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Volumn 278, Issue 19, 2011, Pages 3619-3632

The dynamics of the nucleosome: Thermal effects, external forces and ATP

Author keywords

ATP dependent processes; chromatin remodeling; DNA; kinetic proofreading; nucleosome; nucleosome breathing; nucleosome sliding

Indexed keywords

ADENOSINE TRIPHOSPHATE; DNA BINDING PROTEIN;

EID: 80052966432     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08283.x     Document Type: Review
Times cited : (60)

References (78)
  • 1
    • 68349125112 scopus 로고    scopus 로고
    • What controls nucleosome positions?
    • Segal E, &, Widom J, (2009) What controls nucleosome positions? Trends Genet 25, 335-343.
    • (2009) Trends Genet , vol.25 , pp. 335-343
    • Segal, E.1    Widom, J.2
  • 3
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • DOI 10.1126/science.1059493
    • Cramer P, Bushnell DA, &, Kornberg R, (2001) Structural basis of transcription: RNA polymerase II at 2.8 A resolution. Science 292, 1863-1876. (Pubitemid 32538356)
    • (2001) Science , vol.292 , Issue.5523 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 4
    • 77954759030 scopus 로고    scopus 로고
    • The human mediator complex: Averstalie, genome-wide regulator of transcription
    • Tattjes DJ, (2010) The human mediator complex: averstalie, genome-wide regulator of transcription. Trends Biochem Sci 35, 315-322.
    • (2010) Trends Biochem Sci , vol.35 , pp. 315-322
    • Tattjes, D.J.1
  • 5
    • 77954218952 scopus 로고    scopus 로고
    • Structure and function of SWI/SNF chromatin remodeling complexes and mechanistic implications for transcription
    • Tang L, Nogales E, &, Ciferri C, (2010) Structure and function of SWI/SNF chromatin remodeling complexes and mechanistic implications for transcription. Prog Biophys Mol Biol 102, 122-128.
    • (2010) Prog Biophys Mol Biol , vol.102 , pp. 122-128
    • Tang, L.1    Nogales, E.2    Ciferri, C.3
  • 6
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • DOI 10.1038/38444
    • Luger K, Mäder AW, Richmond RK, Sargent DF, &, Richmond TJ, (1997) Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389, 251-260. (Pubitemid 27406632)
    • (1997) Nature , vol.389 , Issue.6648 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 8
    • 0028791330 scopus 로고
    • Mechanism of protein access to specific DNA sequences in chromatin: A dynamic equilibrium model for gene regulation
    • Polach KJ, &, Widom J, (1995) Mechanism of protein access to specific DNA sequences in chromatin: a dynamic equilibrium model for gene regulation. J Mol Biol 254, 130-149.
    • (1995) J Mol Biol , vol.254 , pp. 130-149
    • Polach, K.J.1    Widom, J.2
  • 9
    • 3542998667 scopus 로고    scopus 로고
    • Nucleosomes facilitate their own invasion
    • DOI 10.1038/nsmb801
    • Li G, &, Widom J, (2004) Nucleosomes facilitate their own invasion. Nat Struct Mol Biol 11, 763-769. (Pubitemid 39014502)
    • (2004) Nature Structural and Molecular Biology , vol.11 , Issue.8 , pp. 763-769
    • Li, G.1    Widom, J.2
  • 12
    • 33847672264 scopus 로고    scopus 로고
    • Sequence-dependent nucleosome structure and stability variations detected by Förster resonance energy transfer
    • DOI 10.1021/bi061289l
    • Kelbauskas L, Chan N, Bash R, Yodh J, Woodbury N, &, Lohr D, (2007) Sequence-dependent nucleosome structure and stability variations detected by Förster resonance energy transfer. Biochemistry 46, 2239-2248. (Pubitemid 46355333)
    • (2007) Biochemistry , vol.46 , Issue.8 , pp. 2239-2248
    • Kelbauskas, L.1    Chan, N.2    Bash, R.3    Yodh, J.4    Woodbury, N.5    Lohr, D.6
  • 13
    • 51549086312 scopus 로고    scopus 로고
    • Nucleosomal stability and dynamics vary significantly when viewed by internal versus terminal labels
    • Kelbauskas L, Sun J, Woodbury N, &, Lohr D, (2008) Nucleosomal stability and dynamics vary significantly when viewed by internal versus terminal labels. Biochemistry 47, 9627-9635.
    • (2008) Biochemistry , vol.47 , pp. 9627-9635
    • Kelbauskas, L.1    Sun, J.2    Woodbury, N.3    Lohr, D.4
  • 14
    • 65249116968 scopus 로고    scopus 로고
    • DNA sequence-dependent variation in nucleosome structure, stability, and dynamics detected by a FRET-based analysis
    • Kelbauskas L, Woodbury N, &, Lohr D, (2009) DNA sequence-dependent variation in nucleosome structure, stability, and dynamics detected by a FRET-based analysis. Biochem Cell Biol 87, 323-335.
    • (2009) Biochem Cell Biol , vol.87 , pp. 323-335
    • Kelbauskas, L.1    Woodbury, N.2    Lohr, D.3
  • 15
    • 65249182676 scopus 로고    scopus 로고
    • Structural variability of nucleosomes detected by single-pair Förster resonance energy transfer: Histone acetylation, sequence variation, and salt effects
    • Gansen A, Toth K, Schwarz N, &, Langowski J, (2009) Structural variability of nucleosomes detected by single-pair Förster resonance energy transfer: histone acetylation, sequence variation, and salt effects. J Phys Chem B 113, 2604-2613.
    • (2009) J Phys Chem B , vol.113 , pp. 2604-2613
    • Gansen, A.1    Toth, K.2    Schwarz, N.3    Langowski, J.4
  • 17
    • 68949085807 scopus 로고    scopus 로고
    • SpFRET using alternating excitation and FCS reveals progressive DNA unwrapping in nucleosomes
    • Koopmans WJA, Buning R, Schmidt T, &, van Noort J, (2009) spFRET using alternating excitation and FCS reveals progressive DNA unwrapping in nucleosomes. Biophys J 97, 195-204.
    • (2009) Biophys J , vol.97 , pp. 195-204
    • Koopmans, W.J.A.1    Buning, R.2    Schmidt, T.3    Van Noort, J.4
  • 18
    • 80052969332 scopus 로고    scopus 로고
    • Reference withdrawn
    • Reference withdrawn.
  • 19
    • 33750998762 scopus 로고    scopus 로고
    • Kinetic accessibility of buried DNA sites in nucleosomes
    • Möbius W, Neher RA, &, Gerland U, (2006) Kinetic accessibility of buried DNA sites in nucleosomes. Phys Rev Lett 97, 208102.
    • (2006) Phys Rev Lett , vol.97 , pp. 208102
    • Möbius, W.1    Neher, R.A.2    Gerland, U.3
  • 20
    • 0034598944 scopus 로고    scopus 로고
    • Sequence and position dependence of the equilibrium accessibility of nucleosomal DNA target sites
    • Anderson JD, &, Widom J, (2000) Sequence and position dependence of the equilibrium accessibility of nucleosomal DNA target sites. J Mol Biol 296, 979-987.
    • (2000) J Mol Biol , vol.296 , pp. 979-987
    • Anderson, J.D.1    Widom, J.2
  • 21
    • 0034999881 scopus 로고    scopus 로고
    • Poly(dA-dT) promoter elements increase the equilibrium accessibility of nucleosomal DNA target sites
    • DOI 10.1128/MCB.21.11.3830-3839.2001
    • Anderson JD, &, Widom J, (2001) Poly(dA-dT) promoter elements increase the equilibrium accessibility of nucleosomal DNA target sites. Mol Cell Biol 21, 3830-3839. (Pubitemid 32466994)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.11 , pp. 3830-3839
    • Anderson, J.D.1    Widom, J.2
  • 22
    • 0035815105 scopus 로고    scopus 로고
    • Effects of histone acetylation on the equilibrium accessibility of nucleosomal DNA target sites
    • DOI 10.1006/jmbi.2001.4528
    • Anderson JD, Lowary PT, &, Widom J, (2001) Effects of histone acetylation on the equilibrium accessibility of nucleosomal DNA target sites. J Mol Biol 307, 977-985. (Pubitemid 33029947)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.4 , pp. 977-985
    • Anderson, J.D.1    Lowary, P.T.2    Widom, J.3
  • 23
    • 0036786970 scopus 로고    scopus 로고
    • Spontaneous access of proteins to buried nucleosomal DNA target sites occurs via a mechanism that is distinct from nucleosome translocation
    • Anderson JD, Thaström A, &, Widom J, (2002) Spontaneous access of proteins to buried nucleosomal DNA target sites occurs via a mechanism that is distinct from nucleosome translocation. Mol Cell Biol 22, 7147-7157.
    • (2002) Mol Cell Biol , vol.22 , pp. 7147-7157
    • Anderson, J.D.1    Thaström, A.2    Widom, J.3
  • 24
    • 78650252649 scopus 로고    scopus 로고
    • Nucleosome stability and accessibility of its DNA to proteins
    • Prinsen P, &, Schiessel H, (2010) Nucleosome stability and accessibility of its DNA to proteins. Biochimie 92, 1722-1728.
    • (2010) Biochimie , vol.92 , pp. 1722-1728
    • Prinsen, P.1    Schiessel, H.2
  • 26
    • 0034958378 scopus 로고    scopus 로고
    • Unfolding individual nucleosomes by stretching single chromatin fibers with optical tweezers
    • DOI 10.1038/89646
    • Bennink ML, Leuba SH, Leno GH, Zlatanova J, de Grooth BG, &, Greve J, (2001) Unfolding individual nucleosomes by stretching single chromatin fibers with optical tweezers. Nat Struct Biol 8, 606-610. (Pubitemid 32613009)
    • (2001) Nature Structural Biology , vol.8 , Issue.7 , pp. 606-610
    • Bennink, M.L.1    Leuba, S.H.2    Leno, G.H.3    Zlatanova, J.4    De Grooth, B.G.5    Greve, J.6
  • 27
    • 12344284012 scopus 로고    scopus 로고
    • Specific contributions of histone tails and their acetylation to the mechanical stability of nucleosomes
    • DOI 10.1016/j.jmb.2004.11.056, PII S002228360401527X
    • Brower-Toland B, Wacker DA, Fulbright RM, Lis JT, Kraus WL, &, Wang MD, (2005) Specific contributions of histone tails and their acetylation to the mechanical stability of nucleosomes. J Mol Biol 346, 135-146. (Pubitemid 40136589)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.1 , pp. 135-146
    • Brower-Toland, B.1    Wacker, D.A.2    Fulbright, R.M.3    Lis, J.T.4    Kraus, W.L.5    Wang, M.D.6
  • 28
    • 17844364466 scopus 로고    scopus 로고
    • Single chromatin fiber stretching reveals physically distinct populations of disassembly events
    • DOI 10.1529/biophysj.104.053074
    • Pope LH, Bennink ML, van Leijenhorst-Groener KA, Nikova D, Greve J, &, Marko JF, (2005) Single chromatin fiber stretching reveals physically distinct populations of disassembly events. Biophys J 88, 3572-3583. (Pubitemid 40586605)
    • (2005) Biophysical Journal , vol.88 , Issue.5 , pp. 3572-3583
    • Pope, L.H.1    Bennink, M.L.2    Van Leijenhorst-Groener, K.A.3    Nikova, D.4    Greve, J.5    Marko, J.F.6
  • 29
    • 22044436367 scopus 로고    scopus 로고
    • Forced unraveling of nucleosomes assembled on heterogeneous DNA using core histones, NAP-1, and ACF
    • DOI 10.1016/j.jmb.2005.05.058, PII S0022283605006133
    • Gemmen GJ, Sim R, Haushalter KA, Ke PC, Kadonaga JT, &, Smith DE, (2005) Forced unraveling of nucleosomes assembled on heterogeneous DNA using core histones, NAP-1, and ACF. J Mol Biol 351, 89-99. (Pubitemid 40967057)
    • (2005) Journal of Molecular Biology , vol.351 , Issue.1 , pp. 89-99
    • Gemmen, G.J.1    Sim, R.2    Haushalter, K.A.3    Ke, P.C.4    Kadonaga, J.T.5    Smith, D.E.6
  • 31
    • 0033552676 scopus 로고    scopus 로고
    • Looking inside molecular bonds at biological interfaces with dynamic force spectroscopy
    • Evans E, (1999) Looking inside molecular bonds at biological interfaces with dynamic force spectroscopy. Biophys Chem 82, 83-97.
    • (1999) Biophys Chem , vol.82 , pp. 83-97
    • Evans, E.1
  • 32
    • 3042834082 scopus 로고    scopus 로고
    • DNA spools under tension
    • Kulić IM, &, Schiessel H, (2004) DNA spools under tension. Phys Rev Lett 92, 228101-1-4.
    • (2004) Phys Rev Lett , vol.92 , pp. 22810114
    • Kulić, I.M.1    Schiessel, H.2
  • 34
    • 0026642219 scopus 로고
    • Mobile nucleosomes - A general behavior
    • Meersseman G, Pennings A, &, Bradbury EM, (1992) Mobile nucleosomes-a general behavior. EMBO J 11, 2951-2959.
    • (1992) EMBO J , vol.11 , pp. 2951-2959
    • Meersseman, G.1    Pennings, A.2    Bradbury, E.M.3
  • 36
    • 0032559424 scopus 로고    scopus 로고
    • Positioning and stability of nucleosomes on MMTV 3'LTR sequences
    • DOI 10.1006/jmbi.1997.1464
    • Flaus A, &, Richmond TJ, (1998) Positioning and stability of nucleosomes on MMTV 3′LTR sequences. J Mol Biol 275, 427-441. (Pubitemid 28055063)
    • (1998) Journal of Molecular Biology , vol.275 , Issue.3 , pp. 427-441
    • Flaus, A.1    Richmond, T.J.2
  • 37
    • 0037388372 scopus 로고    scopus 로고
    • Mechanisms for nucleosome mobilization
    • DOI 10.1002/bip.10323
    • Flaus A, &, Owen-Hughes T, (2003) Mechanisms for nucleosome mobilization. Biopolymers 68, 563-578. (Pubitemid 36427880)
    • (2003) Biopolymers , vol.68 , Issue.4 , pp. 563-578
    • Flaus, A.1    Owen-Hughes, T.2
  • 38
    • 0035820523 scopus 로고    scopus 로고
    • Polymer reptation and nucleosome repositioning
    • DOI 10.1103/PhysRevLett.86.4414
    • Schiessel H, Widom J, Bruinsma RF, &, Gelbart WM, (2001) Polymer reptation and nucleosome repositioning. Phys Rev Lett 86, 4414-4417. (Pubitemid 32469567)
    • (2001) Physical Review Letters , vol.86 , Issue.19 , pp. 4414-4417
    • Schiessel, H.1    Widom, J.2    Bruinsma, R.F.3    Gelbart, W.M.4
  • 39
    • 0038298709 scopus 로고    scopus 로고
    • Nucleosome repositioning via loop formation
    • Kulić IM, &, Schiessel H, (2003) Nucleosome repositioning via loop formation. Biophys J 84, 3197-3211. (Pubitemid 36531767)
    • (2003) Biophysical Journal , vol.84 , Issue.5 , pp. 3197-3211
    • Kulic, I.M.1    Schiessel, H.2
  • 40
    • 0242677113 scopus 로고    scopus 로고
    • Chromatin dynamics: Nucleosomes go mobile through twist defects
    • 1-4
    • Kulić IM, &, Schiessel H, (2003) Chromatin dynamics: nucleosomes go mobile through twist defects. Phys Rev Lett 91, 148103, 1-4.
    • (2003) Phys Rev Lett , vol.91 , pp. 148103
    • Kulić, I.M.1    Schiessel, H.2
  • 42
    • 0031031106 scopus 로고    scopus 로고
    • In vitro low propensity to form nucleosomes of four telomeric sequences
    • DOI 10.1016/S0014-5793(96)01318-X, PII S001457939601318X
    • Cacchione S, Cerione MA, &, Savino M, (1997) In vitro low propensity to form nucleosomes of four telomeric sequences. FEBS Lett 400, 37-41. (Pubitemid 27046817)
    • (1997) FEBS Letters , vol.400 , Issue.1 , pp. 37-41
    • Cacchione, S.1    Cerone, M.A.2    Savino, M.3
  • 43
    • 0032510809 scopus 로고    scopus 로고
    • Nucleosome assembly on telomeric sequences
    • DOI 10.1021/bi9726180
    • Rossetti L, Cacchione S, Fua M, &, Savino M, (1998) Nucleosome assembly on telomeric sequences. Biochemistry 37, 6727-6737. (Pubitemid 28228106)
    • (1998) Biochemistry , vol.37 , Issue.19 , pp. 6727-6737
    • Rossetti, L.1    Cacchione, S.2    Fua, M.3    Savino, M.4
  • 44
    • 0033988692 scopus 로고    scopus 로고
    • The main role of the sequence-dependent DNA elasticity in determining the free energy of nucleosome formation on telomeric DNAs
    • DOI 10.1016/S0301-4622(99)00143-X, PII S030146229900143X
    • Filesi I, Cacchione S, De Santis P, Rossetti L, &, Savino M, (1999) The main role of the sequence-dependent DNA elasticity in determining the free energy of nucleosome formation on telomeric DNAs. Biophys Chem 83, 223-237. (Pubitemid 30012086)
    • (2000) Biophysical Chemistry , vol.83 , Issue.3 , pp. 223-237
    • Filesi, I.1    Cacchione, S.2    De Santis, P.3    Rossetti, L.4    Savino, M.5
  • 46
  • 49
    • 7044220398 scopus 로고    scopus 로고
    • Theory of nucleosome corkscrew sliding in the presence of synthetic DNA ligands
    • DOI 10.1016/j.jmb.2004.09.027, PII S0022283604011702
    • Mohammad-Rafiee F, Kulić IM, &, Schiessel H, (2004) Theory of nucleosome corkscrew sliding in the presence of synthetic DNA ligands. J Mol Biol 344, 47-58. (Pubitemid 39422373)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.1 , pp. 47-58
    • Mohammad-Rafiee, F.1    Kulic, I.M.2    Schiessel, H.3
  • 50
    • 0028125847 scopus 로고
    • A histone octamer can step around a transcribing polymerase without leaving the template
    • DOI 10.1016/0092-8674(94)90343-3
    • Studitsky VM, Clark DJ, &, Felsenfeld G, (1994) A histone octamer can step around a transcribing polymerase without leaving the template. Cell 76, 371-382. (Pubitemid 24046698)
    • (1994) Cell , vol.76 , Issue.2 , pp. 371-382
    • Studitsky, V.M.1    Clark, D.J.2    Felsenfeld, G.3
  • 51
    • 0028850059 scopus 로고
    • Overcoming a nucleosomal barrier to transcription
    • Studitsky VM, Clark DJ, &, Felsenfeld G, (1995) Overcoming a nucleosomal barrier to transcription. Cell 83, 19-27.
    • (1995) Cell , vol.83 , pp. 19-27
    • Studitsky, V.M.1    Clark, D.J.2    Felsenfeld, G.3
  • 52
    • 0033197561 scopus 로고    scopus 로고
    • The nature of the nucleosomal barrier to transcription: Direct observation of paused intermediates by electron cryomicroscopy
    • DOI 10.1016/S1097-2765(00)80339-1
    • Bednar J, Studitsky VM, Gregoryev SA, Felsenfeld G, &, Woodcock CL, (1999) The nature of the nucleosomal barrier to transcription: direct observation of paused intermediates by electron cryomicroscopy. Mol Cell 4, 377-386. (Pubitemid 29499790)
    • (1999) Molecular Cell , vol.4 , Issue.3 , pp. 377-386
    • Bednar, J.1    Studitsky, V.M.2    Grigoryev, S.A.3    Felsenfeld, G.4    Woodcock, C.L.5
  • 53
    • 0035800808 scopus 로고    scopus 로고
    • Facilitated transcription through the nucleosome at high ionic strength occurs via a histone octamer transfer mechanism
    • Walter W, &, Studitsky VM, (2001) Facilitated transcription through the nucleosome at high ionic strength occurs via a histone octamer transfer mechanism. J Biol Chem 276, 29104-29110.
    • (2001) J Biol Chem , vol.276 , pp. 29104-29110
    • Walter, W.1    Studitsky, V.M.2
  • 54
    • 0031451329 scopus 로고    scopus 로고
    • Mechanism of transcription through the nucleosome by eukaryotic RNA polymerase
    • DOI 10.1126/science.278.5345.1960
    • Studitsky VM, Kassavetis GA, Geiduschek EP, &, Felsenfeld G, (1997) Mechanism of transcription through the nucleosomeby eukaryotic RNA polymerase. Science 278, 1960-1963. (Pubitemid 28013240)
    • (1997) Science , vol.278 , Issue.5345 , pp. 1960-1963
    • Studitsky, V.M.1    Kassavetis, G.A.2    Geiduschek, E.P.3    Felsenfeldt, G.4
  • 55
    • 0036203807 scopus 로고    scopus 로고
    • Nucleosome remodeling induced by RNA polymerase II: Loss of the H2A/H2B dimer during transcription
    • DOI 10.1016/S1097-2765(02)00472-0
    • Kireeva ML, Walter W, Tchernajenko V, Bondarenko V, Kashlev M, &, Studitsky VM, (2002) Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription. Mol Cell 9, 541-552. (Pubitemid 34273785)
    • (2002) Molecular Cell , vol.9 , Issue.3 , pp. 541-552
    • Kireeva, M.L.1    Walter, W.2    Tchernajenko, V.3    Bondarenko, V.4    Kashlev, M.5    Studitsky, V.M.6
  • 57
    • 68149120313 scopus 로고    scopus 로고
    • Nucleosomal fluctuations govern the transcription dynamics of RNA polymerase II
    • Hodges C, Bintu L, Lubkowska L, Kashlev M, &, Bustamante C, (2009) Nucleosomal fluctuations govern the transcription dynamics of RNA polymerase II. Science 325, 626-628.
    • (2009) Science , vol.325 , pp. 626-628
    • Hodges, C.1    Bintu, L.2    Lubkowska, L.3    Kashlev, M.4    Bustamante, C.5
  • 58
    • 1242318837 scopus 로고    scopus 로고
    • Functional properties of ATP-dependent chromatin remodeling enzymes
    • DOI 10.1016/S0065-3233(04)67006-9
    • Imbalzano AN, &, Xiao H, (2004) Functional properties of ATP-dependent chromatin remodeling enzymes. Adv Protein Chem 67, 157-179. (Pubitemid 38229054)
    • (2004) Advances in Protein Chemistry , vol.67 , pp. 157-179
    • Imbalzano, A.N.1    Xiao, H.2
  • 59
    • 67650725820 scopus 로고    scopus 로고
    • The biology of chromatin remodeling complexes
    • Clapier CR, &, Cairns BR, (2009) The biology of chromatin remodeling complexes. Annu Rev Biochem 78, 273-304.
    • (2009) Annu Rev Biochem , vol.78 , pp. 273-304
    • Clapier, C.R.1    Cairns, B.R.2
  • 60
    • 77749322697 scopus 로고    scopus 로고
    • Mechanisms of ATP-dependent nucleosome sliding
    • Bowman G, (2010) Mechanisms of ATP-dependent nucleosome sliding. Curr Opin Struct Biol 20, 73-81.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 73-81
    • Bowman, G.1
  • 61
    • 80052970429 scopus 로고    scopus 로고
    • Mechanisms for ATP dependent chromatin remodelling: The means to an end
    • Flaus A, &, Owen-Hughes T, (2011) Mechanisms for ATP dependent chromatin remodelling: the means to an end. FEBS J 278, 3579-3595.
    • (2011) FEBS J , vol.278 , pp. 3579-3595
    • Flaus, A.1    Owen-Hughes, T.2
  • 62
    • 80052965260 scopus 로고    scopus 로고
    • Nucleosome remodeling machines and other molecular motors observed at the single-molecule level
    • Croquette V, Lavelle C, Praly E, Bensimon D, &, LeCam E, (2011) Nucleosome remodeling machines and other molecular motors observed at the single-molecule level. FEBS J 278, 3596-3607.
    • (2011) FEBS J , vol.278 , pp. 3596-3607
    • Croquette, V.1    Lavelle, C.2    Praly, E.3    Bensimon, D.4    Lecam, E.5
  • 63
    • 0034724562 scopus 로고    scopus 로고
    • Effects of corehistone taildomains on the equilibrium constantsfor dynamic DNA site accessibility in nucleosomes
    • Polach KJ, Lowary PT, &, Widom J, (2000) Effects of corehistone taildomains on the equilibrium constantsfor dynamic DNA site accessibility in nucleosomes. J Mol Biol 298, 211-223.
    • (2000) J Mol Biol , vol.298 , pp. 211-223
    • Polach, K.J.1    Lowary, P.T.2    Widom, J.3
  • 64
    • 0037292355 scopus 로고    scopus 로고
    • SWI/SNF unwraps, slides, and rewraps the nucleosome
    • DOI 10.1016/S1097-2765(03)00039-X
    • Kassabov SR, Zhang B, Persinger J, &, Bartholomew B, (2003) SWI/SNF unwraps, slides, and rewraps the nucleosome. Mol Cell 11, 391-403. (Pubitemid 36293833)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 391-403
    • Kassabov, S.R.1    Zhang, B.2    Persinger, J.3    Bartholomew, B.4
  • 65
    • 63849217888 scopus 로고    scopus 로고
    • Kinetic proofreading of gene activation by chromatin remodeling
    • Blossey R, &, Schiessel H, (2008) Kinetic proofreading of gene activation by chromatin remodeling. HFSP J 2, 167-170.
    • (2008) HFSP J , vol.2 , pp. 167-170
    • Blossey, R.1    Schiessel, H.2
  • 66
    • 0000359208 scopus 로고
    • Kinetic proofreading: A new mechanismfor reducing errors in biosynthetic processes requiring high specificity
    • Hopfield JJ, (1974) Kinetic proofreading: a new mechanismfor reducing errors in biosynthetic processes requiring high specificity. Proc Natl Acad Sci USA 71, 4135-4139.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4135-4139
    • Hopfield, J.J.1
  • 67
    • 77957749787 scopus 로고    scopus 로고
    • A proposal for kinetic proofreading by ISWI family chromatin remodeling motors
    • Narlikar GJ, (2010) A proposal for kinetic proofreading by ISWI family chromatin remodeling motors. Curr Opin Chem Biol 14, 1-6.
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 1-6
    • Narlikar, G.J.1
  • 68
    • 0033681250 scopus 로고    scopus 로고
    • Ordered recruitment of chromatin modifying and general transcription factors to the IFN-β promoter
    • Agalioti T, Lomvardas S, Parekh B, Yie J, Maniatis T, &, Thanos D, (2000) Ordered recruitment of chromatin modifying and general transcription factors to the IFN-β promoter. Cell 103, 667-678.
    • (2000) Cell , vol.103 , pp. 667-678
    • Agalioti, T.1    Lomvardas, S.2    Parekh, B.3    Yie, J.4    Maniatis, T.5    Thanos, D.6
  • 69
    • 0036850346 scopus 로고    scopus 로고
    • Deciphering the transcriptional histone acetylation code for a human gene
    • DOI 10.1016/S0092-8674(02)01077-2
    • Agalioti T, Chen G, &, Thanos D, (2002) Deciphering the transcriptional histone acetylation code for a human gene. Cell 111, 381-392. (Pubitemid 35341391)
    • (2002) Cell , vol.111 , Issue.3 , pp. 381-392
    • Agalioti, T.1    Chen, G.2    Thanos, D.3
  • 70
    • 80052965296 scopus 로고    scopus 로고
    • Reference withdrawn
    • Reference withdrawn.
  • 71
    • 33845356072 scopus 로고    scopus 로고
    • The chromatin-remodeling enzyme ACF is an ATP-dependent DNA length sensor that regulates nucleosome spacing
    • DOI 10.1038/nsmb1170, PII NSMB1170
    • Yang JG, Madrid TS, Sevastopoulos E, &, Narlikar GJ, (2006) The chromatin-remodeling enzyme ACF is an ATP-dependent DNA length sensor that regulates nucleosome spacing. Nat Struct Mol Biol 13, 1078-1083. (Pubitemid 44885917)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.12 , pp. 1078-1083
    • Yang, J.G.1    Madrid, T.S.2    Sevastopoulos, E.3    Narlikar, G.J.4
  • 73
    • 72949099668 scopus 로고    scopus 로고
    • Dynamics of nucleosome remodeling by individual ACF complexes
    • Blosser TR, Yang JG, Stone MD, Narlikar GJ, &, Zhuang X, (2009) Dynamics of nucleosome remodeling by individual ACF complexes. Nature 426, 1022-1028.
    • (2009) Nature , vol.426 , pp. 1022-1028
    • Blosser, T.R.1    Yang, J.G.2    Stone, M.D.3    Narlikar, G.J.4    Zhuang, X.5
  • 74
    • 80052962505 scopus 로고    scopus 로고
    • ISWI chromatin remodelers in mammalian cells - Where, when and why?
    • Erdel F, &, Rippe K, (2011) ISWI chromatin remodelers in mammalian cells-where, when and why? FEBS J 278, 3608-3618.
    • (2011) FEBS J , vol.278 , pp. 3608-3618
    • Erdel, F.1    Rippe, K.2
  • 76
    • 33749626224 scopus 로고    scopus 로고
    • Regulation of ISW2 by concerted action of histone H4 tail and extranucleosomal DNA
    • DOI 10.1128/MCB.01159-06
    • Dang W, Kagalwala MN, &, Bartholomew B, (2006) Regulation of ISW2 by concerted action of histone H4 tail and extranucleosomal DNA. Mol Cell Biol 26, 7388-7396. (Pubitemid 44547691)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.20 , pp. 7388-7396
    • Dang, W.1    Kagalwala, M.N.2    Bartholomew, B.3
  • 77
    • 67649668797 scopus 로고    scopus 로고
    • Conformational changes associated with template commitment in ATP-dependent chromatin remodeling by ISW2
    • Gangaraju VK, Prasad P, Srour A, Kagalwala MN, &, Bartholomew B, (2009) Conformational changes associated with template commitment in ATP-dependent chromatin remodeling by ISW2. Mol Cell 35, 58-69.
    • (2009) Mol Cell , vol.35 , pp. 58-69
    • Gangaraju, V.K.1    Prasad, P.2    Srour, A.3    Kagalwala, M.N.4    Bartholomew, B.5
  • 78
    • 0036208153 scopus 로고    scopus 로고
    • Modulation of ISWI function by site-specific histone acetylation
    • DOI 10.1093/embo-reports/kvf056
    • Corona DFV, Clapier CR, Becker PB, &, Tamkun JW, (2002) Modulation of ISWI function by site-specific histone acetylation. EMBO Rep 31, 242-247. (Pubitemid 34269517)
    • (2002) EMBO Reports , vol.3 , Issue.3 , pp. 242-247
    • Corona, D.F.V.1    Clapier, C.R.2    Becker, P.B.3    Tamkun, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.