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Volumn 74, Issue 3, 1998, Pages 1186-1202

Force generation in RNA polymerase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PYROPHOSPHATE; RNA POLYMERASE;

EID: 0031934004     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77834-8     Document Type: Article
Times cited : (111)

References (28)
  • 1
    • 0027365641 scopus 로고
    • Torque generated by the flagellar motor of Escherichia coli
    • Berg, H. C., and L. Turner. 1993. Torque generated by the flagellar motor of Escherichia coli. Biophys. J. 65:2201-2216.
    • (1993) Biophys. J. , vol.65 , pp. 2201-2216
    • Berg, H.C.1    Turner, L.2
  • 2
    • 0013881083 scopus 로고
    • Adenylate oligomers in single- And double-strand conformation
    • Brahms, J., A. M. Michelson, and K. E. van Holde. 1966. Adenylate oligomers in single-and double-strand conformation. J. Mol. Biol. 15-467-488.
    • (1966) J. Mol. Biol. , vol.15 , pp. 467-488
    • Brahms, J.1    Michelson, A.M.2    Van Holde, K.E.3
  • 3
    • 0027106595 scopus 로고
    • New models for the mechanism of transcription elongation and its regulation
    • Chamberlin, M. J. 1994. New models for the mechanism of transcription elongation and its regulation. Harvey Lect. 88:1-21.
    • (1994) Harvey Lect. , vol.88 , pp. 1-21
    • Chamberlin, M.J.1
  • 4
    • 0026728955 scopus 로고
    • The single-nucleotide addition cycle in transcription: A biophysical and biochemical perspective
    • Erie, D. A., T. D. Yager, and P. von Hippel. 1992. The single-nucleotide addition cycle in transcription: a biophysical and biochemical perspective. Annu. Rev. Biophys. Biomol. Struct. 21:379-415.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 379-415
    • Erie, D.A.1    Yager, T.D.2    Von Hippel, P.3
  • 5
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometre steps
    • Finer, J. T., R. M. Simmons, and J. A. Spudich. 1994. Single myosin molecule mechanics: piconewton forces and nanometre steps. Nature. 368:113-119.
    • (1994) Nature , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 6
    • 0347193736 scopus 로고
    • Reaction-rate theory: 50 Years after Kramers
    • Hanggi, P., P. Talkner, and M. Borkovec. 1990. Reaction-rate theory: 50 years after Kramers. Rev. Mod. Phys. 62:254-341.
    • (1990) Rev. Mod. Phys. , vol.62 , pp. 254-341
    • Hanggi, P.1    Talkner, P.2    Borkovec, M.3
  • 7
    • 0017670597 scopus 로고
    • Biochemical cycles and free energy transduction
    • Hill, T. L. 1977. Biochemical cycles and free energy transduction. Trends Biochem. Sci. 2:204-207.
    • (1977) Trends Biochem. Sci. , vol.2 , pp. 204-207
    • Hill, T.L.1
  • 9
    • 0028145209 scopus 로고
    • The force exerted by a single kinesin molecule against a viscous load
    • Hunt, A. J., F. Gittes, and J. Howard. 1994. The force exerted by a single kinesin molecule against a viscous load. Biophys. J. 67:766-781.
    • (1994) Biophys. J. , vol.67 , pp. 766-781
    • Hunt, A.J.1    Gittes, F.2    Howard, J.3
  • 10
    • 0014198528 scopus 로고
    • Deoxynucleotide-polymerizing enzymes of calf thymus gland. II. Properties of the terminal deoxynucleotidyltransferase
    • Kato, K., J. M. Goncalves, G. E. Houts, and F. J. Bollum. 1967. Deoxynucleotide-polymerizing enzymes of calf thymus gland. II. Properties of the terminal deoxynucleotidyltransferase. J. Biol. Chem. 242: 2780-2789.
    • (1967) J. Biol. Chem. , vol.242 , pp. 2780-2789
    • Kato, K.1    Goncalves, J.M.2    Houts, G.E.3    Bollum, F.J.4
  • 11
    • 0026766857 scopus 로고
    • Structural analysis of ternary complexes of Escherichia coli RNA polymerase. Deoxyribonuclease I footprinting of defined complexes
    • Krummel, B., and M. J. Chamberlin. 1992. Structural analysis of ternary complexes of Escherichia coli RNA polymerase. Deoxyribonuclease I footprinting of defined complexes. J. Mol. Biol. 225:239-250.
    • (1992) J. Mol. Biol. , vol.225 , pp. 239-250
    • Krummel, B.1    Chamberlin, M.J.2
  • 12
    • 0030969278 scopus 로고    scopus 로고
    • RNA polymerase slides home: Pause and termination site recognition
    • Landick, R. 1997. RNA polymerase slides home: pause and termination site recognition. Cell 88:741-744.
    • (1997) Cell , vol.88 , pp. 741-744
    • Landick, R.1
  • 13
    • 0029775654 scopus 로고    scopus 로고
    • Cell motility driven by actin polymerization
    • Mogilner, A., and G. Oster. 1996. Cell motility driven by actin polymerization. Biophys. J. 71:3030-3045.
    • (1996) Biophys. J. , vol.71 , pp. 3030-3045
    • Mogilner, A.1    Oster, G.2
  • 15
    • 0031552174 scopus 로고    scopus 로고
    • The RNA-DNA hybrid maintains the register of transcription by preventing back-tracking of RNA polymerase
    • Nudler, E., A. Mustaev, E. Lukhtanov, and A. Goldfarb. 1997. The RNA-DNA hybrid maintains the register of transcription by preventing back-tracking of RNA polymerase. Cell. 89:33-41.
    • (1997) Cell , vol.89 , pp. 33-41
    • Nudler, E.1    Mustaev, A.2    Lukhtanov, E.3    Goldfarb, A.4
  • 16
    • 0017225974 scopus 로고
    • On the free-energy changes in the synthesis and degradation of nucleic acids
    • Peller, L. 1976. On the free-energy changes in the synthesis and degradation of nucleic acids. Biochemistry. 15:141-146.
    • (1976) Biochemistry , vol.15 , pp. 141-146
    • Peller, L.1
  • 17
    • 0026057680 scopus 로고
    • 1-type ATP synthases and ATPases
    • A. Meister, editor. John Wiley and Sons, New York
    • 1-type ATP synthases and ATPases. In Advances In Enzymology. A. Meister, editor. John Wiley and Sons, New York. 173-214.
    • (1991) Advances in Enzymology , pp. 173-214
    • Penefsky, H.S.1
  • 18
    • 0027194759 scopus 로고
    • Cellular motions and thermal fluctuations: The Brownian ratchet
    • Peskin, C. S., G. M. Odell, and G. Oster. 1993. Cellular motions and thermal fluctuations: the Brownian ratchet. Biophys. J. 65:316-324.
    • (1993) Biophys. J. , vol.65 , pp. 316-324
    • Peskin, C.S.1    Odell, G.M.2    Oster, G.3
  • 19
    • 0028952024 scopus 로고
    • Coordinated hydrolysis explains the mechanical behavior of kinesin
    • Peskin, C. S., and G. Oster. 1995. Coordinated hydrolysis explains the mechanical behavior of kinesin. Biophys. J. 68:202s-210s.
    • (1995) Biophys. J. , vol.68
    • Peskin, C.S.1    Oster, G.2
  • 20
    • 0028875725 scopus 로고
    • Three-dimensional structure of E. coli core RNA polymerase: Promoter binding and elongation conformations of the enzyme
    • Polyakov, A., E. Severinova, and S. A. Darst. 1995. Three-dimensional structure of E. coli core RNA polymerase: promoter binding and elongation conformations of the enzyme. Cell. 83:365-373.
    • (1995) Cell , vol.83 , pp. 365-373
    • Polyakov, A.1    Severinova, E.2    Darst, S.A.3
  • 23
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyses one ATP per 8-nm step
    • Schnitzer, M. J., and S. M. Block. 1997. Kinesin hydrolyses one ATP per 8-nm step. Nature. 388:386-390.
    • (1997) Nature , vol.388 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 24
    • 0028362896 scopus 로고
    • Force and velocity measured for single kinesin molecules
    • Svoboda, K., and S. M. Block. 1994. Force and velocity measured for single kinesin molecules. Cell. 77:773-784.
    • (1994) Cell , vol.77 , pp. 773-784
    • Svoboda, K.1    Block, S.M.2
  • 25
    • 0028113846 scopus 로고
    • Fluctuation analysis of motor protein movement and single enzyme kinetics
    • Svoboda, K., P. P. Mitra, and S. M. Block. 1994. Fluctuation analysis of motor protein movement and single enzyme kinetics. Proc. Natl. Acad. Sci. USA. 91:11782-11786.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11782-11786
    • Svoboda, K.1    Mitra, P.P.2    Block, S.M.3
  • 26
    • 0031588861 scopus 로고    scopus 로고
    • Catalytic mechanism of F1-ATPase
    • Weber, J., and A. E. Senior. 1997. Catalytic mechanism of F1-ATPase. Biochim. Biophys. Acta. 1319:19-58.
    • (1997) Biochim. Biophys. Acta , vol.1319 , pp. 19-58
    • Weber, J.1    Senior, A.E.2
  • 27
    • 0001323636 scopus 로고
    • Transcript elongation and termination in Escherichia coli
    • F. Neidhardt, editor. American Society for Microbiology, Washington, DC
    • Yager, T. D., and P. von Hippel. 1987. Transcript elongation and termination in Escherichia coli. In Escherichia coli and Salmonella typhimurium. F. Neidhardt, editor. American Society for Microbiology, Washington, DC. 1241-1275.
    • (1987) Escherichia Coli and Salmonella Typhimurium , pp. 1241-1275
    • Yager, T.D.1    Von Hippel, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.