메뉴 건너뛰기




Volumn 8, Issue 36, 2012, Pages 9285-9301

Electrostatics of DNA compaction in viruses, bacteria and eukaryotes: Functional insights and evolutionary perspective

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; COMPACTION; ELECTROSTATICS; GENES; LIQUID CRYSTALS; VIRUSES;

EID: 84865518143     PISSN: 1744683X     EISSN: 17446848     Source Type: Journal    
DOI: 10.1039/c2sm25789k     Document Type: Review
Times cited : (54)

References (252)
  • 1
    • 0033609566 scopus 로고    scopus 로고
    • Nucleosome dynamics. Protein and DNA contributions in the chiral transition of the tetrasome, the histone (H3-H4)2 tetramer-DNA particle
    • M. Alilat A. Sivolob B. Revet A. Prunell Nucleosome dynamics. Protein and DNA contributions in the chiral transition of the tetrasome, the histone (H3-H4)2 tetramer-DNA particle J. Mol. Biol. 1999 291 815 841
    • (1999) J. Mol. Biol. , vol.291 , pp. 815-841
    • Alilat, M.1    Sivolob, A.2    Revet, B.3    Prunell, A.4
  • 2
    • 0001457369 scopus 로고
    • The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid
    • B. N. Ames D. T. Dubin The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid J. Biol. Chem. 1960 235 769 775
    • (1960) J. Biol. Chem. , vol.235 , pp. 769-775
    • Ames, B.N.1    Dubin, D.T.2
  • 3
    • 3042784127 scopus 로고    scopus 로고
    • The two faces of Alba: The evolutionary connection between proteins participating in chromatin structure and RNA metabolism
    • L. Aravind L. M. Iyer V. Anantharaman The two faces of Alba: the evolutionary connection between proteins participating in chromatin structure and RNA metabolism Genome Biol. 2003 4 R64
    • (2003) Genome Biol. , vol.4 , pp. 64
    • Aravind, L.1    Iyer, L.M.2    Anantharaman, V.3
  • 4
    • 34249278819 scopus 로고    scopus 로고
    • Generalized electrostatic model of the wrapping of DNA around oppositely charged proteins
    • L. Arcesi G. La Penna A. Perico Generalized electrostatic model of the wrapping of DNA around oppositely charged proteins Biopolymers 2007 86 127 135
    • (2007) Biopolymers , vol.86 , pp. 127-135
    • Arcesi, L.1    La Penna, G.2    Perico, A.3
  • 5
    • 0033869982 scopus 로고    scopus 로고
    • Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid
    • T. A. Azam S. Hiraga A. Ishihama Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid Genes Cells 2000 5 613 626
    • (2000) Genes Cells , vol.5 , pp. 613-626
    • Azam, T.A.1    Hiraga, S.2    Ishihama, A.3
  • 6
    • 0032731196 scopus 로고    scopus 로고
    • Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity
    • T. A. Azam A. Ishihama Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity J. Biol. Chem. 1999 274 33105 33113
    • (1999) J. Biol. Chem. , vol.274 , pp. 33105-33113
    • Azam, T.A.1    Ishihama, A.2
  • 7
    • 0021930472 scopus 로고
    • The incorporation of radiolabeled polyamines and methionine into turnip yellow mosaic virus in protoplasts from infected plants
    • R. Balint S. S. Cohen The incorporation of radiolabeled polyamines and methionine into turnip yellow mosaic virus in protoplasts from infected plants Virology 1985 144 181 193
    • (1985) Virology , vol.144 , pp. 181-193
    • Balint, R.1    Cohen, S.S.2
  • 8
    • 0001424375 scopus 로고
    • Counterion-driven sphere to cylinder transition in reverse micelles: A small angle X-ray scattering and conductometric study
    • E. Bardez N. C. Vy T. Zemb Counterion-driven sphere to cylinder transition in reverse micelles: a small angle X-ray scattering and conductometric study Langmuir 1995 11 3374 3381
    • (1995) Langmuir , vol.11 , pp. 3374-3381
    • Bardez, E.1    Vy, N.C.2    Zemb, T.3
  • 9
    • 0026547544 scopus 로고
    • Nucleoid condensation in Escherichia coli that express a chlamydial histone homolog
    • C. E. Barry S. F. Hayes T. Hackstadt Nucleoid condensation in Escherichia coli that express a chlamydial histone homolog Science 1992 256 377 379
    • (1992) Science , vol.256 , pp. 377-379
    • Barry, C.E.1    Hayes, S.F.2    Hackstadt, T.3
  • 11
    • 0038136948 scopus 로고    scopus 로고
    • Contribution of DNA conformation and topology in right-handed DNA wrapping by the Bacillus subtilis LrpC protein
    • C. Beloin J. Jeusset B. Révet G. Mirambeau F. Le Hégarat E. Le Cam Contribution of DNA conformation and topology in right-handed DNA wrapping by the Bacillus subtilis LrpC protein J. Biol. Chem. 2003 278 5333 5342
    • (2003) J. Biol. Chem. , vol.278 , pp. 5333-5342
    • Beloin, C.1    Jeusset, J.2    Révet, B.3    Mirambeau, G.4    Le Hégarat, F.5    Le Cam, E.6
  • 12
    • 0034064386 scopus 로고    scopus 로고
    • Prokaryotic and eukaryotic chromosomes: What's the difference?
    • A. J. Bendich K. Drlica Prokaryotic and eukaryotic chromosomes: what's the difference? BioEssays 2000 22 481 486
    • (2000) BioEssays , vol.22 , pp. 481-486
    • Bendich, A.J.1    Drlica, K.2
  • 13
    • 36549075245 scopus 로고    scopus 로고
    • Structure and phase diagram of nucleosome core particles aggregated by multivalent cations
    • B. Bertin S. Mangenot M. Renouard D. Durand F. Livolant Structure and phase diagram of nucleosome core particles aggregated by multivalent cations Biophys. J. 2007 93 3652 3663
    • (2007) Biophys. J. , vol.93 , pp. 3652-3663
    • Bertin, B.1    Mangenot, S.2    Renouard, M.3    Durand, D.4    Livolant, F.5
  • 15
    • 0031447208 scopus 로고    scopus 로고
    • DNA condensation by multivalent cations
    • V. A. Bloomfield DNA condensation by multivalent cations Biopolymers 1997 44 269 282
    • (1997) Biopolymers , vol.44 , pp. 269-282
    • Bloomfield, V.A.1
  • 16
    • 0034090341 scopus 로고    scopus 로고
    • Immunofluorescent studies of human chromosomes with antibodies against phosphorylated H1 histone
    • B. A. Boggs C. D. Allis A. C. Chinault Immunofluorescent studies of human chromosomes with antibodies against phosphorylated H1 histone Chromosoma 2000 108 485 490
    • (2000) Chromosoma , vol.108 , pp. 485-490
    • Boggs, B.A.1    Allis, C.D.2    Chinault, A.C.3
  • 17
    • 23744458729 scopus 로고    scopus 로고
    • Interaction between macroions mediated by divalent rod-like ions
    • K. Bohinc A. Igli S. May Interaction between macroions mediated by divalent rod-like ions Europhys. Lett. 2004 68 494 500
    • (2004) Europhys. Lett. , vol.68 , pp. 494-500
    • Bohinc, K.1    Igli, A.2    May, S.3
  • 18
    • 84861168563 scopus 로고    scopus 로고
    • The interactions between charged colloids with rod-like counterions
    • K. Bohinc J. M. A. Grime L. Lue The interactions between charged colloids with rod-like counterions Soft Matter 2012 8 5679 5686
    • (2012) Soft Matter , vol.8 , pp. 5679-5686
    • Bohinc, K.1    Grime, J.M.A.2    Lue, L.3
  • 19
    • 34247628510 scopus 로고    scopus 로고
    • H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing
    • E. Bouffartigues M. Buckle C. Badaut A. Travers S. Rimsky H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing Nat. Struct. Mol. Biol. 2007 14 441 448
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 441-448
    • Bouffartigues, E.1    Buckle, M.2    Badaut, C.3    Travers, A.4    Rimsky, S.5
  • 20
    • 0019578292 scopus 로고
    • Thermodynamics and equilibrium sedimentation analysis of the close approach of DNA molecules and a molecular ordering transition
    • A. A. Brian H. L. Frisch L. S. Lerman Thermodynamics and equilibrium sedimentation analysis of the close approach of DNA molecules and a molecular ordering transition Biopolymers 1981 20 1305 1328
    • (1981) Biopolymers , vol.20 , pp. 1305-1328
    • Brian, A.A.1    Frisch, H.L.2    Lerman, L.S.3
  • 21
    • 78649640318 scopus 로고    scopus 로고
    • Effects of nucleoid-associated proteins on bacterial chromosome structure and gene expression
    • D. F. Browning D. C. Grainger S. J. Busby Effects of nucleoid-associated proteins on bacterial chromosome structure and gene expression Curr. Opin. Microbiol. 2010 13 773 780
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 773-780
    • Browning, D.F.1    Grainger, D.C.2    Busby, S.J.3
  • 22
    • 0023041804 scopus 로고
    • Interaction of the Escherichia coli HU protein with DNA. Evidence for formation of nucleosome-like structures with altered DNA helical pitch
    • S. S. Broyles D. E. Pettijohn Interaction of the Escherichia coli HU protein with DNA. Evidence for formation of nucleosome-like structures with altered DNA helical pitch J. Mol. Biol. 1986 187 47 60
    • (1986) J. Mol. Biol. , vol.187 , pp. 47-60
    • Broyles, S.S.1    Pettijohn, D.E.2
  • 24
    • 0030358586 scopus 로고    scopus 로고
    • High-mobility-group chromosomal proteins: Architectural components that facilitate chromatin function
    • M. Bustin R. Reeves High-mobility-group chromosomal proteins: architectural components that facilitate chromatin function Prog. Nucleic Acid Res. Mol. Biol. 1996 54 35 100
    • (1996) Prog. Nucleic Acid Res. Mol. Biol. , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 25
    • 33749246561 scopus 로고    scopus 로고
    • Epigenetic gene regulation in the bacterial world
    • J. Casadesus D. Low Epigenetic gene regulation in the bacterial world Microbiol. Mol. Biol. Rev. 2006 70 830 856
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 830-856
    • Casadesus, J.1    Low, D.2
  • 26
    • 0036668636 scopus 로고    scopus 로고
    • Competition between histone H1 and HMGN proteins for chromatin binding sites
    • F. Catez D. T. Brown T. Misteli M. Bustin Competition between histone H1 and HMGN proteins for chromatin binding sites EMBO Rep. 2002 3 760 766
    • (2002) EMBO Rep. , vol.3 , pp. 760-766
    • Catez, F.1    Brown, D.T.2    Misteli, T.3    Bustin, M.4
  • 27
    • 77949910116 scopus 로고    scopus 로고
    • Origin of the cell nucleus, mitosis and sex: Roles of intracellular coevolution
    • T. Cavalier-Smith Origin of the cell nucleus, mitosis and sex: roles of intracellular coevolution Biol. Direct 2010 5 7
    • (2010) Biol. Direct , vol.5 , pp. 7
    • Cavalier-Smith, T.1
  • 29
    • 33644674439 scopus 로고    scopus 로고
    • The organization and inheritance of the mitochondrial genome
    • X. J. Chen R. A. Butow The organization and inheritance of the mitochondrial genome Nat. Rev. Genet. 2005 6 815 825
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 815-825
    • Chen, X.J.1    Butow, R.A.2
  • 30
    • 32644446799 scopus 로고    scopus 로고
    • Similarities and differences in interaction of K+ and Na + with condensed ordered DNA. A molecular dynamics computer simulation study
    • Y. Cheng N. Korolev L. Nordenskiöld Similarities and differences in interaction of K+ and Na+ with condensed ordered DNA. A molecular dynamics computer simulation study Nucleic Acids Res. 2006 34 686 696
    • (2006) Nucleic Acids Res. , vol.34 , pp. 686-696
    • Cheng, Y.1    Korolev, N.2    Nordenskiöld, L.3
  • 31
    • 0024264685 scopus 로고
    • Differences in the binding of H1 variants to DNA. Cooperativity and linker-length related distribution
    • D. J. Clark J. O. Thomas Differences in the binding of H1 variants to DNA. Cooperativity and linker-length related distribution Eur. J. Biochem. 1988 178 225 233
    • (1988) Eur. J. Biochem. , vol.178 , pp. 225-233
    • Clark, D.J.1    Thomas, J.O.2
  • 32
    • 47349128082 scopus 로고    scopus 로고
    • Mechanical response of plectonemic DNA: An analytical solution
    • N. Clauvelin B. Audoly S. Neukirch Mechanical response of plectonemic DNA: an analytical solution Macromolecules 2008 41 4479 4483
    • (2008) Macromolecules , vol.41 , pp. 4479-4483
    • Clauvelin, N.1    Audoly, B.2    Neukirch, S.3
  • 33
    • 67650403408 scopus 로고    scopus 로고
    • Elasticity and electrostatics of plectonemic DNA
    • N. Clauvelin B. Audoly S. Neukirch Elasticity and electrostatics of plectonemic DNA Biophys. J. 2009 2009 3716 3723
    • (2009) Biophys. J. , vol.2009 , pp. 3716-3723
    • Clauvelin, N.1    Audoly, B.2    Neukirch, S.3
  • 34
    • 0033593503 scopus 로고    scopus 로고
    • Static curvature and flexibility measurements of DNA with microscopy. A simple renormalization method, its assessment by experiment and simulation
    • J. A. Cognet C. Pakleza D. Cherny E. Delain E. Le Cam Static curvature and flexibility measurements of DNA with microscopy. A simple renormalization method, its assessment by experiment and simulation J. Mol. Biol. 1999 285 997 1009
    • (1999) J. Mol. Biol. , vol.285 , pp. 997-1009
    • Cognet, J.A.1    Pakleza, C.2    Cherny, D.3    Delain, E.4    Le Cam, E.5
  • 35
    • 0001446646 scopus 로고
    • Chromosome structure
    • A. Cole Chromosome structure Theor. Biophys. 1967 1 305 307
    • (1967) Theor. Biophys. , vol.1 , pp. 305-307
    • Cole, A.1
  • 36
    • 0031029477 scopus 로고    scopus 로고
    • Charge density-dependent strength of hydration and biological structure
    • K. D. Collins Charge density-dependent strength of hydration and biological structure Biophys. J. 1997 72 65 76
    • (1997) Biophys. J. , vol.72 , pp. 65-76
    • Collins, K.D.1
  • 37
    • 0013824659 scopus 로고
    • An electron microscopic study of lambda and lambda-dg bacteriophage in thin sections
    • D. J. Cummings V. A. Chapman S. S. DeLong An electron microscopic study of lambda and lambda-dg bacteriophage in thin sections J. Mol. Biol. 1965 14 418 422
    • (1965) J. Mol. Biol. , vol.14 , pp. 418-422
    • Cummings, D.J.1    Chapman, V.A.2    Delong, S.S.3
  • 38
    • 80052472874 scopus 로고    scopus 로고
    • Electrostatic braiding and homologous pairing of DNA double helices
    • R. Cortini A. A. Kornyshev D. J. Lee S. Leikin Electrostatic braiding and homologous pairing of DNA double helices Biophys. J. 2011 101 875 884
    • (2011) Biophys. J. , vol.101 , pp. 875-884
    • Cortini, R.1    Kornyshev, A.A.2    Lee, D.J.3    Leikin, S.4
  • 41
    • 80052139885 scopus 로고    scopus 로고
    • Deciphering condensin action during chromosome segregation
    • S. Cuylen C. H. Haering Deciphering condensin action during chromosome segregation Trends Cell Biol. 2011 21 552 559
    • (2011) Trends Cell Biol. , vol.21 , pp. 552-559
    • Cuylen, S.1    Haering, C.H.2
  • 43
    • 18444369954 scopus 로고    scopus 로고
    • The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin
    • R. T. Dame The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin Mol. Microbiol. 2005 56 858 870
    • (2005) Mol. Microbiol. , vol.56 , pp. 858-870
    • Dame, R.T.1
  • 44
    • 0034666271 scopus 로고    scopus 로고
    • H-NS mediated compaction of DNA visualised by atomic force microscopy
    • R. T. Dame C. Wyman N. Goosen H-NS mediated compaction of DNA visualised by atomic force microscopy Nucleic Acids Res. 2000 28 3504 3510
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3504-3510
    • Dame, R.T.1    Wyman, C.2    Goosen, N.3
  • 45
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution
    • C. A. Davey D. F. Sargent K. Luger A. W. Maeder T. J. Richmond Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution J. Mol. Biol. 2002 319 1097 1113
    • (2002) J. Mol. Biol. , vol.319 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 46
    • 33846839291 scopus 로고    scopus 로고
    • Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly
    • S. de los Rios J. J. Perona Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly J. Mol. Biol. 2007 366 1589 1602
    • (2007) J. Mol. Biol. , vol.366 , pp. 1589-1602
    • De Los Rios, S.1    Perona, J.J.2
  • 47
    • 78049323212 scopus 로고    scopus 로고
    • Cation charge dependence of the forces driving DNA assembly
    • J. De Rouchey V. A. Parsegian D. C. Rau Cation charge dependence of the forces driving DNA assembly Biophys. J. 2010 99 2608 2615
    • (2010) Biophys. J. , vol.99 , pp. 2608-2615
    • De Rouchey, J.1    Parsegian, V.A.2    Rau, D.C.3
  • 48
    • 76949089832 scopus 로고    scopus 로고
    • Bacterial nucleoid-associated proteins, nucleoid structure and gene expression
    • S. C. Dillon C. J. Dorman Bacterial nucleoid-associated proteins, nucleoid structure and gene expression Nat. Rev. Microbiol. 2011 8 185 195
    • (2011) Nat. Rev. Microbiol. , vol.8 , pp. 185-195
    • Dillon, S.C.1    Dorman, C.J.2
  • 49
    • 2442560235 scopus 로고    scopus 로고
    • H-NS: A universal regulator for a dynamic genome
    • C. J. Dorman H-NS: a universal regulator for a dynamic genome Nat. Rev. Microbiol. 2004 2 391 400
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 391-400
    • Dorman, C.J.1
  • 50
    • 33846465923 scopus 로고    scopus 로고
    • H-NS, the genome sentinel
    • C. J. Dorman H-NS, the genome sentinel Nat. Rev. Microbiol. 2007 5 157 161
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 157-161
    • Dorman, C.J.1
  • 51
    • 55149125796 scopus 로고    scopus 로고
    • Histone H3 K56 acetylation, chromatin assembly, and the DNA damage checkpoint
    • J. A. Downs Histone H3 K56 acetylation, chromatin assembly, and the DNA damage checkpoint DNA Repair 2008 7 2020 2024
    • (2008) DNA Repair , vol.7 , pp. 2020-2024
    • Downs, J.A.1
  • 52
    • 0018273790 scopus 로고
    • Nucleosome arcs and helices
    • J. Dubochet M. Noll Nucleosome arcs and helices Science 1978 202 280 286
    • (1978) Science , vol.202 , pp. 280-286
    • Dubochet, J.1    Noll, M.2
  • 53
    • 0029972107 scopus 로고    scopus 로고
    • Electrostatic effects on the stability of condensed DNA in the presence of divalent cations
    • J. G. Duguid V. A. Bloomfield Electrostatic effects on the stability of condensed DNA in the presence of divalent cations Biophys. J. 1996 70 2838 2846
    • (1996) Biophys. J. , vol.70 , pp. 2838-2846
    • Duguid, J.G.1    Bloomfield, V.A.2
  • 54
    • 0018932980 scopus 로고
    • DNA packaging by the double-stranded DNA bacteriophages
    • W. C. Earnshaw S. R. Casjens DNA packaging by the double-stranded DNA bacteriophages Cell 1980 21 319 331
    • (1980) Cell , vol.21 , pp. 319-331
    • Earnshaw, W.C.1    Casjens, S.R.2
  • 55
    • 0020681351 scopus 로고
    • Architecture of metaphase chromosomes and chromosome scaffolds
    • W. C. Earnshaw U. K. Laemmli Architecture of metaphase chromosomes and chromosome scaffolds J. Cell Biol. 1983 96 84 93
    • (1983) J. Cell Biol. , vol.96 , pp. 84-93
    • Earnshaw, W.C.1    Laemmli, U.K.2
  • 56
    • 0017837314 scopus 로고
    • The compaction of DNA helices into either continuous supercoils or folded-fiber rods and toroids
    • T. H. Eickbush E. N. Moudrianakis The compaction of DNA helices into either continuous supercoils or folded-fiber rods and toroids Cell 1978 13 295 306
    • (1978) Cell , vol.13 , pp. 295-306
    • Eickbush, T.H.1    Moudrianakis, E.N.2
  • 57
    • 58149401194 scopus 로고    scopus 로고
    • Analysis of cryo-electron microscopy images does not support the existence of 30-nm chromatin fibers in mitotic chromosomes in situ
    • M. Elstov K. M. Maclellan K. Maeshima A. S. Frangakis J. Dubochet Analysis of cryo-electron microscopy images does not support the existence of 30-nm chromatin fibers in mitotic chromosomes in situ Proc. Natl. Acad. Sci. U. S. A. 2008 105 19732 19737
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 19732-19737
    • Elstov, M.1    MacLellan, K.M.2    Maeshima, K.3    Frangakis, A.S.4    Dubochet, J.5
  • 58
    • 0032846225 scopus 로고    scopus 로고
    • Cationic silanes stabilize intermediates in DNA condensation
    • Y. Fang J. H. Hoh Cationic silanes stabilize intermediates in DNA condensation FEBS Lett. 1999 459 173 176
    • (1999) FEBS Lett. , vol.459 , pp. 173-176
    • Fang, Y.1    Hoh, J.H.2
  • 59
    • 84943002924 scopus 로고    scopus 로고
    • Characterization of DNA condensates by atomic force microscopy
    • Y. Fang J. H. Hoh Characterization of DNA condensates by atomic force microscopy Methods Mol. Med. 2001 65 149 158
    • (2001) Methods Mol. Med. , vol.65 , pp. 149-158
    • Fang, Y.1    Hoh, J.H.2
  • 60
    • 77956562679 scopus 로고    scopus 로고
    • Charge state of the globular histone core controls stability of the nucleosome
    • A. T. Fenley D. A. Adams A. V. Onufriev Charge state of the globular histone core controls stability of the nucleosome Biophys. J. 2010 99 1577 1585
    • (2010) Biophys. J. , vol.99 , pp. 1577-1585
    • Fenley, A.T.1    Adams, D.A.2    Onufriev, A.V.3
  • 61
    • 0026640728 scopus 로고
    • DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein
    • R. P. Fisher T. Lisowsky M. A. Parisi D. A. Clayton DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein J. Biol. Chem. 1992 267 3358 3367
    • (1992) J. Biol. Chem. , vol.267 , pp. 3358-3367
    • Fisher, R.P.1    Lisowsky, T.2    Parisi, M.A.3    Clayton, D.A.4
  • 63
    • 41949110996 scopus 로고    scopus 로고
    • Abrupt buckling transition observed during the plectoneme formation of individual DNA molecules
    • S. Forth C. Deufel M. Y. Sheinin B. Daniels J. P. Sethna M. D. Wang Abrupt buckling transition observed during the plectoneme formation of individual DNA molecules Phys. Rev. Lett. 2008 100 148301
    • (2008) Phys. Rev. Lett. , vol.100 , pp. 148301
    • Forth, S.1    Deufel, C.2    Sheinin, M.Y.3    Daniels, B.4    Sethna, J.P.5    Wang, M.D.6
  • 65
    • 70349768353 scopus 로고    scopus 로고
    • Nanoparticle aggregation controlled by desalting kinetics
    • J. Fresnais C. Lavelle J. F. Berret Nanoparticle aggregation controlled by desalting kinetics J. Phys. Chem. C 2009 113 16371 16379
    • (2009) J. Phys. Chem. C , vol.113 , pp. 16371-16379
    • Fresnais, J.1    Lavelle, C.2    Berret, J.F.3
  • 67
    • 0015421458 scopus 로고
    • Arrangement of herpesvirus deoxyribonucleic acid in the core
    • D. Furlong H. Swift B. Roizman Arrangement of herpesvirus deoxyribonucleic acid in the core J. Virol. 1972 10 1071 1074
    • (1972) J. Virol. , vol.10 , pp. 1071-1074
    • Furlong, D.1    Swift, H.2    Roizman, B.3
  • 72
    • 0015156237 scopus 로고
    • Compartmentalization of spermine and spermidine in the herpes simplex virion
    • W. Gibson B. Roizman Compartmentalization of spermine and spermidine in the herpes simplex virion Proc. Natl. Acad. Sci. U. S. A. 1971 68 2818 2821
    • (1971) Proc. Natl. Acad. Sci. U. S. A. , vol.68 , pp. 2818-2821
    • Gibson, W.1    Roizman, B.2
  • 73
    • 0017238490 scopus 로고
    • Compact form of DNA induced by spermidine
    • L. C. Gosule J. A. Schellman Compact form of DNA induced by spermidine Nature 1976 259 333 335
    • (1976) Nature , vol.259 , pp. 333-335
    • Gosule, L.C.1    Schellman, J.A.2
  • 75
    • 0036158780 scopus 로고    scopus 로고
    • Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation
    • H. Goto Y. Yasui E. A. Nigg M. Inagaki Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation Genes Cells 2002 7 11 17
    • (2002) Genes Cells , vol.7 , pp. 11-17
    • Goto, H.1    Yasui, Y.2    Nigg, E.A.3    Inagaki, M.4
  • 77
    • 0031129933 scopus 로고    scopus 로고
    • DNA binding and nuclease protection by the HMf histones from the hyperthermophilic archaeon Methanothermus fervidus
    • R. A. Grayling K. A. Bailey J. N. Reeve DNA binding and nuclease protection by the HMf histones from the hyperthermophilic archaeon Methanothermus fervidus Extremophiles 1997 1 79 88
    • (1997) Extremophiles , vol.1 , pp. 79-88
    • Grayling, R.A.1    Bailey, K.A.2    Reeve, J.N.3
  • 80
    • 0025870123 scopus 로고
    • Chlamydia trachomatis developmentally regulated protein is homologous to eukaryotic histone H1
    • T. Hackstadt W. Baehr Y. Ying Chlamydia trachomatis developmentally regulated protein is homologous to eukaryotic histone H1 Proc. Natl. Acad. Sci. U. S. A. 1991 88 3937 3941
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 3937-3941
    • Hackstadt, T.1    Baehr, W.2    Ying, Y.3
  • 83
    • 0036847620 scopus 로고    scopus 로고
    • Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes
    • A. H. Hassan P. Prochasson K. E. Neely S. C. Galasinski M. Chandy M. J. Carrozza J. L. Workman Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes Cell 2002 111 369 379
    • (2002) Cell , vol.111 , pp. 369-379
    • Hassan, A.H.1    Prochasson, P.2    Neely, K.E.3    Galasinski, S.C.4    Chandy, M.5    Carrozza, M.J.6    Workman, J.L.7
  • 84
    • 0014965051 scopus 로고
    • Structure of nuclei acid-poly base complexes
    • M. Haynes R. A. Garret W. B. Gratzer Structure of nuclei acid-poly base complexes Biochemistry 1970 9 4410 4416
    • (1970) Biochemistry , vol.9 , pp. 4410-4416
    • Haynes, M.1    Garret, R.A.2    Gratzer, W.B.3
  • 85
    • 34247272005 scopus 로고    scopus 로고
    • The DNA structure responds differently to physiological concentrations of K+ or Na+
    • B. Heddi N. Foloppe E. Hantz B. Hartmann The DNA structure responds differently to physiological concentrations of K+ or Na+ J. Mol. Biol. 2007 368 1403 1411
    • (2007) J. Mol. Biol. , vol.368 , pp. 1403-1411
    • Heddi, B.1    Foloppe, N.2    Hantz, E.3    Hartmann, B.4
  • 86
    • 0030828073 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation
    • M. J. Hendzel Y. Wei M. A. Mancini A. Van Hooser T. Ranalli B. R. Brinkley D. P. Bazett-Jones C. D. Allis Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation Chromosoma 1997 106 348 360
    • (1997) Chromosoma , vol.106 , pp. 348-360
    • Hendzel, M.J.1    Wei, Y.2    Mancini, M.A.3    Van Hooser, A.4    Ranalli, T.5    Brinkley, B.R.6    Bazett-Jones, D.P.7    Allis, C.D.8
  • 88
    • 0034652329 scopus 로고    scopus 로고
    • Closing the ring: Links between SMC proteins and chromosome partitioning, condensation, and supercoiling
    • V. F. Holmes N. R. Cozzarelli Closing the ring: links between SMC proteins and chromosome partitioning, condensation, and supercoiling Proc. Natl. Acad. Sci. U. S. A. 2000 97 1322 1324
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1322-1324
    • Holmes, V.F.1    Cozzarelli, N.R.2
  • 89
    • 0000646401 scopus 로고    scopus 로고
    • Evidence of electrostatic attraction between equally charged macroions induced by divalent counterions
    • B. Hribar V. Vlachy Evidence of electrostatic attraction between equally charged macroions induced by divalent counterions J. Phys. Chem. B 1997 101 3457 3459
    • (1997) J. Phys. Chem. B , vol.101 , pp. 3457-3459
    • Hribar, B.1    Vlachy, V.2
  • 90
    • 0009299057 scopus 로고
    • Elastic model of DNA supercoiling in the infinite length limit
    • N. G. Hunt J. E. Hearst Elastic model of DNA supercoiling in the infinite length limit J. Chem. Phys. 1991 95 9329 9336
    • (1991) J. Chem. Phys. , vol.95 , pp. 9329-9336
    • Hunt, N.G.1    Hearst, J.E.2
  • 92
    • 25144434235 scopus 로고    scopus 로고
    • Topological interaction between cohesin rings and a circular minichromosome
    • D. Ivanov K. A. Nasmyth Topological interaction between cohesin rings and a circular minichromosome Cell 2005 122 849 860
    • (2005) Cell , vol.122 , pp. 849-860
    • Ivanov, D.1    Nasmyth, K.A.2
  • 93
    • 0346258292 scopus 로고    scopus 로고
    • Using electrostatic potentials to predict DNA-binding sites on DNA-binding proteins
    • S. Jones H. P. Shanahan H. M. Berman J. M. Thornton Using electrostatic potentials to predict DNA-binding sites on DNA-binding proteins Nucleic Acids Res. 2003 31 7189 7198
    • (2003) Nucleic Acids Res. , vol.31 , pp. 7189-7198
    • Jones, S.1    Shanahan, H.P.2    Berman, H.M.3    Thornton, J.M.4
  • 95
    • 60049095598 scopus 로고    scopus 로고
    • Counterion-mediated electrostatic interactions between helical molecules
    • M. Kanduc J. Dobnikar R. Podgornik Counterion-mediated electrostatic interactions between helical molecules Soft Matter 2009 5 868 877
    • (2009) Soft Matter , vol.5 , pp. 868-877
    • Kanduc, M.1    Dobnikar, J.2    Podgornik, R.3
  • 96
    • 77953604122 scopus 로고    scopus 로고
    • Counterion-mediated weak and strong coupling electrostatic interaction between like-charged cylindrical dielectrics
    • M. Kanduc A. Naji R. Podgornik Counterion-mediated weak and strong coupling electrostatic interaction between like-charged cylindrical dielectrics J. Chem. Phys. 2010 132 224703
    • (2010) J. Chem. Phys. , vol.132 , pp. 224703
    • Kanduc, M.1    Naji, A.2    Podgornik, R.3
  • 99
    • 0020021767 scopus 로고
    • Interactions of DNA with divalent metal ions. I. 31P-NMR studies
    • J. Granot J. Feigon D. R. Kearns Interactions of DNA with divalent metal ions. I. 31P-NMR studies Biopolymers 1982 21 181 201
    • (1982) Biopolymers , vol.21 , pp. 181-201
    • Granot, J.1    Feigon, J.2    Kearns, D.R.3
  • 100
    • 0020019204 scopus 로고
    • Interactions of DNA with divalent metal ions. II. Proton relaxation enhancement studies
    • J. Granot D. R. Kearns Interactions of DNA with divalent metal ions. II. Proton relaxation enhancement studies Biopolymers 1982 21 203 218
    • (1982) Biopolymers , vol.21 , pp. 203-218
    • Granot, J.1    Kearns, D.R.2
  • 101
    • 0020007066 scopus 로고
    • Interactions of DNA with divalent metal ions. III. Extent of metal binding: Experiment and theory
    • J. Granot D. R. Kearns Interactions of DNA with divalent metal ions. III. Extent of metal binding: experiment and theory Biopolymers 1982 21 219 232
    • (1982) Biopolymers , vol.21 , pp. 219-232
    • Granot, J.1    Kearns, D.R.2
  • 102
    • 0020136547 scopus 로고
    • Interactions of DNA with divalent metal ions. IV. Competitive studies of Mn2+ binding to AT- and GC-rich DNAs
    • J. Granot N. Assa-Munt D. R. Kearns Interactions of DNA with divalent metal ions. IV. Competitive studies of Mn2+ binding to AT- and GC-rich DNAs Biopolymers 1982 21 873 884
    • (1982) Biopolymers , vol.21 , pp. 873-884
    • Granot, J.1    Assa-Munt, N.2    Kearns, D.R.3
  • 103
    • 48249116182 scopus 로고    scopus 로고
    • Nucleosome geometry and internucleosomal interactions control the chromatin fiber conformation
    • N. Kepper D. Foethke R. Stehr G. Wedemann K. Rippe Nucleosome geometry and internucleosomal interactions control the chromatin fiber conformation Biophys. J. 2008 95 3692 3705
    • (2008) Biophys. J. , vol.95 , pp. 3692-3705
    • Kepper, N.1    Foethke, D.2    Stehr, R.3    Wedemann, G.4    Rippe, K.5
  • 104
    • 0033597962 scopus 로고    scopus 로고
    • 13S condensin actively reconfigures DNA by introducing global positive writhe: Implications for chromosome condensation
    • K. Kimura V. V. Rybenkov N. J. Crisona T. Hirano N. R. Cozzarelli 13S condensin actively reconfigures DNA by introducing global positive writhe: implications for chromosome condensation Cell 1999 98 239 248
    • (1999) Cell , vol.98 , pp. 239-248
    • Kimura, K.1    Rybenkov, V.V.2    Crisona, N.J.3    Hirano, T.4    Cozzarelli, N.R.5
  • 108
    • 18144376538 scopus 로고    scopus 로고
    • Electrostatic zipper-motif for DNA aggregation
    • A. A. Kornyshev S. Leikin Electrostatic zipper-motif for DNA aggregation Phys. Rev. Lett. 1999 82 4138 4141
    • (1999) Phys. Rev. Lett. , vol.82 , pp. 4138-4141
    • Kornyshev, A.A.1    Leikin, S.2
  • 109
    • 0035896663 scopus 로고    scopus 로고
    • Sequence recognition in the pairing of DNA duplexes
    • A. A. Kornyshev S. Leikin Sequence recognition in the pairing of DNA duplexes Phys. Rev. Lett. 2001 86 3666 3669
    • (2001) Phys. Rev. Lett. , vol.86 , pp. 3666-3669
    • Kornyshev, A.A.1    Leikin, S.2
  • 110
    • 34848842846 scopus 로고    scopus 로고
    • Physicochemical analysis of electrostatic foundation for DNA-protein interactions in chromatin transformations
    • N. Korolev O. V. Vorontsova L. Nordenskiöld Physicochemical analysis of electrostatic foundation for DNA-protein interactions in chromatin transformations Prog. Biophys. Mol. Biol. 2007 95 23 49
    • (2007) Prog. Biophys. Mol. Biol. , vol.95 , pp. 23-49
    • Korolev, N.1    Vorontsova, O.V.2    Nordenskiöld, L.3
  • 111
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • T. Kouzarides Histone methylation in transcriptional control Curr. Opin. Genet. Dev. 2002 12 198 209
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 112
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • T. Kouzarides Chromatin modifications and their function Cell 2007 128 693 705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 113
    • 0000564128 scopus 로고
    • Characterization of DNA condensates induced by poly(ethylene oxide) and polylysine
    • U. K. Laemmli Characterization of DNA condensates induced by poly(ethylene oxide) and polylysine Proc. Natl. Acad. Sci. U. S. A. 1975 72 4288 4292
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 4288-4292
    • Laemmli, U.K.1
  • 117
    • 34548829891 scopus 로고    scopus 로고
    • Chromatin polymorphism and the nucleosome superfamily: A genealogy
    • C. Lavelle A. Prunell Chromatin polymorphism and the nucleosome superfamily: a genealogy Cell Cycle 2007 6 2113 2119
    • (2007) Cell Cycle , vol.6 , pp. 2113-2119
    • Lavelle, C.1    Prunell, A.2
  • 118
    • 0013550357 scopus 로고    scopus 로고
    • DNA bending induced by the archaebacterial histone-like protein MC1
    • E. Le Cam F. Culard E. Larquet E. Delain J. A. Cognet DNA bending induced by the archaebacterial histone-like protein MC1 J. Mol. Biol. 1999 285 1011 1121
    • (1999) J. Mol. Biol. , vol.285 , pp. 1011-1121
    • Le Cam, E.1    Culard, F.2    Larquet, E.3    Delain, E.4    Cognet, J.A.5
  • 119
    • 67249125585 scopus 로고    scopus 로고
    • Structure of toroidal DNA collapsed inside the phage capsid
    • A. Leforestier F. Livolant Structure of toroidal DNA collapsed inside the phage capsid Proc. Natl. Acad. Sci. U. S. A. 2009 106 9157 91162
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 9157-91162
    • Leforestier, A.1    Livolant, F.2
  • 120
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • M. A. Lever J. P. Th'ng X. Sun M. J. Hendzel Rapid exchange of histone H1.1 on chromatin in living human cells Nature 2000 408 873 876
    • (2000) Nature , vol.408 , pp. 873-876
    • Lever, M.A.1    Th'Ng, J.P.2    Sun, X.3    Hendzel, M.J.4
  • 121
    • 0000345003 scopus 로고    scopus 로고
    • Electrostatic attraction and phase separation in solutions of like-charged colloidal particles
    • P. Linse V. Lobaskin Electrostatic attraction and phase separation in solutions of like-charged colloidal particles Phys. Rev. Lett. 1999 83 4208 4211
    • (1999) Phys. Rev. Lett. , vol.83 , pp. 4208-4211
    • Linse, P.1    Lobaskin, V.2
  • 122
    • 44949277387 scopus 로고
    • Ordered phases of DNA in vivo and in vitro
    • F. Livolant Ordered phases of DNA in vivo and in vitro Phys. A 1991 176 117 137
    • (1991) Phys. A , vol.176 , pp. 117-137
    • Livolant, F.1
  • 124
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • K. Luger A. W. Mäder R. K. Richmond D. F. Sargent T. J. Richmond Crystal structure of the nucleosome core particle at 2.8 Å resolution Nature 1997 389 251 260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 125
    • 33750527566 scopus 로고    scopus 로고
    • The architectural role of nucleoid-associated proteins in the organization of bacterial chromatin: A molecular perspective
    • M. S. Luijsterburg M. C. Noom G. J. Wuite R. T. Dame The architectural role of nucleoid-associated proteins in the organization of bacterial chromatin: a molecular perspective J. Struct. Biol. 2006 156 262 272
    • (2006) J. Struct. Biol. , vol.156 , pp. 262-272
    • Luijsterburg, M.S.1    Noom, M.C.2    Wuite, G.J.3    Dame, R.T.4
  • 126
    • 57749209893 scopus 로고    scopus 로고
    • The major architects of chromatin: Architectural proteins in bacteria, archaea and eukaryotes
    • M. S. Luijsterburg M. F. White R. van Driel R. T. Dame The major architects of chromatin: architectural proteins in bacteria, archaea and eukaryotes Crit. Rev. Biochem. Mol. Biol. 2008 43 393 418
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 393-418
    • Luijsterburg, M.S.1    White, M.F.2    Van Driel, R.3    Dame, R.T.4
  • 127
    • 0001270373 scopus 로고
    • Electron microscopic study of DNA complexes with proteins from the archaebacterium Sulfolobus acidocaldarius
    • R. Lurz M. Grote J. Dijk R. Reinhardt B. Dobrinski Electron microscopic study of DNA complexes with proteins from the archaebacterium Sulfolobus acidocaldarius EMBO J. 1986 5 3715 3721
    • (1986) EMBO J , vol.5 , pp. 3715-3721
    • Lurz, R.1    Grote, M.2    Dijk, J.3    Reinhardt, R.4    Dobrinski, B.5
  • 128
    • 77954819238 scopus 로고    scopus 로고
    • Chromatin structure: Does the 30-nm fibre exist in vivo?
    • K. Maeshima S. Hihara M. Eltsov Chromatin structure: does the 30-nm fibre exist in vivo? Curr. Opin. Cell Biol. 2010 22 291 297
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 291-297
    • Maeshima, K.1    Hihara, S.2    Eltsov, M.3
  • 129
  • 130
    • 0037379723 scopus 로고    scopus 로고
    • X-ray diffraction characterization of the dense phases formed by nucleosome core particles
    • S. Mangenot A. Leforestier D. Durand F. Livolant X-ray diffraction characterization of the dense phases formed by nucleosome core particles Biophys. J. 2003 84 2570 2584
    • (2003) Biophys. J. , vol.84 , pp. 2570-2584
    • Mangenot, S.1    Leforestier, A.2    Durand, D.3    Livolant, F.4
  • 131
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • G. S. Manning The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides Q. Rev. Biophys. 1978 11 179 246
    • (1978) Q. Rev. Biophys. , vol.11 , pp. 179-246
    • Manning, G.S.1
  • 132
    • 33751233867 scopus 로고    scopus 로고
    • The persistence length of DNA is reached from the persistence length of its null isomer through an internal electrostatic stretching force
    • G. S. Manning The persistence length of DNA is reached from the persistence length of its null isomer through an internal electrostatic stretching force Biophys. J. 2006 91 3607 3616
    • (2006) Biophys. J. , vol.91 , pp. 3607-3616
    • Manning, G.S.1
  • 133
    • 84855854479 scopus 로고    scopus 로고
    • Counterion condensation theory of attraction between like charges in the absence of multivalent counterions
    • G. S. Manning Counterion condensation theory of attraction between like charges in the absence of multivalent counterions Eur. Phys. J. E 2011 34 132
    • (2011) Eur. Phys. J. e , vol.34 , pp. 132
    • Manning, G.S.1
  • 134
    • 79955812312 scopus 로고    scopus 로고
    • Conformational analysis and estimation of the persistence length of DNA using atomic force microscopy in solution
    • S. Mantelli P. Muller S. Harlepp M. Maaloum Conformational analysis and estimation of the persistence length of DNA using atomic force microscopy in solution Soft Matter 2011 7 3412 3416
    • (2011) Soft Matter , vol.7 , pp. 3412-3416
    • Mantelli, S.1    Muller, P.2    Harlepp, S.3    Maaloum, M.4
  • 135
    • 0037163112 scopus 로고    scopus 로고
    • Archaeal histone tetramerization determines DNA affinity and the direction of DNA supercoiling
    • F. Marc K. Sandman R. Lurz J. N. Reeve Archaeal histone tetramerization determines DNA affinity and the direction of DNA supercoiling J. Biol. Chem. 2000 277 30879 30886
    • (2000) J. Biol. Chem. , vol.277 , pp. 30879-30886
    • Marc, F.1    Sandman, K.2    Lurz, R.3    Reeve, J.N.4
  • 136
    • 22344457857 scopus 로고    scopus 로고
    • Histone H1 is essential for mitotic chromosome architecture and segregation in Xenopus laevis egg extracts
    • T. J. Maresca B. S. Freedman R. Heald Histone H1 is essential for mitotic chromosome architecture and segregation in Xenopus laevis egg extracts J. Cell Biol. 2005 169 859 869
    • (2005) J. Cell Biol. , vol.169 , pp. 859-869
    • Maresca, T.J.1    Freedman, B.S.2    Heald, R.3
  • 138
    • 0023009428 scopus 로고
    • The condensation of chromatin and histone H1-depleted chromatin by spermine
    • R. Marquet P. Colson C. Houssier The condensation of chromatin and histone H1-depleted chromatin by spermine J. Biomol. Struct. Dyn. 1986 4 205 218
    • (1986) J. Biomol. Struct. Dyn. , vol.4 , pp. 205-218
    • Marquet, R.1    Colson, P.2    Houssier, C.3
  • 139
    • 0023894721 scopus 로고
    • Comparative study of the condensation of chicken erythrocyte and calf thymus chromatins by di- and multivalent cations
    • R. Marquet P. Colson A. M. Matton C. Houssier M. Thiry G. Goessens Comparative study of the condensation of chicken erythrocyte and calf thymus chromatins by di- and multivalent cations J. Biomol. Struct. Dyn. 1988 5 839 857
    • (1988) J. Biomol. Struct. Dyn. , vol.5 , pp. 839-857
    • Marquet, R.1    Colson, P.2    Matton, A.M.3    Houssier, C.4    Thiry, M.5    Goessens, G.6
  • 140
    • 0025744180 scopus 로고
    • Thermodynamics of cation-induced DNA condensation
    • R. Marquet C. Houssier Thermodynamics of cation-induced DNA condensation J. Biomol. Struct. Dyn. 1991 9 159 167
    • (1991) J. Biomol. Struct. Dyn. , vol.9 , pp. 159-167
    • Marquet, R.1    Houssier, C.2
  • 141
    • 0021801395 scopus 로고
    • An electro-optical study of the mechanisms of DNA condensation induced by spermine
    • R. Marquet C. Houssier E. Fredericq An electro-optical study of the mechanisms of DNA condensation induced by spermine Biochim. Biophys. Acta 1985 825 365 374
    • (1985) Biochim. Biophys. Acta , vol.825 , pp. 365-374
    • Marquet, R.1    Houssier, C.2    Fredericq, E.3
  • 142
    • 0037178127 scopus 로고    scopus 로고
    • Thermodynamics of cationic lipid binding to DNA and DNA condensation: Roles of electrostatics and hydrophobicity
    • D. Matulis I. Rouzina V. A. Bloomfield Thermodynamics of cationic lipid binding to DNA and DNA condensation: roles of electrostatics and hydrophobicity J. Am. Chem. Soc. 2002 124 7331 7342
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 7331-7342
    • Matulis, D.1    Rouzina, I.2    Bloomfield, V.A.3
  • 143
    • 39849091053 scopus 로고    scopus 로고
    • Bridging like-charged macroions through long divalent rod-like ions
    • S. May A. Igli J. Rescic S. Maset K. Bohinc Bridging like-charged macroions through long divalent rod-like ions J. Phys. Chem. B 2008 112 1685 1692
    • (2008) J. Phys. Chem. B , vol.112 , pp. 1685-1692
    • May, S.1    Igli, A.2    Rescic, J.3    Maset, S.4    Bohinc, K.5
  • 144
    • 81355137935 scopus 로고    scopus 로고
    • Compartmentalization of the nucleus
    • L. Meldi J. H. Brickner Compartmentalization of the nucleus Trends Cell Biol. 2011 21 701 708
    • (2011) Trends Cell Biol. , vol.21 , pp. 701-708
    • Meldi, L.1    Brickner, J.H.2
  • 145
    • 48449105537 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen and ASF1 modulate silent chromatin in Saccharomyces cerevisiae via lysine 56 on histone H3
    • A. Miller B. Yang T. Foster A. L. Kirchmaier Proliferating cell nuclear antigen and ASF1 modulate silent chromatin in Saccharomyces cerevisiae via lysine 56 on histone H3 Genetics 2008 179 793 809
    • (2008) Genetics , vol.179 , pp. 793-809
    • Miller, A.1    Yang, B.2    Foster, T.3    Kirchmaier, A.L.4
  • 146
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • T. Misteli A. Gunjan R. Hock M. Bustin D. T. Brown Dynamic binding of histone H1 to chromatin in living cells Nature 2000 408 877 881
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 147
    • 0036590901 scopus 로고    scopus 로고
    • Simulations of counterions at charged plates
    • A. Moreira R. R. Netz Simulations of counterions at charged plates Eur. Phys. J. E 2002 8 33 58
    • (2002) Eur. Phys. J. e , vol.8 , pp. 33-58
    • Moreira, A.1    Netz, R.R.2
  • 149
    • 61349129512 scopus 로고    scopus 로고
    • Measurement of the torque on a single stretched and twisted DNA using magnetic tweezers
    • F. Mosconi J. F. Allemand D. Bensimon V. Croquette Measurement of the torque on a single stretched and twisted DNA using magnetic tweezers Phys. Rev. Lett. 2009 102 078301
    • (2009) Phys. Rev. Lett. , vol.102 , pp. 078301
    • Mosconi, F.1    Allemand, J.F.2    Bensimon, D.3    Croquette, V.4
  • 150
    • 30644479149 scopus 로고    scopus 로고
    • A physical model for the condensation and decondensation of eukaryotic chromosomes
    • J. Mozziconacci C. Lavelle M. Barbi A. Lesne J. M. Victor A physical model for the condensation and decondensation of eukaryotic chromosomes FEBS Lett. 2006 580 368 372
    • (2006) FEBS Lett. , vol.580 , pp. 368-372
    • Mozziconacci, J.1    Lavelle, C.2    Barbi, M.3    Lesne, A.4    Victor, J.M.5
  • 151
    • 34547858913 scopus 로고    scopus 로고
    • Structure and acetyl-lysine recognition of the bromodomain
    • S. Mujtaba L. Zeng M. M. Zhou Structure and acetyl-lysine recognition of the bromodomain Oncogene 2007 26 5521 5527
    • (2007) Oncogene , vol.26 , pp. 5521-5527
    • Mujtaba, S.1    Zeng, L.2    Zhou, M.M.3
  • 153
    • 0033485515 scopus 로고    scopus 로고
    • The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition
    • F. V. T. Murphy R. M. Sweet M. E. Churchill The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition EMBO J. 1999 18 6610 6618
    • (1999) EMBO J , vol.18 , pp. 6610-6618
    • Murphy, F.V.T.1    Sweet, R.M.2    Churchill, M.E.3
  • 154
    • 0025885691 scopus 로고
    • DNA binding by the archaeal histone HMf results in positive supercoiling
    • D. R. Musgrave K. M. Sandman J. N. Reeve DNA binding by the archaeal histone HMf results in positive supercoiling Proc. Natl. Acad. Sci. U. S. A. 1991 88 10397 10401
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 10397-10401
    • Musgrave, D.R.1    Sandman, K.M.2    Reeve, J.N.3
  • 155
  • 156
    • 2442437667 scopus 로고    scopus 로고
    • Attraction of like-charged macroions in the strong-coupling limit
    • A. Naji R. R. Netz Attraction of like-charged macroions in the strong-coupling limit Eur. Phys. J. E 2004 13 43 59
    • (2004) Eur. Phys. J. e , vol.13 , pp. 43-59
    • Naji, A.1    Netz, R.R.2
  • 157
    • 0001552389 scopus 로고    scopus 로고
    • Electrostatistics of counter-ions at and between planar charged walls: From Poisson-Boltzmann to the strong-coupling theory
    • R. R. Netz Electrostatistics of counter-ions at and between planar charged walls: from Poisson-Boltzmann to the strong-coupling theory Eur. Phys. J. E 2001 5 557 574
    • (2001) Eur. Phys. J. e , vol.5 , pp. 557-574
    • Netz, R.R.1
  • 158
    • 0001020827 scopus 로고    scopus 로고
    • Poisson Boltzmann: Fluctuations effects and correlation functions
    • R. R. Netz H. Orland Beyond Poisson Boltzmann: fluctuations effects and correlation functions Eur. Phys. J. E 2000 1 203 214
    • (2000) Eur. Phys. J. e , vol.1 , pp. 203-214
    • Netz, R.R.1    Orland Beyond, H.2
  • 159
    • 0000595881 scopus 로고    scopus 로고
    • Wall-mediated forces between like-charged bodies in an electrolyte
    • J. C. Neu Wall-mediated forces between like-charged bodies in an electrolyte Phys. Rev. Lett. 1999 82 1072 1075
    • (1999) Phys. Rev. Lett. , vol.82 , pp. 1072-1075
    • Neu, J.C.1
  • 160
    • 19744364369 scopus 로고    scopus 로고
    • Extracting DNA twist rigidity from experimental supercoiling data
    • S. Neukirch Extracting DNA twist rigidity from experimental supercoiling data Phys. Rev. Lett. 2004 93 198107
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 198107
    • Neukirch, S.1
  • 161
    • 79960647806 scopus 로고    scopus 로고
    • Analytical description of extension, torque, and supercoiling radius of a stretched twisted DNA
    • S. Neukirch J. F. Marko Analytical description of extension, torque, and supercoiling radius of a stretched twisted DNA Phys. Rev. Lett. 2011 106 138104
    • (2011) Phys. Rev. Lett. , vol.106 , pp. 138104
    • Neukirch, S.1    Marko, J.F.2
  • 162
    • 0032514107 scopus 로고    scopus 로고
    • Osmotic compaction of supercoiled DNA into a bacterial nucleoid
    • T. Odijk Osmotic compaction of supercoiled DNA into a bacterial nucleoid Biophys. Chem. 1998 73 23 29
    • (1998) Biophys. Chem. , vol.73 , pp. 23-29
    • Odijk, T.1
  • 163
    • 0015222984 scopus 로고
    • Model nucleohistones: The interaction of F1 and F2al histones with native T7 DNA
    • D. E. Olins A. L. Olins Model nucleohistones: the interaction of F1 and F2al histones with native T7 DNA J. Mol. Biol. 1971 57 437 455
    • (1971) J. Mol. Biol. , vol.57 , pp. 437-455
    • Olins, D.E.1    Olins, A.L.2
  • 164
    • 79956222517 scopus 로고    scopus 로고
    • Identification, chemical synthesis, and biological functions of unusual polyamines produced by extreme thermophiles
    • T. Oshima T. Moriya Y. Terui Identification, chemical synthesis, and biological functions of unusual polyamines produced by extreme thermophiles Methods Mol. Biol. 2011 720 81 111
    • (2011) Methods Mol. Biol. , vol.720 , pp. 81-111
    • Oshima, T.1    Moriya, T.2    Terui, Y.3
  • 166
    • 67651207419 scopus 로고    scopus 로고
    • Poisson-Boltzmann for oppositely charged bodies: An explicit derivation
    • F. Paillusson M. Barbi J. M. Victor Poisson-Boltzmann for oppositely charged bodies: an explicit derivation J. Chem. Phys. 2009 107 1379 1391
    • (2009) J. Chem. Phys. , vol.107 , pp. 1379-1391
    • Paillusson, F.1    Barbi, M.2    Victor, J.M.3
  • 168
  • 169
    • 9744245199 scopus 로고    scopus 로고
    • NMR solution structure of the archaebacterial chromosomal protein MC1 reveals a new protein fold
    • F. Paquet F. Culard F. Barbault J. C. Maurizot G. Lancelot NMR solution structure of the archaebacterial chromosomal protein MC1 reveals a new protein fold Biochemistry 2004 43 14971 14978
    • (2004) Biochemistry , vol.43 , pp. 14971-14978
    • Paquet, F.1    Culard, F.2    Barbault, F.3    Maurizot, J.C.4    Lancelot, G.5
  • 171
    • 0015396878 scopus 로고
    • On the electrostatic interaction across a salt solution between two bodies bearing unequal charges
    • V. A. Parsegian D. Gingell On the electrostatic interaction across a salt solution between two bodies bearing unequal charges Biophys. J. 1972 12 1192 1204
    • (1972) Biophys. J. , vol.12 , pp. 1192-1204
    • Parsegian, V.A.1    Gingell, D.2
  • 172
    • 0027216519 scopus 로고
    • The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures
    • T. T. Paull M. J. Haykinson R. C. Johnson The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures Genes Dev. 1993 7 1521 1534
    • (1993) Genes Dev. , vol.7 , pp. 1521-1534
    • Paull, T.T.1    Haykinson, M.J.2    Johnson, R.C.3
  • 173
    • 0017652886 scopus 로고
    • The structure of histone-depleted metaphase chromosomes
    • J. R. Paulson U. K. Laemmli The structure of histone-depleted metaphase chromosomes Cell 1977 12 817 828
    • (1977) Cell , vol.12 , pp. 817-828
    • Paulson, J.R.1    Laemmli, U.K.2
  • 175
  • 176
    • 84879171166 scopus 로고    scopus 로고
    • Evolutionary origin of the cell nucleus and its functional architecture
    • J. Postberg H. J. Lipps T. Cremer Evolutionary origin of the cell nucleus and its functional architecture Essays Biochem. 2010 48 1 24
    • (2010) Essays Biochem. , vol.48 , pp. 1-24
    • Postberg, J.1    Lipps, H.J.2    Cremer, T.3
  • 179
    • 78650751760 scopus 로고    scopus 로고
    • Divalent counterion-induced condensation of triple-strand DNA
    • X. Qiu V. A. Parsegian D. C. Rau Divalent counterion-induced condensation of triple-strand DNA Proc. Natl. Acad. Sci. U. S. A. 2010 107 21482 21486
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 21482-21486
    • Qiu, X.1    Parsegian, V.A.2    Rau, D.C.3
  • 180
    • 0028466084 scopus 로고
    • An attractive force between two rodlike polyions mediated by the sharing of condensed counterions
    • J. Ray G. S. Manning An attractive force between two rodlike polyions mediated by the sharing of condensed counterions Langmuir 1994 10 2450 2461
    • (1994) Langmuir , vol.10 , pp. 2450-2461
    • Ray, J.1    Manning, G.S.2
  • 181
  • 182
    • 74549187994 scopus 로고    scopus 로고
    • Nuclear functions of the HMG proteins
    • R. Reeves Nuclear functions of the HMG proteins Biochim. Biophys. Acta 2010 1799 3 14
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 3-14
    • Reeves, R.1
  • 183
    • 0024431827 scopus 로고
    • Assembly of nucleosomes and chromatin in vitro
    • D. Rhodes R. A. Laskey Assembly of nucleosomes and chromatin in vitro Methods Enzymol. 1989 170 575 585
    • (1989) Methods Enzymol. , vol.170 , pp. 575-585
    • Rhodes, D.1    Laskey, R.A.2
  • 184
    • 0015839714 scopus 로고
    • The ionic strength of DNA packing within bacteriophage heads
    • K. E. Richards P. C. Williams R. Calendar The ionic strength of DNA packing within bacteriophage heads J. Mol. Biol. 1973 78 255 259
    • (1973) J. Mol. Biol. , vol.78 , pp. 255-259
    • Richards, K.E.1    Williams, P.C.2    Calendar, R.3
  • 185
    • 0017803051 scopus 로고
    • Packaging of DNA in bacteriophage heads: Some considerations on energetics
    • S. C. Riemer V. A. Bloomfield Packaging of DNA in bacteriophage heads: some considerations on energetics Biopolymers 1978 17 785 794
    • (1978) Biopolymers , vol.17 , pp. 785-794
    • Riemer, S.C.1    Bloomfield, V.A.2
  • 186
    • 1842453825 scopus 로고    scopus 로고
    • Structure of the histone-like protein H-NS and its role in regulation and genome superstructure
    • S. Rimsky Structure of the histone-like protein H-NS and its role in regulation and genome superstructure Curr. Opin. Microbiol. 2004 7 109 114
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 109-114
    • Rimsky, S.1
  • 187
    • 33746675190 scopus 로고    scopus 로고
    • Single-molecule experiments in biological physics: Methods and application
    • F. Ritort Single-molecule experiments in biological physics: methods and application J. Phys.: Condens. Matter 2006 18 R351 R358
    • (2006) J. Phys.: Condens. Matter , vol.18
    • Ritort, F.1
  • 188
    • 33646242052 scopus 로고    scopus 로고
    • EM measurements define the dimensions of the "30-nm" chromatin fiber: Evidence for a compact, interdigitated structure
    • P. J. J. Robinson L. Fairall V. A. T. Huynh D. Rhodes EM measurements define the dimensions of the "30-nm" chromatin fiber: evidence for a compact, interdigitated structure Proc. Natl. Acad. Sci. U. S. A. 2007 103 6506 6511
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 6506-6511
    • Robinson, P.J.J.1    Fairall, L.2    Huynh, V.A.T.3    Rhodes, D.4
  • 189
    • 48249103503 scopus 로고    scopus 로고
    • Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure
    • A. Routh S. Sandin D. Rhodes Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure Proc. Natl. Acad. Sci. U. S. A. 2008 105 8872 8877
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 8872-8877
    • Routh, A.1    Sandin, S.2    Rhodes, D.3
  • 190
    • 0030572245 scopus 로고    scopus 로고
    • Macroion attraction due to electrostatic correlation between screening counterions. I. Mobile surface-adsorbed ions and diffuse ion cloud
    • I. Rouzina V. A. Bloomfield Macroion attraction due to electrostatic correlation between screening counterions. I. Mobile surface-adsorbed ions and diffuse ion cloud J. Phys. Chem. 1996 100 9977 9989
    • (1996) J. Phys. Chem. , vol.100 , pp. 9977-9989
    • Rouzina, I.1    Bloomfield, V.A.2
  • 191
    • 0345055328 scopus 로고    scopus 로고
    • DNA bending by small, mobile multivalent cations
    • I. Rouzina V. A. Bloomfield DNA bending by small, mobile multivalent cations Biophys. J. 1998 74 3152 3164
    • (1998) Biophys. J. , vol.74 , pp. 3152-3164
    • Rouzina, I.1    Bloomfield, V.A.2
  • 193
    • 0030740986 scopus 로고    scopus 로고
    • The effect of ionic conditions on DNA helical repeat, effective diameter and free energy of supercoiling
    • V. V. Rybenkov A. V. Vologodskii N. R. Cozzarelli The effect of ionic conditions on DNA helical repeat, effective diameter and free energy of supercoiling Nucleic Acids Res. 1997 25 1412 1418
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1412-1418
    • Rybenkov, V.V.1    Vologodskii, A.V.2    Cozzarelli, N.R.3
  • 194
    • 0033134103 scopus 로고    scopus 로고
    • Long-range electrostatic attractions between identically charged particles in confined geometries: An unresolved problem
    • J. E. Sader D. Y. C. Chan Long-range electrostatic attractions between identically charged particles in confined geometries: an unresolved problem J. Colloid Interface Sci. 1999 213 268 269
    • (1999) J. Colloid Interface Sci. , vol.213 , pp. 268-269
    • Sader, J.E.1    Chan, D.Y.C.2
  • 195
    • 80054874399 scopus 로고    scopus 로고
    • Wigner-crystal formulation of strong-coupling theory for counterions near planar charged interfaces
    • L. Samaj E. Trizac Wigner-crystal formulation of strong-coupling theory for counterions near planar charged interfaces Phys. Rev. E: Stat., Nonlinear, Soft Matter Phys. 2011 84 041401
    • (2011) Phys. Rev. E: Stat., Nonlinear, Soft Matter Phys. , vol.84 , pp. 041401
    • Samaj, L.1    Trizac, E.2
  • 196
    • 79951789040 scopus 로고    scopus 로고
    • Counterions at highly charged interfaces: From one plate to like-charge attraction
    • L. Samaj E. Trizac Counterions at highly charged interfaces: from one plate to like-charge attraction Phys. Rev. Lett. 2011 106 078301
    • (2011) Phys. Rev. Lett. , vol.106 , pp. 078301
    • Samaj, L.1    Trizac, E.2
  • 197
    • 0025301592 scopus 로고
    • HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones
    • K. Sandman J. A. Krzycki B. Dobrinski R. Lurz J. N. Reeve HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones Proc. Natl. Acad. Sci. U. S. A. 1990 87 5788 5791
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 5788-5791
    • Sandman, K.1    Krzycki, J.A.2    Dobrinski, B.3    Lurz, R.4    Reeve, J.N.5
  • 198
    • 84943003803 scopus 로고    scopus 로고
    • Histone-encoding genes from Pyrococcus: Evidence for members of the HMf family of archaeal histones in a non-methanogenic Archaeon
    • K. Sandman F. P. Perler J. N. Reeve Histone-encoding genes from Pyrococcus: evidence for members of the HMf family of archaeal histones in a non-methanogenic Archaeon Curr. Opin. Microbiol. 2006 285 1011 1021
    • (2006) Curr. Opin. Microbiol. , vol.285 , pp. 1011-1021
    • Sandman, K.1    Perler, F.P.2    Reeve, J.N.3
  • 199
    • 0028130396 scopus 로고
    • Archaeal histones and the origin of the histone fold
    • K. Sandman J. N. Reeve Archaeal histones and the origin of the histone fold Gene 1994 150 207 208
    • (1994) Gene , vol.150 , pp. 207-208
    • Sandman, K.1    Reeve, J.N.2
  • 200
    • 33751005022 scopus 로고    scopus 로고
    • Electrostatic, steric, and hydration interactions favor Na++ condensation around DNA compared with K+
    • A. Savelyev G. A. Papoian Electrostatic, steric, and hydration interactions favor Na++ condensation around DNA compared with K + J. Am. Chem. Soc. 2006 28 14506 14518
    • (2006) J. Am. Chem. Soc. , vol.28 , pp. 14506-14518
    • Savelyev, A.1    Papoian, G.A.2
  • 201
    • 82555175927 scopus 로고    scopus 로고
    • Is DNA's rigidity dominated by electrostatic or nonelectrostatic interactions?
    • A. Savelyev C. K. Materese G. A. Papoian Is DNA's rigidity dominated by electrostatic or nonelectrostatic interactions? J. Am. Chem. Soc. 2011 133 19290 19293
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19290-19293
    • Savelyev, A.1    Materese, C.K.2    Papoian, G.A.3
  • 202
    • 84856748887 scopus 로고    scopus 로고
    • Do monovalent mobile ions affect DNA's flexibility at high salt content?
    • A. Savelyev Do monovalent mobile ions affect DNA's flexibility at high
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 2250-2254
    • Savelyev, A.1
  • 203
    • 84860564636 scopus 로고    scopus 로고
    • Nucleosomes stacked with aligned dyad axes are found in native compact chromatin in vitro
    • M. P. Scheffer M. Eltsov J. Bednar A. S. Frangakis Nucleosomes stacked with aligned dyad axes are found in native compact chromatin in vitro J. Struct. Biol. 2012 178 2 207 214
    • (2012) J. Struct. Biol. , vol.178 , Issue.2 , pp. 207-214
    • Scheffer, M.P.1    Eltsov, M.2    Bednar, J.3    Frangakis, A.S.4
  • 204
    • 80054774248 scopus 로고    scopus 로고
    • Evidence for short-range helical order in the 30-nm chromatin fibers of erythrocyte nuclei
    • M. P. Scheffer M. Eltsov A. S. Frangakis Evidence for short-range helical order in the 30-nm chromatin fibers of erythrocyte nuclei Proc. Natl. Acad. Sci. U. S. A. 2011 108 16992 16997
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 16992-16997
    • Scheffer, M.P.1    Eltsov, M.2    Frangakis, A.S.3
  • 207
    • 18344392110 scopus 로고    scopus 로고
    • Wigner crystal model of counterion induced bundle formation of rodlike polyelectrolytes
    • B. I. Shklovskii Wigner crystal model of counterion induced bundle formation of rodlike polyelectrolytes Phys. Rev. Lett. 1999 82 3268 3271
    • (1999) Phys. Rev. Lett. , vol.82 , pp. 3268-3271
    • Shklovskii, B.I.1
  • 208
  • 209
    • 7244245362 scopus 로고    scopus 로고
    • Micromechanical analysis of the binding of DNA-bending proteins HMGB1, NHP6A, and HU reveals their ability to form highly stable DNA-protein complexes
    • D. Skoko B. Wong R. C. Johnson J. F. Marko Micromechanical analysis of the binding of DNA-bending proteins HMGB1, NHP6A, and HU reveals their ability to form highly stable DNA-protein complexes Biochemistry 2004 43 13867 13874
    • (2004) Biochemistry , vol.43 , pp. 13867-13874
    • Skoko, D.1    Wong, B.2    Johnson, R.C.3    Marko, J.F.4
  • 210
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage straight phi29 portal motor can package DNA against a large internal force
    • D. E. Smith S. J. Tans S. B. Smith S. Grimes D. L. Anderson C. Bustamante The bacteriophage straight phi29 portal motor can package DNA against a large internal force Nature 2001 413 748 752
    • (2001) Nature , vol.413 , pp. 748-752
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 211
    • 0037853298 scopus 로고    scopus 로고
    • Conserved eukaryotic histone-fold residues substituted into an Archaeal histone increase DNA affinity but reduce complex flexibility
    • D. J. Soares F. Marc J. N. Reeve Conserved eukaryotic histone-fold residues substituted into an Archaeal histone increase DNA affinity but reduce complex flexibility J. Bacteriol. 2003 185 3453 3457
    • (2003) J. Bacteriol. , vol.185 , pp. 3453-3457
    • Soares, D.J.1    Marc, F.2    Reeve, J.N.3
  • 212
    • 77957836421 scopus 로고    scopus 로고
    • Protein acetylation in archaea, bacteria, and eukaryotes
    • J. Soppa Protein acetylation in archaea, bacteria, and eukaryotes Archaea 2010 2010 820681
    • (2010) Archaea , vol.2010 , pp. 820681
    • Soppa, J.1
  • 213
    • 34247517469 scopus 로고    scopus 로고
    • DNA-protein interactions and bacterial chromosome architecture
    • J. Stavans A. Oppenheim DNA-protein interactions and bacterial chromosome architecture Phys. Biol. 2006 3 R1 R10
    • (2006) Phys. Biol. , vol.3
    • Stavans, J.1    Oppenheim, A.2
  • 214
    • 0024467735 scopus 로고
    • Reconstitution of chromatin from purified components
    • A. Stein Reconstitution of chromatin from purified components Methods Enzymol. 1989 170 585 603
    • (1989) Methods Enzymol. , vol.170 , pp. 585-603
    • Stein, A.1
  • 215
    • 0017389770 scopus 로고
    • Interactions of highly charged colloidal cylinders with applications to double-stranded DNA
    • D. Stigter Interactions of highly charged colloidal cylinders with applications to double-stranded DNA Biopolymers 1977 16 1435 1448
    • (1977) Biopolymers , vol.16 , pp. 1435-1448
    • Stigter, D.1
  • 216
    • 0035842899 scopus 로고    scopus 로고
    • Cation-chromatin binding as shown by ion microscopy is essential for the structural integrity of chromosomes
    • R. Strick P. L. Strissel K. Gavrilov R. Levi-Setti Cation-chromatin binding as shown by ion microscopy is essential for the structural integrity of chromosomes J. Cell Biol. 2001 155 899 910
    • (2001) J. Cell Biol. , vol.155 , pp. 899-910
    • Strick, R.1    Strissel, P.L.2    Gavrilov, K.3    Levi-Setti, R.4
  • 217
    • 0033538531 scopus 로고    scopus 로고
    • Fundamentally different logic of gene regulation in prokaryotes and eukaryotes
    • K. Struhl Fundamentally different logic of gene regulation in prokaryotes and eukaryotes Cell 1999 98 1 4
    • (1999) Cell , vol.98 , pp. 1-4
    • Struhl, K.1
  • 218
    • 0041312645 scopus 로고    scopus 로고
    • Flexible DNA bending in HU-DNA cocrystal structures
    • K. K. Swinger K. M. Lemberg Y. Zhang P. A. Rice Flexible DNA bending in HU-DNA cocrystal structures EMBO J. 2003 22 3749 3760
    • (2003) EMBO J , vol.22 , pp. 3749-3760
    • Swinger, K.K.1    Lemberg, K.M.2    Zhang, Y.3    Rice, P.A.4
  • 219
    • 77949874234 scopus 로고    scopus 로고
    • Histone variants - Ancient wrap artists of the epigenome
    • P. B. Talbert S. Henikoff Histone variants - ancient wrap artists of the epigenome Nat. Rev. Mol. Cell Biol. 2010 11 264 275
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 264-275
    • Talbert, P.B.1    Henikoff, S.2
  • 220
    • 0027172958 scopus 로고
    • Properties of DNA-binding of HU heterotypic and homotypic dimers from Escherichia coli
    • H. Tanaka N. Goshima K. Kohno Y. Kano F. Imamoto Properties of DNA-binding of HU heterotypic and homotypic dimers from Escherichia coli J. Biochem. 1993 113 568 572
    • (1993) J. Biochem. , vol.113 , pp. 568-572
    • Tanaka, H.1    Goshima, N.2    Kohno, K.3    Kano, Y.4    Imamoto, F.5
  • 222
    • 0343340048 scopus 로고    scopus 로고
    • Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA
    • A. Tapias G. Lopez S. Ayora Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA Nucleic Acids Res. 2000 28 552 559
    • (2000) Nucleic Acids Res. , vol.28 , pp. 552-559
    • Tapias, A.1    Lopez, G.2    Ayora, S.3
  • 224
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • F. Thoma T. Koller A. Klug Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin J. Cell Biol. 1979 83 403 427
    • (1979) J. Cell Biol. , vol.83 , pp. 403-427
    • Thoma, F.1    Koller, T.2    Klug, A.3
  • 225
    • 0035281548 scopus 로고    scopus 로고
    • HMG1 and 2, and related 'architectural' DNA-binding proteins
    • J. O. Thomas A. A. Travers HMG1 and 2, and related 'architectural' DNA-binding proteins Trends Biochem. Sci. 2001 26 167 174
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 167-174
    • Thomas, J.O.1    Travers, A.A.2
  • 226
    • 67650409769 scopus 로고    scopus 로고
    • Screen for DNA-damage-responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells
    • J. V. Tjeertes K. M. Miller S. P. Jackson Screen for DNA-damage- responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells EMBO J. 2009 28 1878 1889
    • (2009) EMBO J , vol.28 , pp. 1878-1889
    • Tjeertes, J.V.1    Miller, K.M.2    Jackson, S.P.3
  • 227
    • 77949511946 scopus 로고    scopus 로고
    • Helical chirality: A link between local interactions and global topology in DNA
    • Y. Timsit P. Varnai Helical chirality: a link between local interactions and global topology in DNA PLoS One 2010 5 e9326
    • (2010) PLoS One , vol.5 , pp. 9326
    • Timsit, Y.1    Varnai, P.2
  • 229
    • 0037295617 scopus 로고    scopus 로고
    • Priming the nucleosome: A role for HMGB proteins?
    • A. A. Travers Priming the nucleosome: a role for HMGB proteins? EMBO Rep. 2003 4 131 136
    • (2003) EMBO Rep. , vol.4 , pp. 131-136
    • Travers, A.A.1
  • 231
    • 33847106524 scopus 로고    scopus 로고
    • Higher-order structures of chromatin: The elusive 30 nm fiber
    • D. J. Tremethick Higher-order structures of chromatin: the elusive 30 nm fiber Cell 2007 128 651 654
    • (2007) Cell , vol.128 , pp. 651-654
    • Tremethick, D.J.1
  • 233
    • 0037340654 scopus 로고    scopus 로고
    • Forces and pressures in DNA packaging and release from viral capsids
    • S. Tzlil J. T. Kindt W. M. Gelbart A. Ben-Shaul Forces and pressures in DNA packaging and release from viral capsids Biophys. J. 2003 84 1616 1627
    • (2003) Biophys. J. , vol.84 , pp. 1616-1627
    • Tzlil, S.1    Kindt, J.T.2    Gelbart, W.M.3    Ben-Shaul, A.4
  • 234
    • 0033062960 scopus 로고    scopus 로고
    • Electrostatic-undulatory theory of plectonemically supercoiled DNA
    • J. Ubbink T. Odijk Electrostatic-undulatory theory of plectonemically supercoiled DNA Biophys. J. 1999 76 2502 2519
    • (1999) Biophys. J. , vol.76 , pp. 2502-2519
    • Ubbink, J.1    Odijk, T.2
  • 235
    • 36449008244 scopus 로고
    • Colloid stability: The forces between charged surfaces in an electrolyte
    • J. P. Valleau R. Ivkov G. M. Torrie Colloid stability: the forces between charged surfaces in an electrolyte J. Chem. Phys. 1991 95 520 532
    • (1991) J. Chem. Phys. , vol.95 , pp. 520-532
    • Valleau, J.P.1    Ivkov, R.2    Torrie, G.M.3
  • 237
    • 1542722926 scopus 로고    scopus 로고
    • Fluorescence study on the size and shape of sodium dodecyl sulphate-aluminium salt micelles
    • M. Vasilescu D. Angelescu H. Caldararu M. Almgren A. Khan Fluorescence study on the size and shape of sodium dodecyl sulphate-aluminium salt micelles Colloids Surf., A 2004 235 57 64
    • (2004) Colloids Surf., A , vol.235 , pp. 57-64
    • Vasilescu, M.1    Angelescu, D.2    Caldararu, H.3    Almgren, M.4    Khan, A.5
  • 238
    • 67651102745 scopus 로고    scopus 로고
    • Protein occupancy landscape of a bacterial genome
    • T. Vora A. K. Hottes S. Tavazoie Protein occupancy landscape of a bacterial genome Mol. Cell 2009 35 247 253
    • (2009) Mol. Cell , vol.35 , pp. 247-253
    • Vora, T.1    Hottes, A.K.2    Tavazoie, S.3
  • 239
    • 0345531056 scopus 로고    scopus 로고
    • Structure-specific binding of the proto-oncogene protein DEK to DNA
    • T. Waldmann M. Baack N. Richter C. Gruss Structure-specific binding of the proto-oncogene protein DEK to DNA Nucleic Acids Res. 2003 31 7003 7310
    • (2003) Nucleic Acids Res. , vol.31 , pp. 7003-7310
    • Waldmann, T.1    Baack, M.2    Richter, N.3    Gruss, C.4
  • 240
    • 42449146575 scopus 로고    scopus 로고
    • Role of sindbis virus capsid protein region II in nucleocapsid core assembly and encapsidation of genomic RNA
    • R. Warrier B. R. Linger B. L. Golden R. J. Kuhn Role of sindbis virus capsid protein region II in nucleocapsid core assembly and encapsidation of genomic RNA J. Virol. 2008 82 4461 4470
    • (2008) J. Virol. , vol.82 , pp. 4461-4470
    • Warrier, R.1    Linger, B.R.2    Golden, B.L.3    Kuhn, R.J.4
  • 241
    • 0022273023 scopus 로고
    • Structure of the 3000 Å chromatin filament: X-ray diffraction from oriented samples
    • J. Widom A. Klug Structure of the 3000 Å chromatin filament: X-ray diffraction from oriented samples Cell 1985 43 207 213
    • (1985) Cell , vol.43 , pp. 207-213
    • Widom, J.1    Klug, A.2
  • 242
    • 80155203808 scopus 로고    scopus 로고
    • Evolution: Functional evolution of nuclear structure
    • K. L. Wilson S. C. Dawson Evolution: functional evolution of nuclear structure J. Cell Biol. 2011 195 171 181
    • (2011) J. Cell Biol. , vol.195 , pp. 171-181
    • Wilson, K.L.1    Dawson, S.C.2
  • 243
    • 0038143248 scopus 로고    scopus 로고
    • Histone-like proteins of the dinoflagellate Crypthecodinium cohnii have homologies to bacterial DNA-binding proteins
    • J. T. Wong D. C. New J. C. Wong V. K. Hung Histone-like proteins of the dinoflagellate Crypthecodinium cohnii have homologies to bacterial DNA-binding proteins Eukaryotic Cell 2003 2 646 650
    • (2003) Eukaryotic Cell , vol.2 , pp. 646-650
    • Wong, J.T.1    New, D.C.2    Wong, J.C.3    Hung, V.K.4
  • 244
    • 36749082174 scopus 로고    scopus 로고
    • An all-atom model of the chromatin fiber containing linker histones reveals a versatile structure tuned by the nucleosomal repeat length
    • H. Wong J. M. Victor J. Mozziconacci An all-atom model of the chromatin fiber containing linker histones reveals a versatile structure tuned by the nucleosomal repeat length PLoS One 2007 2 e877
    • (2007) PLoS One , vol.2 , pp. 877
    • Wong, H.1    Victor, J.M.2    Mozziconacci, J.3
  • 245
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • F. Xu K. Zhang M. Grunstein Acetylation in histone H3 globular domain regulates gene expression in yeast Cell 2005 121 375 385
    • (2005) Cell , vol.121 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 246
    • 0032687816 scopus 로고    scopus 로고
    • Formation of a giant toroid from long duplex DNA
    • Y. Yoshikawa K. Yoshikawa T. Kanbe Formation of a giant toroid from long duplex DNA Langmuir 1999 15 4085 4088
    • (1999) Langmuir , vol.15 , pp. 4085-4088
    • Yoshikawa, Y.1    Yoshikawa, K.2    Kanbe, T.3
  • 247
    • 78651463183 scopus 로고    scopus 로고
    • Gene silencing is an ancient means of producing multiple phenotypes from the same genotype: Common mechanisms and functions in epigenetic processes can be seen throughout all life forms
    • N. A. Youngson S. Chong E. Whitelaw Gene silencing is an ancient means of producing multiple phenotypes from the same genotype: common mechanisms and functions in epigenetic processes can be seen throughout all life forms BioEssays 2010 33 95 99
    • (2010) BioEssays , vol.33 , pp. 95-99
    • Youngson, N.A.1    Chong, S.2    Whitelaw, E.3
  • 248
    • 51249100843 scopus 로고    scopus 로고
    • REDOR NMR characterization of DNA packaging in bacteriophage T4
    • T. Y. Yu J. Shaefer REDOR NMR characterization of DNA packaging in bacteriophage T4 J. Mol. Biol. 2008 382 1031 1042
    • (2008) J. Mol. Biol. , vol.382 , pp. 1031-1042
    • Yu, T.Y.1    Shaefer, J.2
  • 250
    • 41149143297 scopus 로고    scopus 로고
    • Maxwell relations for single-DNA experiments: Monitoring protein binding and double-helix torque with force-extension measurements
    • H. Zhang J. F. Marko Maxwell relations for single-DNA experiments: monitoring protein binding and double-helix torque with force-extension measurements Phys. Rev. E: Stat., Nonlinear, Soft Matter Phys. 2008 77 031916
    • (2008) Phys. Rev. E: Stat., Nonlinear, Soft Matter Phys. , vol.77 , pp. 031916
    • Zhang, H.1    Marko, J.F.2
  • 251
    • 0032563864 scopus 로고    scopus 로고
    • Position and orientation of the globular domain of linker histone H5 on the nucleosome
    • Y. B. Zhou S. E. Gerchman V. Ramakrishnan A. Travers S. Muyldermans Position and orientation of the globular domain of linker histone H5 on the nucleosome Nature 1998 395 402 405
    • (1998) Nature , vol.395 , pp. 402-405
    • Zhou, Y.B.1    Gerchman, S.E.2    Ramakrishnan, V.3    Travers, A.4    Muyldermans, S.5
  • 252
    • 80054693831 scopus 로고    scopus 로고
    • The nuclear envelope as a chromatin organizer
    • N. Zuleger M. I. Robson E. C. Schirmer The nuclear envelope as a chromatin organizer Nucleus 2011 2 339 349
    • (2011) Nucleus , vol.2 , pp. 339-349
    • Zuleger, N.1    Robson, M.I.2    Schirmer, E.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.