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Volumn 3, Issue 1, 2002, Pages 50-60

Stress, order and survival

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; DNA BINDING PROTEIN; VIRUS DNA;

EID: 0036358511     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm700     Document Type: Review
Times cited : (110)

References (75)
  • 1
    • 0035826198 scopus 로고    scopus 로고
    • Noise to order
    • Shinbrot, T. & Muzzio, F. J. Noise to order. Nature 410, 251-258 (2001).
    • (2001) Nature , vol.410 , pp. 251-258
    • Shinbrot, T.1    Muzzio, F.J.2
  • 3
    • 0034614357 scopus 로고    scopus 로고
    • Molecular 'vitalism'
    • Kirschner, M., Gerhart, J. & Mitchison, T. Molecular 'vitalism'. Cell 100, 79-88 (2000). A highly instructive review on the essence of molecular machines and self-organization in living systems, in which the fundamental difference between such cellular machines and man-made devices is discussed.
    • (2000) Cell , vol.100 , pp. 79-88
    • Kirschner, M.1    Gerhart, J.2    Mitchison, T.3
  • 4
    • 0026501223 scopus 로고
    • Unscrambling the puzzle of biological machines: The importance of the details
    • Alberts, B. & Miake-Lye, R. Unscrambling the puzzle of biological machines: the importance of the details. Cell 68, 415-420 (1992). This summary highlights the idea that the accuracy, efficiency and directionality of molecular machines derive from coupling the energy of nucleotide hydrolysis to conformational changes that occur in subunits of these machines.
    • (1992) Cell , vol.68 , pp. 415-420
    • Alberts, B.1    Miake-Lye, R.2
  • 5
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts, B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 92, 291-294 (1998).
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 6
    • 0032982866 scopus 로고    scopus 로고
    • EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome
    • Agrawal, R. K., Heagle, A. B., Penczek, P., Grassucci, R. A. & Frank, J. EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome. Nature Struct. Biol. 6, 643-647 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 643-647
    • Agrawal, R.K.1    Heagle, A.B.2    Penczek, P.3    Grassucci, R.A.4    Frank, J.5
  • 7
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Vodges, D., Zwickl, P. & Baumeister, W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68, 1015-1068 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Vodges, D.1    Zwickl, P.2    Baumeister, W.3
  • 8
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J. E. & Wieland, F. T. Protein sorting by transport vesicles. Science 272, 227-234 (1996).
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 10
    • 0026555506 scopus 로고
    • Control of bacterial DNA supercoiling
    • Drlica, K. Control of bacterial DNA supercoiling. Mol. Microbiol. 6, 425-433 (1992).
    • (1992) Mol. Microbiol. , vol.6 , pp. 425-433
    • Drlica, K.1
  • 11
    • 0001175140 scopus 로고    scopus 로고
    • Morphological and physiological changes during stationary phase
    • eds Neidhardt, F. C. et al. ASM Press, Washington DC
    • Huisman, G. W, Siegele, D. A., Zambrano, M. M. & Kolter, R. Morphological and physiological changes during stationary phase. In Escherichia coli and Salmonella, Cellular and Molecular Biology (eds Neidhardt, F. C. et al.) 1672-1682 (ASM Press, Washington DC, 1996). A comprehensive review on the biochemical changes that occur in stationary-state bacteria, and the effects of such changes on bacterial stress resistance.
    • (1996) Escherichia Coli and Salmonella, Cellular and Molecular Biology , pp. 1672-1682
    • Huisman, G.W.1    Siegele, D.A.2    Zambrano, M.M.3    Kolter, R.4
  • 12
    • 0030035132 scopus 로고    scopus 로고
    • Bacterial defense against aging: Role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis
    • Nyström, T., Larsson, C. & Gustafsson, L. Bacterial defense against aging: role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis. EMBO J. 15, 3219-3228 (1996).
    • (1996) EMBO J. , vol.15 , pp. 3219-3228
    • Nyström, T.1    Larsson, C.2    Gustafsson, L.3
  • 13
    • 0001633637 scopus 로고    scopus 로고
    • Environmental regulation of virulence gene expression in Escherichia, Salmonella and Shigella spp.
    • Neidhardt, F. C. et al. eds. ASM Press, Washington DC
    • Mahan, M. J., Slauch, J. M. & Mekalanos, J. J. Environmental regulation of virulence gene expression in Escherichia, Salmonella and Shigella spp. In Escherichia coli and Salmonella, Cellular and Molecular Biology (Neidhardt, F. C. et al. eds.) 2803-2815 (ASM Press, Washington DC, 1996).
    • (1996) Escherichia Coli and Salmonella, Cellular and Molecular Biology , pp. 2803-2815
    • Mahan, M.J.1    Slauch, J.M.2    Mekalanos, J.J.3
  • 14
    • 0035283138 scopus 로고    scopus 로고
    • Regulated phase transitions of bacterial chromatin: A non-enzymatic pathway for generic DNA protection
    • Frenkiel-Krispin, D. et al. Regulated phase transitions of bacterial chromatin: a non-enzymatic pathway for generic DNA protection. EMBO J. 20, 1184-1191 (2001). Electron-microscopic and X-ray-diffraction studies show that chromatin in starved bacteria adopts ordered structures that allow for DNA protection by physical sequestration.
    • (2001) EMBO J. , vol.20 , pp. 1184-1191
    • Frenkiel-Krispin, D.1
  • 15
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almiron, M., Link, A. J., Furlong, D. & Kolter, R. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev. 6, 2646-2654 (1992).
    • (1992) Genes Dev. , vol.6 , pp. 2646-2654
    • Almiron, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 16
    • 0028200484 scopus 로고
    • The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase
    • Altuvia, S., Almiron, M., Huisman, G., Kolter, R. & Storz, G. The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase. Mol. Microbiol. 13, 265-272 (1994).
    • (1994) Mol. Microbiol. , vol.13 , pp. 265-272
    • Altuvia, S.1    Almiron, M.2    Huisman, G.3    Kolter, R.4    Storz, G.5
  • 17
    • 0033168858 scopus 로고    scopus 로고
    • DNA protection by stress-induced biocrystallization
    • Wolf, S. G. et al. DNA protection by stress-induced biocrystallization. Nature 400, 83-85 (1999).
    • (1999) Nature , vol.400 , pp. 83-85
    • Wolf, S.G.1
  • 18
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • Grant, R. A., Filman, D. J., Finkel, S. E., Kolter, R. & Hogle, J. M. The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nature Struct. Biol. 5, 294-303 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 294-303
    • Grant, R.A.1    Filman, D.J.2    Finkel, S.E.3    Kolter, R.4    Hogle, J.M.5
  • 19
    • 0034013295 scopus 로고    scopus 로고
    • Phagosome dynamics and function
    • Tjelle, T. E., Lovdal, T. & Berg, T. Phagosome dynamics and function. BioEssays 22, 255-263 (2000).
    • (2000) BioEssays , vol.22 , pp. 255-263
    • Tjelle, T.E.1    Lovdal, T.2    Berg, T.3
  • 20
    • 0029671310 scopus 로고    scopus 로고
    • 2+ as an extracellular signal: Environmental regulation of Salmonella virulence
    • 2+ as an extracellular signal: environmental regulation of Salmonella virulence. Cell 84, 165-174 (1996).
    • (1996) Cell , vol.84 , pp. 165-174
    • Vescovi, E.G.1    Soncini, F.C.2    Groisman, E.A.3
  • 21
    • 44949277387 scopus 로고
    • Ordered phases of DNA in vivo and in vitro
    • Livolant, F. Ordered phases of DNA in vivo and in vitro. Physica A 176, 117-137 (1991).
    • (1991) Physica A , vol.176 , pp. 117-137
    • Livolant, F.1
  • 22
    • 0027226299 scopus 로고
    • Supramolecular ordering of DNA in the cholesteric liquid crystalline phase: An ultrastructural study
    • Leforestier, A. & Livolant, F. Supramolecular ordering of DNA in the cholesteric liquid crystalline phase: an ultrastructural study. Biophys. J. 65, 56-72 (1993).
    • (1993) Biophys. J. , vol.65 , pp. 56-72
    • Leforestier, A.1    Livolant, F.2
  • 23
    • 0028363139 scopus 로고
    • Liquid-crystalline mesophases of plasmid DNA in bacteria
    • Reich, Z., Wachtel, E. J. & Minsky, A. Liquid-crystalline mesophases of plasmid DNA in bacteria. Science 264, 1460-1463 (1994).
    • (1994) Science , vol.264 , pp. 1460-1463
    • Reich, Z.1    Wachtel, E.J.2    Minsky, A.3
  • 24
    • 0030395810 scopus 로고    scopus 로고
    • Condensed phases of DNA: Structure and phase transitions
    • Livolant, F. & Leforestier, A. Condensed phases of DNA: structure and phase transitions. Prog. Polym. Sci. 21, 1115-1164 (1996). Inclusive survey of the properties of various liquid-crystalline DNA phases and the factors that affect their formation.
    • (1996) Prog. Polym. Sci. , vol.21 , pp. 1115-1164
    • Livolant, F.1    Leforestier, A.2
  • 25
    • 0029093284 scopus 로고
    • Structure and partitioning of bacterial DNA: Determined by a balance of compaction and expansion forces?
    • Woldringh, C. L., Jensen, P. R. & Westerhoff, H. V. Structure and partitioning of bacterial DNA: determined by a balance of compaction and expansion forces? FEMS Microbiol. Lett. 131, 235-242 (1995). The morphology of bacterial chromatin is proposed to reflect an interplay between expansion forces, which are derived from ongoing DNA transactions, and compaction forces, which emanate from crowding, DNA-packaging proteins and supercoiling.
    • (1995) FEMS Microbiol. Lett. , vol.131 , pp. 235-242
    • Woldringh, C.L.1    Jensen, P.R.2    Westerhoff, H.V.3
  • 26
    • 0031558565 scopus 로고    scopus 로고
    • Nucleosomes: A solution to a crowded intracellular environment?
    • Minsky, A., Ghirlando, R. & Reich, Z. Nucleosomes: a solution to a crowded intracellular environment? J. Theor. Biol. 188, 379-385 (1997).
    • (1997) J. Theor. Biol. , vol.188 , pp. 379-385
    • Minsky, A.1    Ghirlando, R.2    Reich, Z.3
  • 27
    • 0033021173 scopus 로고    scopus 로고
    • Modulation of the nucleoid, the transcription apparatus, and the translation machinery in bacteria for stationary phase survival
    • Ishihama, A. Modulation of the nucleoid, the transcription apparatus, and the translation machinery in bacteria for stationary phase survival. Genes Cells 4, 135-143 (1999).
    • (1999) Genes Cells , vol.4 , pp. 135-143
    • Ishihama, A.1
  • 28
    • 0000747364 scopus 로고
    • Ordered DNA-polypeptide complexes of extreme chirality: Effects of polypeptide handedness on DNA long-range asymmetry
    • Weinberger, S., Berman, C. & Minsky, A. Ordered DNA-polypeptide complexes of extreme chirality: effects of polypeptide handedness on DNA long-range asymmetry. J. Am. Chem. Soc. 110, 8231-8232 (1988).
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8231-8232
    • Weinberger, S.1    Berman, C.2    Minsky, A.3
  • 30
    • 0029980119 scopus 로고    scopus 로고
    • Polyamine-induced compaction and aggregation of DNA - A major factor in radioprotection of chromatin under physiological conditions
    • Newton, G. L., Aguilera, J. A., Ward, J. F. & Fahey, R. C. Polyamine-induced compaction and aggregation of DNA - a major factor in radioprotection of chromatin under physiological conditions. Radiat. Res. 145, 776-780 (1996).
    • (1996) Radiat. Res. , vol.145 , pp. 776-780
    • Newton, G.L.1    Aguilera, J.A.2    Ward, J.F.3    Fahey, R.C.4
  • 31
  • 32
    • 0028868465 scopus 로고
    • Mechanisms for the prevention of damage to DNA in spores of Bacillus species
    • Setlow, P. Mechanisms for the prevention of damage to DNA in spores of Bacillus species. Annu. Rev. Microbiol. 49, 29-54 (1995). A thorough account of the factors that promote the survival and stress resistance of bacterial spores.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 29-54
    • Setlow, P.1
  • 33
    • 0027990219 scopus 로고
    • Electron microscopic studies of the interaction between a Bacillus subtilis α/β-type small, acid-soluble spore protein with DNA: Protein binding is cooperative, stiffens the DNA, and induces negative supercoiling
    • Griffith, J., Makhov, A., Santiago-Lara, L. & Setlow, P. Electron microscopic studies of the interaction between a Bacillus subtilis α/β-type small, acid-soluble spore protein with DNA: protein binding is cooperative, stiffens the DNA, and induces negative supercoiling. Proc. Natl Acad. Sci. USA 91, 8224-8228 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8224-8228
    • Griffith, J.1    Makhov, A.2    Santiago-Lara, L.3    Setlow, P.4
  • 34
    • 0026090060 scopus 로고
    • Synthesis of a Bacillus subtilis small acid-soluble spore protein in Escherichia coli causes cell DNA to assume some characteristics of spore DNA
    • Setlow, B., Hand, A. R. & Setlow, P. Synthesis of a Bacillus subtilis small acid-soluble spore protein in Escherichia coli causes cell DNA to assume some characteristics of spore DNA. J. Bacteriol. 173, 1642-1653 (1991).
    • (1991) J. Bacteriol. , vol.173 , pp. 1642-1653
    • Setlow, B.1    Hand, A.R.2    Setlow, P.3
  • 35
    • 0034687374 scopus 로고    scopus 로고
    • Isolation of a 250 million-year-old halotolerant bacterium from a primary salt crystal
    • Wreeland, R. H., Rosenzweig, W. D. & Powers, D. W. Isolation of a 250 million-year-old halotolerant bacterium from a primary salt crystal. Nature 407, 897-900 (2000). A fascinating study of the extreme durability of bacterial spores.
    • (2000) Nature , vol.407 , pp. 897-900
    • Wreeland, R.H.1    Rosenzweig, W.D.2    Powers, D.W.3
  • 36
    • 0022439116 scopus 로고
    • The molecular biology of parasporal crystal body formation in Bacillus thuringiensis
    • Whiteley, H. R. & Schnepf, H. E. The molecular biology of parasporal crystal body formation in Bacillus thuringiensis. Annu. Rev. Microbiol. 40, 549-576 (1986).
    • (1986) Annu. Rev. Microbiol. , vol.40 , pp. 549-576
    • Whiteley, H.R.1    Schnepf, H.E.2
  • 37
    • 0027471465 scopus 로고
    • Evidence that the Cry1A crystal protein from Bacillus thuringiensis is associated with DNA
    • Bietlot, H. P. et al. Evidence that the Cry1A crystal protein from Bacillus thuringiensis is associated with DNA. J. Biol. Chem. 268, 8240-8245 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 8240-8245
    • Bietlot, H.P.1
  • 38
    • 0032502741 scopus 로고    scopus 로고
    • Role of DNA in the activation of the Cry1A insecticidal crystal protein from Bacillus thuringiensis
    • Clairmont, F. R., Milne, R. E., Pham, V. T., Carriere, M. B. & Kaplan, H. Role of DNA in the activation of the Cry1A insecticidal crystal protein from Bacillus thuringiensis. J. Biol. Chem. 273, 9292-9296 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 9292-9296
    • Clairmont, F.R.1    Milne, R.E.2    Pham, V.T.3    Carriere, M.B.4    Kaplan, H.5
  • 39
    • 0025630474 scopus 로고
    • The RecA protein: Structure and function
    • Roca, A. I. & Cox, M. M. The RecA protein: structure and function. Crit. Rev. Biochem. Mol. Biol. 25, 415-456 (1990).
    • (1990) Crit. Rev. Biochem. Mol. Biol. , vol.25 , pp. 415-456
    • Roca, A.I.1    Cox, M.M.2
  • 40
    • 0025891414 scopus 로고
    • Biochemistry of genetic recombination: Energetics and mechanism of DNA strand exchange
    • Kowalczykowski, S. C. Biochemistry of genetic recombination: energetics and mechanism of DNA strand exchange. Annu. Rev. Biophys. Biophys. Chem. 20, 539-575 (1991).
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 539-575
    • Kowalczykowski, S.C.1
  • 41
    • 0026633047 scopus 로고
    • ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of e coli
    • Tsaneva, I. R., Müller, B. & West, S. C. ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E coli. Cell 69, 1171-1180 (1992).
    • (1992) Cell , vol.69 , pp. 1171-1180
    • Tsaneva, I.R.1    Müller, B.2    West, S.C.3
  • 42
    • 0034612347 scopus 로고    scopus 로고
    • Ordered intracellular RecA-DNA assemblies: A potential site of in vivo RecA-mediated activities
    • Levin-Zaidman, S. et al. Ordered intracellular RecA-DNA assemblies: a potential site of in vivo RecA-mediated activities. Proc. Natl Acad. Sci. USA 97, 6791-6796 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6791-6796
    • Levin-Zaidman, S.1
  • 43
    • 0035902544 scopus 로고    scopus 로고
    • Rad52 forms DNA repair and recombination centers during S phase
    • Lisby, M., Rothstein, R. & Mortensen, U. H. Rad52 forms DNA repair and recombination centers during S phase. Proc. Natl Acad. Sci. USA 98, 8276-8282 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8276-8282
    • Lisby, M.1    Rothstein, R.2    Mortensen, U.H.3
  • 44
    • 0027462566 scopus 로고
    • Paracrystalline inclusions of a novel ferritin containing nonheme iron, produced by the human gastric pathogen Helicobacter pylori: Evidence for a third class of ferritins
    • Frazier, B. A. et al. Paracrystalline inclusions of a novel ferritin containing nonheme iron, produced by the human gastric pathogen Helicobacter pylori: evidence for a third class of ferritins. J. Bacteriol. 175, 966-972 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 966-972
    • Frazier, B.A.1
  • 45
    • 0013509662 scopus 로고    scopus 로고
    • Overproduction of Campylobacter ferritin in E. coli and induction of paracrystalline inclusion by ferrous compound
    • Wai, S. N., Nakayama, K., Takade, A. & Amako, K. Overproduction of Campylobacter ferritin in E. coli and induction of paracrystalline inclusion by ferrous compound. Microbiol. Immunol. 41, 461-467 (1997).
    • (1997) Microbiol. Immunol. , vol.41 , pp. 461-467
    • Wai, S.N.1    Nakayama, K.2    Takade, A.3    Amako, K.4
  • 46
    • 0000013061 scopus 로고
    • Paracrystalline protein surface arrays on bacteria
    • Koval, S. F. Paracrystalline protein surface arrays on bacteria. Can. J. Microbiol. 34, 407-414 (1988).
    • (1988) Can. J. Microbiol. , vol.34 , pp. 407-414
    • Koval, S.F.1
  • 47
    • 0033152613 scopus 로고    scopus 로고
    • Bacterial S-layers
    • Sleytr, U. B. & Beveridge, T. J. Bacterial S-layers. Trends Microbiol. 7, 253-260 (1999). A comprehensive account of the structure, properties and potential functions of the surface layer in bacteria and archaea.
    • (1999) Trends Microbiol. , vol.7 , pp. 253-260
    • Sleytr, U.B.1    Beveridge, T.J.2
  • 48
    • 0000568172 scopus 로고
    • Pf1 filamenteous bacteriophage: Refinement of a molecular model by stimulated annealing using 3.3 Å resolution X-ray fibre diffraction data
    • Gonzales, A., Nave, C. & Marvin, D. A. Pf1 filamenteous bacteriophage: refinement of a molecular model by stimulated annealing using 3.3 Å resolution X-ray fibre diffraction data. Acta Crystallogr. D [AU: Biol Crystallogr.?] 51, 792-804 (1995).
    • (1995) Acta Crystallogr. D [AU: Biol Crystallogr.?] , vol.51 , pp. 792-804
    • Gonzales, A.1    Nave, C.2    Marvin, D.A.3
  • 49
    • 0032054113 scopus 로고    scopus 로고
    • Filamentous phage structure, infection and assembly
    • Marvin, D. A. Filamentous phage structure, infection and assembly. Curr. Opin. Struct. Biol. 8, 150-158 (1998).
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 150-158
    • Marvin, D.A.1
  • 50
    • 0032189765 scopus 로고    scopus 로고
    • The atomic structure of the bluetongue virus core
    • Grimes, J. M. et al. The atomic structure of the bluetongue virus core. Nature 295, 470-478 (1998).
    • (1998) Nature , vol.295 , pp. 470-478
    • Grimes, J.M.1
  • 51
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • Wynne, S. A., Crowther, R. A. & Leslie, A. G. W. The crystal structure of the human hepatitis B virus capsid. Mol. Cell 3, 771-780 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.W.3
  • 52
    • 0033854594 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki forest virus
    • Mancini, E. J., Clarke, M., Gowen, B., Rutten, T. & Fuller, S. D. Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki forest virus. Mol. Cell 5, 255-266 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 255-266
    • Mancini, E.J.1    Clarke, M.2    Gowen, B.3    Rutten, T.4    Fuller, S.D.5
  • 53
    • 0034608018 scopus 로고    scopus 로고
    • Seeing the herpesvirus capsid at 8.5 Å
    • Zhou, Z. H. et al. Seeing the herpesvirus capsid at 8.5 Å Science 288, 877-880 (2000).
    • (2000) Science , vol.288 , pp. 877-880
    • Zhou, Z.H.1
  • 54
    • 0034036079 scopus 로고    scopus 로고
    • Structures of virus and virus-like particles
    • Johnson, J. E. & Chiu, W. Structures of virus and virus-like particles. Curr. Opin. Struct. Biol. 10, 229-235 (2000).
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 229-235
    • Johnson, J.E.1    Chiu, W.2
  • 55
    • 0026073819 scopus 로고
    • Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus
    • Booy, F. P. et al. Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus. Cell 64, 1007-1015 (1991).
    • (1991) Cell , vol.64 , pp. 1007-1015
    • Booy, F.P.1
  • 56
    • 0030669286 scopus 로고    scopus 로고
    • Encapsidated conformation of bacteriophage T7 DNA
    • Cerritelli, M. E. et al. Encapsidated conformation of bacteriophage T7 DNA. Cell 91, 271-280 (1997). Cryo-electron microscopy studies of DNA packaging in herpes simplex virus, which shows that it is organized in highly ordered quasi-crystalline concentric rings.
    • (1997) Cell , vol.91 , pp. 271-280
    • Cerritelli, M.E.1
  • 57
    • 0033553535 scopus 로고    scopus 로고
    • The highly ordered double-stranded RNA genome of Bluetongue virus revealed by crystallography
    • Gouet, P. et al. The highly ordered double-stranded RNA genome of Bluetongue virus revealed by crystallography. Cell 97, 481-490 (1999). The remarkable liquid-crystalline order of RNA molecules in the bluetongue virus is shown by X-ray crystallography.
    • (1999) Cell , vol.97 , pp. 481-490
    • Gouet, P.1
  • 59
    • 0034335312 scopus 로고    scopus 로고
    • Effects of UV irradiation on skin and nonskin-associated herpes simplex virus infections in rats
    • Garssen, J., van der Molen, R., de Klerk, A., Norval, M. & van Loveren, H. Effects of UV irradiation on skin and nonskin-associated herpes simplex virus infections in rats. Photochem. Photobiol. 72, 645-651 (2000).
    • (2000) Photochem. Photobiol. , vol.72 , pp. 645-651
    • Garssen, J.1    Van Der Molen, R.2    De Klerk, A.3    Norval, M.4    Van Loveren, H.5
  • 60
    • 0032778876 scopus 로고    scopus 로고
    • Heat stress activates production of herpes simplex virus from quiescently infected neurally differentiated PC12 cells
    • Danaher, R. J., Jacob, R. J., Chorak, M. D., Freeman, C. S. & Miller, C. S. Heat stress activates production of herpes simplex virus from quiescently infected neurally differentiated PC12 cells. J. Neurovirol. 5, 374-383 (1999).
    • (1999) J. Neurovirol. , vol.5 , pp. 374-383
    • Danaher, R.J.1    Jacob, R.J.2    Chorak, M.D.3    Freeman, C.S.4    Miller, C.S.5
  • 62
    • 0034599157 scopus 로고    scopus 로고
    • Induction of vaginal lactobacillus phage by the cigarette smoke chemical benzo[a]pyrene diol epoxide
    • Pavlova, S. I. & Tao, L. Induction of vaginal lactobacillus phage by the cigarette smoke chemical benzo[a]pyrene diol epoxide. Mutat. Res. 466, 57-62 (2000).
    • (2000) Mutat. Res. , vol.466 , pp. 57-62
    • Pavlova, S.I.1    Tao, L.2
  • 63
    • 0033914615 scopus 로고    scopus 로고
    • Sunlight-induced propagation of the lysogenic phage encoding cholera toxin
    • Faruque, S. M., Rahman, M. M., Waldor, M. K. & Sack, D. A. Sunlight-induced propagation of the lysogenic phage encoding cholera toxin. Infect. Immun. 68, 4795-4801 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 4795-4801
    • Faruque, S.M.1    Rahman, M.M.2    Waldor, M.K.3    Sack, D.A.4
  • 64
    • 0033804328 scopus 로고    scopus 로고
    • Frequency of hepatitis B virus reactivation in cancer patients undergoing cytotoxic chemotherapy: A prospective study of 626 patients with identification of risk factors
    • Yeo, W. et al. Frequency of hepatitis B virus reactivation in cancer patients undergoing cytotoxic chemotherapy: a prospective study of 626 patients with identification of risk factors. J. Med. Virol. 62, 299-307 (2000).
    • (2000) J. Med. Virol. , vol.62 , pp. 299-307
    • Yeo, W.1
  • 65
    • 0032514949 scopus 로고    scopus 로고
    • An evolutionary link between sporulation and prophage induction in the structure of a repressonanti-repressor complex
    • Lewis, R. J., Brannigan, J. A., Offen, W. A., Smith, I. & Wilkinson, A. J. An evolutionary link between sporulation and prophage induction in the structure of a repressonanti-repressor complex. J. Mol. Biol. 283, 907-912 (1998). In this study, the intriguing possibility that sporulation and phage induction are evolutionarily linked is proposed on the basis of the structural homology between DNA-binding motifs in SinR - a repressor of genes, which is required for sporulation - and in the protein Cro, which represses phage induction.
    • (1998) J. Mol. Biol. , vol.283 , pp. 907-912
    • Lewis, R.J.1    Brannigan, J.A.2    Offen, W.A.3    Smith, I.4    Wilkinson, A.J.5
  • 66
    • 0032881809 scopus 로고    scopus 로고
    • X-ray crystal structure of 70S ribosome functional complexes
    • Cate, J. H., Yusupov, M. M., Yusupova, G. Z., Earnest, T. N. & Noller, H. F. X-ray crystal structure of 70S ribosome functional complexes. Science 285, 2095-2104 (1999).
    • (1999) Science , vol.285 , pp. 2095-2104
    • Cate, J.H.1    Yusupov, M.M.2    Yusupova, G.Z.3    Earnest, T.N.4    Noller, H.F.5
  • 67
    • 0034268836 scopus 로고    scopus 로고
    • Structure of functionally activated small ribosomal subunit at 3.3 Å resolution
    • Schluenzen. F. et al. Structure of functionally activated small ribosomal subunit at 3.3 Å resolution. Cell 102, 615-623 (2000).
    • (2000) Cell , vol.102 , pp. 615-623
    • Schluenzen, F.1
  • 68
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P. B. & Steitz, T. A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289, 905-920 (2000).
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 69
    • 0034699518 scopus 로고    scopus 로고
    • Structure of the 303 ribosomal subunit
    • Wimberly, B. T. et al. Structure of the 303 ribosomal subunit. Nature 407, 327-339 (2000).
    • (2000) Nature , vol.407 , pp. 327-339
    • Wimberly, B.T.1
  • 71
    • 0347571364 scopus 로고
    • Three-dimensional crystals of ribosomal particle
    • Yonath, A. Three-dimensional crystals of ribosomal particle. Trends Biochem. Sci. 9, 227-230 (1984).
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 227-230
    • Yonath, A.1
  • 72
    • 0029278705 scopus 로고
    • Cell stress and ribosome crystallization
    • Barbieri, M., Vittone, A. & Maraldi, N. M. Cell stress and ribosome crystallization. J. Submicrosc. Cytol. Pathot. 27, 199-207 (1995). An account of the various conditions that result in ribosome crystallization in living systems, which underlies the idea that such crystallization is stress-related.
    • (1995) J. Submicrosc. Cytol. Pathot. , vol.27 , pp. 199-207
    • Barbieri, M.1    Vittone, A.2    Maraldi, N.M.3
  • 74
    • 0004146634 scopus 로고
    • Cambridge Univ. Press, Cambridge
    • Schrödinger, E. What is Life? (Cambridge Univ. Press, Cambridge, 1945).
    • (1945) What Is Life?
    • Schrödinger, E.1
  • 75
    • 0035830951 scopus 로고    scopus 로고
    • Locking the ATP-operated clamp of DNA gyrase: Probing the mechanism of strand passage
    • Williams, N. L., Howells, A. J. & Maxwell, A. Locking the ATP-operated clamp of DNA gyrase: probing the mechanism of strand passage. J. Mol. Biol. 306, 969-984 (2001).
    • (2001) J. Mol. Biol. , vol.306 , pp. 969-984
    • Williams, N.L.1    Howells, A.J.2    Maxwell, A.3


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