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Volumn 36, Issue 4, 2005, Pages 317-330

Model of the TBP-TFIIB complex from Plasmodium falciparum: Interface analysis and perspectives as a new target for antimalarial design

Author keywords

Antimalarials; Drug design; Protein modeling; Protein protein interaction; Transcription

Indexed keywords

ANTIMALARIAL AGENT;

EID: 20444380321     PISSN: 01884409     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.arcmed.2005.03.020     Document Type: Article
Times cited : (7)

References (91)
  • 1
    • 20444379758 scopus 로고    scopus 로고
    • World Health Organization. www.who.int
  • 2
    • 20444409265 scopus 로고    scopus 로고
    • Malaria Foundation International. www.malaria.org
  • 4
    • 20444391133 scopus 로고    scopus 로고
    • National Center of Infectious Diseases, Division of Parasitic Diseases (2004). www.cdc.gov/malaria/facts.htm#USandMalaria
  • 5
    • 0024387301 scopus 로고
    • Plasmodium vivax resistance to chloroquine?
    • K.H. Rieckmann, D.R. Davis, and D.C. Hutton Plasmodium vivax resistance to chloroquine? Lancet 2 1989 1183 1184
    • (1989) Lancet , vol.2 , pp. 1183-1184
    • Rieckmann, K.H.1    Davis, D.R.2    Hutton, D.C.3
  • 11
    • 20444398278 scopus 로고    scopus 로고
    • Centers for Disease Control and Prevention. Atlanta, GA.
    • National Center for Infectious Diseases. Centers for Disease Control and Prevention. Atlanta, GA. www.cdc.gov/ncidod/emergplan/box23.htm
  • 14
    • 0003989708 scopus 로고    scopus 로고
    • Malaria Epidemiology Branch, Centers for Disease Control and Prevention. Chamblee, GA.
    • Bloland PB. Drugs Resistance in Malaria. Malaria Epidemiology Branch, Centers for Disease Control and Prevention. Chamblee, GA. http://www.who.int/ csr/resources/publications/drugresist/malaria.pdf
    • Drugs Resistance in Malaria
    • Bloland, P.B.1
  • 16
    • 0035060361 scopus 로고    scopus 로고
    • Mode of action and mechanism of resistance for antimalarial drugs
    • P. Olliaro Mode of action and mechanism of resistance for antimalarial drugs Pharmacology Ther 89 2001 207 219
    • (2001) Pharmacology Ther , vol.89 , pp. 207-219
    • Olliaro, P.1
  • 18
    • 0033051342 scopus 로고    scopus 로고
    • Towards an understanding of drug resistance in malaria: Three-dimensional structure of Plasmodium falciparum dihydrofolate reductase by homology building
    • T. Lemcke, I.T. Christense, and F.S. Jorgensen Towards an understanding of drug resistance in malaria: three-dimensional structure of Plasmodium falciparum dihydrofolate reductase by homology building Bioorg Med Chem 7 1999 1003 1011
    • (1999) Bioorg Med Chem , vol.7 , pp. 1003-1011
    • Lemcke, T.1    Christense, I.T.2    Jorgensen, F.S.3
  • 19
    • 0037441470 scopus 로고    scopus 로고
    • Comparative properties of a three-dimensional model of Plasmodium falciparum ornithine decarboxylase
    • L. Birkholtz, F. Joubert, A.W. Neitz, and A.I. Louw Comparative properties of a three-dimensional model of Plasmodium falciparum ornithine decarboxylase Proteins 50 2003 464 473
    • (2003) Proteins , vol.50 , pp. 464-473
    • Birkholtz, L.1    Joubert, F.2    Neitz, A.W.3    Louw, A.I.4
  • 20
    • 0035630691 scopus 로고    scopus 로고
    • Protein-protein interfaces: Mimics and inhibitors
    • A.G. Cochran Protein-protein interfaces: mimics and inhibitors Curr Opin Chem Biol 5 2001 654 659
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 654-659
    • Cochran, A.G.1
  • 21
    • 0033981862 scopus 로고    scopus 로고
    • Covalent modification as a strategy to block protein-protein interactions with small-molecule drugs
    • J.C. Way Covalent modification as a strategy to block protein-protein interactions with small-molecule drugs Curr Opin Chem Biol 4 2000 40 46
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 40-46
    • Way, J.C.1
  • 22
    • 0037832188 scopus 로고    scopus 로고
    • Computational methods of analysis of protein-protein interactions
    • L. Salwinski, and D. Eisengerg Computational methods of analysis of protein-protein interactions Curr Opin Struct Biol 13 2003 377 382
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 377-382
    • Salwinski, L.1    Eisengerg, D.2
  • 23
    • 0035141353 scopus 로고    scopus 로고
    • Dynamical view of the positions of key side chains in protein-protein recognition
    • S.R. Kimura, R.C. Brower, S. Vadja, and C.J. Camacho Dynamical view of the positions of key side chains in protein-protein recognition Biophys J 80 2001 635 642
    • (2001) Biophys J , vol.80 , pp. 635-642
    • Kimura, S.R.1    Brower, R.C.2    Vadja, S.3    Camacho, C.J.4
  • 24
    • 0037380150 scopus 로고    scopus 로고
    • Basal transcription factors
    • J.C. Reese Basal transcription factors Curr Opin Genet Dev 13 2003 114 118
    • (2003) Curr Opin Genet Dev , vol.13 , pp. 114-118
    • Reese, J.C.1
  • 25
    • 0029984256 scopus 로고    scopus 로고
    • Characterization of the interaction between the acidic activation domain of VP16 and the RNA polymerase II initiation factor TFIIB
    • R. Gupta, A. Emili, G. Pan, H. Xiao, M. Shales, J. Greenblatt, and C.J. Ingles Characterization of the interaction between the acidic activation domain of VP16 and the RNA polymerase II initiation factor TFIIB Nucleic Acids Res 24 1996 2324 2330
    • (1996) Nucleic Acids Res , vol.24 , pp. 2324-2330
    • Gupta, R.1    Emili, A.2    Pan, G.3    Xiao, H.4    Shales, M.5    Greenblatt, J.6    Ingles, C.J.7
  • 26
    • 0034624739 scopus 로고    scopus 로고
    • The conformation of the transcriptional activators in vivo
    • N.A. Hawkes, R. Evans, and S.G. Roberts The conformation of the transcriptional activators in vivo Curr Biol 10 2000 273 276
    • (2000) Curr Biol , vol.10 , pp. 273-276
    • Hawkes, N.A.1    Evans, R.2    Roberts, S.G.3
  • 27
    • 0030769058 scopus 로고    scopus 로고
    • Conserved interaction of the papillomavirus E2 transcriptional activator proteins with human and yeast TFIIB proteins
    • J.D. Benson, R. Lawande, and P.M. Howley Conserved interaction of the papillomavirus E2 transcriptional activator proteins with human and yeast TFIIB proteins J Virol 71 1997 8041 8047
    • (1997) J Virol , vol.71 , pp. 8041-8047
    • Benson, J.D.1    Lawande, R.2    Howley, P.M.3
  • 28
    • 0031932893 scopus 로고    scopus 로고
    • Hepatitis B virus pX targets TFIIB in transcription coactivation
    • I. Haviv, M. Shamay, G. Doitsh, and Y. Shaul Hepatitis B virus pX targets TFIIB in transcription coactivation Mol Cell Biol 18 1998 1562 1569
    • (1998) Mol Cell Biol , vol.18 , pp. 1562-1569
    • Haviv, I.1    Shamay, M.2    Doitsh, G.3    Shaul, Y.4
  • 29
    • 0030572623 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vpr transactivator: Cooperation with promoter-bound activator domains and binding to TFIIB
    • I. Agostini, J.M. Navarro, M. Bouhamdan, F. Rey, B. Spire, R. Vigne, and J. Sire The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB J Mol Biol 261 1996 599 606
    • (1996) J Mol Biol , vol.261 , pp. 599-606
    • Agostini, I.1    Navarro, J.M.2    Bouhamdan, M.3    Rey, F.4    Spire, B.5    Vigne, R.6    Sire, J.7
  • 30
    • 0030885186 scopus 로고    scopus 로고
    • Biochemical and functional interaction of the human immunodeficiency virus type 1 Tat transactivator with the general transcription factor TFIIB
    • P. Veschambre, A. Roisin, and P. Jalinot Biochemical and functional interaction of the human immunodeficiency virus type 1 Tat transactivator with the general transcription factor TFIIB J Gen Virol 78 1997 2235 2245
    • (1997) J Gen Virol , vol.78 , pp. 2235-2245
    • Veschambre, P.1    Roisin, A.2    Jalinot, P.3
  • 31
    • 0037321811 scopus 로고    scopus 로고
    • Interaction of the equine herpesvirus 1 EICPO protein with the immediate-early (IE) protein, TFIIB, and TBP may mediate the antagonism between the IE and EICPO proteins
    • S.K. Kim, H.K. Jang, R.A. Albrecht, W.A. Derbigny, Y. Zhang, and D.J. O'Callaghan Interaction of the equine herpesvirus 1 EICPO protein with the immediate-early (IE) protein, TFIIB, and TBP may mediate the antagonism between the IE and EICPO proteins J Virol 77 2003 2675 2685
    • (2003) J Virol , vol.77 , pp. 2675-2685
    • Kim, S.K.1    Jang, H.K.2    Albrecht, R.A.3    Derbigny, W.A.4    Zhang, Y.5    O'Callaghan, D.J.6
  • 32
    • 0030989802 scopus 로고    scopus 로고
    • Hepatitis B virus X protein is a transcriptional modulator that communicates with transcription factor IIB and the RNA polymerase II subunit 5
    • Y. Lin, T. Nomura, J. Cheong, D. Dorjsuren, K. Iida, and S. Murakami Hepatitis B virus X protein is a transcriptional modulator that communicates with transcription factor IIB and the RNA polymerase II subunit 5 J Biol Chem 272 1997 7132 7139
    • (1997) J Biol Chem , vol.272 , pp. 7132-7139
    • Lin, Y.1    Nomura, T.2    Cheong, J.3    Dorjsuren, D.4    Iida, K.5    Murakami, S.6
  • 33
    • 0028944804 scopus 로고
    • In vitro interaction of the immunodeficiency virus type I Tat transactivator and the general transcription factor TFIIB with the cellular protein TAP
    • L. Yu, P.M. Loewenstein, Z. Zhang, and M. Green In vitro interaction of the immunodeficiency virus type I Tat transactivator and the general transcription factor TFIIB with the cellular protein TAP J Virol 69 1995 3017 3023
    • (1995) J Virol , vol.69 , pp. 3017-3023
    • Yu, L.1    Loewenstein, P.M.2    Zhang, Z.3    Green, M.4
  • 34
    • 0028950983 scopus 로고
    • Transcription factor TFIIB and the vitamin D receptor cooperatively activate ligand-dependent transcription
    • J.C.G. Blanco, I. Wang, S.Y. Tsai, M. Tsai, B.W. O'Malley, P.W. Jurutka, M.R. Haussler, and K. Ozato Transcription factor TFIIB and the vitamin D receptor cooperatively activate ligand-dependent transcription PNAS 92 1995 1535 1539
    • (1995) PNAS , vol.92 , pp. 1535-1539
    • Blanco, J.C.G.1    Wang, I.2    Tsai, S.Y.3    Tsai, M.4    O'Malley, B.W.5    Jurutka, P.W.6    Haussler, M.R.7    Ozato, K.8
  • 35
    • 0033016146 scopus 로고    scopus 로고
    • Specificity of cyclin E-Cdk2, TFIIB, and E1A interactions with a common domain of the p300 coactivator
    • L.K. Felzien, S. Farell, J.C. Betts, R. Mosavin, and G.J. Nabel Specificity of cyclin E-Cdk2, TFIIB, and E1A interactions with a common domain of the p300 coactivator Mol Cell Biol 19 1999 4241 4246
    • (1999) Mol Cell Biol , vol.19 , pp. 4241-4246
    • Felzien, L.K.1    Farell, S.2    Betts, J.C.3    Mosavin, R.4    Nabel, G.J.5
  • 36
    • 0031026293 scopus 로고    scopus 로고
    • Characterization of the transcriptional regulator YY1
    • M. Austen, B. Lüscher, and L.J. Firzlaff Characterization of the transcriptional regulator YY1 J Biol Chem 272 1997 1709 1717
    • (1997) J Biol Chem , vol.272 , pp. 1709-1717
    • Austen, M.1    Lüscher, B.2    Firzlaff, L.J.3
  • 37
    • 0029044001 scopus 로고
    • A 10-amino-acid sequence in the N-terminal A/B domain of thyroid hormone receptor alpha is essential for transcriptional activation and interaction with the general transcription factor TFIIB
    • E. Hadzic, V. Desai-Yajnik, E. Helmer, S. Guo, S. Wu, N. Koudinova, J. Casanova, B.M. Raaka, and H.H. Samuels A 10-amino-acid sequence in the N-terminal A/B domain of thyroid hormone receptor alpha is essential for transcriptional activation and interaction with the general transcription factor TFIIB Mol Cell Biol 15 1995 4507 4517
    • (1995) Mol Cell Biol , vol.15 , pp. 4507-4517
    • Hadzic, E.1    Desai-Yajnik, V.2    Helmer, E.3    Guo, S.4    Wu, S.5    Koudinova, N.6    Casanova, J.7    Raaka, B.M.8    Samuels, H.H.9
  • 38
    • 0032483539 scopus 로고    scopus 로고
    • The human forkhead protein FREAC-2 contains two functionally redundant activation domains and interacts with TBP and TFIIB
    • M. Hellqvist, M. Mahlapuu, A. Blixt, S. Enerbäck, and P. Carlsson The human forkhead protein FREAC-2 contains two functionally redundant activation domains and interacts with TBP and TFIIB J Biol Chem 273 1998 23335 23343
    • (1998) J Biol Chem , vol.273 , pp. 23335-23343
    • Hellqvist, M.1    Mahlapuu, M.2    Blixt, A.3    Enerbäck, S.4    Carlsson, P.5
  • 40
    • 0033305584 scopus 로고    scopus 로고
    • Function of steroidogenic factor 1 domains in nuclear localization, transactivation, and interaction with transcription factor TFIIB
    • L.-A. Li, E.F.-L. Chiang, J.-C. Chen, N.-C. Hsu, Y.-J. Chen, and B.-C. Chung Function of steroidogenic factor 1 domains in nuclear localization, transactivation, and interaction with transcription factor TFIIB Mol Endocrinol 13 1999 1588 1598
    • (1999) Mol Endocrinol , vol.13 , pp. 1588-1598
    • Li, L.-A.1    Chiang, E.F.-L.2    Chen, J.-C.3    Hsu, N.-C.4    Chen, Y.-J.5    Chung, B.-C.6
  • 41
    • 0027374736 scopus 로고
    • Efficient transcriptional activation of many simple modular promoters by simian virus 40 large T antigen
    • P.W. Rice, and C.N. Cole Efficient transcriptional activation of many simple modular promoters by simian virus 40 large T antigen J Virol 67 1993 6689 6697
    • (1993) J Virol , vol.67 , pp. 6689-6697
    • Rice, P.W.1    Cole, C.N.2
  • 42
    • 0034602192 scopus 로고    scopus 로고
    • A basal transcription factor that activates or represses transcription
    • P.J. Willy, R. Kobayashi, and J.T. Kadonaga A basal transcription factor that activates or represses transcription Science 290 2000 982 985
    • (2000) Science , vol.290 , pp. 982-985
    • Willy, P.J.1    Kobayashi, R.2    Kadonaga, J.T.3
  • 43
    • 0037115591 scopus 로고    scopus 로고
    • The NC2 α and β subunits play different roles in vivo
    • S. Creton, J.Q. Svejstrup, and M.A. Collart The NC2 α and β subunits play different roles in vivo Genes Dev 16 2002 3265 3276
    • (2002) Genes Dev , vol.16 , pp. 3265-3276
    • Creton, S.1    Svejstrup, J.Q.2    Collart, M.A.3
  • 44
    • 0034644732 scopus 로고    scopus 로고
    • Biochemical characterization of the TATA-binding protein-Gal4 activation domain complex
    • Y. Xie, C. Denison, S.H. Yang, D.A. Fancy, and T. Kodadek Biochemical characterization of the TATA-binding protein-Gal4 activation domain complex J Biol Chem 275 2000 31914 31920
    • (2000) J Biol Chem , vol.275 , pp. 31914-31920
    • Xie, Y.1    Denison, C.2    Yang, S.H.3    Fancy, D.A.4    Kodadek, T.5
  • 45
    • 0027454228 scopus 로고
    • Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-kappa B
    • L.D. Kerr, L.J. Ransone, P. Wamsley, M.J. Schmitt, T.G. Boyer, Q. Zhou, A.J. Berk, and I.M. Verma Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-kappa B Nature 365 1993 412 419
    • (1993) Nature , vol.365 , pp. 412-419
    • Kerr, L.D.1    Ransone, L.J.2    Wamsley, P.3    Schmitt, M.J.4    Boyer, T.G.5    Zhou, Q.6    Berk, A.J.7    Verma, I.M.8
  • 46
    • 0025345242 scopus 로고
    • Direct and selective binding of an acidic transcriptional activation domain to the TATA-box factor TFIID
    • K.F. Stringer, C.J. Ingles, and J. Greenblatt Direct and selective binding of an acidic transcriptional activation domain to the TATA-box factor TFIID Nature 345 1990 783 786
    • (1990) Nature , vol.345 , pp. 783-786
    • Stringer, K.F.1    Ingles, C.J.2    Greenblatt, J.3
  • 47
    • 0034609446 scopus 로고    scopus 로고
    • Control of gene expression through regulation of the TATA-binding protein
    • B.F. Pugh Control of gene expression through regulation of the TATA-binding protein Gene 225 2000 1 14
    • (2000) Gene , vol.225 , pp. 1-14
    • Pugh, B.F.1
  • 48
    • 0035853690 scopus 로고    scopus 로고
    • High affinity interaction of yeast transcriptional regulator, Mot1, with TATA box-binding protein (TBP)
    • J.I. Adamkewicz, K.E. Hansen, and J. Thorner High affinity interaction of yeast transcriptional regulator, Mot1, with TATA box-binding protein (TBP) J Biol Chem 276 2001 11883 11894
    • (2001) J Biol Chem , vol.276 , pp. 11883-11894
    • Adamkewicz, J.I.1    Hansen, K.E.2    Thorner, J.3
  • 49
    • 0032523882 scopus 로고    scopus 로고
    • Regulation of gene expression by TBP-associated protein
    • T.I. Lee, and R.A. Young Regulation of gene expression by TBP-associated protein Genes Dev 12 1998 1398 1408
    • (1998) Genes Dev , vol.12 , pp. 1398-1408
    • Lee, T.I.1    Young, R.A.2
  • 50
    • 0028079760 scopus 로고
    • Activator-induced conformational change in general transcription factor TFIIB
    • S.G. Roberts, and M.R. Green Activator-induced conformational change in general transcription factor TFIIB Nature 371 1994 717 720
    • (1994) Nature , vol.371 , pp. 717-720
    • Roberts, S.G.1    Green, M.R.2
  • 52
    • 1142274214 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II-TFIIB cocrystal at 4.5 angstroms
    • D.A. Bushnell, K.D. Westover, R.E. Davis, and R.D. Kornberg Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 angstroms Science 303 2004 983 988
    • (2004) Science , vol.303 , pp. 983-988
    • Bushnell, D.A.1    Westover, K.D.2    Davis, R.E.3    Kornberg, R.D.4
  • 53
    • 0028903904 scopus 로고
    • TATA-binding protein residues implicated in a functional interplay between negative cofactor NC2 (DR1) and general factors TFIIA and TFIIB
    • T.K. Kim, Y. Zhao, H. Ge, R. Bernstein, and G.R. Roeder TATA-binding protein residues implicated in a functional interplay between negative cofactor NC2 (DR1) and general factors TFIIA and TFIIB J Biol Chem 270 1995 10976 10981
    • (1995) J Biol Chem , vol.270 , pp. 10976-10981
    • Kim, T.K.1    Zhao, Y.2    Ge, H.3    Bernstein, R.4    Roeder, G.R.5
  • 55
    • 20444383635 scopus 로고    scopus 로고
    • http://www.pdb.org/
  • 56
    • 0034602843 scopus 로고    scopus 로고
    • Structural basis of preinitiation complex assembly on human Pol II promoters
    • T.F. Tsai, and P.B. Sigler Structural basis of preinitiation complex assembly on human Pol II promoters EMBO J 19 2000 25 36
    • (2000) EMBO J , vol.19 , pp. 25-36
    • Tsai, T.F.1    Sigler, P.B.2
  • 58
    • 0031562901 scopus 로고    scopus 로고
    • The 2.1 Å crystal structure of an archaeal preinitiation complex TATA-box-binding protein/transcription factor (II)B core/TATA-box
    • P.F. Kosa, G. Ghosh, B.S. Dedecker, and P.B. Sigler The 2.1 Å crystal structure of an archaeal preinitiation complex TATA-box-binding protein/transcription factor (II)B core/TATA-box PNAS 94 1997 6042 6047
    • (1997) PNAS , vol.94 , pp. 6042-6047
    • Kosa, P.F.1    Ghosh, G.2    Dedecker, B.S.3    Sigler, P.B.4
  • 59
    • 0033598826 scopus 로고    scopus 로고
    • The structural basis for oriented assembly of a TBP/TFB/promoter complex
    • O. Littlefield, Y. Korkhin, and P.B. Sigler The structural basis for oriented assembly of a TBP/TFB/promoter complex PNAS 96 1999 13668 13673
    • (1999) PNAS , vol.96 , pp. 13668-13673
    • Littlefield, O.1    Korkhin, Y.2    Sigler, P.B.3
  • 60
    • 0028156696 scopus 로고
    • Accuracy of refined proteins structures. II. Comparison of four independently refined models of human interleukin 1α
    • D.H. Ohlendorf Accuracy of refined proteins structures. II. Comparison of four independently refined models of human interleukin 1α Acta Crystallogr D50 1994 808 812
    • (1994) Acta Crystallogr , vol.50 , pp. 808-812
    • Ohlendorf, D.H.1
  • 61
    • 0027172878 scopus 로고
    • Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy
    • G.M. Clore, M.A. Robien, and A.M. Gronenborn Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy J Mol Biol 231 1993 82 102
    • (1993) J Mol Biol , vol.231 , pp. 82-102
    • Clore, G.M.1    Robien, M.A.2    Gronenborn, A.M.3
  • 62
    • 0028232369 scopus 로고
    • An assessment of the precision and accuracy of protein structures determined by NMR. Dependence on distance errors
    • D. Zhao, and O. Jardetzky An assessment of the precision and accuracy of protein structures determined by NMR. Dependence on distance errors J Mol Biol 239 1994 601 607
    • (1994) J Mol Biol , vol.239 , pp. 601-607
    • Zhao, D.1    Jardetzky, O.2
  • 63
    • 0033626545 scopus 로고    scopus 로고
    • Structure of a (Cys3His) zinc ribbon, a ubiquitous motif in archaeal and eukaryal transcription
    • H.T. Chen, P. Legault, J. Glushka, J.G. Omichinski, and R.A. Scott Structure of a (Cys3His) zinc ribbon, a ubiquitous motif in archaeal and eukaryal transcription Protein Sci 9 2000 1743 1752
    • (2000) Protein Sci , vol.9 , pp. 1743-1752
    • Chen, H.T.1    Legault, P.2    Glushka, J.3    Omichinski, J.G.4    Scott, R.A.5
  • 65
    • 0031024906 scopus 로고    scopus 로고
    • Selective use of TBP and TFIIB reveled by a TATA-TBP-TFIIB array with altered specificity
    • W.P. Tansey, and W. Herr Selective use of TBP and TFIIB reveled by a TATA-TBP-TFIIB array with altered specificity Science 275 1997 829 831
    • (1997) Science , vol.275 , pp. 829-831
    • Tansey, W.P.1    Herr, W.2
  • 66
    • 0033950379 scopus 로고    scopus 로고
    • Role of the TATA binding protein-transcription factor IIB in supporting basal and activated transcription in plant cells
    • S. Pan, E. Czarnecka-Verner, and W.B. Gurley Role of the TATA binding protein-transcription factor IIB in supporting basal and activated transcription in plant cells Plant Cell 12 2000 125 135
    • (2000) Plant Cell , vol.12 , pp. 125-135
    • Pan, S.1    Czarnecka-Verner, E.2    Gurley, W.B.3
  • 67
    • 0031025295 scopus 로고    scopus 로고
    • A severely defective TATA-binding protein-TFIIB interaction does not preclude transcriptional activation in vivo
    • M. Lee, and K. Struhl A severely defective TATA-binding protein-TFIIB interaction does not preclude transcriptional activation in vivo Mol Cell Biol 17 1997 1336 1345
    • (1997) Mol Cell Biol , vol.17 , pp. 1336-1345
    • Lee, M.1    Struhl, K.2
  • 68
    • 0035856501 scopus 로고    scopus 로고
    • Promoter-specific activation defects by a novel yeast TBP mutant compromised for TFIIB interaction
    • C.M. Virbasius, F.C. Holstege, R.A. Young, and M.R. Green Promoter-specific activation defects by a novel yeast TBP mutant compromised for TFIIB interaction Curr Biol 11 2001 1794 1798
    • (2001) Curr Biol , vol.11 , pp. 1794-1798
    • Virbasius, C.M.1    Holstege, F.C.2    Young, R.A.3    Green, M.R.4
  • 69
    • 0036892063 scopus 로고    scopus 로고
    • Interdependent interaction between TFIIB, TATA binding protein and DNA
    • R.M. Buratowski, J. Downs, and S. Buratowski Interdependent interaction between TFIIB, TATA binding protein and DNA Mol Cell Biol 22 2002 8735 8743
    • (2002) Mol Cell Biol , vol.22 , pp. 8735-8743
    • Buratowski, R.M.1    Downs, J.2    Buratowski, S.3
  • 70
    • 4243071596 scopus 로고    scopus 로고
    • The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum
    • Z. Bozdech, M. Llinas, B.L. Pulliam, E.D. Wong, J. Zhu, and J.L. DeRisi The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum PloS Biol 1 2003 1 16
    • (2003) PloS Biol , vol.1 , pp. 1-16
    • Bozdech, Z.1    Llinas, M.2    Pulliam, B.L.3    Wong, E.D.4    Zhu, J.5    Derisi, J.L.6
  • 72
    • 0027340219 scopus 로고
    • Characterization of the gene encoding an unusually divergent TATA-binding protein (TBP) from the extremely A+T-rich human malaria parasite Plasmodium falciparum
    • M.B. McAndrew, M. Read, P.F. Sims, and J.E. Hyde Characterization of the gene encoding an unusually divergent TATA-binding protein (TBP) from the extremely A+T-rich human malaria parasite Plasmodium falciparum Gene 124 1993 165 171
    • (1993) Gene , vol.124 , pp. 165-171
    • McAndrew, M.B.1    Read, M.2    Sims, P.F.3    Hyde, J.E.4
  • 74
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • A. Sali, and T.L. Blundell Comparative protein modeling by satisfaction of spatial restraints J Mol Biol 234 1993 779 815
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 75
    • 0028051828 scopus 로고
    • Derivation of rules for comparative protein modeling from a database of protein structure alignments
    • A. Sali, and J.P. Overington Derivation of rules for comparative protein modeling from a database of protein structure alignments Protein Sci 3 1994 1582 1596
    • (1994) Protein Sci , vol.3 , pp. 1582-1596
    • Sali, A.1    Overington, J.P.2
  • 76
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • A. Fiser, L.K. Do, and A. Sali Modeling of loops in protein structures Protein Sci 9 2000 1753 1773
    • (2000) Protein Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, L.K.2    Sali, A.3
  • 78
    • 0242593434 scopus 로고    scopus 로고
    • Development and current status of the CHARMM force field for nucleic acids
    • A.D. MacKerell Jr., N. Banavali, and N. Foloppe Development and current status of the CHARMM force field for nucleic acids Biopolymers 56 2000 257 265
    • (2000) Biopolymers , vol.56 , pp. 257-265
    • MacKerell Jr., A.D.1    Banavali, N.2    Foloppe, N.3
  • 80
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J Appl Crystallogr 26 1993 283 291
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 82
    • 0025398721 scopus 로고
    • WHATIF: A molecular modeling and drug design program
    • G. Vriend WHATIF: a molecular modeling and drug design program J Mol Graph 8 1990 52 56
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 83
    • 0035896024 scopus 로고    scopus 로고
    • Consurf: An algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information
    • A. Armon, D. Graur, and N. Ben-Tal Consurf: an algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information J Mol Biol 307 2001 447 463
    • (2001) J Mol Biol , vol.307 , pp. 447-463
    • Armon, A.1    Graur, D.2    Ben-Tal, N.3
  • 84
    • 20444413538 scopus 로고    scopus 로고
    • Consurf web http://consurf.tau.ac.il
  • 85
    • 20444389159 scopus 로고    scopus 로고
    • Rate4Site: http://ashtoret.tau.ac.il/
  • 87
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice Nucleic Acids Res 22 1994 4673 4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 88
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • T. Pupko, R.E. Bell, I. Mayrose, F. Glaser, and N. Ben-Tal Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues Bioinformatics 18 2002 71 77
    • (2002) Bioinformatics , vol.18 , pp. 71-77
    • Pupko, T.1    Bell, R.E.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 89
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K. Sharp, and H. Honig Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins 11 1991 281 296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, H.3
  • 90
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • R.A. Engh, and R. Huber Accurate bond and angle parameters for X-ray protein structure refinement Acta Crystallogr A47 1991 392 400
    • (1991) Acta Crystallogr , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 91
    • 0027542118 scopus 로고
    • Quality control of protein models: Directional atomic contact analysis
    • G. Vriend, and C. Sander Quality control of protein models: directional atomic contact analysis J Appl Crystallogr 26 1993 47 60
    • (1993) J Appl Crystallogr , vol.26 , pp. 47-60
    • Vriend, G.1    Sander, C.2


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