메뉴 건너뛰기




Volumn 40, Issue 8, 2012, Pages 3316-3328

Gene silencing H-NS paralogue StpA forms a rigid protein filament along DNA that blocks DNA accessibility

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; HISTONE LIKE NUCLEOID STRUCTURING PROTEIN; MAGNESIUM; NAKED DNA; PROTEIN STPA; UNCLASSIFIED DRUG;

EID: 84860359300     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr1247     Document Type: Article
Times cited : (62)

References (58)
  • 1
    • 18444369954 scopus 로고    scopus 로고
    • The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin
    • Dame, R.T. (2005) The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin. Mol. Microbiol., 56, 858-870.
    • (2005) Mol. Microbiol. , vol.56 , pp. 858-870
    • Dame, R.T.1
  • 2
    • 78649640318 scopus 로고    scopus 로고
    • Effects of nucleoid-associated proteins on bacterial chromosome structure and gene expression
    • Browning, D.F., Grainger, D.C. and Busby, S.J.W. (2010) Effects of nucleoid-associated proteins on bacterial chromosome structure and gene expression. Curr. Opin. Microbiol., 13, 773-780.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 773-780
    • Browning, D.F.1    Grainger, D.C.2    Busby, S.J.W.3
  • 3
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Azam, T.A., Iwata, A., Nishimura, A., Ueda, S. and Ishihama, A. (1999) Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J. Bacteriol., 181, 6361-6370.
    • (1999) J. Bacteriol. , vol.181 , pp. 6361-6370
    • Azam, T.A.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 5
    • 49349109694 scopus 로고    scopus 로고
    • Single-molecule micromanipulation studies of DNA and architectural proteins
    • Dame, R.T. (2008) Single-molecule micromanipulation studies of DNA and architectural proteins. Biochem. Soc. T., 36, 732-737.
    • (2008) Biochem. Soc. T. , vol.36 , pp. 732-737
    • Dame, R.T.1
  • 6
    • 2342454974 scopus 로고    scopus 로고
    • Dual architectural roles of HU: Formation of flexible hinges and rigid filaments
    • van Noort, J., Verbrugge, S., Goosen, N., Dekker, C. and Dame, R.T. (2004) Dual architectural roles of HU: formation of flexible hinges and rigid filaments. Proc. Natl Acad. Sci. USA, 101, 6969-6974.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6969-6974
    • Van Noort, J.1    Verbrugge, S.2    Goosen, N.3    Dekker, C.4    Dame, R.T.5
  • 7
    • 53449102029 scopus 로고    scopus 로고
    • Anti-silencing: Overcoming H-NS-mediated repression of transcription in Gram-negative enteric bacteria
    • Stoebel, D.M., Free, A. and Dorman, C.J. (2008) Anti-silencing: overcoming H-NS-mediated repression of transcription in Gram-negative enteric bacteria. Microbiology, 154, 2533-2545.
    • (2008) Microbiology , vol.154 , pp. 2533-2545
    • Stoebel, D.M.1    Free, A.2    Dorman, C.J.3
  • 8
    • 0030972952 scopus 로고    scopus 로고
    • H-NS: A modulator of environmentally regulated gene expression
    • Atlung, T. and Ingmer, H. (1997) H-NS: a modulator of environmentally regulated gene expression. Mol. Microbiol., 24, 7-17.
    • (1997) Mol. Microbiol. , vol.24 , pp. 7-17
    • Atlung, T.1    Ingmer, H.2
  • 9
    • 33846465923 scopus 로고    scopus 로고
    • H-NS the genome sentinel
    • Dorman, C.J. (2007) H-NS, the genome sentinel. Nat. Rev. Microbiol., 5, 157-161.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 157-161
    • Dorman, C.J.1
  • 10
    • 0015441270 scopus 로고
    • Two heat-resistant low molecular weight proteins from Escherichia coli that stimulate DNA-directed RNA synthesis
    • Cukier-Kahn, R., Jacquet, M. and Gros, F. (1972) Two heat-resistant, low molecular weight proteins from Escherichia coli that stimulate DNA-directed RNA synthesis. Proc. Natl Acad. Sci. USA, 69, 3643-3647.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 3643-3647
    • Cukier-Kahn, R.1    Jacquet, M.2    Gros, F.3
  • 11
  • 12
    • 0024004997 scopus 로고
    • Proteins from the prokaryotic nucleoid: Primary and quaternary structure of the 15-kD Escherichia coli DNA binding protein H-NS
    • Falconi, M., Gualtieri, M.T., La Teana, A., Losso, M.A. and Pon, C.L. (1988) Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 15-kD Escherichia coli DNA binding protein H-NS. Mol. Microbiol., 2, 323-329.
    • (1988) Mol. Microbiol. , vol.2 , pp. 323-329
    • Falconi, M.1    Gualtieri, M.T.2    La Teana, A.3    Losso, M.A.4    Pon, C.L.5
  • 13
    • 0034666271 scopus 로고    scopus 로고
    • H-NS mediated compaction of DNA visualised by atomic force microscopy
    • Dame, R.T., Wyman, C. and Goosen, N. (2000) H-NS mediated compaction of DNA visualised by atomic force microscopy. Nucleic Acids Res., 28, 3504-3510.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3504-3510
    • Dame, R.T.1    Wyman, C.2    Goosen, N.3
  • 14
    • 33751098486 scopus 로고    scopus 로고
    • Bacterial chromatin organization by H-NS protein unravelled using dual DNA manipulation
    • Dame, R.T., Noom, M.C. and Wuite, G.J. (2006) Bacterial chromatin organization by H-NS protein unravelled using dual DNA manipulation. Nature, 444, 387-390.
    • (2006) Nature , vol.444 , pp. 387-390
    • Dame, R.T.1    Noom, M.C.2    Wuite, G.J.3
  • 15
    • 0037381991 scopus 로고    scopus 로고
    • Increased bending rigidity of single DNA molecules by H-NS a temperature and osmolarity sensor
    • Amit, R., Oppenheim, A.B. and Stavans, J. (2003) Increased bending rigidity of single DNA molecules by H-NS, a temperature and osmolarity sensor. Biophys. J., 84, 2467-2473.
    • (2003) Biophys. J. , vol.84 , pp. 2467-2473
    • Amit, R.1    Oppenheim, A.B.2    Stavans, J.3
  • 16
    • 76749118994 scopus 로고    scopus 로고
    • A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes
    • Liu, Y., Chen, H., Kenney, L.J. and Yan, J. (2010) A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes. Genes Dev., 24, 339-344.
    • (2010) Genes Dev. , vol.24 , pp. 339-344
    • Liu, Y.1    Chen, H.2    Kenney, L.J.3    Yan, J.4
  • 17
    • 34447321831 scopus 로고    scopus 로고
    • The response regulator SsrB activates expression of diverse Salmonella pathogenicity island 2 promoters and counters silencing by the nucleoid-associated protein H-NS
    • Walthers, D., Carroll, R.K., Navarre, W.W., Libby, S.J., Fang, F.C. and Kenney, L.J. (2007) The response regulator SsrB activates expression of diverse Salmonella pathogenicity island 2 promoters and counters silencing by the nucleoid-associated protein H-NS. Mol. Microbiol., 65, 477-493.
    • (2007) Mol. Microbiol. , vol.65 , pp. 477-493
    • Walthers, D.1    Carroll, R.K.2    Navarre, W.W.3    Libby, S.J.4    Fang, F.C.5    Kenney, L.J.6
  • 18
    • 78751479182 scopus 로고    scopus 로고
    • Salmonella enterica response regulator SsrB relieves H-NS silencing by displacing H-NS bound in polymerization mode and directly activates transcription
    • Walthers, D., Li, Y., Liu, Y.J., Anand, G., Yan, J. and Kenney, L.J. (2011) Salmonella enterica response regulator SsrB relieves H-NS silencing by displacing H-NS bound in polymerization mode and directly activates transcription. J. Biol. Chem., 286, 1895-1902.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1895-1902
    • Walthers, D.1    Li, Y.2    Liu, Y.J.3    Anand, G.4    Yan, J.5    Kenney, L.J.6
  • 21
    • 0027073133 scopus 로고
    • Nucleotide-sequence of a newly-identified Escherichia coli gene, StpA, encoding an H-NS-like protein
    • Zhang, A.X. and Belfort, M. (1992) Nucleotide-sequence of a newly-identified Escherichia coli gene, StpA, encoding an H-NS-like protein. Nucleic Acids Res., 20, 6735-6735.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6735-6735
    • Zhang, A.X.1    Belfort, M.2
  • 22
    • 0027999823 scopus 로고
    • Plasmids bearing Hfq and the Hns-like gene StpA complement HNS mutants in modulating arginine decarboxylase gene-expression in Escherichia coli
    • Shi, X.L. and Bennett, G.N. (1994) Plasmids bearing Hfq and the Hns-like gene StpA complement HNS mutants in modulating arginine decarboxylase gene-expression in Escherichia coli. J. Bacteriol., 176, 6769-6775.
    • (1994) J. Bacteriol. , vol.176 , pp. 6769-6775
    • Shi, X.L.1    Bennett, G.N.2
  • 23
    • 0029913710 scopus 로고    scopus 로고
    • Escherichia coli protein analogs StpA and H-NS: Regulatory loops, similar and disparate effects on nucleic acid dynamics
    • Zhang, A.X., Rimsky, S., Reaban, M.E., Buc, H. and Belfort, M. (1996) Escherichia coli protein analogs StpA and H-NS: regulatory loops, similar and disparate effects on nucleic acid dynamics. EMBO J., 15, 1340-1349.
    • (1996) EMBO J. , vol.15 , pp. 1340-1349
    • Zhang, A.X.1    Rimsky, S.2    Reaban, M.E.3    Buc, H.4    Belfort, M.5
  • 24
    • 0029812469 scopus 로고    scopus 로고
    • Coordinated and differential expression of histone-like proteins in Escherichia coli: Regulation and function of the H-NS analog StpA
    • Sonden, B. and Uhlin, B.E. (1996) Coordinated and differential expression of histone-like proteins in Escherichia coli: regulation and function of the H-NS analog StpA. EMBO J., 15, 4970-4980.
    • (1996) EMBO J. , vol.15 , pp. 4970-4980
    • Sonden, B.1    Uhlin, B.E.2
  • 25
    • 0031035206 scopus 로고    scopus 로고
    • The Escherichia coli stpA gene is transiently expressed during growth in rich medium and is induced in minimal medium and by stress conditions
    • Free, A. and Dorman, C.J. (1997) The Escherichia coli stpA gene is transiently expressed during growth in rich medium and is induced in minimal medium and by stress conditions. J. Bacteriol., 179, 909-18.
    • (1997) J. Bacteriol. , vol.179 , pp. 909-18
    • Free, A.1    Dorman, C.J.2
  • 26
    • 74349105205 scopus 로고    scopus 로고
    • Differential effects and interactions of endogenous and horizontally acquired H-NS-like proteins in pathogenic Escherichia coli
    • Muller, C.M., Schneider, G., Dobrindt, U., Emody, L., Hacker, J. and Uhlin, B.E. (2010) Differential effects and interactions of endogenous and horizontally acquired H-NS-like proteins in pathogenic Escherichia coli. Mol. Microbiol., 75, 280-293.
    • (2010) Mol. Microbiol. , vol.75 , pp. 280-293
    • Muller, C.M.1    Schneider, G.2    Dobrindt, U.3    Emody, L.4    Hacker, J.5    Uhlin, B.E.6
  • 27
    • 0036829677 scopus 로고    scopus 로고
    • The degree of oligomerization of the H-NS nucleoid structuring protein is related to specific binding to DNA
    • Badaut, C., Williams, R., Arluison, V., Bouffartigues, E., Robert, B., Buc, H. and Rimsky, S. (2002) The degree of oligomerization of the H-NS nucleoid structuring protein is related to specific binding to DNA. J. Biol. Chem., 277, 41657-41666.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41657-41666
    • Badaut, C.1    Williams, R.2    Arluison, V.3    Bouffartigues, E.4    Robert, B.5    Buc, H.6    Rimsky, S.7
  • 28
    • 0035078382 scopus 로고    scopus 로고
    • Heteromeric interactions among nucleoid-associated bacterial proteins: Localization of StpA-stabilizing regions in H-NS of Escherichia coli
    • Johansson, J., Eriksson, S., Sonden, B., Wai, S.N. and Uhlin, B.E. (2001) Heteromeric interactions among nucleoid-associated bacterial proteins: localization of StpA-stabilizing regions in H-NS of Escherichia coli. J. Bacteriol., 183, 2343-2347.
    • (2001) J. Bacteriol. , vol.183 , pp. 2343-2347
    • Johansson, J.1    Eriksson, S.2    Sonden, B.3    Wai, S.N.4    Uhlin, B.E.5
  • 29
    • 0030601826 scopus 로고    scopus 로고
    • Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS
    • Ueguchi, C., Suzuki, T., Yoshida, T., Tanaka, K. and Mizuno, T. (1996) Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS. J. Mol. Biol., 263, 149-162.
    • (1996) J. Mol. Biol. , vol.263 , pp. 149-162
    • Ueguchi, C.1    Suzuki, T.2    Yoshida, T.3    Tanaka, K.4    Mizuno, T.5
  • 30
    • 28844463650 scopus 로고    scopus 로고
    • Nature and mechanism of the in vivo oligomerization of nucleoid protein H-NS
    • Stella, S., Spurio, R., Falconi, M., Pon, C.L. and Gualerzi, C.O. (2005) Nature and mechanism of the in vivo oligomerization of nucleoid protein H-NS. EMBO J., 24, 2896-2905.
    • (2005) EMBO J. , vol.24 , pp. 2896-2905
    • Stella, S.1    Spurio, R.2    Falconi, M.3    Pon, C.L.4    Gualerzi, C.O.5
  • 31
    • 0030976054 scopus 로고    scopus 로고
    • The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending
    • Spurio, R., Falconi, M., Brandi, A., Pon, C.L. and Gualerzi, C.O. (1997) The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending. EMBO J., 16, 1795-1805.
    • (1997) EMBO J. , vol.16 , pp. 1795-1805
    • Spurio, R.1    Falconi, M.2    Brandi, A.3    Pon, C.L.4    Gualerzi, C.O.5
  • 33
    • 29144474208 scopus 로고    scopus 로고
    • StpA protein from Escherichia coli condenses supercoiled DNA in preference to linear DNA and protects it from digestion by DNase i and EcoKI
    • Keatch, S.A., Leonard, P.G., Ladbury, J.E. and Dryden, D.T. (2005) StpA protein from Escherichia coli condenses supercoiled DNA in preference to linear DNA and protects it from digestion by DNase I and EcoKI. Nucleic Acids Res., 33, 6540-6546.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6540-6546
    • Keatch, S.A.1    Leonard, P.G.2    Ladbury, J.E.3    Dryden, D.T.4
  • 34
    • 78049422210 scopus 로고    scopus 로고
    • Modulation of HU-DNA interactions by salt concentration and applied force
    • Xiao, B., Johnson, R.C. and Marko, J.F. (2010) Modulation of HU-DNA interactions by salt concentration and applied force. Nucleic Acids Res., 38, 6176-6185.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 6176-6185
    • Xiao, B.1    Johnson, R.C.2    Marko, J.F.3
  • 35
    • 0036931098 scopus 로고    scopus 로고
    • Glutaraldehyde modified mica: A new surface for atomic force microscopy of chromatin
    • Wang, H.D., Bash, R., Yodh, J.G., Hager, G.L., Lohr, D. and Lindsay, S.M. (2002) Glutaraldehyde modified mica: a new surface for atomic force microscopy of chromatin. Biophys. J., 83, 3619-3625.
    • (2002) Biophys. J. , vol.83 , pp. 3619-3625
    • Wang, H.D.1    Bash, R.2    Yodh, J.G.3    Hager, G.L.4    Lohr, D.5    Lindsay, S.M.6
  • 36
    • 79959723276 scopus 로고    scopus 로고
    • Atomic force microscope imaging of chromatin assembled in Xenopus laevis egg extract
    • Fu, H., Freedman, B.S., Lim, C.T., Heald, R. and Yan, J. (2011) Atomic force microscope imaging of chromatin assembled in Xenopus laevis egg extract. Chromosoma, 120, 245-254.
    • (2011) Chromosoma , vol.120 , pp. 245-254
    • Fu, H.1    Freedman, B.S.2    Lim, C.T.3    Heald, R.4    Yan, J.5
  • 37
  • 40
    • 70450213719 scopus 로고    scopus 로고
    • The H-NS-like protein StpA represses the RpoS (sigma 38) regulon during exponential growth of Salmonella Typhimurium
    • Lucchini, S., McDermott, P., Thompson, A. and Hinton, J.C. (2009) The H-NS-like protein StpA represses the RpoS (sigma 38) regulon during exponential growth of Salmonella Typhimurium. Mol. Microbiol., 74, 1169-1186.
    • (2009) Mol. Microbiol. , vol.74 , pp. 1169-1186
    • Lucchini, S.1    McDermott, P.2    Thompson, A.3    Hinton, J.C.4
  • 42
    • 0017191534 scopus 로고
    • Magnesium metabolism-brief review
    • Paymaster, N.J. (1976) Magnesium metabolism-brief review. Ann. Roy. Coll. Surg., 58, 309-314.
    • (1976) Ann. Roy. Coll. Surg. , vol.58 , pp. 309-314
    • Paymaster, N.J.1
  • 43
    • 70349957921 scopus 로고    scopus 로고
    • Protein-mediated molecular bridging: A key mechanism in biopolymer organization
    • Wiggins, P.A., Dame, R.T., Noom, M.C. and Wuite, G.J. (2009) Protein-mediated molecular bridging: a key mechanism in biopolymer organization. Biophys. J., 97, 1997-2003.
    • (2009) Biophys. J. , vol.97 , pp. 1997-2003
    • Wiggins, P.A.1    Dame, R.T.2    Noom, M.C.3    Wuite, G.J.4
  • 44
    • 80053468063 scopus 로고    scopus 로고
    • Influence of mobile DNA-protein-DNA bridges on DNA configurations: Coarse-grained Monte-Carlo simulations
    • de Vries, R. (2011) Influence of mobile DNA-protein-DNA bridges on DNA configurations: coarse-grained Monte-Carlo simulations. J. Chem. Phys., 135, 125104.
    • (2011) J. Chem. Phys. , vol.135 , pp. 125104
    • De Vries, R.1
  • 45
    • 67650439289 scopus 로고    scopus 로고
    • Investigation of the self-association and hetero-association interactions of H-NS and StpA from Enterobacteria
    • Leonard, P.G., Ono, S., Gor, J., Perkins, S.J. and Ladbury, J.E. (2009) Investigation of the self-association and hetero-association interactions of H-NS and StpA from Enterobacteria. Mol. Microbiol., 73, 165-179.
    • (2009) Mol. Microbiol. , vol.73 , pp. 165-179
    • Leonard, P.G.1    Ono, S.2    Gor, J.3    Perkins, S.J.4    Ladbury, J.E.5
  • 47
    • 0029013817 scopus 로고
    • Mutational analysis of Dnase-I DNA interactions-design, expression and characterization of a Dnase-I loop insertion mutant with altered sequence selectivity
    • Wolf, E., Brukner, I. and Suck, D. (1995) Mutational analysis of Dnase-I DNA interactions-design, expression and characterization of a Dnase-I loop insertion mutant with altered sequence selectivity. Protein Eng, 8, 283-291.
    • (1995) Protein Eng , vol.8 , pp. 283-291
    • Wolf, E.1    Brukner, I.2    Suck, D.3
  • 48
    • 0028785899 scopus 로고
    • Structure of open promoter complexes with Escherichia coli Rna-polymerase as revealed by the Dnase-I footprinting technique-compilation analysis
    • Ozoline, O.N. and Tsyganov, M.A. (1995) Structure of open promoter complexes with Escherichia coli Rna-polymerase as revealed by the Dnase-I footprinting technique-compilation analysis. Nucleic Acids Res., 23, 4533-4541.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4533-4541
    • Ozoline, O.N.1    Tsyganov, M.A.2
  • 49
    • 64049096202 scopus 로고    scopus 로고
    • Differential binding profiles of StpA in wild-type and HNS mutant cells: A comparative analysis of cooperative partners by chromatin immunoprecipitation- microarray analysis
    • Uyar, E., Kurokawa, K., Yoshimura, M., Ishikawa, S., Ogasawara, N. and Oshima, T. (2009) Differential binding profiles of StpA in wild-type and HNS mutant cells: a comparative analysis of cooperative partners by chromatin immunoprecipitation-microarray analysis. J. Bacteriol., 191, 2388-2391.
    • (2009) J. Bacteriol. , vol.191 , pp. 2388-2391
    • Uyar, E.1    Kurokawa, K.2    Yoshimura, M.3    Ishikawa, S.4    Ogasawara, N.5    Oshima, T.6
  • 50
    • 80052643394 scopus 로고    scopus 로고
    • Chromosome organization by a nucleoid-associated protein in live bacteria
    • Wang, W., Li, G.W., Chen, C., Xie, X.S. and Zhuang, X. (2011) Chromosome organization by a nucleoid-associated protein in live bacteria. Science, 333, 1445-1449.
    • (2011) Science , vol.333 , pp. 1445-1449
    • Wang, W.1    Li, G.W.2    Chen, C.3    Xie, X.S.4    Zhuang, X.5
  • 51
    • 79955573136 scopus 로고    scopus 로고
    • Transition dynamics and selection of the distinct S-DNA and strand unpeeling modes of double helix overstretching
    • Fu, H., Chen, H., Zhang, X., Qu, Y., Marko, J.F. and Yan, J. (2011) Transition dynamics and selection of the distinct S-DNA and strand unpeeling modes of double helix overstretching. Nucleic Acids Res., 39, 3473-3481.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 3473-3481
    • Fu, H.1    Chen, H.2    Zhang, X.3    Qu, Y.4    Marko, J.F.5    Yan, J.6
  • 52
    • 33847286857 scopus 로고    scopus 로고
    • A divalent metal-mediated switch controlling protein-induced DNA bending
    • Bao, Q., Chen, H., Liu, Y., Yan, J., Droge, P. and Davey, C.A. (2007) A divalent metal-mediated switch controlling protein-induced DNA bending. J. Mol. Biol., 367, 731-740.
    • (2007) J. Mol. Biol. , vol.367 , pp. 731-740
    • Bao, Q.1    Chen, H.2    Liu, Y.3    Yan, J.4    Droge, P.5    Davey, C.A.6
  • 53
    • 0035106406 scopus 로고    scopus 로고
    • Accurate length determination of DNA molecules visualized by atomic force microscopy: Evidence for a partial B-to A-form transition on mica
    • Rivetti, C. and Codeluppi, S. (2001) Accurate length determination of DNA molecules visualized by atomic force microscopy: evidence for a partial B-to A-form transition on mica. Ultramicroscopy, 87, 55-66.
    • (2001) Ultramicroscopy , vol.87 , pp. 55-66
    • Rivetti, C.1    Codeluppi, S.2
  • 54
    • 0020330531 scopus 로고
    • Vector code probability and metrication error in the representation of straight-lines of finite length
    • Vossepoel, A.M. and Smeulders, A.W.M. (1982) Vector code probability and metrication error in the representation of straight-lines of finite length. Comput Graphics Image Proc., 20, 347-364.
    • (1982) Comput Graphics Image Proc. , vol.20 , pp. 347-364
    • Vossepoel, A.M.1    Smeulders, A.W.M.2
  • 55
    • 0030002635 scopus 로고    scopus 로고
    • The elasticity of a single supercoiled DNA molecule
    • vol 271, pg 1835, 1996
    • Allemand, J.F., Bensimon, D. and Croquette, V. (1996) The elasticity of a single supercoiled DNA molecule. Science, 272, 797-797 (vol 271, pg 1835, 1996).
    • (1996) Science , vol.272 , pp. 797-797
    • Allemand, J.F.1    Bensimon, D.2    Croquette, V.3
  • 57
    • 0028071373 scopus 로고
    • Entropic elasticity of lambda-phage DNA
    • Bustamante, C., Marko, J.F., Siggia, E.D. and Smith, S. (1994) Entropic elasticity of lambda-phage DNA. Science, 265, 1599-1600.
    • (1994) Science , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Siggia, E.D.3    Smith, S.4
  • 58
    • 0026495432 scopus 로고
    • Direct mechanical measurements of the elasticity of single DNA molecules by using magnetic beads
    • Smith, S.B., Finzi, L. and Bustamante, C. (1992) Direct mechanical measurements of the elasticity of single DNA molecules by using magnetic beads. Science, 258, 1122-1126.
    • (1992) Science , vol.258 , pp. 1122-1126
    • Smith, S.B.1    Finzi, L.2    Bustamante, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.