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Volumn 8, Issue 9, 2010, Pages

Complete structural model of Escherichia coli RNA polymerase from a Hybrid Approach

Author keywords

[No Author keywords available]

Indexed keywords

RNA POLYMERASE;

EID: 77957921869     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1000483     Document Type: Article
Times cited : (101)

References (70)
  • 1
    • 0024557468 scopus 로고
    • Analysis of the gene encoding the largest subunit of RNA polymerase II in Drosophila
    • Jokerst RS, Weeks JR, Zehring WA, Greenleaf AL (1989) Analysis of the gene encoding the largest subunit of RNA polymerase II in Drosophila. Mol Gen Genet 215: 266-275.
    • (1989) Mol Gen Genet , vol.215 , pp. 266-275
    • Jokerst, R.S.1    Weeks, J.R.2    Zehring, W.A.3    Greenleaf, A.L.4
  • 2
    • 0344271983 scopus 로고
    • Prokaryotic and eukaryotic RNA polymerases have homologous core subunits
    • Sweetser D, Nonet M, Young RA (1987) Prokaryotic and eukaryotic RNA polymerases have homologous core subunits. Proc Natl Acad Sci U S A 84: 1192-1196.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 1192-1196
    • Sweetser, D.1    Nonet, M.2    Young, R.A.3
  • 3
    • 73649138940 scopus 로고    scopus 로고
    • Molecular evolution of multi-subunit RNA polymerases: Sequence analysis
    • Lane WJ, Darst SA (2009) Molecular evolution of multi-subunit RNA polymerases: sequence analysis. J Mol Biol 395: 671-685.
    • (2009) J Mol Biol , vol.395 , pp. 671-685
    • Lane, W.J.1    Darst, S.A.2
  • 4
    • 2942576138 scopus 로고    scopus 로고
    • Evolution of bacterial RNA polymerase: Implications for large-scale bacterial phylogeny, domain accretion, and horizontal gene transfer
    • Iyer LM, Koonin EV, Aravind L (2004) Evolution of bacterial RNA polymerase: implications for large-scale bacterial phylogeny, domain accretion, and horizontal gene transfer. Gene 335: 73-88.
    • (2004) Gene , vol.335 , pp. 73-88
    • Iyer, L.M.1    Koonin, E.V.2    Aravind, L.3
  • 5
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    • Zhang G, Campbell EA, Minakhin L, Richter C, Severinov K, et al. (1999) Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution. Cell 98: 811-824.
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1    Campbell, E.A.2    Minakhin, L.3    Richter, C.4    Severinov, K.5
  • 6
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • Murakami K, Masuda S, Darst SA (2002) Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution. Science 296: 1280-1284.
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.1    Masuda, S.2    Darst, S.A.3
  • 7
    • 0037071844 scopus 로고    scopus 로고
    • Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution
    • Vassylyev DG, Sekine S, Laptenko O, Lee J, Vassylyeva MN, et al. (2002) Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution. Nature 417: 712-719.
    • (2002) Nature , vol.417 , pp. 712-719
    • Vassylyev, D.G.1    Sekine, S.2    Laptenko, O.3    Lee, J.4    Vassylyeva, M.N.5
  • 9
    • 0037791613 scopus 로고    scopus 로고
    • Evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNAdependent RNA polymerases and the origin of RNA polymerases
    • Iyer LM, Koonin EV, Aravind L (2003) Evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNAdependent RNA polymerases and the origin of RNA polymerases. BMC Struct Biol 3: 1-23.
    • (2003) BMC Struct Biol , vol.3 , pp. 1-23
    • Iyer, L.M.1    Koonin, E.V.2    Aravind, L.3
  • 10
    • 25144510935 scopus 로고    scopus 로고
    • Structure and function of lineage-specific sequence insertions in the bacterial RNA polymerase b' subunit
    • Chlenov M, Masuda S, Murakami KS, Nikiforov V, Darst SA, et al. (2005) Structure and function of lineage-specific sequence insertions in the bacterial RNA polymerase b' subunit. J Mol Biol 353: 138-154.
    • (2005) J Mol Biol , vol.353 , pp. 138-154
    • Chlenov, M.1    Masuda, S.2    Murakami, K.S.3    Nikiforov, V.4    Darst, S.A.5
  • 12
    • 0031801743 scopus 로고    scopus 로고
    • Information processing by RNA polymerase: Recognition of regulatory signals during RNA chain elongation
    • Mooney RA, Artsimovitch I, Landick R (1998) Information processing by RNA polymerase: recognition of regulatory signals during RNA chain elongation. J Bacteriol 180: 3265-3275.
    • (1998) J Bacteriol , vol.180 , pp. 3265-3275
    • Mooney, R.A.1    Artsimovitch, I.2    Landick, R.3
  • 14
    • 55249113939 scopus 로고    scopus 로고
    • Organization of an activator-bound RNA polymerase holoenzyme
    • Bose D, Pape T, Burrows PC, Rappas M, Wigneshweraraj S, et al. (2008) Organization of an activator-bound RNA polymerase holoenzyme. Mol Cell 32: 337-346.
    • (2008) Mol Cell , vol.32 , pp. 337-346
    • Bose, D.1    Pape, T.2    Burrows, P.C.3    Rappas, M.4    Wigneshweraraj, S.5
  • 15
    • 73949094255 scopus 로고    scopus 로고
    • Three-dimensional EM structure of an intact activator-dependent transcription initiation complex
    • Hudson B, Quispe J, Lara-Gonzalez S, Kim Y, Berman H, et al. (2009) Three-dimensional EM structure of an intact activator-dependent transcription initiation complex. Proc Natl Acad Sci U S A 106: 19830-19835.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19830-19835
    • Hudson, B.1    Quispe, J.2    Lara-Gonzalez, S.3    Kim, Y.4    Berman, H.5
  • 16
    • 3242887695 scopus 로고    scopus 로고
    • Protein structure prediction and analysis using the Robetta server
    • Kim DE, Chivian D, Baker D (2004) Protein structure prediction and analysis using the Robetta server. Nucleic Acids Res 32 Suppl 2: W526-W531.
    • (2004) Nucleic Acids Res 32 Suppl , vol.2
    • Kim, D.E.1    Chivian, D.2    Baker, D.3
  • 17
    • 0028270742 scopus 로고
    • A non-essential domain of E. coli RNA polymerase required for the action of the termination factor Alc
    • Severinov K, Kashlev M, Severinova E, Bass I, McWilliams K, et al. (1994) A non-essential domain of E. coli RNA polymerase required for the action of the termination factor Alc. J Biol Chem 269: 14254-14259.
    • (1994) J Biol Chem , vol.269 , pp. 14254-14259
    • Severinov, K.1    Kashlev, M.2    Severinova, E.3    Bass, I.4    McWilliams, K.5
  • 18
    • 0038823636 scopus 로고    scopus 로고
    • Co-overexpression of Escherichia coli RNA polymerase subunits allows isolation and analysis of mutant enzymes lacking lineage-specific sequence insertions
    • Artsimovitch I, Svetlov V, Murakami KS, Landick R (2003) Co-overexpression of Escherichia coli RNA polymerase subunits allows isolation and analysis of mutant enzymes lacking lineage-specific sequence insertions. J Biol Chem 278: 12344-12355.
    • (2003) J Biol Chem , vol.278 , pp. 12344-12355
    • Artsimovitch, I.1    Svetlov, V.2    Murakami, K.S.3    Landick, R.4
  • 19
    • 73649093377 scopus 로고    scopus 로고
    • Molecular evolution of multi-subunit RNA polymerases: Structural analysis
    • Lane WJ, Darst SA (2009) Molecular evolution of multi-subunit RNA polymerases: structural analysis. J Mol Biol 395: 686-704.
    • (2009) J Mol Biol , vol.395 , pp. 686-704
    • Lane, W.J.1    Darst, S.A.2
  • 20
    • 0031053054 scopus 로고    scopus 로고
    • Reductive alkylation of lysine residues to alter crystallization properties of proteins
    • Rayment I (1997) Reductive alkylation of lysine residues to alter crystallization properties of proteins. Methods Enzymol 276: 171-179.
    • (1997) Methods Enzymol , vol.276 , pp. 171-179
    • Rayment, I.1
  • 21
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD)
    • Hendrickson W, Norton JR, LeMaster DM (1990) Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD). EMBO J 9: 1665-1672.
    • (1990) EMBO J , vol.9 , pp. 1665-1672
    • Hendrickson, W.1    Norton, J.R.2    Lemaster, D.M.3
  • 22
    • 0026346986 scopus 로고
    • Mapping of trypsin cleavage and antibody-binding sites and delineation of a dispensable domain in the ß subunit of Escherichia coli RNA polymerase
    • Borukhov S, Severinov K, Kashlev M, Lebedev A, Bass I, et al. (1991) Mapping of trypsin cleavage and antibody-binding sites and delineation of a dispensable domain in the ß subunit of Escherichia coli RNA polymerase. J Biol Chem 266: 23921-23926.
    • (1991) J Biol Chem , vol.266 , pp. 23921-23926
    • Borukhov, S.1    Severinov, K.2    Kashlev, M.3    Lebedev, A.4    Bass, I.5
  • 23
    • 0034681167 scopus 로고    scopus 로고
    • Direct localization of a b subunit domain on the three-dimensional structure of Escherichia coli RNA polymerase
    • Opalka N, Mooney RA, Richter C, Severinov K, Landick R, et al. (1999) Direct localization of a b subunit domain on the three-dimensional structure of Escherichia coli RNA polymerase. Proc Natl Acad Sci USA 97: 617-622.
    • (1999) Proc Natl Acad Sci USA , vol.97 , pp. 617-622
    • Opalka, N.1    Mooney, R.A.2    Richter, C.3    Severinov, K.4    Landick, R.5
  • 24
    • 35348908913 scopus 로고    scopus 로고
    • Digital filter design using the hyperbolic tangent functions
    • Basokur AT (1998) Digital filter design using the hyperbolic tangent functions. J Balkan Geophys Soc 1: 14-18.
    • (1998) J Balkan Geophys Soc , vol.1 , pp. 14-18
    • Basokur, A.T.1
  • 26
    • 37749007365 scopus 로고    scopus 로고
    • GraFix: Sample preparation for single-particle electron cryomicroscopy
    • Kastner B, Fischer N, Golas MM, Sander B, Dube P, et al. (2008) GraFix: sample preparation for single-particle electron cryomicroscopy. Nature Meth 5: 53-55.
    • (2008) Nature Meth , vol.5 , pp. 53-55
    • Kastner, B.1    Fischer, N.2    Golas, M.M.3    Sander, B.4    Dube, P.5
  • 27
    • 46749096676 scopus 로고    scopus 로고
    • YUP.SCX: Coaxing atomic models into medium resolution electron density maps
    • Tan RK-Z, Devkota B, Harvey SC (2008) YUP.SCX: coaxing atomic models into medium resolution electron density maps. J Structural Biol 163: 163-174.
    • (2008) J Structural Biol , vol.163 , pp. 163-174
    • Tan, R.K.-Z.1    Devkota, B.2    Harvey, S.C.3
  • 29
    • 0032504132 scopus 로고    scopus 로고
    • Structure of the Escherichia coli RNA polymerase a subunit amino-terminal domain
    • Zhang G, Darst SA (1998) Structure of the Escherichia coli RNA polymerase a subunit amino-terminal domain. Science 281: 262-266.
    • (1998) Science , vol.281 , pp. 262-266
    • Zhang, G.1    Darst, S.A.2
  • 30
    • 44449102824 scopus 로고    scopus 로고
    • Rapid isolation and identification of bacteriophage T4-encoded modifications of Escherichia coli RNA polymerase: A generic method to study bacteriophage/host interactions
    • Westblade LF, Minakhin L, Kuznedelov K, Tackett AJ, Chang E, et al. (2008) Rapid isolation and identification of bacteriophage T4-encoded modifications of Escherichia coli RNA polymerase: a generic method to study bacteriophage/host interactions. J Proteome Res 7: 1244-1250.
    • (2008) J Proteome Res , vol.7 , pp. 1244-1250
    • Westblade, L.F.1    Minakhin, L.2    Kuznedelov, K.3    Tackett, A.J.4    Chang, E.5
  • 31
    • 0017174272 scopus 로고
    • A gene of bacteriophage T4 whose product prevents true late transcription on cytosine-containing T4 DNA
    • Snyder L, Gold L, Kutter E (1976) A gene of bacteriophage T4 whose product prevents true late transcription on cytosine-containing T4 DNA. Proc Natl Acad Sci U S A 73: 3098-3102.
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 3098-3102
    • Snyder, L.1    Gold, L.2    Kutter, E.3
  • 32
    • 0023954038 scopus 로고
    • Escherichia coli mutations that prevent the action of the T4 unf/alc protein map in an RNA polymerase gene
    • Snyder L, Jorissen L (1988) Escherichia coli mutations that prevent the action of the T4 unf/alc protein map in an RNA polymerase gene. Genetics 118: 173-180.
    • (1988) Genetics , vol.118 , pp. 173-180
    • Snyder, L.1    Jorissen, L.2
  • 33
    • 0021191338 scopus 로고
    • Genetic studies on the b subunit of Escherichia coli RNA polyerase VI. A redundant region in the b polypeptide
    • Nene V, Glass R (1984) Genetic studies on the b subunit of Escherichia coli RNA polyerase VI. A redundant region in the b polypeptide. Mol Gen Genet 196: 64-67.
    • (1984) Mol Gen Genet , vol.196 , pp. 64-67
    • Nene, V.1    Glass, R.2
  • 34
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme/DNA complex
    • Murakami K, Masuda S, Campbell EA, Muzzin O, Darst SA (2002) Structural basis of transcription initiation: an RNA polymerase holoenzyme/DNA complex. Science 296: 1285-1290.
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 35
    • 0032584668 scopus 로고    scopus 로고
    • Mutations in and monoclonal antibody binding to evolutionary hypervariable region of E. coli RNA polymerase b' subunit inhibit transcript cleavage and transcript elongation
    • Zakharova N, Bass I, Arsenieva E, Nikiforov V, Severinov K (1998) Mutations in and monoclonal antibody binding to evolutionary hypervariable region of E. coli RNA polymerase b' subunit inhibit transcript cleavage and transcript elongation. J Biol Chem 273: 19371-19374.
    • (1998) J Biol Chem , vol.273 , pp. 19371-19374
    • Zakharova, N.1    Bass, I.2    Arsenieva, E.3    Nikiforov, V.4    Severinov, K.5
  • 36
    • 0026781560 scopus 로고
    • Characterization and epitope mapping of monoclonal antibodies directed against the beta' subunit of the Escherichia coli RNA polymerase
    • Luo J, Krakow JS (1992) Characterization and epitope mapping of monoclonal antibodies directed against the beta' subunit of the Escherichia coli RNA polymerase. J Biol Chem 267: 18175-18181.
    • (1992) J Biol Chem , vol.267 , pp. 18175-18181
    • Luo, J.1    Krakow, J.S.2
  • 37
    • 0028104343 scopus 로고
    • Termination-altering amino acid substitutions in the beta' subunit of Escherichia coli RNA polymerase identify regions involved in RNA chain elongation
    • Weilbacher RG, Hebron C, Feng G, Landick R (1994) Termination-altering amino acid substitutions in the beta' subunit of Escherichia coli RNA polymerase identify regions involved in RNA chain elongation. Genes & Development 8: 2913-2927.
    • (1994) Genes & Development , vol.8 , pp. 2913-2927
    • Weilbacher, R.G.1    Hebron, C.2    Feng, G.3    Landick, R.4
  • 38
    • 33751235874 scopus 로고    scopus 로고
    • Structural basis of transcription: Role of the trigger loop in substrate specificity and catalysis
    • Wang D, Bushnell DA, Westover KD, Kaplan CD, Kornberg RD (2006) Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis. Cell 127: 941-954.
    • (2006) Cell , vol.127 , pp. 941-954
    • Wang, D.1    Bushnell, D.A.2    Westover, K.D.3    Kaplan, C.D.4    Kornberg, R.D.5
  • 40
    • 44449103640 scopus 로고    scopus 로고
    • The RNA polymerase II trigger loop functions in substrate selection and is directly targeted by alphaamanitin
    • Kaplan CD, Larsson K-M, Kornberg RD (2008) The RNA polymerase II trigger loop functions in substrate selection and is directly targeted by alphaamanitin. Mol Cell 30: 547-556.
    • (2008) Mol Cell , vol.30 , pp. 547-556
    • Kaplan, C.D.1    Larsson, K.-M.2    Kornberg, R.D.3
  • 41
    • 44449094019 scopus 로고    scopus 로고
    • Transient reversal of RNA polymerase II active site closing controls fidelity of transcription elongation
    • Kireeva ML, Nedialkov YA, Cremona GH, Purtov YA, Lubkowska L, et al. (2008) Transient reversal of RNA polymerase II active site closing controls fidelity of transcription elongation. Mol Cell 30: 557-566.
    • (2008) Mol Cell , vol.30 , pp. 557-566
    • Kireeva, M.L.1    Nedialkov, Y.A.2    Cremona, G.H.3    Purtov, Y.A.4    Lubkowska, L.5
  • 42
  • 43
    • 0034932730 scopus 로고    scopus 로고
    • Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25
    • Delgado MA, Rintoul MR, Farias RN, Salomon RA (2001) Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25. J Bacteriol 183: 4543-4550.
    • (2001) J Bacteriol , vol.183 , pp. 4543-4550
    • Delgado, M.A.1    Rintoul, M.R.2    Farias, R.N.3    Salomon, R.A.4
  • 44
    • 2942696237 scopus 로고    scopus 로고
    • Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the RNA polymerase secondary channel
    • Mukhopadhyay J, Sineva E, Knight J, Levy RM, Ebright RH (2004) Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the RNA polymerase secondary channel. Mol Cell 14: 739-751.
    • (2004) Mol Cell , vol.14 , pp. 739-751
    • Mukhopadhyay, J.1    Sineva, E.2    Knight, J.3    Levy, R.M.4    Ebright, R.H.5
  • 45
    • 0026526445 scopus 로고
    • Microcin-25, a novel antimicrobial peptide produced by Escherichia-coli
    • Salomon RA, Farias RN (1992) Microcin-25, a novel antimicrobial peptide produced by Escherichia-coli. J Bacteriol 174: 7428-7435.
    • (1992) J Bacteriol , vol.174 , pp. 7428-7435
    • Salomon, R.A.1    Farias, R.N.2
  • 46
    • 0346890209 scopus 로고    scopus 로고
    • Mutations of bacterial RNA polymerase leading to resistance to microcin J25
    • Yuzenkova J, Delgado MA, Nechaev S, Savalia D, Epshtein V, et al. (2002) Mutations of bacterial RNA polymerase leading to resistance to microcin J25. J Biol Chem 277: 50867-50875.
    • (2002) J Biol Chem , vol.277 , pp. 50867-50875
    • Yuzenkova, J.1    Delgado, M.A.2    Nechaev, S.3    Savalia, D.4    Epshtein, V.5
  • 47
    • 0016760411 scopus 로고
    • In vivo and in vitro phosphorylation of DNA-dependent RNA polymerase of Escherichia coli by bacteriophage-T7-induced protein kinase
    • Zillig W, Fujiki H, Blum W, Janekovi D, Schweig M, et al. (1975) In vivo and in vitro phosphorylation of DNA-dependent RNA polymerase of Escherichia coli by bacteriophage-T7-induced protein kinase. Proc Natl Acad Sci U S A 72: 2506-2510.
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 2506-2510
    • Zillig, W.1    Fujiki, H.2    Blum, W.3    Janekovi, D.4    Schweig, M.5
  • 48
    • 33646545351 scopus 로고    scopus 로고
    • Localization of the Escherichia coli RNA polymerase beta' subunit residue phosphorylated by bacteriophage T7 kinase Gp0.7
    • Severinova E, Severinov K (2006) Localization of the Escherichia coli RNA polymerase beta' subunit residue phosphorylated by bacteriophage T7 kinase Gp0.7. J Bacteriol 188: 3470-3476.
    • (2006) J Bacteriol , vol.188 , pp. 3470-3476
    • Severinova, E.1    Severinov, K.2
  • 49
    • 0030808646 scopus 로고    scopus 로고
    • Tethering of the large subunits of Escherichia coli RNA polymerase
    • Severinov K, Mooney R, Darst SA, Landick R (1997) Tethering of the large subunits of Escherichia coli RNA polymerase. J Biol Chem 272: 24137-24140.
    • (1997) J Biol Chem , vol.272 , pp. 24137-24140
    • Severinov, K.1    Mooney, R.2    Darst, S.A.3    Landick, R.4
  • 50
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie S (1997) Preparation of selenomethionyl proteins for phase determination. Methods Enzymol 276: 523-530.
    • (1997) Methods Enzymol , vol.276 , pp. 523-530
    • Doublie, S.1
  • 51
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 52
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM (2008) A short history of SHELX. Acta Crystallogr A 64: 112-122.
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 53
    • 0003292939 scopus 로고    scopus 로고
    • SHARP: A maximum-likelihood heavy-atom parameter refinement and phasing program for the MIR and MAD methods
    • In: Bourne P, Watenpaugh K, eds., Boston: Kluwer Academic Publishers
    • de La Fortelle E, Irwin JJ, Bricogne G (1997) SHARP: a maximum-likelihood heavy-atom parameter refinement and phasing program for the MIR and MAD methods. In: Bourne P, Watenpaugh K, eds. Crystallographic computing. Boston: Kluwer Academic Publishers. pp 1-9.
    • (1997) Crystallographic Computing , pp. 1-9
    • de La Fortelle, E.1    Irwin, J.J.2    Bricogne, G.3
  • 54
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer G, Cohen SX, Lamzin VS, Perrakis A (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nature Protocols 3: 1171-1179.
    • (2008) Nature Protocols , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 55
  • 57
    • 10644220255 scopus 로고    scopus 로고
    • The bacteriophage T4 late-transcription coactivator gp33 binds the flap domain of Escherichia coli RNA polymerase
    • Nechaev S, Kamali-Moghaddam M, Andre E, Leonetti J-P, Geiduschek EP (2004) The bacteriophage T4 late-transcription coactivator gp33 binds the flap domain of Escherichia coli RNA polymerase. Proc Natl Acad Sci U S A 101: 17365-17370.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17365-17370
    • Nechaev, S.1    Kamali-Moghaddam, M.2    Andre, E.3    Leonetti, J.-P.4    Geiduschek, E.P.5
  • 58
    • 0034733377 scopus 로고    scopus 로고
    • The anti-s factor SpoIIAB forms a 2:1 complex with sF, contacting multiple conserved regions of the s factor
    • Campbell EA, Darst SA (2000) The anti-s factor SpoIIAB forms a 2:1 complex with sF, contacting multiple conserved regions of the s factor. J Mol Biol 300: 17-28.
    • (2000) J Mol Biol , vol.300 , pp. 17-28
    • Campbell, E.A.1    Darst, S.A.2
  • 60
    • 0043244877 scopus 로고    scopus 로고
    • Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase
    • Opalka N, Chlenov M, Chacon P, Rice WJ, Wriggers W, et al. (2003) Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase. Cell 114: 335-345.
    • (2003) Cell , vol.114 , pp. 335-345
    • Opalka, N.1    Chlenov, M.2    Chacon, P.3    Rice, W.J.4    Wriggers, W.5
  • 61
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semi-automated software for high resolution single particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: semi-automated software for high resolution single particle reconstructions. J Structural Biol 128: 82-97.
    • (1999) J Structural Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 62
    • 0036690340 scopus 로고    scopus 로고
    • Structure of yeast RNA polymerase II in solution: Implications for enzyme regulation and interaction with promoter DNA
    • Craighead JL, Chang WH, Asturias FJ (2002) Structure of yeast RNA polymerase II in solution: implications for enzyme regulation and interaction with promoter DNA. Structure (Camb) 10: 1117-1125.
    • (2002) Structure (Camb) , vol.10 , pp. 1117-1125
    • Craighead, J.L.1    Chang, W.H.2    Asturias, F.J.3
  • 63
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, Radermacher M, Penczek P, Zhu J, Li Y, et al. (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116: 190-199.
    • (1996) J Struct Biol , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5
  • 64
    • 0028393194 scopus 로고
    • The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles
    • Penczek P, Grassucci RA, Frank J (1994) The ribosome at improved resolution: new techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles. Ultramicroscopy 53: 251-270.
    • (1994) Ultramicroscopy , vol.53 , pp. 251-270
    • Penczek, P.1    Grassucci, R.A.2    Frank, J.3
  • 65
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • Edgar RC (2004) MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformat 5: 113.
    • (2004) BMC Bioinformat , vol.5 , pp. 113
    • Edgar, R.C.1
  • 66
    • 0037433034 scopus 로고    scopus 로고
    • PCMA: Fast and accurate multiple sequence alignment based on profile consistency
    • Pei J, Sadreyev R, Grishin NV (2003) PCMA: fast and accurate multiple sequence alignment based on profile consistency. Bioinformatics 19: 427-428.
    • (2003) Bioinformatics , vol.19 , pp. 427-428
    • Pei, J.1    Sadreyev, R.2    Grishin, N.V.3
  • 67
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial-cell envelope protein
    • Saxton WO, Baumeister W (1982) The correlation averaging of a regularly arranged bacterial-cell envelope protein. J Microsc 127: 127-138.
    • (1982) J Microsc , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 68
    • 0000313739 scopus 로고
    • Exact filters for general geometry threedimensional reconstruction
    • Harauz G, van Heel M (1986) Exact filters for general geometry threedimensional reconstruction. Optik 73: 146-156.
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    van Heel, M.2
  • 70
    • 36549005538 scopus 로고    scopus 로고
    • PFAAT version 2.0: A tool for editing, annotating, and analyzing multiple sequence alignments
    • Caffrey DR, Dana PH, Mathur V, Ocano M, Hong E-J, et al. (2007) PFAAT version 2.0: a tool for editing, annotating, and analyzing multiple sequence alignments. BMC Bioinformat 8: 381.
    • (2007) BMC Bioinformat , vol.8 , pp. 381
    • Caffrey, D.R.1    Dana, P.H.2    Mathur, V.3    Ocano, M.4    Hong, E.-J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.