petersen, J.M.2    Graves, B.J.3    McIntosh, L.P.4
  • 24
    • 0022230224 scopus 로고
    • DNA bending and its relation to nucleosome positioning
    • Drew H, Travers A. 1985. DNA bending and its relation to nucleosome positioning. J. Mol. Biol. 186:773-90
    • (1985) J. Mol. Biol. , vol.186 , pp. 773-790
    • Drew, H.1    Travers, A.2
  • 25
    • 0028118685 scopus 로고
    • Getting a grip on DNA recognition: Structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains
    • Ellenberger T. 1994. Getting a grip on DNA recognition: structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains. Curr. Opin. Struct. Biol. 4:12-21
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 12-21
    • Ellenberger, T.1
  • 26
    • 0028329080 scopus 로고
    • Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer
    • Ellenberger T, Fass D, Arnaud M, Harrison SC. 1994. Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer. Genes Dev. 8:970-80
    • (1994) Genes Dev. , vol.8 , pp. 970-980
    • Ellenberger, T.1    Fass, D.2    Arnaud, M.3    Harrison, S.C.4
  • 27
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α-helices: Crystal structure of the protein-DNA complex
    • Ellenberger TE, Brandi CJ, Struhl K, Harrison SC. 1992. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α-helices: crystal structure of the protein-DNA complex. Cell 71:1223-37
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandi, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 28
    • 0018862597 scopus 로고
    • Specific interaction of a purified transcription factor with an internal control region of 5S RNA genes
    • Engelke DR, Ng S-Y, Shastry BS, Roeder RG. 1980. Specific interaction of a purified transcription factor with an internal control region of 5S RNA genes. Cell 19:717-28
    • (1980) Cell , vol.19 , pp. 717-728
    • Engelke, D.R.1    Ng, S.-Y.2    Shastry, B.S.3    Roeder, R.G.4
  • 29
    • 0027749348 scopus 로고
    • The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition
    • Fairall L, Schwabe JW, Chapman L, Finch JT, Rhodes D. 1993. The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition. Nature 366:483-87
    • (1993) Nature , vol.366 , pp. 483-487
    • Fairall, L.1    Schwabe, J.W.2    Chapman, L.3    Finch, J.T.4    Rhodes, D.5
  • 32
  • 33
    • 0024745871 scopus 로고
    • The price of lost freedom: Entropy of bimolecular complex formation
    • Finkelstein AV, Janin J. 1989. The price of lost freedom: entropy of bimolecular complex formation. Prot. Eng. 3:1-3
    • (1989) Prot. Eng. , vol.3 , pp. 1-3
    • Finkelstein, A.V.1    Janin, J.2
  • 34
    • 0027399193 scopus 로고
    • High affinity DNA-binding myc analogs: Recognition by an α-helix
    • Fisher DE, Parent LA, Sharp PA. 1993. High affinity DNA-binding myc analogs: recognition by an α-helix. Cell 72:467-76
    • (1993) Cell , vol.72 , pp. 467-476
    • Fisher, D.E.1    Parent, L.A.2    Sharp, P.A.3
  • 35
    • 0027498883 scopus 로고
    • On the mechanism of DNA binding by nuclear hormone receptor: A structural and functional perspective
    • Freedman LP, Luisi BF. 1993. On the mechanism of DNA binding by nuclear hormone receptor: a structural and functional perspective. J. Cell. Biochem. 51:140-50
    • (1993) J. Cell. Biochem. , vol.51 , pp. 140-150
    • Freedman, L.P.1    Luisi, B.F.2
  • 36
    • 0028360796 scopus 로고
    • Macromolecular crowding and confinement in cells exposed to hypertonicity
    • Garner MM, Burg MB. 1994. Macromolecular crowding and confinement in cells exposed to hypertonicity. Am. J. Physiol. Cell Physiol. 266:877-92
    • (1994) Am. J. Physiol. Cell Physiol. , vol.266 , pp. 877-892
    • Garner, M.M.1    Burg, M.B.2
  • 37
    • 0028018945 scopus 로고
    • Purification, cloning and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes
    • Ge H, Roeder RG. 1994. Purification, cloning and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes. Cell 78:513-23
    • (1994) Cell , vol.78 , pp. 513-523
    • Ge, H.1    Roeder, R.G.2
  • 38
    • 0029930779 scopus 로고    scopus 로고
    • The crystal structure of the yeast TFIIA/TBP/DNA complex
    • Geiger JH, Hahn S, Lee S, Sigler PB. 1996. The crystal structure of the yeast TFIIA/TBP/DNA complex. Science 272:830-36
    • (1996) Science , vol.272 , pp. 830-836
    • Geiger, J.H.1    Hahn, S.2    Lee, S.3    Sigler, P.B.4
  • 39
    • 0028979479 scopus 로고
    • Structure of the NF-κB p50 homodimer bound to a kB site
    • Ghosh G, Duyne GV, Ghosh S, Sigler PB. 1995. Structure of the NF-κB p50 homodimer bound to a kB site. Nature 373:303-10
    • (1995) Nature , vol.373 , pp. 303-310
    • Ghosh, G.1    Duyne, G.V.2    Ghosh, S.3    Sigler, P.B.4
  • 40
    • 0028408337 scopus 로고
    • Taking the initiative
    • Gill G. 1994. Taking the initiative. Curr. Biol. 4:374-76
    • (1994) Curr. Biol. , vol.4 , pp. 374-376
    • Gill, G.1
  • 41
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
    • Glover JNM, Harrison SC. 1995. Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature 373:257-61
    • (1995) Nature , vol.373 , pp. 257-261
    • Glover, J.N.M.1    Harrison, S.C.2
  • 42
    • 0026734111 scopus 로고
    • Pax in development
    • Gruss P, Walther C. 1992. Pax in development. Cell 69:719-22
    • (1992) Cell , vol.69 , pp. 719-722
    • Gruss, P.1    Walther, C.2
  • 43
    • 0024378717 scopus 로고
    • Role of the hydrophobic effect in stability of site-specific protein-DNA complexes
    • Ha J-H, Spolar RS, Record TMJ. 1989. Role of the hydrophobic effect in stability of site-specific protein-DNA complexes. J. Mol. Biol. 209:801-16
    • (1989) J. Mol. Biol. , vol.209 , pp. 801-816
    • Ha, J.-H.1    Spolar, R.S.2    Record, T.M.J.3
  • 44
    • 0001187488 scopus 로고
    • The Yin and Yang of mammalian transcription
    • Hahn S. 1992. The Yin and Yang of mammalian transcription. Curr. Biol. 2:152-54
    • (1992) Curr. Biol. , vol.2 , pp. 152-154
    • Hahn, S.1
  • 46
  • 47
    • 0025335811 scopus 로고
    • Solution structure of the glucocorticoid receptor DNA-binding domain
    • Hard T, Kellenbach E, Boelens R, Maler BA, Dahlman K, et al. 1990. Solution structure of the glucocorticoid receptor DNA-binding domain. Science 249:157-60
    • (1990) Science , vol.249 , pp. 157-160
    • Hard, T.1    Kellenbach, E.2    Boelens, R.3    Maler, B.A.4    Dahlman, K.5
  • 48
    • 0027489384 scopus 로고
    • Clinical implications of the p53 tumor-suppressor gene
    • Harris C, Hollstein M. 1993. Clinical implications of the p53 tumor-suppressor gene. N. Engl. J. Med. 329:1318-27
    • (1993) N. Engl. J. Med. , vol.329 , pp. 1318-1327
    • Harris, C.1    Hollstein, M.2
  • 49
    • 0027958045 scopus 로고
    • Crystal structure of the DNA binding domain of the heat shock transcription factor
    • Harrison CJ, Bohm AA, Nelson HCM. 1994. Crystal structure of the DNA binding domain of the heat shock transcription factor. Science 263:224-27
    • (1994) Science , vol.263 , pp. 224-227
    • Harrison, C.J.1    Bohm, A.A.2    Nelson, H.C.M.3
  • 50
    • 0026656038 scopus 로고
    • Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target
    • Hegde RS, Grossman SR, Laimins LA, Sigler PB. 1992. Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target. Nature 359:505-12
    • (1992) Nature , vol.359 , pp. 505-512
    • Hegde, R.S.1    Grossman, S.R.2    Laimins, L.A.3    Sigler, P.B.4
  • 51
    • 0023918675 scopus 로고
    • Structure and function of bacterial sigma factors
    • Helmann J, Chamberlin M. 1988. Structure and function of bacterial sigma factors. Annu. Rev. Biochem. 57:839-72
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 839-872
    • Helmann, J.1    Chamberlin, M.2
  • 52
    • 0029595248 scopus 로고
    • Structure of the even-skipped homeodomain complexed with AT-rich DNA: New perspectives on homeodomain specificity
    • Hirsch JA, Aggarwal AK. 1995. Structure of the even-skipped homeodomain complexed with AT-rich DNA: new perspectives on homeodomain specificity. EMBO J. 14:6280-91
    • (1995) EMBO J. , vol.14 , pp. 6280-6291
    • Hirsch, J.A.1    Aggarwal, A.K.2
  • 53
    • 0026665954 scopus 로고
    • Kinetic analysis of yeast TFIID-TATA box complex formation suggests a multistep pathway
    • Hoopes B, LeBlanc J, Hawley D. 1992 Kinetic analysis of yeast TFIID-TATA box complex formation suggests a multistep pathway. J. Biol. Chem. 267:11539-46
    • (1992) J. Biol. Chem. , vol.267 , pp. 11539-11546
    • Hoopes, B.1    LeBlanc, J.2    Hawley, D.3
  • 54
    • 0028212908 scopus 로고
    • The role of activators in assembly of RNA polymerase II transcription complexes
    • Hori R, Carey M. 1994. The role of activators in assembly of RNA polymerase II transcription complexes. Curr. Opin. Genet. Dev. 4:236-44
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 236-244
    • Hori, R.1    Carey, M.2
  • 55
  • 56
    • 0028861437 scopus 로고
    • Elusive affinities
    • Janin J. 1995. Elusive affinities. Proteins 21:30-39
    • (1995) Proteins , vol.21 , pp. 30-39
    • Janin, J.1
  • 57
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks WP. 1981. On the attribution and additivity of binding energies. Proc. Natl. Acad. Sci. USA 78:4046-50
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 58
    • 0028157348 scopus 로고
    • Mutagenesis supports water mediated recognition in the trp repressor-operator system
    • Joachimiak A, Haran TE, Sigler PB. 1994. Mutagenesis supports water mediated recognition in the trp repressor-operator system. EMBO J. 13:367-72
    • (1994) EMBO J. , vol.13 , pp. 367-372
    • Joachimiak, A.1    Haran, T.E.2    Sigler, P.B.3
  • 60
    • 0027974851 scopus 로고
    • 1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG
    • Kim JL, Burley SK. 1994. 1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG. Nature Struct. Biol. 1:638-53
    • (1994) Nature Struct. Biol. , vol.1 , pp. 638-653
    • Kim, J.L.1    Burley, S.K.2
  • 61
    • 0027483012 scopus 로고
    • Co-crystal structure of TBP recognizing the minor groove of a TATA element
    • Kim JL, Nikolov DB, Burley SK. 1993. Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature 365:520-27
    • (1993) Nature , vol.365 , pp. 520-527
    • Kim, J.L.1    Nikolov, D.B.2    Burley, S.K.3
  • 62
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA-box complex
    • Kim Y, Geiger JH, Hahn S, Sigler PB. 1993. Crystal structure of a yeast TBP/TATA-box complex. Nature 365:512-20
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 63
    • 0025188837 scopus 로고
    • Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: A framework for understanding homeodomain-DNA interactions
    • Kissinger CR, Liu B, Martin-Blanco E, Kornberg TB, Pabo CO. 1990. Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: a framework for understanding homeodomain-DNA interactions. Cell 63:579-90
    • (1990) Cell , vol.63 , pp. 579-590
    • Kissinger, C.R.1    Liu, B.2    Martin-Blanco, E.3    Kornberg, T.B.4    Pabo, C.O.5
  • 64
    • 0028200262 scopus 로고
    • Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding domains
    • Klemm JD, Rould MA, Aurora R, Herr W, Pabo CO. 1994. Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding domains. Cell 77:21-32
    • (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
  • 65
    • 0029670530 scopus 로고    scopus 로고
    • A new pattern for helix-turn-helix recognition revealed by the PU. 1 Ets-domain-DNA complex
    • Kodandapani R, Pio F, Ni C-Z, Piccailli G, Klemsz M. et al. 1996. A new pattern for helix-turn-helix recognition revealed by the PU. 1 Ets-domain-DNA complex. Nature 380:456-59
    • (1996) Nature , vol.380 , pp. 456-459
    • Kodandapani, R.1    Pio, F.2    Ni, C.-Z.3    Piccailli, G.4    Klemsz, M.5
  • 66
    • 0028904453 scopus 로고
    • The RNA polymerase II holoenzyme and its implications for gene regulation
    • Koleske A, Young R. 1995. The RNA polymerase II holoenzyme and its implications for gene regulation. Trends Biochem. Sci. 20:113-16
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 113-116
    • Koleske, A.1    Young, R.2
  • 67
    • 0027377202 scopus 로고
    • The X-ray structure of the GCN4-bZip bound to ATF/CREB site DNA shows the complex depends on DNA flexibility
    • König P, Richmond TJ. 1993. The X-ray structure of the GCN4-bZip bound to ATF/CREB site DNA shows the complex depends on DNA flexibility. J. Mol. Biol. 233:139-54
    • (1993) J. Mol. Biol. , vol.233 , pp. 139-154
    • König, P.1    Richmond, T.J.2
  • 68
    • 0021834118 scopus 로고
    • The binding of an antitumor drug to DNA. Netropsin and CGCGAATTBrCGCG
    • Kopka M, Yoon C, Goodsell D, Pjura P, Dickerson R. 1985. The binding of an antitumor drug to DNA. Netropsin and CGCGAATTBrCGCG. J. Mol. Biol. 183:553-63
    • (1985) J. Mol. Biol. , vol.183 , pp. 553-563
    • Kopka, M.1    Yoon, C.2    Goodsell, D.3    Pjura, P.4    Dickerson, R.5
  • 69
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland DE Jr. 1958. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. USA 44:98-114
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-114
    • Koshland Jr., D.E.1
  • 70
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24:946-50
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 72
    • 0027482831 scopus 로고
    • Hepatocyte nuclear factor 3/fork head or "winged helix" proteins: A family of transcription factors of diverse biological function
    • Lai E, Clark KL, Burley SK, Darnell JE. 1993. Hepatocyte nuclear factor 3/fork head or "winged helix" proteins: A family of transcription factors of diverse biological function. Proc. Natl. Acad. Sci. USA 90:10421-23
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10421-10423
    • Lai, E.1    Clark, K.L.2    Burley, S.K.3    Darnell, J.E.4
  • 74
    • 0027372621 scopus 로고
    • Tandem binding in crystals of a trp repressor/operator half-site complex
    • Lawson CL, Carey J. 1993. Tandem binding in crystals of a trp repressor/operator half-site complex. Nature 366:178-82
    • (1993) Nature , vol.366 , pp. 178-182
    • Lawson, C.L.1    Carey, J.2
  • 75
    • 0024744322 scopus 로고
    • The Oct-2 protein binds cooperatively to adjacent octamer sites
    • LeBowitz JH, Clerc RG, Brenowitz M, Sharp PA. 1989. The Oct-2 protein binds cooperatively to adjacent octamer sites. Genes Dev. 3:1625-38
    • (1989) Genes Dev. , vol.3 , pp. 1625-1638
    • LeBowitz, J.H.1    Clerc, R.G.2    Brenowitz, M.3    Sharp, P.A.4
  • 76
    • 0024341072 scopus 로고
    • Three-dimensional solution structure of a single zinc finger DNA-binding domain
    • Lee MS, Gippert GP, Soman KV, Case DA, Wright PE. 1989. Three-dimensional solution structure of a single zinc finger DNA-binding domain. Science 245:635-37
    • (1989) Science , vol.245 , pp. 635-637
    • Lee, M.S.1    Gippert, G.P.2    Soman, K.V.3    Case, D.A.4    Wright, P.E.5
  • 77
    • 0028828745 scopus 로고
    • Crystal structure of the Mata1/Mata2 homeodomain heterodimer bound to DNA
    • Li T, Stark MR, Johnson AD, Wolberger C. 1995. Crystal structure of the Mata1/Mata2 homeodomain heterodimer bound to DNA. Science 270: 262-69
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 78
    • 23444439791 scopus 로고
    • RNA polymerase II initiation factor interactions and transcription start site selection
    • Li Y, Flanagan PM, Tschochner H, Kornberg RD. 1994. RNA polymerase II initiation factor interactions and transcription start site selection. Science 263:805-7
    • (1994) Science , vol.263 , pp. 805-807
    • Li, Y.1    Flanagan, P.M.2    Tschochner, H.3    Kornberg, R.D.4
  • 80
    • 0025906146 scopus 로고
    • Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area
    • Livingstone J, Spolar R, Record MJ. 1991. Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area. Biochemistry 30:4237-44
    • (1991) Biochemistry , vol.30 , pp. 4237-4244
    • Livingstone, J.1    Spolar, R.2    Record, M.J.3
  • 81
    • 0029131298 scopus 로고
    • Structural basis by DNA bending by the architectural transcription factor LEF-1
    • Love JJ, Li X, Case DA, Giese K, Grosschedl R, et al. 1995. Structural basis by DNA bending by the architectural transcription factor LEF-1. Nature 376:791-95
    • (1995) Nature , vol.376 , pp. 791-795
    • Love, J.J.1    Li, X.2    Case, D.A.3    Giese, K.4    Grosschedl, R.5
  • 82
    • 0025780755 scopus 로고
    • Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
    • Luisi BF, Xu WX, Otwinowski Z, Feedman LP, Yamamoto KR, et al. 1991. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature 352:497-505
    • (1991) Nature , vol.352 , pp. 497-505
    • Luisi, B.F.1    Xu, W.X.2    Otwinowski, Z.3    Feedman, L.P.4    Yamamoto, K.R.5
  • 83
    • 0028215362 scopus 로고
    • Crystal structure of MyoD bHLH domain-DNA complex: Perspectives on DNA recognition and implications for transcriptional activation
    • Ma PCM, Rould MA, Weintraub H, Pabo CO. 1994. Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation. Cell 77:451-59
    • (1994) Cell , vol.77 , pp. 451-459
    • Ma, P.C.M.1    Rould, M.A.2    Weintraub, H.3    Pabo, C.O.4
  • 84
    • 0026547747 scopus 로고
    • DNA recognition by Gal4: Structure of a protein-DNA complex
    • Marmorstein R, Carey M, Ptashne M, Harrison SC. 1992. DNA recognition by Gal4: structure of a protein-DNA complex. Nature 356:408-14
    • (1992) Nature , vol.356 , pp. 408-414
    • Marmorstein, R.1    Carey, M.2    Ptashne, M.3    Harrison, S.C.4
  • 86
    • 0019333274 scopus 로고
    • Multiple factors required for accurate initiation of transcription by purified RNA polymerase II
    • Matsui T, Segall J, Weil P, Roeder R. 1980. Multiple factors required for accurate initiation of transcription by purified RNA polymerase II. J. Biol. Chem. 255:11992-96
    • (1980) J. Biol. Chem. , vol.255 , pp. 11992-11996
    • Matsui, T.1    Segall, J.2    Weil, P.3    Roeder, R.4
  • 87
    • 0024294636 scopus 로고
    • Protein-DNA interaction. No code for recognition
    • Matthews BW. 1988. Protein-DNA interaction. No code for recognition. Nature 335:294-95
    • (1988) Nature , vol.335 , pp. 294-295
    • Matthews, B.W.1
  • 88
    • 0025647724 scopus 로고
    • Recombinant yeast TFIID, a general transcription factor, mediates activation by the gene-specific factor USF in a chromatin assembly assay
    • Meisterernst M, Horikoshi M, Roeder RG. 1990. Recombinant yeast TFIID, a general transcription factor, mediates activation by the gene-specific factor USF in a chromatin assembly assay. Proc. Natl. Acad. Sci. USA 87:9153-57
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9153-9157
    • Meisterernst, M.1    Horikoshi, M.2    Roeder, R.G.3
  • 89
    • 0040215628 scopus 로고
    • Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus ooctyes
    • Miller J, McLachlan AD, Klug A. 1985. Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus ooctyes. EMBO J. 4:1609-14
    • (1985) EMBO J. , vol.4 , pp. 1609-1614
    • Miller, J.1    McLachlan, A.D.2    Klug, A.3
  • 91
    • 0024554495 scopus 로고
    • A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins
    • Murre C, McCaw PS, Baltimore D. 1989. A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell 56:777-83
    • (1989) Cell , vol.56 , pp. 777-783
    • Murre, C.1    McCaw, P.S.2    Baltimore, D.3
  • 92
    • 0028241531 scopus 로고
    • Distinctive DNA conformation with enlarged major groove is found in Zn-finger-DNA and other protein-DNA complexes
    • Nekludova L, Pabo C. 1994. Distinctive DNA conformation with enlarged major groove is found in Zn-finger-DNA and other protein-DNA complexes. Proc. Natl. Acad. Sci. USA 91:6948-52
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6948-6952
    • Nekludova, L.1    Pabo, C.2
  • 93
    • 0028056035 scopus 로고
    • 2.1 Å Resolution refined structure of a TATA box-binding protein (TBP)
    • Nikolov DB, Burley SK. 1994. 2.1 Å Resolution refined structure of a TATA box-binding protein (TBP). Nature Struct. Biol. 1:621-37
    • (1994) Nature Struct. Biol. , vol.1 , pp. 621-637
    • Nikolov, D.B.1    Burley, S.K.2
  • 94
    • 0028978670 scopus 로고
    • Crystal structure of a TFIIB-TBP-TATA element ternary complex
    • Nikolov DB, Chen H, Halay E, Usheva A, Hisatake K, et al. 1995. Crystal structure of a TFIIB-TBP-TATA element ternary complex. Nature 377:119-28
    • (1995) Nature , vol.377 , pp. 119-128
    • Nikolov, D.B.1    Chen, H.2    Halay, E.3    Usheva, A.4    Hisatake, K.5
  • 96
    • 0024206625 scopus 로고
    • Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element
    • Norman C, Runswick M, Pollock R, Treisman R. 1988. Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element. Cell 55:989-1003
    • (1988) Cell , vol.55 , pp. 989-1003
    • Norman, C.1    Runswick, M.2    Pollock, R.3    Treisman, R.4
  • 97
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea EK, Klemm JD, Kim PS, Alber T. 1991. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254:539-44
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 98
    • 0026776412 scopus 로고
    • Solution structure of a DNA-binding unit of Myb: A helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core
    • Ogata K, Hojo H, Aimoto S, Nakai T, Nakamura H, et al. 1992. Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core. Proc. Natl. Acad. Sci. USA 89:6428-32
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6428-6432
    • Ogata, K.1    Hojo, H.2    Aimoto, S.3    Nakai, T.4    Nakamura, H.5
  • 99
    • 0028138773 scopus 로고
    • Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices
    • Ogata K, Morikawa S, Nakamura H, Serikawa A, Inoue T, et al. 1994. Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices. Cell 79:639-48
    • (1994) Cell , vol.79 , pp. 639-648
    • Ogata, K.1    Morikawa, S.2    Nakamura, H.3    Serikawa, A.4    Inoue, T.5
  • 100
    • 0027284167 scopus 로고
    • NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1
    • Omichinski JG, Clore GM, Schaad O, Felsenfeld G, Trainor C, et al. 1993. NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1. Science 261:438-46
    • (1993) Science , vol.261 , pp. 438-446
    • Omichinski, J.G.1    Clore, G.M.2    Schaad, O.3    Felsenfeld, G.4    Trainor, C.5
  • 101
    • 0026691333 scopus 로고
    • GATA-binding transcription factors in hematopoietic cells
    • Orkin SH. 1992. GATA-binding transcription factors in hematopoietic cells. Blood 80:575-81
    • (1992) Blood , vol.80 , pp. 575-581
    • Orkin, S.H.1
  • 102
    • 0024997404 scopus 로고
    • Protein-DNA contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy
    • Otting G, Qian YQ, Billeter M, Muller M, Affolter M, et al. 1990. Protein-DNA contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy. EMBO J. 9:3085-92
    • (1990) EMBO J. , vol.9 , pp. 3085-3092
    • Otting, G.1    Qian, Y.Q.2    Billeter, M.3    Muller, M.4    Affolter, M.5
  • 103
  • 104
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principles of DNA recognition
    • Pabo CO, Sauer RT. 1992. Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem. 61:1053-95
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1053-1095
    • Pabo, C.O.1    Sauer, R.T.2
  • 105
    • 0028245303 scopus 로고
    • DNA targets for certain BZIP proteins distinguished by an intrinsic bend
    • Paolella DN, Palmer CR, Schepartz A. 1994. DNA targets for certain BZIP proteins distinguished by an intrinsic bend. Science 264:1130-33
    • (1994) Science , vol.264 , pp. 1130-1133
    • Paolella, D.N.1    Palmer, C.R.2    Schepartz, A.3
  • 106
    • 0029943025 scopus 로고    scopus 로고
    • Simultaneous binding and bending of promoter DNA by TBP: Real-time kinetic measurements
    • Parkhurst K, Brenowitz M, Parkhurst L. 1996. Simultaneous binding and bending of promoter DNA by TBP: real-time kinetic measurements. Biochemistry 35:7459-65
    • (1996) Biochemistry , vol.35 , pp. 7459-7465
    • Parkhurst, K.1    Brenowitz, M.2    Parkhurst, L.3
  • 107
    • 0028919503 scopus 로고
    • Pre-bending of a promoter sequence enhances affinity for the TATA-binding factor
    • Parvin J, McCormick R, Sharp P, Fisher D. 1995. Pre-bending of a promoter sequence enhances affinity for the TATA-binding factor. Nature 273:724-27
    • (1995) Nature , vol.273 , pp. 724-727
    • Parvin, J.1    McCormick, R.2    Sharp, P.3    Fisher, D.4
  • 108
    • 0027168221 scopus 로고
    • DNA topology and a minimal set of basal factors for transcription by RNA polymerase II
    • Parvin J, Sharp P. 1993. DNA topology and a minimal set of basal factors for transcription by RNA polymerase II. Cell 73:533-40
    • (1993) Cell , vol.73 , pp. 533-540
    • Parvin, J.1    Sharp, P.2
  • 109
    • 8244238920 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 110
    • 0025773296 scopus 로고
    • Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1 Å
    • Pavletich NP, Pabo CO. 1991. Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 Å. Science 252:809-17
    • (1991) Science , vol.252 , pp. 809-817
    • Pavletich, N.P.1    Pabo, C.O.2
  • 111
    • 0027423758 scopus 로고
    • Crystal structure of a five-finger GLI-DNA complex: New perspectives on zinc fingers
    • Pavletich NP, Pabo CO. 1993. Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers. Science 261:1701-7
    • (1993) Science , vol.261 , pp. 1701-1707
    • Pavletich, N.P.1    Pabo, C.O.2
  • 112
    • 0029102041 scopus 로고
    • Structure of serum response factor core bound to DNA
    • Pellegrini L, Tan S, Richmond TJ. 1995. Structure of serum response factor core bound to DNA. Nature 376:490-98
    • (1995) Nature , vol.376 , pp. 490-498
    • Pellegrini, L.1    Tan, S.2    Richmond, T.J.3
  • 113
    • 0028019848 scopus 로고
    • Characterization of sua7 mutations defines a domain of TFIIB involved in transcription start site selection in yeast
    • Pinto I, Wu W-H, Na JG, Hampsey M. 1994. Characterization of sua7 mutations defines a domain of TFIIB involved in transcription start site selection in yeast. J. Biol. Chem. 269:30569-73
    • (1994) J. Biol. Chem. , vol.269 , pp. 30569-30573
    • Pinto, I.1    Wu, W.-H.2    Na, J.G.3    Hampsey, M.4
  • 114
    • 0028269401 scopus 로고
    • Competition between chromatin and transcription complex assembly regulates gene expression during early development
    • Prioleau M-N, Huet J, Sentenac A, Mechali M. 1994. Competition between chromatin and transcription complex assembly regulates gene expression during early development. Cell 77:439-49
    • (1994) Cell , vol.77 , pp. 439-449
    • Prioleau, M.-N.1    Huet, J.2    Sentenac, A.3    Mechali, M.4
  • 115
    • 0027328862 scopus 로고
    • Structure of a new nucleic-acid-binding motif in eukaryotic transcription elongation factor TFIIA
    • Qian X, Jeon CJ, Yoon HS, Agarwal K, Weiss MA. 1993. Structure of a new nucleic-acid-binding motif in eukaryotic transcription elongation factor TFIIA. Nature 365:277-79
    • (1993) Nature , vol.365 , pp. 277-279
    • Qian, X.1    Jeon, C.J.2    Yoon, H.S.3    Agarwal, K.4    Weiss, M.A.5
  • 116
    • 0027746065 scopus 로고
    • Nuclear magnetic resonance spectroscopy of a DNA complex with the uniformly 13C labeled antennapedia homeodomain and structure determination of the DNA-bound homeodomain
    • Qian YQ, Otting G, Billeter M, Müller M, Gehring W, et al. 1993. Nuclear magnetic resonance spectroscopy of a DNA complex with the uniformly 13C labeled antennapedia homeodomain and structure determination of the DNA-bound homeodomain. J. Mol. Biol. 234:1070-83
    • (1993) J. Mol. Biol. , vol.234 , pp. 1070-1083
    • Qian, Y.Q.1    Otting, G.2    Billeter, M.3    Müller, M.4    Gehring, W.5
  • 117
    • 0000764227 scopus 로고
    • NMR detection of hydration water in the intermolecular interface of a protein-DNA complex
    • Qian YQ, Otting G, Wüthrich K. 1993. NMR detection of hydration water in the intermolecular interface of a protein-DNA complex. J. Am. Chem. Soc. 115:1189-90
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 1189-1190
    • Qian, Y.Q.1    Otting, G.2    Wüthrich, K.3
  • 118
    • 0027402969 scopus 로고
    • Crystal structure of the globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan V, Finch J, Graziano V, Sweet R. 1993. Crystal structure of the globular domain of histone H5 and its implications for nucleosome binding. Nature 362:219-23
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.2    Graziano, V.3    Sweet, R.4
  • 119
    • 0029044997 scopus 로고
    • Structural determinants of nuclear receptor assembly on DNA direct repeats
    • Rastinejad F, Perlmann T, Evans RM, Sigler PB. 1995. Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature 375:203-11
    • (1995) Nature , vol.375 , pp. 203-211
    • Rastinejad, F.1    Perlmann, T.2    Evans, R.M.3    Sigler, P.B.4
  • 120
    • 0026323912 scopus 로고
    • Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA
    • Record TM, Ha J-H, Fisher MA. 1991. Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA. Meth. Enzymol. 208:291-343
    • (1991) Meth. Enzymol. , vol.208 , pp. 291-343
    • Record, T.M.1    Ha, J.-H.2    Fisher, M.A.3
  • 121
    • 0025790171 scopus 로고
    • In vivo foot-printing of rat TAT gene: Dynamic interplay between the glucocorticoid receptor and a liver-specific transcription factor
    • Rigaud G, Roux J, Pictet R, Grange T. 1991. In vivo foot-printing of rat TAT gene: dynamic interplay between the glucocorticoid receptor and a liver-specific transcription factor. Cell 67:977-86
    • (1991) Cell , vol.67 , pp. 977-986
    • Rigaud, G.1    Roux, J.2    Pictet, R.3    Grange, T.4
  • 122
    • 0030249381 scopus 로고    scopus 로고
    • The role of general initiation factors by RNA polymerase II
    • Roeder RG. 1996. The role of general initiation factors by RNA polymerase II. Trends Biochem. Sci. 21:327-35
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 327-335
    • Roeder, R.G.1
  • 123
    • 0025735101 scopus 로고
    • POU-domain transcription factors: Pou-er-ful developmental regulators
    • Rosenfeld MG. 1991. POU-domain transcription factors: pou-er-ful developmental regulators. Genes Dev. 5:897-907
    • (1991) Genes Dev. , vol.5 , pp. 897-907
    • Rosenfeld, M.G.1
  • 124
    • 0023001414 scopus 로고
    • Sequence periodicities in chicken nucleosomal core DNA
    • Satchwell S, Drew H, Travers A. 1986. Sequence periodicities in chicken nucleosomal core DNA. J. Mol. Biol. 191:659-79
    • (1986) J. Mol. Biol. , vol.191 , pp. 659-679
    • Satchwell, S.1    Drew, H.2    Travers, A.3
  • 126
    • 0029417005 scopus 로고
    • Multiple TAFIIs directing synergistic activation of transcription
    • Sauer F, Hansen S, Tjian R. 1995. Multiple TAFIIs directing synergistic activation of transcription. Science 270:1783-88
    • (1995) Science , vol.270 , pp. 1783-1788
    • Sauer, F.1    Hansen, S.2    Tjian, R.3
  • 127
    • 0029618433 scopus 로고
    • DNA template and activator-coactivator requirements for transcriptional synergism by Drosophila bicoid
    • Sauer F, Hansen S, Tjian R. 1995. DNA template and activator-coactivator requirements for transcriptional synergism by Drosophila bicoid. Science 270:1825-28
    • (1995) Science , vol.270 , pp. 1825-1828
    • Sauer, F.1    Hansen, S.2    Tjian, R.3
  • 128
    • 0022374891 scopus 로고
    • Interaction of a gene-specific transcription factor with the Adenovirus major late promoter upstream of the TATA box region
    • Sawadogo M, Roeder RG. 1985. Interaction of a gene-specific transcription factor with the Adenovirus major late promoter upstream of the TATA box region. Cell 43:165-75
    • (1985) Cell , vol.43 , pp. 165-175
    • Sawadogo, M.1    Roeder, R.G.2
  • 129
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90°
    • Schultz SC, Shields GC, Steitz TA. 1991. Crystal structure of a CAP-DNA complex: the DNA is bent by 90°. Science 253:1001-7
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 130
    • 0027365669 scopus 로고
    • The crystal structure of the oestrogen receptor DNA-binding domain bound to DNA: How receptors discriminate between their response elements
    • Schwabe JWR, Chapman L, Finch JT, Rhodes D. 1993. The crystal structure of the oestrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell 75:567-78
    • (1993) Cell , vol.75 , pp. 567-578
    • Schwabe, J.W.R.1    Chapman, L.2    Finch, J.T.3    Rhodes, D.4
  • 131
    • 0027141842 scopus 로고
    • DNA recognition by the oestrogen receptor: From solution to the crystal
    • Schwabe JWR, Chapman L, Finch JT, Rhodes D. 1993. DNA recognition by the oestrogen receptor: from solution to the crystal. Structure 1:187-204
    • (1993) Structure , vol.1 , pp. 187-204
    • Schwabe, J.W.R.1    Chapman, L.2    Finch, J.T.3    Rhodes, D.4
  • 132
    • 0029643958 scopus 로고
    • The oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation
    • Schwabe JWR, Chapman L, Rhodes D. 1995. The oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation. Structure 3:201-13
    • (1995) Structure , vol.3 , pp. 201-213
    • Schwabe, J.W.R.1    Chapman, L.2    Rhodes, D.3
  • 134
    • 0025223160 scopus 로고
    • Solution structure of the DNA-binding domain of the oestrogen receptor
    • 133a. Schwabe JWR, Neuhans D, Rhodes D. 1990. Solution structure of the DNA-binding domain of the oestrogen receptor. Nature 348:458-461
    • (1990) Nature , vol.348 , pp. 458-461
    • Schwabe, J.W.R.1    Neuhans, D.2    Rhodes, D.3
  • 135
    • 0026072263 scopus 로고
    • YY1 is an initiator sequence-binding protein that directs and activates transcription in vitro
    • Seto E, Shi Y, Shenk T. 1991. YY1 is an initiator sequence-binding protein that directs and activates transcription in vitro. Nature 354:241-45
    • (1991) Nature , vol.354 , pp. 241-245
    • Seto, E.1    Shi, Y.2    Shenk, T.3
  • 136
    • 0028315988 scopus 로고
    • Determinants of repressor/operator recognition from the structure of the trp operator binding site
    • Shakked Z, Guzikevish-Guerstein G, Frolow F, Rabinovich D, Joachimiak A, et al. 1994. Determinants of repressor/operator recognition from the structure of the trp operator binding site. Nature 368:469-73
    • (1994) Nature , vol.368 , pp. 469-473
    • Shakked, Z.1    Guzikevish-Guerstein, G.2    Frolow, F.3    Rabinovich, D.4    Joachimiak, A.5
  • 137
    • 0028956789 scopus 로고
    • Specific DNA-RNA hybrid binding by zinc-finger proteins
    • Shi Y, Berg J. 1995. Specific DNA-RNA hybrid binding by zinc-finger proteins. Science 268:282-84
    • (1995) Science , vol.268 , pp. 282-284
    • Shi, Y.1    Berg, J.2
  • 138
    • 0029930225 scopus 로고
    • DNA unwinding induced by zinc finger protein binding
    • Shi Y, Berg JM. 1995. DNA unwinding induced by zinc finger protein binding. Biochemistry 35:3845-48
    • (1995) Biochemistry , vol.35 , pp. 3845-3848
    • Shi, Y.1    Berg, J.M.2
  • 139
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar RS, Record TM. 1994. Coupling of local folding to site-specific binding of proteins to DNA. Science 263:777-84
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, T.M.2
  • 141
    • 0025280401 scopus 로고
    • Structural studies of protein-nucleic acid interaction: The sources of sequence-specific binding
    • Steitz TA. 1990. Structural studies of protein-nucleic acid interaction: the sources of sequence-specific binding. Q. Rev. Biophys. 23:105-80
    • (1990) Q. Rev. Biophys. , vol.23 , pp. 105-180
    • Steitz, T.A.1
  • 142
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant JM. 1977. Heat capacity and entropy changes in processes involving proteins. Proc. Natl. Acad. Sci. USA 74:2236-40
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 143
    • 0029328528 scopus 로고
    • TBP unwinding of the TATA box induces a specific downstream unwinding site that is targeted by pluramycin
    • Sun D, Hurley L. 1995. TBP unwinding of the TATA box induces a specific downstream unwinding site that is targeted by pluramycin. Chem. Biol. 2:457-69
    • (1995) Chem. Biol. , vol.2 , pp. 457-469
    • Sun, D.1    Hurley, L.2
  • 144
    • 0029870514 scopus 로고    scopus 로고
    • Crystal structure of a yeast TFIIA/TBP/DNA complex
    • Tan S, Hunziker Y, Sargent DF, Richmond TJ. 1996. Crystal structure of a yeast TFIIA/TBP/DNA complex. Nature 381:127-34
    • (1996) Nature , vol.381 , pp. 127-134
    • Tan, S.1    Hunziker, Y.2    Sargent, D.F.3    Richmond, T.J.4
  • 145
    • 0028337542 scopus 로고
    • Transcriptional activation: A complex puzzle with few easy pieces
    • Tjian R, Maniatis T. 1994. Transcriptional activation: a complex puzzle with few easy pieces. Cell 77:5-8
    • (1994) Cell , vol.77 , pp. 5-8
    • Tjian, R.1    Maniatis, T.2
  • 146
    • 0028223852 scopus 로고
    • TATA-binding protein-independent initiation: YY1, TFIIB, and RNA polymerase II direct basal transcription on supercoiled template DNA
    • Usheva A, Shenk T. 1994. TATA-binding protein-independent initiation: YY1, TFIIB, and RNA polymerase II direct basal transcription on supercoiled template DNA. Cell 76:1115-21
    • (1994) Cell , vol.76 , pp. 1115-1121
    • Usheva, A.1    Shenk, T.2
  • 147
    • 0030472774 scopus 로고    scopus 로고
    • TFIIB and the large subunit of RNA polymerase II bind directly to YY1 to mediate transcription initiation
    • Usheva A, Shenk T. 1996. TFIIB and the large subunit of RNA polymerase II bind directly to YY1 to mediate transcription initiation. Proc. Natl. Acad. Sci. USA. 93:13571-76
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13571-13576
    • Usheva, A.1    Shenk, T.2
  • 148
    • 0024370748 scopus 로고
    • Scissors-grip model for DNA recognition by a family of leucine zipper proteins
    • Vinson CR, Sigler PB, Mcknight SL. 1989. Scissors-grip model for DNA recognition by a family of leucine zipper proteins. Science 246:911-16
    • (1989) Science , vol.246 , pp. 911-916
    • Vinson, C.R.1    Sigler, P.B.2    Mcknight, S.L.3
  • 149
    • 0025155512 scopus 로고
    • Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA
    • Weiss MA, Ellenberger T, Wobbe RC, Lee JP, Harrison SC, et al. 1990. Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA. Nature 347:575-78
    • (1990) Nature , vol.347 , pp. 575-578
    • Weiss, M.A.1    Ellenberger, T.2    Wobbe, R.C.3    Lee, J.P.4    Harrison, S.C.5
  • 150
    • 0029075461 scopus 로고
    • Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional structure of the human SRY-DNA complex
    • Werner M, Huth J, Gronenborn A, Clore M. 1995. Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional structure of the human SRY-DNA complex. Cell 81:705-14
    • (1995) Cell , vol.81 , pp. 705-714
    • Werner, M.1    Huth, J.2    Gronenborn, A.3    Clore, M.4
  • 151
    • 0028785254 scopus 로고    scopus 로고
    • The solution structure of the human Ets 1-DNA complex reveals a novel mode of DNA binding and true side chain intercalation
    • Werner MH, Clore GM, Fisher CL, Fisher RJ, Trihn L, et al. 1996. The solution structure of the human Ets 1-DNA complex reveals a novel mode of DNA binding and true side chain intercalation. Cell 83:761-71
    • (1996) Cell , vol.83 , pp. 761-771
    • Werner, M.H.1    Clore, G.M.2    Fisher, C.L.3    Fisher, R.J.4    Trihn, L.5
  • 152
    • 0029160486 scopus 로고
    • Crystal structure of a paired (PAX) class cooperative homeodomain dimer on DNA
    • Wilson DS, Guenther B, Desplan C, Kuriyan J. 1995. Crystal structure of a paired (PAX) class cooperative homeodomain dimer on DNA. Cell 82:709-19
    • (1995) Cell , vol.82 , pp. 709-719
    • Wilson, D.S.1    Guenther, B.2    Desplan, C.3    Kuriyan, J.4
  • 153
    • 0026002757 scopus 로고
    • Crystal structure of a MAT α2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions
    • Wolberger C, Vershon AK, Liu B, Johnson AD, Pabo C. 1991. Crystal structure of a MAT α2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions. Cell 67:517-28
    • (1991) Cell , vol.67 , pp. 517-528
    • Wolberger, C.1    Vershon, A.K.2    Liu, B.3    Johnson, A.D.4    Pabo, C.5
  • 154
    • 0023661185 scopus 로고
    • Binding of transcription factor TFIID to the major late promoter during in vitro nucleosome assembly potentiates subsequent initiation by RNA polymerase II
    • Workman JL, Roeder RG. 1987. Binding of transcription factor TFIID to the major late promoter during in vitro nucleosome assembly potentiates subsequent initiation by RNA polymerase II. Cell 51:613-22
    • (1987) Cell , vol.51 , pp. 613-622
    • Workman, J.L.1    Roeder, R.G.2
  • 155
    • 0028919759 scopus 로고
    • Crystal structure of a paired domain-DNA complex at 2.5 Å resolution reveals structural basis for Pax developmental mutations
    • Xu W, Rould MA, Jun S, Desplan C, Pabo CO. 1995. Crystal structure of a paired domain-DNA complex at 2.5 Å resolution reveals structural basis for Pax developmental mutations. Cell 80:639-50
    • (1995) Cell , vol.80 , pp. 639-650
    • Xu, W.1    Rould, M.A.2    Jun, S.3    Desplan, C.4    Pabo, C.O.5
  • 156
    • 0029074137 scopus 로고
    • Recycling of the general transcription factors during RNA polymerase II transcription
    • Zawel L, Kumar K, Reinberg D. 1995. Recycling of the general transcription factors during RNA polymerase II transcription. Genes Dev. 9:1479-90
    • (1995) Genes Dev. , vol.9 , pp. 1479-1490
    • Zawel, L.1    Kumar, K.2    Reinberg, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.