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Volumn 357, Issue 6349, 2017, Pages

ChromEMT: Visualizing 3D chromatin structure and compaction in interphase and mitotic cells

Author keywords

[No Author keywords available]

Indexed keywords

DIAMINOBENZIDINE; FLUORESCENT DYE; OSMIUM; POLYMER; 1,5-BIS((2-(METHYLAMINO)ETHYL)AMINO)-4,8-DIHYDROXYANTHRACENE-9,10-DIONE; ANTHRAQUINONE DERIVATIVE; DNA;

EID: 85026314548     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aag0025     Document Type: Article
Times cited : (602)

References (88)
  • 1
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids; a structure for deoxyribose nucleic acid
    • pmid: 13054692
    • J. D. Watson, F. H. Crick, Molecular structure of nucleic acids; a structure for deoxyribose nucleic acid. Nature 171, 737–738 (1953). doi: 10.1038/171737a0; pmid: 13054692
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.2
  • 2
    • 0037992395 scopus 로고    scopus 로고
    • The structure of DNA in the nucleosome core
    • pmid: 12736678
    • T. J. Richmond, C. A. Davey, The structure of DNA in the nucleosome core. Nature 423, 145–150 (2003). doi: 10.1038/ nature01595; pmid: 12736678
    • (2003) Nature , vol.423 , pp. 145-150
    • Richmond, T.J.1    Davey, C.A.2
  • 3
    • 29244467484 scopus 로고    scopus 로고
    • Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length
    • pmid: 16506093
    • C. L. Woodcock, A. I. Skoultchi, Y. Fan, Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length. Chromosome Res. 14, 17–25 (2006). doi: 10.1007/s10577-005-1024-3; pmid: 16506093
    • (2006) Chromosome Res. , vol.14 , pp. 17-25
    • Woodcock, C.L.1    Skoultchi, A.I.2    Fan, Y.3
  • 4
    • 77955283768 scopus 로고    scopus 로고
    • Chromatin higher-order structure and dynamics
    • pmid: 20452954
    • C. L. Woodcock, R. P. Ghosh, Chromatin higher-order structure and dynamics. Cold Spring Harb. Perspect. Biol. 2, a000596 (2010). doi: 10.1101/cshperspect.a000596; pmid: 20452954
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2 , pp. a000596
    • Woodcock, C.L.1    Ghosh, R.P.2
  • 5
    • 84875190221 scopus 로고    scopus 로고
    • Genome architecture: Domain organization of interphase chromosomes
    • pmid: 23498936
    • W. A. Bickmore, B. van Steensel, Genome architecture: Domain organization of interphase chromosomes. Cell 152, 1270–1284 (2013). doi: 10.1016/j.cell.2013.02.001; pmid: 23498936
    • (2013) Cell , vol.152 , pp. 1270-1284
    • Bickmore, W.A.1    Van Steensel, B.2
  • 6
    • 0032564478 scopus 로고    scopus 로고
    • Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin
    • pmid: 9826673
    • J. Bednar et al., Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin. Proc. Natl. Acad. Sci. U.S.A. 95, 14173–14178 (1998). doi: 10.1073/ pnas.95.24.14173; pmid: 9826673
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14173-14178
    • Bednar, J.1
  • 7
    • 33646242052 scopus 로고    scopus 로고
    • EM measurements define the dimensions of the “30-nm” chromatin fiber: Evidence for a compact, interdigitated structure
    • pmid: 16617109
    • P. J. Robinson, L. Fairall, V. A. 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. 103, 6506–6511 (2006). doi: 10.1073/pnas.0601212103; pmid: 16617109
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6506-6511
    • Robinson, P.J.1    Fairall, L.2    Huynh, V.A.3    Rhodes, D.4
  • 8
    • 21844436803 scopus 로고    scopus 로고
    • X-ray structure of a tetranucleosome and its implications for the chromatin fibre
    • pmid: 16001076
    • T. Schalch, S. Duda, D. F. Sargent, T. J. Richmond, X-ray structure of a tetranucleosome and its implications for the chromatin fibre. Nature 436, 138–141 (2005). doi: 10.1038/ nature03686; pmid: 16001076
    • (2005) Nature , vol.436 , pp. 138-141
    • Schalch, T.1    Duda, S.2    Sargent, D.F.3    Richmond, T.J.4
  • 9
    • 84899570718 scopus 로고    scopus 로고
    • Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units
    • pmid: 24763583
    • F. Song et al., Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units. Science 344, 376–380 (2014). doi: 10.1126/science.1251413; pmid: 24763583
    • (2014) Science , vol.344 , pp. 376-380
    • Song, F.1
  • 10
    • 0024319521 scopus 로고
    • Large-scale chromatin structural domains within mitotic and interphase chromosomes in vivo and in vitro
    • pmid: 2476279
    • A. S. Belmont, M. B. Braunfeld, J. W. Sedat, D. A. Agard, Large-scale chromatin structural domains within mitotic and interphase chromosomes in vivo and in vitro. Chromosoma 98, 129–143 (1989). doi: 10.1007/BF00291049; pmid: 2476279
    • (1989) Chromosoma , vol.98 , pp. 129-143
    • Belmont, A.S.1    Braunfeld, M.B.2    Sedat, J.W.3    Agard, D.A.4
  • 11
    • 0028019457 scopus 로고
    • Visualization of G1 chromosomes: A folded, twisted, supercoiled chromonema model of interphase chromatid structure
    • pmid: 7929576
    • A. S. Belmont, K. Bruce, Visualization of G1 chromosomes: A folded, twisted, supercoiled chromonema model of interphase chromatid structure. J. Cell Biol. 127, 287–302 (1994). doi: 10.1083/jcb.127.2.287; pmid: 7929576
    • (1994) J. Cell Biol. , vol.127 , pp. 287-302
    • Belmont, A.S.1    Bruce, K.2
  • 12
    • 0017281914 scopus 로고
    • Ultrastructural features of chromatin nu bodies
    • pmid: 1035912
    • A. L. Olins, M. B. Senior, D. E. Olins, Ultrastructural features of chromatin nu bodies. J. Cell Biol. 68, 787–793 (1976). doi: 10.1083/jcb.68.3.787; pmid: 1035912
    • (1976) J. Cell Biol. , vol.68 , pp. 787-793
    • Olins, A.L.1    Senior, M.B.2    Olins, D.E.3
  • 13
    • 0016631410 scopus 로고
    • Visualization of chromatin substructure: Upsilon bodies
    • pmid: 1150743
    • A. L. Olins, R. D. Carlson, D. E. Olins, Visualization of chromatin substructure: Upsilon bodies. J. Cell Biol. 64, 528–537 (1975). doi: 10.1083/jcb.64.3.528; pmid: 1150743
    • (1975) J. Cell Biol. , vol.64 , pp. 528-537
    • Olins, A.L.1    Carlson, R.D.2    Olins, D.E.3
  • 14
    • 0017583351 scopus 로고
    • A direct approach to the structure of eukaryotic chromosomes
    • pmid: 98280
    • J. Sedat, L. Manuelidis, A direct approach to the structure of eukaryotic chromosomes. Cold Spring Harb. Symp. Quant. Biol. 42, 331–350 (1978). doi: 10.1101/ SQB.1978.042.01.035; pmid: 98280
    • (1978) Cold Spring Harb. Symp. Quant. Biol. , vol.42 , pp. 331-350
    • Sedat, J.1    Manuelidis, L.2
  • 15
    • 0022386283 scopus 로고
    • Radial loops and helical coils coexist in metaphase chromosomes
    • pmid: 4016953
    • J. B. Rattner, C. C. Lin, Radial loops and helical coils coexist in metaphase chromosomes. Cell 42, 291–296 (1985). doi: 10.1016/S0092-8674(85)80124-0; pmid: 4016953
    • (1985) Cell , vol.42 , pp. 291-296
    • Rattner, J.B.1    Lin, C.C.2
  • 16
    • 0023368794 scopus 로고
    • A three-dimensional approach to mitotic chromosome structure: Evidence for a complex hierarchical organization
    • pmid: 3112167
    • A. S. Belmont, J. W. Sedat, D. A. Agard, A three-dimensional approach to mitotic chromosome structure: Evidence for a complex hierarchical organization. J. Cell Biol. 105, 77–92 (1987). doi: 10.1083/jcb.105.1.77; pmid: 3112167
    • (1987) J. Cell Biol. , vol.105 , pp. 77-92
    • Belmont, A.S.1    Sedat, J.W.2    Agard, D.A.3
  • 17
    • 4644360416 scopus 로고    scopus 로고
    • Visualization of early chromosome condensation
    • pmid: 15353545
    • N. Kireeva, M. Lakonishok, I. Kireev, T. Hirano, A. S. Belmont, Visualization of early chromosome condensation. J. Cell Biol. 166, 775–785 (2004). doi: 10.1083/jcb.200406049; pmid: 15353545
    • (2004) J. Cell Biol. , vol.166 , pp. 775-785
    • Kireeva, N.1    Lakonishok, M.2    Kireev, I.3    Hirano, T.4    Belmont, A.S.5
  • 18
    • 11144321432 scopus 로고    scopus 로고
    • Organization of chromatin in the interphase mammalian cell
    • pmid: 15629642
    • H. Dehghani, G. Dellaire, D. P. Bazett-Jones, Organization of chromatin in the interphase mammalian cell. Micron 36, 95–108 (2005). doi: 10.1016/j.micron.2004.10.003; pmid: 15629642
    • (2005) Micron , vol.36 , pp. 95-108
    • Dehghani, H.1    Dellaire, G.2    Bazett-Jones, D.P.3
  • 19
    • 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
    • pmid: 19064912
    • M. Eltsov, 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. 105, 19732–19737 (2008). doi: 10.1073/pnas.0810057105; pmid: 19064912
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 19732-19737
    • Eltsov, M.1    Maclellan, K.M.2    Maeshima, K.3    Frangakis, A.S.4    Dubochet, J.5
  • 20
    • 0022726854 scopus 로고
    • Cryo-electron microscopy of vitrified chromosomes in situ
    • pmid: 3755397
    • A. W. McDowall, J. M. Smith, J. Dubochet, Cryo-electron microscopy of vitrified chromosomes in situ. EMBO J. 5, 1395–1402 (1986). pmid: 3755397
    • (1986) EMBO J. , vol.5 , pp. 1395-1402
    • McDowall, A.W.1    Smith, J.M.2    Dubochet, J.3
  • 21
    • 84859421494 scopus 로고    scopus 로고
    • Human mitotic chromosomes consist predominantly of irregularly folded nucleosome fibres without a 30-nm chromatin structure
    • pmid: 22343941
    • Y. Nishino et al., Human mitotic chromosomes consist predominantly of irregularly folded nucleosome fibres without a 30-nm chromatin structure. EMBO J. 31, 1644–1653 (2012). doi: 10.1038/emboj.2012.35; pmid: 22343941
    • (2012) EMBO J. , vol.31 , pp. 1644-1653
    • Nishino, Y.1
  • 22
    • 77956272401 scopus 로고    scopus 로고
    • Global chromatin architecture reflects pluripotency and lineage commitment in the early mouse embryo
    • pmid: 20479880
    • K. Ahmed et al., Global chromatin architecture reflects pluripotency and lineage commitment in the early mouse embryo. PLOS ONE 5, e10531 (2010). doi: 10.1371/journal. pone.0010531; pmid: 20479880
    • (2010) PLOS ONE , vol.5 , pp. e10531
    • Ahmed, K.1
  • 23
    • 84868690351 scopus 로고    scopus 로고
    • Open and closed domains in the mouse genome are configured as 10-nm chromatin fibres
    • pmid: 22986547
    • E. Fussner et al., Open and closed domains in the mouse genome are configured as 10-nm chromatin fibres. EMBO Rep. 13, 992–996 (2012). doi: 10.1038/embor.2012.139; pmid: 22986547
    • (2012) EMBO Rep. , vol.13 , pp. 992-996
    • Fussner, E.1
  • 24
    • 84959419478 scopus 로고    scopus 로고
    • Visualizing the molecular sociology at the HeLa cell nuclear periphery
    • pmid: 26917770
    • J. Mahamid et al., Visualizing the molecular sociology at the HeLa cell nuclear periphery. Science 351, 969–972 (2016). doi: 10.1126/science.aad8857; pmid: 26917770
    • (2016) Science , vol.351 , pp. 969-972
    • Mahamid, J.1
  • 25
    • 30044447160 scopus 로고    scopus 로고
    • Cryoelectron microscopy of vitrified sections: A new challenge for the analysis of functional nuclear architecture
    • pmid: 16328430
    • C. Bouchet-Marquis, J. Dubochet, S. Fakan, Cryoelectron microscopy of vitrified sections: A new challenge for the analysis of functional nuclear architecture. Histochem. Cell Biol. 125, 43–51 (2006). doi: 10.1007/s00418-005-0093-x; pmid: 16328430
    • (2006) Histochem. Cell Biol. , vol.125 , pp. 43-51
    • Bouchet-Marquis, C.1    Dubochet, J.2    Fakan, S.3
  • 26
    • 77958569747 scopus 로고    scopus 로고
    • Condensed mitotic chromosome structure at nanometer resolution using PALM and EGFP- Histones
    • pmid: 20856676
    • A. Matsuda et al., Condensed mitotic chromosome structure at nanometer resolution using PALM and EGFP- histones. PLOS ONE 5, e12768 (2010). doi: 10.1371/journal. pone.0012768; pmid: 20856676
    • (2010) PLOS ONE , vol.5 , pp. e12768
    • Matsuda, A.1
  • 27
    • 45549091077 scopus 로고    scopus 로고
    • Subdiffraction multicolor imaging of the nuclear periphery with 3D structured illumination microscopy
    • pmid: 18535242
    • L. Schermelleh et al., Subdiffraction multicolor imaging of the nuclear periphery with 3D structured illumination microscopy. Science 320, 1332–1336 (2008). doi: 10.1126/ science.1156947; pmid: 18535242
    • (2008) Science , vol.320 , pp. 1332-1336
    • Schermelleh, L.1
  • 28
    • 84900824181 scopus 로고    scopus 로고
    • Three-dimensional super-resolution microscopy of the inactive X chromosome territory reveals a collapse of its active nuclear compartment harboring distinct Xist RNA foci
    • pmid: 25057298
    • D. Smeets et al., Three-dimensional super-resolution microscopy of the inactive X chromosome territory reveals a collapse of its active nuclear compartment harboring distinct Xist RNA foci. Epigenetics Chromatin 7, 8 (2014). doi: 10.1186/1756-8935-7-8; pmid: 25057298
    • (2014) Epigenetics Chromatin , vol.7 , pp. 8
    • Smeets, D.1
  • 29
    • 84857032212 scopus 로고    scopus 로고
    • Super-resolution fluorescence imaging of chromosomal DNA
    • pmid: 22226957
    • P. J. Zessin, K. Finan, M. Heilemann, Super-resolution fluorescence imaging of chromosomal DNA. J. Struct. Biol. 177, 344–348 (2012). doi: 10.1016/j.jsb.2011.12.015; pmid: 22226957
    • (2012) J. Struct. Biol. , vol.177 , pp. 344-348
    • Zessin, P.J.1    Finan, K.2    Heilemann, M.3
  • 30
    • 84924559967 scopus 로고    scopus 로고
    • Chromatin fibers are formed by heterogeneous groups of nucleosomes in vivo
    • pmid: 25768910
    • M. A. Ricci, C. Manzo, M. F. García-Parajo, M. Lakadamyali, M. P. Cosma, Chromatin fibers are formed by heterogeneous groups of nucleosomes in vivo. Cell 160, 1145–1158 (2015). doi: 10.1016/j.cell.2015.01.054; pmid: 25768910
    • (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
  • 31
    • 84955290042 scopus 로고    scopus 로고
    • Super-resolution imaging reveals distinct chromatin folding for different epigenetic states
    • pmid: 26760202
    • A. N. Boettiger et al., Super-resolution imaging reveals distinct chromatin folding for different epigenetic states. Nature 529, 418–422 (2016). doi: 10.1038/nature16496; pmid: 26760202
    • (2016) Nature , vol.529 , pp. 418-422
    • Boettiger, A.N.1
  • 32
    • 0022967955 scopus 로고
    • A stable lead by modification of Sato’s method
    • pmid: 2440973
    • T. Hanaichi et al., A stable lead by modification of Sato’s method. J. Electron Microsc. (Tokyo) 35, 304–306 (1986). pmid: 2440973
    • (1986) J. Electron Microsc. (Tokyo) , vol.35 , pp. 304-306
    • Hanaichi, T.1
  • 33
    • 0000523688 scopus 로고
    • Staining of tissue sections for electron microscopy with heavy metals
    • pmid: 13610936
    • M. L. Watson, Staining of tissue sections for electron microscopy with heavy metals. J. Biophys. Biochem. Cytol. 4, 727–730 (1958). doi: 10.1083/jcb.4.6.727; pmid: 13610936
    • (1958) J. Biophys. Biochem. Cytol. , vol.4 , pp. 727-730
    • Watson, M.L.1
  • 34
    • 0001032086 scopus 로고
    • Preferential staining of nucleic acid-containing structures for electron microscopy
    • pmid: 14450292
    • H. E. Huxley, G. Zubay, Preferential staining of nucleic acid-containing structures for electron microscopy. J. Biophys. Biochem. Cytol. 11, 273–296 (1961). doi: 10.1083/jcb.11.2.273; pmid: 14450292
    • (1961) J. Biophys. Biochem. Cytol. , vol.11 , pp. 273-296
    • Huxley, H.E.1    Zubay, G.2
  • 35
    • 0015847493 scopus 로고
    • Mise en évidence de l’ADN et des polysaccharides à l’aide d’un nouveau réactif “de type Schiff”
    • pmid: 4198810
    • R. Cogliati, A. Gautier, Mise en évidence de l’ADN et des polysaccharides à l’aide d’un nouveau réactif “de type Schiff.” C. R. Acad. Sci. Hebd. Seances Acad. Sci. D 276, 3041–3044 (1973). pmid: 4198810
    • (1973) C. R. Acad. Sci. Hebd. Seances Acad. Sci. D , vol.276 , pp. 3041-3044
    • Cogliati, R.1    Gautier, A.2
  • 36
    • 0024598768 scopus 로고
    • Synthesis of a more stable osmium ammine electron-dense DNA stain
    • pmid: 2465337
    • A. L. Olins, B. A. Moyer, S. H. Kim, D. P. Allison, Synthesis of a more stable osmium ammine electron-dense DNA stain. J. Histochem. Cytochem. 37, 395–398 (1989). doi: 10.1177/ 37.3.2465337; pmid: 2465337
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 395-398
    • Olins, A.L.1    Moyer, B.A.2    Kim, S.H.3    Allison, D.P.4
  • 37
    • 34447634290 scopus 로고    scopus 로고
    • Control and selectivity of photosensitized singlet oxygen production: Challenges in complex biological systems
    • pmid: 17323398
    • E. Cló, J. W. Snyder, P. R. Ogilby, K. V. Gothelf, Control and selectivity of photosensitized singlet oxygen production: Challenges in complex biological systems. ChemBioChem 8, 475–481 (2007). doi: 10.1002/cbic.200600454; pmid: 17323398
    • (2007) Chembiochem , vol.8 , pp. 475-481
    • Cló, E.1    Snyder, J.W.2    Ogilby, P.R.3    Gothelf, K.V.4
  • 38
    • 0025295136 scopus 로고
    • Photoconversion of fluorescent retrograde tracers
    • pmid: 1695999
    • M. Bentivoglio, H. S. Su, Photoconversion of fluorescent retrograde tracers. Neurosci. Lett. 113, 127–133 (1990). doi: 10.1016/0304-3940(90)90291-G; pmid: 1695999
    • (1990) Neurosci. Lett. , vol.113 , pp. 127-133
    • Bentivoglio, M.1    Su, H.S.2
  • 39
    • 0027989511 scopus 로고
    • Fluorescence photooxidation with eosin: A method for high resolution immunolocalization and in situ hybridization detection for light and electron microscopy
    • pmid: 7519623
    • T. J. Deerinck et al., Fluorescence photooxidation with eosin: A method for high resolution immunolocalization and in situ hybridization detection for light and electron microscopy. J. Cell Biol. 126, 901–910 (1994). doi: 10.1083/ jcb.126.4.901; pmid: 7519623
    • (1994) J. Cell Biol. , vol.126 , pp. 901-910
    • Deerinck, T.J.1
  • 40
    • 84947487599 scopus 로고    scopus 로고
    • Visualizing viral protein structures in cells using genetic probes for correlated light and electron microscopy
    • pmid: 26066760
    • H. D. Ou, T. J. Deerinck, E. Bushong, M. H. Ellisman, C. C. O’Shea, Visualizing viral protein structures in cells using genetic probes for correlated light and electron microscopy. Methods 90, 39–48 (2015). doi: 10.1016/j.ymeth.2015.06.002; pmid: 26066760
    • (2015) Methods , vol.90 , pp. 39-48
    • Ou, H.D.1    Deerinck, T.J.2    Bushong, E.3    Ellisman, M.H.4    O’Shea, C.C.5
  • 41
    • 0013895415 scopus 로고
    • The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: Ultrastructural cytochemistry by a new technique
    • pmid: 5962951
    • R. C. Graham Jr., M. J. Karnovsky, The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: Ultrastructural cytochemistry by a new technique. J. Histochem. Cytochem. 14, 291–302 (1966). doi: 10.1177/14.4.291; pmid: 5962951
    • (1966) J. Histochem. Cytochem. , vol.14 , pp. 291-302
    • Graham, R.C.1    Karnovsky, M.J.2
  • 42
    • 79955504165 scopus 로고    scopus 로고
    • A genetically encoded tag for correlated light and electron microscopy of intact cells, tissues, and organisms
    • pmid: 21483721
    • X. Shu et al., A genetically encoded tag for correlated light and electron microscopy of intact cells, tissues, and organisms. PLOS Biol. 9, e1001041 (2011). doi: 10.1371/journal. pbio.1001041; pmid: 21483721
    • (2011) PLOS Biol. , vol.9 , pp. e1001041
    • Shu, X.1
  • 43
    • 84867564497 scopus 로고    scopus 로고
    • A structural basis for the assembly and functions of a viral polymer that inactivates multiple tumor suppressors
    • pmid: 23063122
    • H. D. Ou et al., A structural basis for the assembly and functions of a viral polymer that inactivates multiple tumor suppressors. Cell 151, 304–319 (2012). doi: 10.1016/ j.cell.2012.08.035; pmid: 23063122
    • (2012) Cell , vol.151 , pp. 304-319
    • Ou, H.D.1
  • 44
    • 0030057562 scopus 로고    scopus 로고
    • Improving the efficacy of fluorescent labeling for histological tracking of cells in early mammalian and avian embryos
    • pmid: 8838429
    • H. J. Garton, G. C. Schoenwolf, Improving the efficacy of fluorescent labeling for histological tracking of cells in early mammalian and avian embryos. Anat. Rec. 244, 112–117 (1996). doi: 10.1002/(SICI)1097-0185(199601)244:1〈112::AIDAR11〉3.0.CO;2-S; pmid: 8838429
    • (1996) Anat. Rec. , vol.244 , pp. 112-117
    • Garton, H.J.1    Schoenwolf, G.C.2
  • 45
    • 0026448285 scopus 로고
    • Electron microscopic analysis of fluorescent neuronal labeling after photoconversion
    • pmid: 1283435
    • G. Balercia, S. Chen, M. Bentivoglio, Electron microscopic analysis of fluorescent neuronal labeling after photoconversion. J. Neurosci. Methods 45, 87–98 (1992). doi: 10.1016/ 0165-0270(92)90046-G; pmid: 1283435
    • (1992) J. Neurosci. Methods , vol.45 , pp. 87-98
    • Balercia, G.1    Chen, S.2    Bentivoglio, M.3
  • 46
    • 55249116998 scopus 로고    scopus 로고
    • DRAQ5 labeling of nuclear DNA in live and fixed cells
    • P. J. Smith, M. Wiltshire, R. J. Errington, DRAQ5 labeling of nuclear DNA in live and fixed cells. Current Protoc. Cytom. 28, 7.25.1–7.21.11 (2004). .doi: 10.1002/0471142956.cy0725s28
    • (2004) Current Protoc. Cytom. , vol.28 , pp. 7.25.1-7.21.11
    • Smith, P.J.1    Wiltshire, M.2    Errington, R.J.3
  • 47
    • 33749146554 scopus 로고    scopus 로고
    • Spectral analysis of the DNA targeting bisalkylaminoanthraquinone DRAQ5 in intact living cells
    • pmid: 16969814
    • K. L. Njoh et al., Spectral analysis of the DNA targeting bisalkylaminoanthraquinone DRAQ5 in intact living cells. Cytometry A 69A, 805–814 (2006). doi: 10.1002/cyto. a.20308; pmid: 16969814
    • (2006) Cytometry A , vol.69 A , pp. 805-814
    • Njoh, K.L.1
  • 48
    • 24944488016 scopus 로고    scopus 로고
    • DNA labeling in living cells
    • pmid: 16082711
    • R. M. Martin, H. Leonhardt, M. C. Cardoso, DNA labeling in living cells. Cytometry A 67A, 45–52 (2005). doi: 10.1002/ cyto.a.20172; pmid: 16082711
    • (2005) Cytometry A , vol.67 A , pp. 45-52
    • Martin, R.M.1    Leonhardt, H.2    Cardoso, M.C.3
  • 49
    • 78650656887 scopus 로고    scopus 로고
    • Short exposure to the DNA intercalator DRAQ5 dislocates the transcription machinery and induces cell death
    • pmid: 21175643
    • E. Richard et al., Short exposure to the DNA intercalator DRAQ5 dislocates the transcription machinery and induces cell death. Photochem. Photobiol. 87, 256–261 (2011). doi: 10.1111/ j.1751-1097.2010.00852.x; pmid: 21175643
    • (2011) Photochem. Photobiol. , vol.87 , pp. 256-261
    • Richard, E.1
  • 50
    • 44949098358 scopus 로고    scopus 로고
    • Interaction of a DNA intercalator DRAQ5, and a minor groove binder SYTO17, with chromatin in live cells—influence on chromatin organization and histone-DNA interactions
    • pmid: 18459157
    • K. Wojcik, J. W. Dobrucki, Interaction of a DNA intercalator DRAQ5, and a minor groove binder SYTO17, with chromatin in live cells—influence on chromatin organization and histone-DNA interactions. Cytometry A 73A, 555–562 (2008). doi: 10.1002/cyto.a.20573; pmid: 18459157
    • (2008) Cytometry A , vol.73 A , pp. 555-562
    • Wojcik, K.1    Dobrucki, J.W.2
  • 52
    • 0016252660 scopus 로고
    • Observations on nucleolar staining with osmium tetroxide
    • pmid: 4136260
    • J. C. Stockert, O. D. Colman, Observations on nucleolar staining with osmium tetroxide. Experientia 30, 751–752 (1974). doi: 10.1007/BF01924164; pmid: 4136260
    • (1974) Experientia , vol.30 , pp. 751-752
    • Stockert, J.C.1    Colman, O.D.2
  • 54
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: An approach with alignment methods that preserve resolution
    • pmid: 9441937
    • D. N. Mastronarde, Dual-axis tomography: An approach with alignment methods that preserve resolution. J. Struct. Biol. 120, 343–352 (1997). doi: 10.1006/jsbi.1997.3919; pmid: 9441937
    • (1997) J. Struct. Biol. , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 55
    • 85036582843 scopus 로고    scopus 로고
    • 3D reconstruction of biological structures: Automated procedures for alignment and reconstruction of multiple tilt series in electron tomography
    • pmid: 27547706
    • S. Phan et al., 3D reconstruction of biological structures: Automated procedures for alignment and reconstruction of multiple tilt series in electron tomography. Adv Struct Chem Imaging 2, 8 (2017). doi: 10.1186/s40679-016-0021-2; pmid: 27547706
    • (2017) Adv Struct Chem Imaging , vol.2 , pp. 8
    • Phan, S.1
  • 56
    • 84866984821 scopus 로고    scopus 로고
    • TxBR montage reconstruction for large field electron tomography
    • pmid: 22749959
    • S. Phan et al., TxBR montage reconstruction for large field electron tomography. J. Struct. Biol. 180, 154–164 (2012). doi: 10.1016/j.jsb.2012.06.006; pmid: 22749959
    • (2012) J. Struct. Biol. , vol.180 , pp. 154-164
    • Phan, S.1
  • 57
    • 33646070293 scopus 로고    scopus 로고
    • Transform-based backprojection for volume reconstruction of large format electron microscope tilt series
    • pmid: 16542854
    • A. Lawrence, J. C. Bouwer, G. Perkins, M. H. Ellisman, Transform-based backprojection for volume reconstruction of large format electron microscope tilt series. J. Struct. Biol. 154, 144–167 (2006). doi: 10.1016/j.jsb.2005.12.012; pmid: 16542854
    • (2006) J. Struct. Biol. , vol.154 , pp. 144-167
    • Lawrence, A.1    Bouwer, J.C.2    Perkins, G.3    Ellisman, M.H.4
  • 58
    • 0012934579 scopus 로고
    • S. H. Paul, Ed. Academic Press Professional, San Diego, CA
    • K. Zuiderveld, in Graphics Gems IV, S. H. Paul, Ed. (Academic Press Professional, San Diego, CA, 1994), pp. 474–485.
    • (1994) Graphics Gems IV , pp. 474-485
    • Zuiderveld, K.1
  • 59
    • 0032090603 scopus 로고    scopus 로고
    • An iterative algorithm for minimum cross entropy thresholding
    • C. H. Li, P. K. S. Tam, An iterative algorithm for minimum cross entropy thresholding. Pattern Recognit. Lett. 19, 771–776 (1998). doi: 10.1016/S0167-8655(98)00057-9
    • (1998) Pattern Recognit. Lett. , vol.19 , pp. 771-776
    • Li, C.H.1    Tam, P.K.S.2
  • 60
    • 0018306059 scopus 로고
    • A threshold selection method from gray-level histograms
    • N. Otsu, A threshold selection method from gray-level histograms. IEEE Trans. Syst. Man Cybern. 9, 62–66 (1979). doi: 10.1109/TSMC.1979.4310076
    • (1979) IEEE Trans. Syst. Man Cybern. , vol.9 , pp. 62-66
    • Otsu, N.1
  • 61
    • 84882878737 scopus 로고    scopus 로고
    • C. D. Hansen, C. R. Johnson, Eds. Butterworth-Heinemann, Burlington, MA
    • D. Stalling, M. Westerhoff, H.-C. Hege, in The Visualization Handbook, C. D. Hansen, C. R. Johnson, Eds. (Butterworth-Heinemann, Burlington, MA, 2005), pp. 749–767.
    • (2005) The Visualization Handbook , pp. 749-767
    • Stalling, D.1    Westerhoff, M.2    Hege, H.-C.3
  • 62
    • 0019197619 scopus 로고
    • The higher order structure of chicken erythrocyte chromosomes in vivo
    • pmid: 7442809
    • J. P. Langmore, C. Schutt, The higher order structure of chicken erythrocyte chromosomes in vivo. Nature 288, 620–622 (1980). doi: 10.1038/288620a0; pmid: 7442809
    • (1980) Nature , vol.288 , pp. 620-622
    • Langmore, J.P.1    Schutt, C.2
  • 63
    • 80054774248 scopus 로고    scopus 로고
    • Evidence for short-range helical order in the 30-nm chromatin fibers of erythrocyte nuclei
    • pmid: 21969536
    • 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. 108, 16992–16997 (2011). doi: 10.1073/pnas.1108268108; pmid: 21969536
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 16992-16997
    • Scheffer, M.P.1    Eltsov, M.2    Frangakis, A.S.3
  • 64
    • 77950517260 scopus 로고    scopus 로고
    • Evolutionary tabu search strategies for the simultaneous registration of multiple atomic structures in cryo-EM reconstructions
    • pmid: 20056148
    • M. Rusu, S. Birmanns, Evolutionary tabu search strategies for the simultaneous registration of multiple atomic structures in cryo-EM reconstructions. J. Struct. Biol. 170, 164–171 (2010). doi: 10.1016/j.jsb.2009.12.028; pmid: 20056148
    • (2010) J. Struct. Biol. , vol.170 , pp. 164-171
    • Rusu, M.1    Birmanns, S.2
  • 65
    • 79851508025 scopus 로고    scopus 로고
    • Using Sculptor and Situs for simultaneous assembly of atomic components into low-resolution shapes
    • pmid: 21078392
    • S. Birmanns, M. Rusu, W. Wriggers, Using Sculptor and Situs for simultaneous assembly of atomic components into low-resolution shapes. J. Struct. Biol. 173, 428–435 (2011). doi: 10.1016/j.jsb.2010.11.002; pmid: 21078392
    • (2011) J. Struct. Biol. , vol.173 , pp. 428-435
    • Birmanns, S.1    Rusu, M.2    Wriggers, W.3
  • 67
    • 84939574342 scopus 로고    scopus 로고
    • Structural mechanisms of nucleosome recognition by linker histones
    • pmid: 26212454
    • B. R. Zhou et al., Structural mechanisms of nucleosome recognition by linker histones. Mol. Cell 59, 628–638 (2015). doi: 10.1016/j.molcel.2015.06.025; pmid: 26212454
    • (2015) Mol. Cell , vol.59 , pp. 628-638
    • Zhou, B.R.1
  • 68
    • 84961972153 scopus 로고    scopus 로고
    • High mobility group (HMG) proteins: Modulators of chromatin structure and DNA repair in mammalian cells
    • pmid: 26411874
    • R. Reeves, High mobility group (HMG) proteins: Modulators of chromatin structure and DNA repair in mammalian cells. DNA Repair (Amst.) 36, 122–136 (2015). doi: 10.1016/ j.dnarep.2015.09.015; pmid: 26411874
    • (2015) DNA Repair (amst.) , vol.36 , pp. 122-136
    • Reeves, R.1
  • 69
    • 0017652886 scopus 로고
    • The structure of histone-depleted metaphase chromosomes
    • pmid: 922894
    • J. R. Paulson, U. K. Laemmli, The structure of histone-depleted metaphase chromosomes. Cell 12, 817–828 (1977). doi: 10.1016/0092-8674(77)90280-X; pmid: 922894
    • (1977) Cell , vol.12 , pp. 817-828
    • Paulson, J.R.1    Laemmli, U.K.2
  • 70
    • 34347247308 scopus 로고    scopus 로고
    • The three-dimensional structure of in vitro reconstituted Xenopus laevis chromosomes by EM tomography
    • pmid: 17333236
    • P. König, M. B. Braunfeld, J. W. Sedat, D. A. Agard, The three-dimensional structure of in vitro reconstituted Xenopus laevis chromosomes by EM tomography. Chromosoma 116, 349–372 (2007). doi: 10.1007/s00412-007-0101-0; pmid: 17333236
    • (2007) Chromosoma , vol.116 , pp. 349-372
    • König, P.1    Braunfeld, M.B.2    Sedat, J.W.3    Agard, D.A.4
  • 71
    • 0013968931 scopus 로고
    • Isolation and characterization of human metaphase chromosomes
    • pmid: 5230305
    • N. P. Salzman, D. E. Moore, J. Mendelsohn, Isolation and characterization of human metaphase chromosomes. Proc. Natl. Acad. Sci. U.S.A. 56, 1449–1456 (1966). doi: 10.1073/ pnas.56.5.1449; pmid: 5230305
    • (1966) Proc. Natl. Acad. Sci. U.S.A. , vol.56 , pp. 1449-1456
    • Salzman, N.P.1    Moore, D.E.2    Mendelsohn, J.3
  • 72
    • 0022384496 scopus 로고
    • Unstained microtubules studied by cryo-electron microscopy: Substructure, supertwist and disassembly
    • pmid: 3981631
    • E. M. Mandelkow, E. Mandelkow, Unstained microtubules studied by cryo-electron microscopy: Substructure, supertwist and disassembly. J. Mol. Biol. 181, 123–135 (1985). doi: 10.1016/0022-2836(85)90330-4; pmid: 3981631
    • (1985) J. Mol. Biol. , vol.181 , pp. 123-135
    • Mandelkow, E.M.1    Mandelkow, E.2
  • 73
    • 78650194806 scopus 로고    scopus 로고
    • Nanotribology results show that DNA forms a mechanically resistant 2D network in metaphase chromatin plates
    • pmid: 21156137
    • I. Gállego, G. Oncins, X. Sisquella, X. Fernàndez-Busquets, J. R. Daban, Nanotribology results show that DNA forms a mechanically resistant 2D network in metaphase chromatin plates. Biophys. J. 99, 3951–3958 (2010). doi: 10.1016/ j.bpj.2010.11.015; pmid: 21156137
    • (2010) Biophys. J. , vol.99 , pp. 3951-3958
    • Gállego, I.1    Oncins, G.2    Sisquella, X.3    Fernàndez-Busquets, X.4    Daban, J.R.5
  • 75
    • 84964237877 scopus 로고    scopus 로고
    • Click-EM for imaging metabolically tagged nonprotein biomolecules
    • pmid: 27110681
    • J. T. Ngo et al., Click-EM for imaging metabolically tagged nonprotein biomolecules. Nat. Chem. Biol. 12, 459–465 (2016). doi: 10.1038/nchembio.2076; pmid: 27110681
    • (2016) Nat. Chem. Biol. , vol.12 , pp. 459-465
    • Ngo, J.T.1
  • 76
    • 84904172931 scopus 로고    scopus 로고
    • Chromatin as dynamic 10-nm fibers
    • pmid: 24737122
    • K. Maeshima, R. Imai, S. Tamura, T. Nozaki, Chromatin as dynamic 10-nm fibers. Chromosoma 123, 225–237 (2014). doi: 10.1007/s00412-014-0460-2; pmid: 24737122
    • (2014) Chromosoma , vol.123 , pp. 225-237
    • Maeshima, K.1    Imai, R.2    Tamura, S.3    Nozaki, T.4
  • 77
    • 79551685899 scopus 로고    scopus 로고
    • Nucleosome structural studies
    • pmid: 21176878
    • S. Tan, C. A. Davey, Nucleosome structural studies. Curr. Opin. Struct. Biol. 21, 128–136 (2011). doi: 10.1016/j.sbi.2010.11.006; pmid: 21176878
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 128-136
    • Tan, S.1    Davey, C.A.2
  • 78
    • 84899415723 scopus 로고    scopus 로고
    • Every amino acid matters: Essential contributions of histone variants to mammalian development and disease
    • pmid: 24614311
    • I. Maze, K. M. Noh, A. A. Soshnev, C. D. Allis, Every amino acid matters: Essential contributions of histone variants to mammalian development and disease. Nat. Rev. Genet. 15, 259–271 (2014). doi: 10.1038/nrg3673; pmid: 24614311
    • (2014) Nat. Rev. Genet. , vol.15 , pp. 259-271
    • Maze, I.1    Noh, K.M.2    Soshnev, A.A.3    Allis, C.D.4
  • 79
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • pmid: 11101893
    • R. K. Suto, M. J. Clarkson, D. J. Tremethick, K. Luger, Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat. Struct. Biol. 7, 1121–1124 (2000). doi: 10.1038/81971; pmid: 11101893
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1121-1124
    • Suto, R.K.1    Clarkson, M.J.2    Tremethick, D.J.3    Luger, K.4
  • 80
    • 84901840684 scopus 로고    scopus 로고
    • Chromatin fiber polymorphism triggered by variations of DNA linker lengths
    • pmid: 24847063
    • R. Collepardo-Guevara, T. Schlick, Chromatin fiber polymorphism triggered by variations of DNA linker lengths. Proc. Natl. Acad. Sci. U.S.A. 111, 8061–8066 (2014). doi: 10.1073/pnas.1315872111; pmid: 24847063
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 8061-8066
    • Collepardo-Guevara, R.1    Schlick, T.2
  • 81
    • 84857340459 scopus 로고    scopus 로고
    • Toward convergence of experimental studies and theoretical modeling of the chromatin fiber
    • pmid: 22157002
    • T. Schlick, J. Hayes, S. Grigoryev, Toward convergence of experimental studies and theoretical modeling of the chromatin fiber. J. Biol. Chem. 287, 5183–5191 (2012). doi: 10.1074/jbc.R111.305763; pmid: 22157002
    • (2012) J. Biol. Chem. , vol.287 , pp. 5183-5191
    • Schlick, T.1    Hayes, J.2    Grigoryev, S.3
  • 82
    • 33645286183 scopus 로고    scopus 로고
    • Polymer chain models of DNA and chromatin
    • pmid: 16547610
    • J. Langowski, Polymer chain models of DNA and chromatin. Eur. Phys. J. E Soft Matter 19, 241–249 (2006). doi: 10.1140/ epje/i2005-10067-9; pmid: 16547610
    • (2006) Eur. Phys. J. E Soft Matter , vol.19 , pp. 241-249
    • Langowski, J.1
  • 83
    • 79952807125 scopus 로고    scopus 로고
    • Chromatin folding—from biology to polymer models and back
    • pmid: 21378305
    • M. Tark-Dame, R. van Driel, D. W. Heermann, Chromatin folding—from biology to polymer models and back. J. Cell Sci. 124, 839–845 (2011). doi: 10.1242/jcs.077628; pmid: 21378305
    • (2011) J. Cell Sci. , vol.124 , pp. 839-845
    • Tark-Dame, M.1    Van Driel, R.2    Heermann, D.W.3
  • 84
    • 9344239339 scopus 로고    scopus 로고
    • Long-range compaction and flexibility of interphase chromatin in budding yeast analyzed by high-resolution imaging techniques
    • pmid: 15545610
    • K. Bystricky, P. Heun, L. Gehlen, J. Langowski, S. M. Gasser, Long-range compaction and flexibility of interphase chromatin in budding yeast analyzed by high-resolution imaging techniques. Proc. Natl. Acad. Sci. U.S.A. 101, 16495–16500 (2004). doi: 10.1073/pnas.0402766101; pmid: 15545610
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16495-16500
    • Bystricky, K.1    Heun, P.2    Gehlen, L.3    Langowski, J.4    Gasser, S.M.5
  • 85
    • 84857430552 scopus 로고    scopus 로고
    • Chromatin replication and epigenome maintenance
    • pmid: 22358331
    • C. Alabert, A. Groth, Chromatin replication and epigenome maintenance. Nat. Rev. Mol. Cell Biol. 13, 153–167 (2012). doi: 10.1038/nrm3288; pmid: 22358331
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 153-167
    • Alabert, C.1    Groth, A.2
  • 86
    • 0028783965 scopus 로고
    • Displacement of sequence-specific transcription factors from mitotic chromatin
    • pmid: 7553870
    • M. A. Martínez-Balbás, A. Dey, S. K. Rabindran, K. Ozato, C. Wu, Displacement of sequence-specific transcription factors from mitotic chromatin. Cell 83, 29–38 (1995). doi: 10.1016/ 0092-8674(95)90231-7; pmid: 7553870
    • (1995) Cell , vol.83 , pp. 29-38
    • Martínez-Balbás, M.A.1    Dey, A.2    Rabindran, S.K.3    Ozato, K.4    Wu, C.5
  • 87
    • 45149084413 scopus 로고    scopus 로고
    • Domain organization of human chromosomes revealed by mapping of nuclear lamina interactions
    • pmid: 18463634
    • L. Guelen et al., Domain organization of human chromosomes revealed by mapping of nuclear lamina interactions. Nature 453, 948–951 (2008). doi: 10.1038/nature06947; pmid: 18463634
    • (2008) Nature , vol.453 , pp. 948-951
    • Guelen, L.1
  • 88
    • 84864652613 scopus 로고    scopus 로고
    • The conundrum of gel formation by molecular nanofibers, wormlike micelles, and filamentous proteins: Gelation without cross-links?
    • S. R. Raghavan, J. F. Douglas, The conundrum of gel formation by molecular nanofibers, wormlike micelles, and filamentous proteins: Gelation without cross-links? Soft Matter 8, 8539–8546 (2012). doi: 10.1039/c2sm25107h
    • (2012) Soft Matter , vol.8 , pp. 8539-8546
    • Raghavan, S.R.1    Douglas, J.F.2


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