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Volumn 343, Issue 1, 2006, Pages 90-98

Structure and dynamics of RNA polymerase II elongation complex

Author keywords

Molecular dynamics; Molecular modeling; Molecular motor; RNA polymerase II; Transcription

Indexed keywords

RNA POLYMERASE II;

EID: 33645109502     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.02.124     Document Type: Article
Times cited : (8)

References (35)
  • 2
    • 0035827346 scopus 로고    scopus 로고
    • Structural bases of transcription: RNA polymerase II at 2.8 Å resolution
    • P. Cramer, D.A. Bushnell, and R.D. Kornberg Structural bases of transcription: RNA polymerase II at 2.8 Å resolution Science 292 2001 1863 1876
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 3
    • 0035827332 scopus 로고    scopus 로고
    • Structural bases of transcription: RNA polymerase II elongation complex at 3.3 Å resolution
    • A.L. Gnatt, P. Cramer, J. Fu, D.A. Bushnell, and R.D. Kornberg Structural bases of transcription: RNA polymerase II elongation complex at 3.3 Å resolution Science 292 2001 1876 1882
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 4
    • 1142274214 scopus 로고    scopus 로고
    • Structural bases of transcription: An RNA polymerase II-TFIIB cocrystal at 4.5 Å
    • D.A. Bushnell, K.D. Westover, R.E. Davis, and R.D. Kornberg Structural bases of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Å 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
  • 5
    • 1142310578 scopus 로고    scopus 로고
    • Structural bases of transcription: Separation of RNA from DNA by RNA polymerase II
    • K.D. Westover, D.A. Bushnell, and R.D. Kornberg Structural bases of transcription: separation of RNA from DNA by RNA polymerase II Science 303 2004 1014 1016
    • (2004) Science , vol.303 , pp. 1014-1016
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 6
    • 10944232674 scopus 로고    scopus 로고
    • Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
    • H. Kettenberger, K.-J. Armache, and P. Cramer Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS Mol. Cell 22 2004 955 965
    • (2004) Mol. Cell , vol.22 , pp. 955-965
    • Kettenberger, H.1    Armache, K.-J.2    Cramer, P.3
  • 7
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    • G. Zhang, E.A. Campbell, L. Minakhin, C. Richter, K. Severinov, and S.A. Darst Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution Cell 98 1999 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    Darst, S.A.6
  • 8
    • 0037123659 scopus 로고    scopus 로고
    • Structural bases of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • K.S. Murakami, S. Masuda, and S.A. Darst Structural bases of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution Science 296 2002 1280 1284
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.S.1    Masuda, S.2    Darst, S.A.3
  • 9
    • 0037123602 scopus 로고    scopus 로고
    • Structural bases of transcription initiation: RNA polymerase holoenzyme-DNA complex
    • K.S. Murakami, S. Masuda, E.A. Campbell, O. Muzzin, and S.A. Darst Structural bases of transcription initiation: RNA polymerase holoenzyme-DNA complex Science 296 2002 1285 1290
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.S.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 13
    • 1342313235 scopus 로고    scopus 로고
    • The structural mechanism of transcription and helicase activity in T7 RNA polymerase
    • W.Y. Yin, and T.A. Steitz The structural mechanism of transcription and helicase activity in T7 RNA polymerase Cell 116 2004 393 404
    • (2004) Cell , vol.116 , pp. 393-404
    • Yin, W.Y.1    Steitz, T.A.2
  • 14
    • 0034625251 scopus 로고    scopus 로고
    • Structural organization of the RNA polymerase-promoter open complex
    • N. Naryshkin, A. Revyakin, Y. Kim, V. Mekler, and R.H. Ebright Structural organization of the RNA polymerase-promoter open complex Cell 101 2000 601 611
    • (2000) Cell , vol.101 , pp. 601-611
    • Naryshkin, N.1    Revyakin, A.2    Kim, Y.3    Mekler, V.4    Ebright, R.H.5
  • 16
    • 0026754015 scopus 로고
    • Accurate modeling of protein conformation by automatic segment matching
    • M. Levitt Accurate modeling of protein conformation by automatic segment matching J. Mol. Biol. 226 1992 507 533
    • (1992) J. Mol. Biol. , vol.226 , pp. 507-533
    • Levitt, M.1
  • 18
    • 0342926714 scopus 로고
    • Molecular dynamics simulations of proteins in water without the truncation of long-range Coulomb interactions
    • M. Saito Molecular dynamics simulations of proteins in water without the truncation of long-range Coulomb interactions Mol. Simul. 8 1995 321 333
    • (1995) Mol. Simul. , vol.8 , pp. 321-333
    • Saito, M.1
  • 19
    • 0029110156 scopus 로고
    • Toward the accurate modeling of DNA-the importance of long-range electrostatics
    • D.M. York, W. Yang, H. Lee, T.A. Darden, and L.G. Pedersen Toward the accurate modeling of DNA-the importance of long-range electrostatics J. Am. Chem. Soc. 117 1995 5001 5002
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5001-5002
    • York, D.M.1    Yang, W.2    Lee, H.3    Darden, T.A.4    Pedersen, L.G.5
  • 20
    • 0001099087 scopus 로고
    • Molecular dynamics machine: Special-purpose computer for molecular dynamics simulations
    • T. Narumi, R. Susukita, T. Ebisuzaki, G. McNiven, and B. Elmergreen Molecular dynamics machine: special-purpose computer for molecular dynamics simulations Mol. Simul. 21 1995 401 415
    • (1995) Mol. Simul. , vol.21 , pp. 401-415
    • Narumi, T.1    Susukita, R.2    Ebisuzaki, T.3    McNiven, G.4    Elmergreen, B.5
  • 25
    • 5644282595 scopus 로고    scopus 로고
    • Cooperative motions of protein and hydration water molecules: Molecular dynamics study of Scytalone dehydratase
    • N. Okimoto, T. Nakamura, A. Suenaga, N. Futatsugi, Y. Hirano, I. Yamaguchi, and T. Ebisuzaki Cooperative motions of protein and hydration water molecules: molecular dynamics study of Scytalone dehydratase J. Am. Chem. Soc. 126 2004 13132 13139
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 13132-13139
    • Okimoto, N.1    Nakamura, T.2    Suenaga, A.3    Futatsugi, N.4    Hirano, Y.5    Yamaguchi, I.6    Ebisuzaki, T.7
  • 28
    • 0002098417 scopus 로고    scopus 로고
    • The development/application of a 'minimalist' organic/biochemical molecular mechanic force field using a combination of ab initio calculations and experimental data
    • A. Wilkinson P. Weiner W.F. van Gunsteren Elsevier
    • P.A. Kollman, R. Dixon, W. Cornell, T. Fox, C. Chipot, and A. Pohorille The development/application of a 'minimalist' organic/biochemical molecular mechanic force field using a combination of ab initio calculations and experimental data A. Wilkinson P. Weiner W.F. van Gunsteren Computer Simulations of Biological Systems vol. 3 1997 Elsevier 83 96
    • (1997) Computer Simulations of Biological Systems , vol.3 , pp. 83-96
    • Kollman, P.A.1    Dixon, R.2    Cornell, W.3    Fox, T.4    Chipot, C.5    Pohorille, A.6
  • 29
    • 33646940952 scopus 로고    scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.-P. Ryckeart, G. Ciccotti, and H.J.C. Berendsen Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J. Comput. Chem. 23 1997 327 341
    • (1997) J. Comput. Chem. , vol.23 , pp. 327-341
    • Ryckeart, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 31
    • 0029633176 scopus 로고
    • A method to explore transition paths in macromolecules-applications to hemoglobin and phosphoglycerate kinase
    • C. Guilbert, D. Perahia, and L.A. Mouawad A method to explore transition paths in macromolecules-applications to hemoglobin and phosphoglycerate kinase Comput. Phys. Comm. 91 1995 263 273
    • (1995) Comput. Phys. Comm. , vol.91 , pp. 263-273
    • Guilbert, C.1    Perahia, D.2    Mouawad, L.A.3
  • 32
    • 0037086450 scopus 로고    scopus 로고
    • Structure-based analysis of RNA polymerase function: The largest subunit's rudder contributes critically to elongation complex stability and is not involved in the maintenance of RNA-DNA hybrid length
    • K. Kuznedelov, N. Korzheva, A. Mustaev, and K. Severinov Structure-based analysis of RNA polymerase function: the largest subunit's rudder contributes critically to elongation complex stability and is not involved in the maintenance of RNA-DNA hybrid length EMBO J. 21 2002 1369 1378
    • (2002) EMBO J. , vol.21 , pp. 1369-1378
    • Kuznedelov, K.1    Korzheva, N.2    Mustaev, A.3    Severinov, K.4
  • 35
    • 0031552174 scopus 로고    scopus 로고
    • The DNA-RNA hybrid maintains the register of transcription by preventing backtracking of RNA polymerase
    • E. Nudler, A. Mustaev, E. Lukhtanov, and A. Goldfarb The DNA-RNA hybrid maintains the register of transcription by preventing backtracking of RNA polymerase Cell 89 1997 33 41
    • (1997) Cell , vol.89 , pp. 33-41
    • Nudler, E.1    Mustaev, A.2    Lukhtanov, E.3    Goldfarb, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.