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Volumn 6, Issue 3, 2015, Pages 751-776

Chromatin dynamics in vivo: A game of musical chairs

Author keywords

CENP A; Chaperones; Chromatin; H2A.Z; H3.3; Histones; macroH2A

Indexed keywords

CENTROMERE PROTEIN A; CHAPERONE; HISTONE H2AZ; HISTONE H3.3; HISTONE MACROH2A; NUCLEAR PROTEIN; UNCLASSIFIED DRUG;

EID: 84940983863     PISSN: None     EISSN: 20734425     Source Type: Journal    
DOI: 10.3390/genes6030751     Document Type: Review
Times cited : (28)

References (180)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K.; Mader, A.W.; Richmond, R.K.; Sargent, D.F.; Richmond, T.J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997, 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
    • 51449112574 scopus 로고    scopus 로고
    • Superposition of transcriptional behaviors determines gene state
    • Efroni, S.; Carmel, L.; Schaefer, C.G.; Buetow, K.H. Superposition of transcriptional behaviors determines gene state. PLoS ONE 2008, 3, e2901.
    • (2008) PLoS ONE , vol.3
    • Efroni, S.1    Carmel, L.2    Schaefer, C.G.3    Buetow, K.H.4
  • 5
    • 84868699301 scopus 로고    scopus 로고
    • Through thick and thin: The conundrum of chromatin fibre folding in vivo
    • Quénet, D.; McNally, J.G.; Dalal, Y. Through thick and thin: The conundrum of chromatin fibre folding in vivo. EMBO Rep. 2012, 13, 943-944.
    • (2012) EMBO Rep , vol.13 , pp. 943-944
    • Quénet, D.1    McNally, J.G.2    Dalal, Y.3
  • 6
    • 0242407193 scopus 로고    scopus 로고
    • Phylogenomics of the nucleosome
    • Malik, H.S. Henikoff, S. Phylogenomics of the nucleosome. Nat. Struct. Biol. 2003, 10, 882-891.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 882-891
    • Malik, H.S.1    Henikoff, S.2
  • 8
    • 0035371920 scopus 로고    scopus 로고
    • Visualizing chromosome dynamics with GFP
    • Belmont, A.S. Visualizing chromosome dynamics with GFP. Trends Cell Biol. 2001, 11, 250-257.
    • (2001) Trends Cell Biol , vol.11 , pp. 250-257
    • Belmont, A.S.1
  • 9
    • 84875207723 scopus 로고    scopus 로고
    • Chromatin movement in the maintenance of genome stability
    • Dion, V.; Gasser, S.M. Chromatin movement in the maintenance of genome stability. Cell 2013, 152, 1355-1364.
    • (2013) Cell , vol.152 , pp. 1355-1364
    • Dion, V.1    Gasser, S.M.2
  • 11
    • 84877795975 scopus 로고    scopus 로고
    • The role of chromatin insulators in nuclear architecture and genome function
    • Van Bortle, K.; Corces, V.G. The role of chromatin insulators in nuclear architecture and genome function. Curr. Opin. Genet. Dev. 2013, 23, 212-218.
    • (2013) Curr. Opin. Genet. Dev , vol.23 , pp. 212-218
    • Van Bortle, K.1    Corces, V.G.2
  • 13
    • 84924559967 scopus 로고    scopus 로고
    • Chromatin fibers are formed by heterogeneous groups of nucleosomes in vivo
    • Ricci, M.A.; Manzo, C.; García-Parajo, M.F.; Lakadamyali, M.; Cosma, M.P. Chromatin fibers are formed by heterogeneous groups of nucleosomes in vivo. Cell 2015, 160, 1145-1158.
    • (2015) Cell , vol.160 , pp. 1145-1158
    • Ricci, M.A.1    Manzo, C.2    García-Parajo, M.F.3    Lakadamyali, M.4    Cosma, M.P.5
  • 15
    • 84899415723 scopus 로고    scopus 로고
    • Every amino acid matters: Essential contributions of histone variants to mammalian development and disease
    • Maze, I.; Noh, K.M.; Soshnev, A.A.; Allis, C.D. Every amino acid matters: Essential contributions of histone variants to mammalian development and disease. Nat. Rev. Genet. 2014, 15, 259-271.
    • (2014) Nat. Rev. Genet , vol.15 , pp. 259-271
    • Maze, I.1    Noh, K.M.2    Soshnev, A.A.3    Allis, C.D.4
  • 17
    • 41549112501 scopus 로고    scopus 로고
    • FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16
    • Heo, K.; Kim, H.; Choi, S.H.; Choi, J.; Kim, K.; Gu, J.; Lieber, M.R.; Yang, A.S.; An, W. FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16. Mol. Cell 2008, 30, 86-97.
    • (2008) Mol. Cell , vol.30 , pp. 86-97
    • Heo, K.1    Kim, H.2    Choi, S.H.3    Choi, J.4    Kim, K.5    Gu, J.6    Lieber, M.R.7    Yang, A.S.8    An, W.9
  • 20
    • 38949091078 scopus 로고    scopus 로고
    • H2A.Z: View from the top
    • Zlatanova, J.; Thakar, A. H2A.Z: View from the top. Structure 2008, 16, 166-179.
    • (2008) Structure , vol.16 , pp. 166-179
    • Zlatanova, J.1    Thakar, A.2
  • 21
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • Suto, R.K.; Clarkson, M.J.; Tremethick, D.J.; Luger, K. Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat. Struct. Biol. 2000, 7, 1121-1124.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 1121-1124
    • Suto, R.K.1    Clarkson, M.J.2    Tremethick, D.J.3    Luger, K.4
  • 23
    • 77951169141 scopus 로고    scopus 로고
    • Chromatin remodeling by imitation switch (ISWI) class ATP-dependent remodelers is stimulated by histone variant H2A.Z
    • Goldman, J.A.; Garlick, J.D.; Kingston, R.E. Chromatin remodeling by imitation switch (ISWI) class ATP-dependent remodelers is stimulated by histone variant H2A.Z. J. Biol. Chem. 2010, 285, 4645-4651.
    • (2010) J. Biol. Chem , vol.285 , pp. 4645-4651
    • Goldman, J.A.1    Garlick, J.D.2    Kingston, R.E.3
  • 24
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin
    • Meneghini, M.D.; Wu, M.; Madhani, H.D. Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin. Cell 2003, 112, 725-736.
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 26
    • 80052962505 scopus 로고    scopus 로고
    • Chromatin remodelling in mammalian cells by ISWI-type complexes-Where, when and why?
    • Erdel, F.; Rippe, K. Chromatin remodelling in mammalian cells by ISWI-type complexes-Where, when and why? FEBS J. 2011, 278, 3608-3618.
    • (2011) FEBS J , vol.278 , pp. 3608-3618
    • Erdel, F.1    Rippe, K.2
  • 27
    • 76249114074 scopus 로고    scopus 로고
    • Histone variant H2A.Z regulates centromere silencing and chromosome segregation in fission yeast
    • Hou, H.; Wang, Y.; Kallgren, S.P.; Thompson, J.; Yates, J.R., III; Jia, S. Histone variant H2A.Z regulates centromere silencing and chromosome segregation in fission yeast. J. Biol. Chem. 2010, 285, 1909-1918.
    • (2010) J. Biol. Chem , vol.285 , pp. 1909-1918
    • Hou, H.1    Wang, Y.2    Kallgren, S.P.3    Thompson, J.4    Yates, J.R.5    Jia, S.6
  • 28
    • 27944478598 scopus 로고    scopus 로고
    • Assembly and disassembly of nucleosome core particles containing histone variants by human nucleosome assembly protein I
    • Okuwaki, M.; Kato, K.; Shimahara, H.; Tate, S.; Nagata, K. Assembly and disassembly of nucleosome core particles containing histone variants by human nucleosome assembly protein I. Mol. Cell Biol. 2005, 25, 10639-10651.
    • (2005) Mol. Cell Biol , vol.25 , pp. 10639-10651
    • Okuwaki, M.1    Kato, K.2    Shimahara, H.3    Tate, S.4    Nagata, K.5
  • 29
    • 41249093432 scopus 로고    scopus 로고
    • Quickly evolving histones, nucleosome stability and chromatin folding: All about histone H2A.Bbd
    • González-Romero, R.; Méndez, J.; Ausió, J.; Eirín-López, J.M. Quickly evolving histones, nucleosome stability and chromatin folding: All about histone H2A.Bbd. Gene 2008, 413, 1-7.
    • (2008) Gene , vol.413 , pp. 1-7
    • González-Romero, R.1    Méndez, J.2    Ausió, J.3    Eirín-López, J.M.4
  • 30
    • 84890675102 scopus 로고    scopus 로고
    • Structural basis of a nucleosome containing histone H2A.B/H2A.Bbd that transiently associates with reorganized chromatin
    • Arimura, Y.; Kimura, H.; Oda, T.; Sato, K.; Osakabe, A.; Tachiwana, H.; Sato, Y.; Kinugasa, Y.; Ikura, T.; Sugiyama, M.; et al. Structural basis of a nucleosome containing histone H2A.B/H2A.Bbd that transiently associates with reorganized chromatin. Sci. Rep. 2013, 16, doi:10.1038/srep03510.
    • (2013) Sci. Rep , vol.16
    • Arimura, Y.1    Kimura, H.2    Oda, T.3    Sato, K.4    Osakabe, A.5    Tachiwana, H.6    Sato, Y.7    Kinugasa, Y.8    Ikura, T.9    Sugiyama, M.10
  • 33
    • 79952536146 scopus 로고    scopus 로고
    • The double face of the histone variant H3.3
    • Szenker, E.; Ray-Gallet, D.; Almouzni, G. The double face of the histone variant H3.3. Cell Res. 2011, 21, 421-434.
    • (2011) Cell Res , vol.21 , pp. 421-434
    • Szenker, E.1    Ray-Gallet, D.2    Almouzni, G.3
  • 34
    • 84859467582 scopus 로고    scopus 로고
    • Evolution of histone H3: Emergence of variants and conservation of post-translational modification sites
    • Waterborg, J.H. Evolution of histone H3: Emergence of variants and conservation of post-translational modification sites. Biochem. Cell Biol. 2012, 90, 79-95.
    • (2012) Biochem. Cell Biol , vol.90 , pp. 79-95
    • Waterborg, J.H.1
  • 35
    • 77955794751 scopus 로고    scopus 로고
    • The evolutionary history of histone H3 suggests a deep eukaryotic root of chromatin modifying mechanisms
    • Postberg, J.; Forcob, S.; Chang, W.J.; Lipps, H.J. The evolutionary history of histone H3 suggests a deep eukaryotic root of chromatin modifying mechanisms. BMC Evol. Biol. 2010, 10, doi:10.1186/1471-2148-10-259.
    • (2010) BMC Evol. Biol , vol.10
    • Postberg, J.1    Forcob, S.2    Chang, W.J.3    Lipps, H.J.4
  • 36
    • 0036849262 scopus 로고    scopus 로고
    • Epigenetic consequences of nucleosome dynamics
    • Ahmad, K.; Henikoff, S. Epigenetic consequences of nucleosome dynamics. Cell 2002, 111, 281-284.
    • (2002) Cell , vol.111 , pp. 281-284
    • Ahmad, K.1    Henikoff, S.2
  • 38
    • 0032739343 scopus 로고    scopus 로고
    • A retroviral gene trap insertion into the histone 3.3A gene causes partial neonatal lethality, stunted growth, neuromuscular deficits and male sub-fertility in transgenic mice
    • Couldrey, C.; Carlton, M.B.; Nolan, P.M.; Colledge, W.H.; Evans, M.J. A retroviral gene trap insertion into the histone 3.3A gene causes partial neonatal lethality, stunted growth, neuromuscular deficits and male sub-fertility in transgenic mice. Hum. Mol. Genet. 1999, 8, 2489-2495.
    • (1999) Hum. Mol. Genet , vol.8 , pp. 2489-2495
    • Couldrey, C.1    Carlton, M.B.2    Nolan, P.M.3    Colledge, W.H.4    Evans, M.J.5
  • 40
    • 84863088107 scopus 로고    scopus 로고
    • A developmental requirement for HIRA-dependent H3.3 deposition revealed at gastrulation in Xenopus
    • Szenker, E.; Lacoste, N.; Almouzni, G. A developmental requirement for HIRA-dependent H3.3 deposition revealed at gastrulation in Xenopus. Cell Rep. 2012, 1, 730-740.
    • (2012) Cell Rep , vol.1 , pp. 730-740
    • Szenker, E.1    Lacoste, N.2    Almouzni, G.3
  • 42
    • 84930939091 scopus 로고    scopus 로고
    • Histone H3.3 is required for endogenous retroviral element silencing in embryonic stem cells
    • Elsässer, S.J.; Noh, K.M.; Diaz, N.; Allis, C.D.; Banaszynski, L.A. Histone H3.3 is required for endogenous retroviral element silencing in embryonic stem cells. Nature 2015, 522, 240-244.
    • (2015) Nature , vol.522 , pp. 240-244
    • Elsässer, S.J.1    Noh, K.M.2    Diaz, N.3    Allis, C.D.4    Banaszynski, L.A.5
  • 46
    • 84922343527 scopus 로고    scopus 로고
    • Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-dependent deposition at centromeres
    • Yu, Z.; Zhou, X.; Wang, W.; Deng, W.; Fang, J.; Hu, H.; Wang, Z.; Li, S.; Cui, L.; Shen, J.; et al. Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-dependent deposition at centromeres. Dev. Cell 2015, 32, 68-81.
    • (2015) Dev. Cell , vol.32 , pp. 68-81
    • Yu, Z.1    Zhou, X.2    Wang, W.3    Deng, W.4    Fang, J.5    Hu, H.6    Wang, Z.7    Li, S.8    Cui, L.9    Shen, J.10
  • 47
    • 84924444021 scopus 로고    scopus 로고
    • CENP-A K124 Ubiquitylation is required for CENP-A deposition at the centromere
    • Niikura, Y.; Kitagawa, R.; Ogi, H.; Abdulle, R.; Pagala, V.; Kitagawa, K. CENP-A K124 Ubiquitylation is required for CENP-A deposition at the centromere. Dev. Cell 2015, 32, 589-603.
    • (2015) Dev. Cell , vol.32 , pp. 589-603
    • Niikura, Y.1    Kitagawa, R.2    Ogi, H.3    Abdulle, R.4    Pagala, V.5    Kitagawa, K.6
  • 49
    • 84928797239 scopus 로고    scopus 로고
    • DNA sequence-specific binding of CENP-B enhances the fidelity of human centromere function
    • Fachinetti, D.; Han, J.S.; McMahon, M.A.; Ly, P.; Abdullah, A.; Wong, A.J.; Cleveland, D.W. DNA sequence-specific binding of CENP-B enhances the fidelity of human centromere function. Dev. Cell 2015, 33, 314-327.
    • (2015) Dev. Cell , vol.33 , pp. 314-327
    • Fachinetti, D.1    Han, J.S.2    McMahon, M.A.3    Ly, P.4    Abdullah, A.5    Wong, A.J.6    Cleveland, D.W.7
  • 51
    • 33646589676 scopus 로고    scopus 로고
    • Chaperone-mediated assembly of centromeric chromatin in vitro
    • Furuyama, T.; Dalal, Y.; Henikoff, S. Chaperone-mediated assembly of centromeric chromatin in vitro. Proc. Natl. Acad. Sci. USA 2006, 103, 6172-6177.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6172-6177
    • Furuyama, T.1    Dalal, Y.2    Henikoff, S.3
  • 52
    • 84924620908 scopus 로고    scopus 로고
    • Histone H3 variants and their chaperones during development and disease: Contributing to epigenetic control
    • Filipescu, D.; Müller, S.; Almouzni, G. Histone H3 variants and their chaperones during development and disease: Contributing to epigenetic control. Annu. Rev. Cell Dev. Biol. 2014, 30, 615-646.
    • (2014) Annu. Rev. Cell Dev. Biol , vol.30 , pp. 615-646
    • Filipescu, D.1    Müller, S.2    Almouzni, G.3
  • 53
    • 84929955270 scopus 로고    scopus 로고
    • Histone H3 mutations-A special role for H3.3 in tumorigenesis?
    • Kallappagoudar, S.; Yadav, R.K.; Lowe, B.R.; Partridge, J.F. Histone H3 mutations-A special role for H3.3 in tumorigenesis? Chromosoma 2015, 124, 177-189.
    • (2015) Chromosoma , vol.124 , pp. 177-189
    • Kallappagoudar, S.1    Yadav, R.K.2    Lowe, B.R.3    Partridge, J.F.4
  • 54
    • 84917692890 scopus 로고    scopus 로고
    • Molecular pathways in gliomagenesis and their relevance to neuropathologic diagnosis
    • Appin, C.L. Brat, D.J. Molecular pathways in gliomagenesis and their relevance to neuropathologic diagnosis. Adv. Anat. Pathol. 2015, 22, 50-58.
    • (2015) Adv. Anat. Pathol , vol.22 , pp. 50-58
    • Appin, C.L.1    Brat, D.J.2
  • 63
    • 0035839066 scopus 로고    scopus 로고
    • The centromere paradox: Stable inheritance with rapidly evolving DNA
    • Henikoff, S.; Ahmad, K.; Malik, H.S. The centromere paradox: Stable inheritance with rapidly evolving DNA. Science 2001, 293, 1098-1102.
    • (2001) Science , vol.293 , pp. 1098-1102
    • Henikoff, S.1    Ahmad, K.2    Malik, H.S.3
  • 64
    • 70149095590 scopus 로고    scopus 로고
    • Major evolutionary transitions in centromere complexity
    • Malik, H.S.; Henikoff, S. Major evolutionary transitions in centromere complexity. Cell 2009, 138, 1067-1082.
    • (2009) Cell , vol.138 , pp. 1067-1082
    • Malik, H.S.1    Henikoff, S.2
  • 65
    • 84928674884 scopus 로고    scopus 로고
    • Recurrent loss of CenH3 is associated with independent transitions to holocentricity in insects
    • Drinnenberg, I.A.; de Young, D.; Henikoff, S.; Malik, H.S. Recurrent loss of CenH3 is associated with independent transitions to holocentricity in insects. Elife 2014, 3, doi:10.7554/eLife.03676.
    • (2014) Elife , vol.3
    • Drinnenberg, I.A.1    de Young, D.2    Henikoff, S.3    Malik, H.S.4
  • 66
    • 12344257200 scopus 로고    scopus 로고
    • A variant histone H3 is enriched at telomeres in Trypanosoma brucei
    • Lowell, J.E.; Cross, G.A. A variant histone H3 is enriched at telomeres in Trypanosoma brucei. J. Cell Sci. 2004, 117, 5937-5947.
    • (2004) J. Cell Sci , vol.117 , pp. 5937-5947
    • Lowell, J.E.1    Cross, G.A.2
  • 68
    • 84896398000 scopus 로고    scopus 로고
    • Discovery of unconventional kinetochores in kinetoplastids
    • Akiyoshi, B.; Gull, K. Discovery of unconventional kinetochores in kinetoplastids. Cell 2014, 156, 1247-1258.
    • (2014) Cell , vol.156 , pp. 1247-1258
    • Akiyoshi, B.1    Gull, K.2
  • 70
    • 84924365661 scopus 로고    scopus 로고
    • Naturally occurring differences in CENH3 affect chromosome segregation in zygotic mitosis of hybrids
    • Maheshwari, S.; Tan, E.H.; West, A.; Franklin, F.C.; Comai, L.; Chan, S.W. Naturally occurring differences in CENH3 affect chromosome segregation in zygotic mitosis of hybrids. PLoS Genet. 2015, 11, e1004970.
    • (2015) PLoS Genet , vol.11
    • Maheshwari, S.1    Tan, E.H.2    West, A.3    Franklin, F.C.4    Comai, L.5    Chan, S.W.6
  • 71
    • 79951709224 scopus 로고    scopus 로고
    • Epigenetic centromere propagation and the nature of CENP-A nucleosomes
    • Black, B.E.; Cleveland, D.W. Epigenetic centromere propagation and the nature of CENP-A nucleosomes. Cell 2011, 144, 471-479.
    • (2011) Cell , vol.144 , pp. 471-479
    • Black, B.E.1    Cleveland, D.W.2
  • 74
    • 84893015721 scopus 로고    scopus 로고
    • CENP-A octamers do not confer a reduction in nucleosome height by AFM
    • Walkiewicz, M.P.; Dimitriadis, E.K.; Dalal, Y. CENP-A octamers do not confer a reduction in nucleosome height by AFM. Nat. Struct. Mol. Biol. 2014, 21, 2-3.
    • (2014) Nat. Struct. Mol. Biol , vol.21 , pp. 2-3
    • Walkiewicz, M.P.1    Dimitriadis, E.K.2    Dalal, Y.3
  • 76
    • 79951711785 scopus 로고    scopus 로고
    • Biophysical characertization of the centromere-specific nulceosome from budding yeast
    • Kingston, I.J.; Yung, J.S.; Singleton, M.R. Biophysical characertization of the centromere-specific nulceosome from budding yeast. J. Biol. Chem. 2011, 286, 4021-4026.
    • (2011) J. Biol. Chem , vol.286 , pp. 4021-4026
    • Kingston, I.J.1    Yung, J.S.2    Singleton, M.R.3
  • 77
    • 79956267847 scopus 로고    scopus 로고
    • Structure of Scm3-mediated assembly of budding yeast centromeric nucleosomes
    • Dechasse, M.L.; Wyns, K.; Li, M.; Hall, M.A.; Wang, M.D.; Luger, K. Structure of Scm3-mediated assembly of budding yeast centromeric nucleosomes. Nat. Commun. 2011, 2, doi:10.1038/ncomms1320.
    • (2011) Nat. Commun , vol.2
    • Dechasse, M.L.1    Wyns, K.2    Li, M.3    Hall, M.A.4    Wang, M.D.5    Luger, K.6
  • 78
    • 84878893101 scopus 로고    scopus 로고
    • Reconstitution of hemisomes on budding yeast centromeric DNA
    • Furuyama, T.; Codomo, C.A.; Henikoff, S. Reconstitution of hemisomes on budding yeast centromeric DNA. Nucleic Acid Res. 2013, 41, 5769-5783.
    • (2013) Nucleic Acid Res , vol.41 , pp. 5769-5783
    • Furuyama, T.1    Codomo, C.A.2    Henikoff, S.3
  • 80
    • 77956897642 scopus 로고    scopus 로고
    • The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres
    • Sekulic, N.; Bassett, E. A.; Rogers, D. J.; Black, D. E. The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres. Nature 2010, 467, 347-351.
    • (2010) Nature , vol.467 , pp. 347-351
    • Sekulic, N.1    Bassett, E.A.2    Rogers, D.J.3    Black, D.E.4
  • 83
    • 84901341958 scopus 로고    scopus 로고
    • Imaging the fate of histone Cse4 reveals de novo replacement in S phase and subsequent stable residence at centromeres
    • Wisniewski, J.; Hajj, B.; Chen, J.; Mizuguchi, G.; Xiao, H.; Wei, D.; Dahan, M.; Wu, C. Imaging the fate of histone Cse4 reveals de novo replacement in S phase and subsequent stable residence at centromeres. Elife 2014, 3, doi:10.7554/eLife.02203.
    • (2014) Elife , vol.3
    • Wisniewski, J.1    Hajj, B.2    Chen, J.3    Mizuguchi, G.4    Xiao, H.5    Wei, D.6    Dahan, M.7    Wu, C.8
  • 84
    • 33846638827 scopus 로고    scopus 로고
    • Incorporation of Drosophila CID/CENP-A and CENP-C into centromeres during early embryonic anaphase
    • Schuh, M.; Lehner, C.F.; Heidmann, S. Incorporation of Drosophila CID/CENP-A and CENP-C into centromeres during early embryonic anaphase. Curr. Biol. 2007, 17, 237-243.
    • (2007) Curr. Biol , vol.17 , pp. 237-243
    • Schuh, M.1    Lehner, C.F.2    Heidmann, S.3
  • 85
    • 33947274529 scopus 로고    scopus 로고
    • Propagation of centromeric chromatin requires exit from mitosis
    • Jansen, L.E.; Black, B.E.; Foltz, D.R.; Cleveland, D.W. Propagation of centromeric chromatin requires exit from mitosis. J. Cell Biol. 2007, 176, 795-805.
    • (2007) J. Cell Biol , vol.176 , pp. 795-805
    • Jansen, L.E.1    Black, B.E.2    Foltz, D.R.3    Cleveland, D.W.4
  • 88
    • 0035945340 scopus 로고    scopus 로고
    • CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis
    • Zeitlin, S.G.; Shebly, R.D.; Sullivan, K.F. CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis. J. Cell Biol. 2001, 155, 1147-1158.
    • (2001) J. Cell Biol , vol.155 , pp. 1147-1158
    • Zeitlin, S.G.1    Shebly, R.D.2    Sullivan, K.F.3
  • 90
    • 84929468570 scopus 로고    scopus 로고
    • A long non-coding RNA is required for targeting centromeric protein A to the human centromere
    • Quénet, D.; Dalal, Y. A long non-coding RNA is required for targeting centromeric protein A to the human centromere. Elife 2014, 3, doi:10.7554/eLife.03254.
    • (2014) Elife , vol.3
    • Quénet, D.1    Dalal, Y.2
  • 91
  • 94
    • 34250745886 scopus 로고    scopus 로고
    • Nucleosome stability mediated by histone variants H3.3 and H2A.Z
    • Jin, C.; Felsenfeld, G. Nucleosome stability mediated by histone variants H3.3 and H2A.Z. Genes Dev. 2007, 21, 1519-1529.
    • (2007) Genes Dev , vol.21 , pp. 1519-1529
    • Jin, C.1    Felsenfeld, G.2
  • 96
    • 84898464557 scopus 로고    scopus 로고
    • Holocentromeres are dispersed point centromeres localized at transcription factor hotspots
    • Steiner, F.A.; Henikoff, S. Holocentromeres are dispersed point centromeres localized at transcription factor hotspots. Elife 2014, 3, doi:10.7554/eLife.02025.
    • (2014) Elife , vol.3
    • Steiner, F.A.1    Henikoff, S.2
  • 97
    • 84855956123 scopus 로고    scopus 로고
    • H3.3 is deposited at centromeres in S phase as a placeholder for newly assembled CENP-A in G1 phase
    • Dunleavy, E.M.; Almouzni, G.; Karpen, G.H. H3.3 is deposited at centromeres in S phase as a placeholder for newly assembled CENP-A in G1 phase. Nucleus 2011, 2, 146-157.
    • (2011) Nucleus , vol.2 , pp. 146-157
    • Dunleavy, E.M.1    Almouzni, G.2    Karpen, G.H.3
  • 98
    • 84928655383 scopus 로고    scopus 로고
    • Separase cleaves the N-Tail of the CENP-A related protein CPAR-1 at the meiosis I metaphase-anaphase transition in C
    • Monen, J.; Hattersley, N.; Muroyama, A.; Stevens, D.; Oegema, K.; Desai, A. Separase cleaves the N-Tail of the CENP-A related protein CPAR-1 at the meiosis I metaphase-anaphase transition in C. elegans. PLoS ONE 2015, 10, e0125382.
    • (2015) Elegans. PLoS ONE , vol.10
    • Monen, J.1    Hattersley, N.2    Muroyama, A.3    Stevens, D.4    Oegema, K.5    Desai, A.6
  • 100
    • 84936873683 scopus 로고    scopus 로고
    • Centromeres off the hook: Massive changes in centromere size and structure following duplication of CenH3 gene in Fabeae species
    • Neumann, P.; Pavlíková, Z.; Koblížkova, A.; Fuková, I.; Jedličkova, V.; Novák, P.; Macas, J. Centromeres off the hook: Massive changes in centromere size and structure following duplication of CenH3 gene in Fabeae species. Mol. Biol. Evol. 2015, doi:10.1093/molbev/msv070.
    • (2015) Mol. Biol. Evol
    • Neumann, P.1    Pavlíková, Z.2    Koblížkova, A.3    Fuková, I.4    Jedličkova, V.5    Novák, P.6    Macas, J.7
  • 101
    • 77956637117 scopus 로고    scopus 로고
    • The expression level of HJURP has an independent prognostic impact and predicts the sensitivity to radiotherapy in breast cancer
    • Hu, Z.; Huang, G.; Sadanandam, A.; Gu, S.; Lenburg, M.E.; Pai, M.; Bayani, N.; Blakely, E.A.; Gray, J.W.; Mao, J.H. The expression level of HJURP has an independent prognostic impact and predicts the sensitivity to radiotherapy in breast cancer. Breast Cancer Res. 2010, 12, doi:10.1186/bcr2487.
    • (2010) Breast Cancer Res , vol.12
    • Hu, Z.1    Huang, G.2    Sadanandam, A.3    Gu, S.4    Lenburg, M.E.5    Pai, M.6    Bayani, N.7    Blakely, E.A.8    Gray, J.W.9    Mao, J.H.10
  • 103
    • 84901872365 scopus 로고    scopus 로고
    • Prognostic significance of EDN/RB, HJURP, p60/CAF-1 and PDLI4, four new markers in high-grade gliomas
    • De Tayrac, M.; Saikali, S.; Aubry, M.; Bellaud, P.; Boniface, R.; Quillien, V.; Mosser, J. Prognostic significance of EDN/RB, HJURP, p60/CAF-1 and PDLI4, four new markers in high-grade gliomas. PLoS ONE 2013, 8, e73332.
    • (2013) PLoS ONE , vol.8
    • De Tayrac, M.1    Saikali, S.2    Aubry, M.3    Bellaud, P.4    Boniface, R.5    Quillien, V.6    Mosser, J.7
  • 106
    • 82755192843 scopus 로고    scopus 로고
    • The CCAN complex: Linking centromere specification to control of kinetochore-microtubule dynamics
    • McAinsh, A.D.; Meraldi, P. The CCAN complex: Linking centromere specification to control of kinetochore-microtubule dynamics. Semin. Cell Dev. Biol. 2011, 22, 946-952.
    • (2011) Semin. Cell Dev. Biol , vol.22 , pp. 946-952
    • McAinsh, A.D.1    Meraldi, P.2
  • 111
  • 112
    • 84859719858 scopus 로고    scopus 로고
    • Putative CENP-B paralogues are not present at mammalian centromeres
    • Marshall, O.J.; Choo, K.H. Putative CENP-B paralogues are not present at mammalian centromeres. Chromosoma 2012, 121, 169-179.
    • (2012) Chromosoma , vol.121 , pp. 169-179
    • Marshall, O.J.1    Choo, K.H.2
  • 113
    • 77953795615 scopus 로고    scopus 로고
    • Adaptive evolution of foundation kinetochore proteins in primates
    • Schueler, M.G.; Swanson, W.; Thomas, P.J.; Green, E.D. Adaptive evolution of foundation kinetochore proteins in primates. Mol. Biol. Evol. 2010, 27, 1585-1597.
    • (2010) Mol. Biol. Evol , vol.27 , pp. 1585-1597
    • Schueler, M.G.1    Swanson, W.2    Thomas, P.J.3    Green, E.D.4
  • 114
    • 84878562344 scopus 로고    scopus 로고
    • A novel role of the N terminus of budding yeast histone H3 variant Cse4 in ubiquitin-mediated proteolysis
    • Au, W.C.; Dawson, A.R.; Rawson, D.W.; Taylor, S.B.; Baker, R.E.; Basrai, M.A. A novel role of the N terminus of budding yeast histone H3 variant Cse4 in ubiquitin-mediated proteolysis. Genetics 2013, 194, 513-518.
    • (2013) Genetics , vol.194 , pp. 513-518
    • Au, W.C.1    Dawson, A.R.2    Rawson, D.W.3    Taylor, S.B.4    Baker, R.E.5    Basrai, M.A.6
  • 116
    • 84930404764 scopus 로고    scopus 로고
    • Pat1 protects centromere-specific histone H3 variant Cse4 from Psh1-mediated ubiquitination
    • Mishra, P.K.; Guo, J.; Dittman, L.E.; Haase, J.; Yeh, E.; Bloom, K.; Basrai, M.A. Pat1 protects centromere-specific histone H3 variant Cse4 from Psh1-mediated ubiquitination. Mol. Biol. Cell 2015, 26, 2067-2079.
    • (2015) Mol. Biol. Cell , vol.26 , pp. 2067-2079
    • Mishra, P.K.1    Guo, J.2    Dittman, L.E.3    Haase, J.4    Yeh, E.5    Bloom, K.6    Basrai, M.A.7
  • 122
    • 23744460663 scopus 로고    scopus 로고
    • Variant histone H3.3 is deposited at sites of nucleosomal displacement throughout transcribed genes while active histone modifications show a promoter-proximal bias
    • Wirbelauer, C.; Bell, O.; Schübeler, D. Variant histone H3.3 is deposited at sites of nucleosomal displacement throughout transcribed genes while active histone modifications show a promoter-proximal bias. Genes Dev. 2005, 19, 1761-1766.
    • (2005) Genes Dev , vol.19 , pp. 1761-1766
    • Wirbelauer, C.1    Bell, O.2    Schübeler, D.3
  • 124
    • 84870904979 scopus 로고    scopus 로고
    • Histone H2A.Z controls a critical chromatin remodeling step required for DNA double-strand break repair
    • Xu, Y.; Ayrapetov, M.K.; Xu, C.; Gursoy-Yuzugullu, O.; Hu, Y.; Price, B.D. Histone H2A.Z controls a critical chromatin remodeling step required for DNA double-strand break repair. Mol. Cell 2012, 48, 723-733.
    • (2012) Mol. Cell , vol.48 , pp. 723-733
    • Xu, Y.1    Ayrapetov, M.K.2    Xu, C.3    Gursoy-Yuzugullu, O.4    Hu, Y.5    Price, B.D.6
  • 125
    • 84883506560 scopus 로고    scopus 로고
    • Histone variant H2A.Z functions in sister chromatid cohesion in Saccharomyces cerevisiae
    • Sharma, U.; Stefanova, D.; Holmes, S.G. Histone variant H2A.Z functions in sister chromatid cohesion in Saccharomyces cerevisiae. Mol. Cell Biol. 2013, 33, 3473-3481.
    • (2013) Mol. Cell Biol , vol.33 , pp. 3473-3481
    • Sharma, U.1    Stefanova, D.2    Holmes, S.G.3
  • 128
    • 81055135515 scopus 로고    scopus 로고
    • Heat shock reduces stalled RNA polymerase II and nucleosome turnover genome-wide
    • Teves, S.S.; Henikoff, S. Heat shock reduces stalled RNA polymerase II and nucleosome turnover genome-wide. Genes Dev. 2011, 25, 2387-2397.
    • (2011) Genes Dev , vol.25 , pp. 2387-2397
    • Teves, S.S.1    Henikoff, S.2
  • 129
    • 84922235253 scopus 로고    scopus 로고
    • Dynamics of histone variant H3.3 and its coregulation with H2A.Z at enhancers and promoters
    • Chen, P.; Wang, Y.; Li, G. Dynamics of histone variant H3.3 and its coregulation with H2A.Z at enhancers and promoters. Nucleus 2014, 5, 21-27.
    • (2014) Nucleus , vol.5 , pp. 21-27
    • Chen, P.1    Wang, Y.2    Li, G.3
  • 130
    • 0028231021 scopus 로고
    • Phylogenetic analysis of the core histones H2A, H2B, H3, and H4
    • Thatcher, T.H.; Gorovsky, M.A. Phylogenetic analysis of the core histones H2A, H2B, H3, and H4. Nucleic Acids Res. 1994, 22, 174-179.
    • (1994) Nucleic Acids Res , vol.22 , pp. 174-179
    • Thatcher, T.H.1    Gorovsky, M.A.2
  • 131
    • 84880775985 scopus 로고    scopus 로고
    • The variant histone H2A.V of Drosophila-Three roles, two guises
    • Baldi, S.; Becker, P.B. The variant histone H2A.V of Drosophila-Three roles, two guises. Chromosoma 2013, 122, 245-258.
    • (2013) Chromosoma , vol.122 , pp. 245-258
    • Baldi, S.1    Becker, P.B.2
  • 132
    • 84923605889 scopus 로고    scopus 로고
    • The Drosophila histone variant H2A.V works in concert with HP1 to promote kinetochore-driven microtubule formation
    • Vernì, F.; Cenci, G. The Drosophila histone variant H2A.V works in concert with HP1 to promote kinetochore-driven microtubule formation. Cell Cycle 2015, 14, 577-588.
    • (2015) Cell Cycle , vol.14 , pp. 577-588
    • Vernì, F.1    Cenci, G.2
  • 133
    • 0025325429 scopus 로고
    • Conservation of intron position indicates separation of major and variant H2As is an early event in the evolution of eukaryotes
    • Van Daal, A.; White, E.M.; Elgin, S.C.; Gorovsky, M.A. Conservation of intron position indicates separation of major and variant H2As is an early event in the evolution of eukaryotes. J. Mol. Evol. 1990, 30, 449-455.
    • (1990) J. Mol. Evol , vol.30 , pp. 449-455
    • Van Daal, A.1    White, E.M.2    Elgin, S.C.3    Gorovsky, M.A.4
  • 134
    • 0029954395 scopus 로고    scopus 로고
    • Essential and nonessential histone H2A variants in Tetrahymena thermophila
    • Liu, X.; Li, B.; Gorovsky, M.A. Essential and nonessential histone H2A variants in Tetrahymena thermophila. Mol. Cell Biol. 1996, 16, 4305-4311.
    • (1996) Mol. Cell Biol , vol.16 , pp. 4305-4311
    • Liu, X.1    Li, B.2    Gorovsky, M.A.3
  • 136
    • 0019877029 scopus 로고
    • Metabolism of ubiquitinated histones
    • Wu, R.S.; Kohn, K.W.; Bonner, W.M. Metabolism of ubiquitinated histones. J. Biol. Chem. 1981, 256, 5916-5920.
    • (1981) J. Biol. Chem , vol.256 , pp. 5916-5920
    • Wu, R.S.1    Kohn, K.W.2    Bonner, W.M.3
  • 137
    • 29444454191 scopus 로고    scopus 로고
    • Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling
    • Li, B.; Pattenden, S.G.; Lee, D.; Gutiérrez, J.; Chen, J.; Seidel, C.; Gerton, J.; Workman, J.L. Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling. Proc. Natl. Acad. Sci. USA 2005, 102, 18385-18390.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18385-18390
    • Li, B.1    Pattenden, S.G.2    Lee, D.3    Gutiérrez, J.4    Chen, J.5    Seidel, C.6    Gerton, J.7    Workman, J.L.8
  • 139
    • 26844489856 scopus 로고    scopus 로고
    • Genome-wide dynamics of Htz1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss
    • Zhang, H.; Roberts, D.N.; Cairns, B.R. Genome-wide dynamics of Htz1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss. Cell 2005, 123, 219-231.
    • (2005) Cell , vol.123 , pp. 219-231
    • Zhang, H.1    Roberts, D.N.2    Cairns, B.R.3
  • 140
    • 84884214357 scopus 로고    scopus 로고
    • Nucleosome-free region dominates histone acetylation in targeting SWR1 to promoters for H2A.Z replacement
    • Ranjan, A.; Mizuguchi, G.; FitzGerald, P.C.; Wei, D.; Wang, F.; Huang, Y.; Luk, E.; Woodcock, C.L.; Wu, C. Nucleosome-free region dominates histone acetylation in targeting SWR1 to promoters for H2A.Z replacement. Cell 2013, 154, 1232-1245.
    • (2013) Cell , vol.154 , pp. 1232-1245
    • Ranjan, A.1    Mizuguchi, G.2    FitzGerald, P.C.3    Wei, D.4    Wang, F.5    Huang, Y.6    Luk, E.7    Woodcock, C.L.8    Wu, C.9
  • 141
    • 84876313606 scopus 로고    scopus 로고
    • A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme
    • Watanabe, S.; Radman-Livaja, M.; Rando, O.J.; Peterson, C.L. A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme. Science 2013, 340, 195-199.
    • (2013) Science , vol.340 , pp. 195-199
    • Watanabe, S.1    Radman-Livaja, M.2    Rando, O.J.3    Peterson, C.L.4
  • 142
    • 84896786505 scopus 로고    scopus 로고
    • Nucleosomes are context-specific, H2A.Z-modulated barriers to RNA polymerase
    • Weber, C.M.; Ramachandran, S.; Henikoff, S. Nucleosomes are context-specific, H2A.Z-modulated barriers to RNA polymerase. Mol. Cell 2014, 53, 819-830.
    • (2014) Mol. Cell , vol.53 , pp. 819-830
    • Weber, C.M.1    Ramachandran, S.2    Henikoff, S.3
  • 144
    • 84937640515 scopus 로고    scopus 로고
    • The histone chaperones FACT and Spt6 restrict H2A.Z from intragenic locations
    • Jeronimo, C.; Watanabe, S.; Kaplan, C.D.; Peterson, C.L.; Robert, F. The histone chaperones FACT and Spt6 restrict H2A.Z from intragenic locations. Mol. Cell 2015, 58, 1113-1123.
    • (2015) Mol. Cell , vol.58 , pp. 1113-1123
    • Jeronimo, C.1    Watanabe, S.2    Kaplan, C.D.3    Peterson, C.L.4    Robert, F.5
  • 146
    • 84890238141 scopus 로고    scopus 로고
    • Epigenetically induced paucity of histone H2A.Z stabilizes fission-yeast ecoptic centromeres
    • Ogiyama, Y.; Ohno, Y.; Kubota, Y.; Ishii, K. Epigenetically induced paucity of histone H2A.Z stabilizes fission-yeast ecoptic centromeres. Nat. Struct. Mol. Biol. 2013, 20, 1397-1406.
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 1397-1406
    • Ogiyama, Y.1    Ohno, Y.2    Kubota, Y.3    Ishii, K.4
  • 147
    • 3042642001 scopus 로고    scopus 로고
    • RNA interference demonstrates a novel role for H2A.Z in chromosome segregation
    • Rangasamy, D.; Greaves, I.; Tremethick, D.J. RNA interference demonstrates a novel role for H2A.Z in chromosome segregation. Nat. Struct. Mol. Biol. 2004, 11, 650-655.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 650-655
    • Rangasamy, D.1    Greaves, I.2    Tremethick, D.J.3
  • 149
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • Costanzi, C.; Pehrson, J.R. Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 1998, 393, 599-601.
    • (1998) Nature , vol.393 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 151
    • 85027919146 scopus 로고    scopus 로고
    • HDAC-mediated suppression of histone turnover promotes epigenetic stability of heterochromatin
    • Aygün, O.; Mehta, S.; Grewal, S.I. HDAC-mediated suppression of histone turnover promotes epigenetic stability of heterochromatin. Nat. Struct. Mol. Biol. 2013, 20, 547-554.
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 547-554
    • Aygün, O.1    Mehta, S.2    Grewal, S.I.3
  • 155
    • 34447099478 scopus 로고    scopus 로고
    • The histone domain of macroH2A1 contains several dispersed elements that are each sufficient to direct enrichment on the inactive X chromosome
    • Nusinow, D.A.; Sharp, J.A.; Morris, A.; Salas, S.; Plath, K.; Panning, B. The histone domain of macroH2A1 contains several dispersed elements that are each sufficient to direct enrichment on the inactive X chromosome. J. Mol. Biol. 2007, 371, 11-18.
    • (2007) J. Mol. Biol , vol.371 , pp. 11-18
    • Nusinow, D.A.1    Sharp, J.A.2    Morris, A.3    Salas, S.4    Plath, K.5    Panning, B.6
  • 156
    • 84880330797 scopus 로고    scopus 로고
    • The expanding role of PARPs in the establishment and maintenance of heterochromatin
    • Dantzer, F.; Santoro, R. The expanding role of PARPs in the establishment and maintenance of heterochromatin. FEBS J. 2013, 280, 3508-3518.
    • (2013) FEBS J , vol.280 , pp. 3508-3518
    • Dantzer, F.1    Santoro, R.2
  • 157
    • 84908875248 scopus 로고    scopus 로고
    • MacroH2A1.1 and PARP-1 cooperate to regulate transcription by promoting CBP-mediated H2B acetylation
    • Chen, H.; Ruiz, P.D.; Novikov, L.; Casill, A.D.; Park, J.W.; Gamble, M.J. MacroH2A1.1 and PARP-1 cooperate to regulate transcription by promoting CBP-mediated H2B acetylation. Nat. Struct. Mol. Biol. 2014, 21, 981-989.
    • (2014) Nat. Struct. Mol. Biol , vol.21 , pp. 981-989
    • Chen, H.1    Ruiz, P.D.2    Novikov, L.3    Casill, A.D.4    Park, J.W.5    Gamble, M.J.6
  • 159
    • 24944578123 scopus 로고    scopus 로고
    • Phosphoserines on maize CENTROMERIC HISTONE H3 and histone H3 demarcate the centromere and pericentromere during chromosome segregation
    • Zhang, X.; Li, X.; Marshall, J.B.; Zhong, C.X.; Dawe, R.K. Phosphoserines on maize CENTROMERIC HISTONE H3 and histone H3 demarcate the centromere and pericentromere during chromosome segregation. Plant Cell 2005, 17, 572-583.
    • (2005) Plant Cell , vol.17 , pp. 572-583
    • Zhang, X.1    Li, X.2    Marshall, J.B.3    Zhong, C.X.4    Dawe, R.K.5
  • 161
    • 84908874060 scopus 로고    scopus 로고
    • PARP1 and CBP lose their footing in cancer
    • Timinszky, G.; Ladurner, A.G. PARP1 and CBP lose their footing in cancer. Nat. Struct. Mol. Biol. 2014, 21, 947-948.
    • (2014) Nat. Struct. Mol. Biol , vol.21 , pp. 947-948
    • Timinszky, G.1    Ladurner, A.G.2
  • 166
    • 84878282462 scopus 로고    scopus 로고
    • Histone variants in pluripotency and disease
    • Skene, P.J.; Henikoff, S. Histone variants in pluripotency and disease. Development 2013, 140, 2513-2524.
    • (2013) Development , vol.140 , pp. 2513-2524
    • Skene, P.J.1    Henikoff, S.2
  • 168
    • 0034570369 scopus 로고    scopus 로고
    • Rearrangement of chromatin domains in cancer and development
    • Vassetzky, Y.S.; Hair, A.; Razin, S.V. Rearrangement of chromatin domains in cancer and development. J. Cell. Biochem. Suppl. 2000, 35, 54-60.
    • (2000) J. Cell. Biochem. Suppl , vol.35 , pp. 54-60
    • Vassetzky, Y.S.1    Hair, A.2    Razin, S.V.3
  • 169
    • 14844362770 scopus 로고    scopus 로고
    • Organization of the genome and gene expression in a nuclear environment lacking histones and nucleosomes: The amazing dinoflagellates
    • De la Espina, S.M.D.; Alverca, E.; Cuadrado, A.; Franca, S. Organization of the genome and gene expression in a nuclear environment lacking histones and nucleosomes: The amazing dinoflagellates. Eur. J. Cell Biol. 2005, 84, 137-149.
    • (2005) Eur. J. Cell Biol , vol.84 , pp. 137-149
    • De la Espina, S.M.D.1    Alverca, E.2    Cuadrado, A.3    Franca, S.4
  • 170
    • 33747295520 scopus 로고    scopus 로고
    • Alveolata histone-like proteins have different evolutionary origins
    • Chan, Y.H.; Kwok, A.C.; Tsang, J.S.; Wong, J.T. Alveolata histone-like proteins have different evolutionary origins. J. Evol. Biol. 2006, 19, 1717-1721.
    • (2006) J. Evol. Biol , vol.19 , pp. 1717-1721
    • Chan, Y.H.1    Kwok, A.C.2    Tsang, J.S.3    Wong, J.T.4
  • 171
    • 84871289612 scopus 로고    scopus 로고
    • Loss of nucleosomal DNA condensation coincides with appearance of a novel nuclear protein in dinoflagellates
    • Gornik, S.G.; Ford, K.L.; Mulhern, T.D.; Bacic, A.; McFadden, G.I.; Waller, R.F. Loss of nucleosomal DNA condensation coincides with appearance of a novel nuclear protein in dinoflagellates. Curr. Biol. 2012, 22, 2303-2312.
    • (2012) Curr. Biol , vol.22 , pp. 2303-2312
    • Gornik, S.G.1    Ford, K.L.2    Mulhern, T.D.3    Bacic, A.4    McFadden, G.I.5    Waller, R.F.6
  • 172
    • 33748706963 scopus 로고    scopus 로고
    • Archaeal histones and the origin of the histone fold
    • Sandman, K.; Reeve, J.N. Archaeal histones and the origin of the histone fold. Curr. Opin. Microbiol. 2006, 9, 520-525.
    • (2006) Curr. Opin. Microbiol , vol.9 , pp. 520-525
    • Sandman, K.1    Reeve, J.N.2
  • 174
    • 0034644722 scopus 로고    scopus 로고
    • Crystal structures of recombinant histones HMfA and HMfB from the hyperthermophilic archaeon Methanothermus fervidus
    • Decanniere, K.; Babu, A.M.; Sandman, K.; Reeve, J.N.; Heinemann, U. Crystal structures of recombinant histones HMfA and HMfB from the hyperthermophilic archaeon Methanothermus fervidus. J. Mol. Biol. 2000, 303, 35-47.
    • (2000) J. Mol. Biol , vol.303 , pp. 35-47
    • Decanniere, K.1    Babu, A.M.2    Sandman, K.3    Reeve, J.N.4    Heinemann, U.5
  • 175
    • 0028867087 scopus 로고
    • The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization
    • Arents, G.; Moudrianakis, E.N. The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization. Proc. Natl. Acad. Sci. USA 1995, 92, 11170-11174.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11170-11174
    • Arents, G.1    Moudrianakis, E.N.2
  • 176
    • 84928966683 scopus 로고    scopus 로고
    • Genesis of chromatin and transcription dynamics in the origin of species
    • Koster, M.J.; Snel, B.; Timmers, H.T. Genesis of chromatin and transcription dynamics in the origin of species. Cell 2015, 161, 724-736.
    • (2015) Cell , vol.161 , pp. 724-736
    • Koster, M.J.1    Snel, B.2    Timmers, H.T.3
  • 177
    • 84902758295 scopus 로고    scopus 로고
    • Molecular evolution of NASP and conserved histone H3/H4 transport pathway
    • Nabeel-Shah, S.; Ashraf, K.; Pearlman, R.E.; Fillingham, J. Molecular evolution of NASP and conserved histone H3/H4 transport pathway. BMC Evol. Biol. 2014, 14, 139, doi:10.1186/1471-2148-14-139.
    • (2014) BMC Evol. Biol , vol.14 , pp. 139
    • Nabeel-Shah, S.1    Ashraf, K.2    Pearlman, R.E.3    Fillingham, J.4
  • 178
    • 84922182239 scopus 로고    scopus 로고
    • Histone H2A.Z subunit exchange controls consolidation of recent and remote memory
    • Zovkic, I.B.; Paulukaitis, B.S.; Day, J.J.; Etikala, D.M.; Sweatt, J.D. Histone H2A.Z subunit exchange controls consolidation of recent and remote memory. Nature 2014, 515, 582-586.
    • (2014) Nature , vol.515 , pp. 582-586
    • Zovkic, I.B.1    Paulukaitis, B.S.2    Day, J.J.3    Etikala, D.M.4    Sweatt, J.D.5
  • 179
    • 8444231721 scopus 로고    scopus 로고
    • Non-B DNA conformations, genomic rearrangements, and human disease
    • Bacolla, A.; Wells, R.D. Non-B DNA conformations, genomic rearrangements, and human disease. J. Biol. Chem. 2004, 279, 47411-47414.
    • (2004) J. Biol. Chem , vol.279 , pp. 47411-47414
    • Bacolla, A.1    Wells, R.D.2
  • 180
    • 66149136847 scopus 로고    scopus 로고
    • Discovery of the role of non-B DNA structures in mutagenesis and human genomic disorders
    • Wells, R.D. Discovery of the role of non-B DNA structures in mutagenesis and human genomic disorders. J. Biol. Chem. 2009, 284, 8997-9009.
    • (2009) J. Biol. Chem , vol.284 , pp. 8997-9009
    • Wells, R.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.