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Volumn 86, Issue 2-3, 2000, Pages 141-153

Analytical ultracentrifugation and the characterization of chromatin structure

Author keywords

Analytical ultracentrifuge; Chromatin; Histones; Nucleosome; Sedimentation equilibrium; Sedimentation velocity

Indexed keywords

HISTONE;

EID: 0034734277     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(00)00144-7     Document Type: Conference Paper
Times cited : (39)

References (82)
  • 6
    • 0017806223 scopus 로고
    • Boundary analysis of sedimentation velocity experiments with monodisperse and paucidisperse solutes
    • van Holde K.E., Weischet W.O. Boundary analysis of sedimentation velocity experiments with monodisperse and paucidisperse solutes. Biopolymers. 17:1978;1387-1403.
    • (1978) Biopolymers , vol.17 , pp. 1387-1403
    • Van Holde, K.E.1    Weischet, W.O.2
  • 7
    • 0031020113 scopus 로고    scopus 로고
    • Identification and interpretation off complexity in sedimentation velocity boundaries
    • Demeler B., Saber H., Hansen J.C. Identification and interpretation off complexity in sedimentation velocity boundaries. Biophys. J. 72:1997;397-401.
    • (1997) Biophys. J. , vol.72 , pp. 397-401
    • Demeler, B.1    Saber, H.2    Hansen, J.C.3
  • 8
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments: A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • Stafford W.F. III Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal. Biochem. 203:1992;295-301.
    • (1992) Anal. Biochem. , vol.203 , pp. 295-301
    • Stafford W.F. III1
  • 9
    • 0031982612 scopus 로고    scopus 로고
    • Determination of molecular parameters by fitting sedimentation data to finite-element solutions of the Lamm equation
    • Demeler B., Saber H. Determination of molecular parameters by fitting sedimentation data to finite-element solutions of the Lamm equation. Biophys. J. 74:1998;444-454.
    • (1998) Biophys. J. , vol.74 , pp. 444-454
    • Demeler, B.1    Saber, H.2
  • 10
    • 0001038767 scopus 로고
    • Equilibrium ultracentrifugation in dilute solutions
    • Yphantis D.A. Equilibrium ultracentrifugation in dilute solutions. Biochemistry. 3:1964;297-317.
    • (1964) Biochemistry , vol.3 , pp. 297-317
    • Yphantis, D.A.1
  • 11
    • 84981866444 scopus 로고
    • Ultracentrifuge studies with Rayleigh interference optics. III. Computational methods applied to high-speed sedimentation equilibrium experiments
    • Teller D.C., Horbett T.A., Richards E.G., Schachman H.K. Ultracentrifuge studies with Rayleigh interference optics. III. Computational methods applied to high-speed sedimentation equilibrium experiments. Ann. N.Y. Acad. Sci. 164:1970;66-101.
    • (1970) Ann. N.Y. Acad. Sci. , vol.164 , pp. 66-101
    • Teller, D.C.1    Horbett, T.A.2    Richards, E.G.3    Schachman, H.K.4
  • 13
    • 0014667364 scopus 로고
    • Studies of self-associating systems by equilibrium ultracentrifugation
    • Roark D.E., Yphantis D.A. Studies of self-associating systems by equilibrium ultracentrifugation. Ann. N.Y. Acad. Sci. 164:1969;245-278.
    • (1969) Ann. N.Y. Acad. Sci. , vol.164 , pp. 245-278
    • Roark, D.E.1    Yphantis, D.A.2
  • 15
    • 0015786441 scopus 로고
    • Chromatin sub-structure. The digestion of chromatin DNA at regularly spaced sites by a nuclear deoxyribonuclease
    • Hewish D.R., Burgoyne L.A. Chromatin sub-structure. The digestion of chromatin DNA at regularly spaced sites by a nuclear deoxyribonuclease. Biochem. Biophys. Res. Commun. 52:1973;504-510.
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 504-510
    • Hewish, D.R.1    Burgoyne, L.A.2
  • 16
    • 0015919073 scopus 로고
    • Properties of nuclease-resistant fragments of calf thymus chromatin
    • Rill R., van Holde K.E. Properties of nuclease-resistant fragments of calf thymus chromatin. J. Biol. Chem. 248:1973;1080-1083.
    • (1973) J. Biol. Chem. , vol.248 , pp. 1080-1083
    • Rill, R.1    Van Holde, K.E.2
  • 17
    • 0015962745 scopus 로고
    • The effect of trypsin on nuclease-resistant chromatin fragments
    • Sahasrabuddhe C.G., van Holde K.E. The effect of trypsin on nuclease-resistant chromatin fragments. J. Biol. Chem. 249:1974;152-156.
    • (1974) J. Biol. Chem. , vol.249 , pp. 152-156
    • Sahasrabuddhe, C.G.1    Van Holde, K.E.2
  • 18
    • 0015795319 scopus 로고
    • Fractionation of native and denatured deoxyribonucleic acid on agarose columns
    • Prunell A., Bernardi G. Fractionation of native and denatured deoxyribonucleic acid on agarose columns. J. Biol. Chem. 248:1973;3433-3440.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3433-3440
    • Prunell, A.1    Bernardi, G.2
  • 19
    • 0141887600 scopus 로고
    • Spheroid chromatin units (ν bodies)
    • Olins A.L., Olins D.E. Spheroid chromatin units (ν bodies). J. Cell Biol. 59:1973;252a.
    • (1973) J. Cell Biol. , vol.59
    • Olins, A.L.1    Olins, D.E.2
  • 20
    • 0015964401 scopus 로고
    • Spheroid chromatin units (ν bodies)
    • Olins A.L., Olins D.E. Spheroid chromatin units (ν bodies). Science. 183:1974;330-332.
    • (1974) Science , vol.183 , pp. 330-332
    • Olins, A.L.1    Olins, D.E.2
  • 21
    • 0000546369 scopus 로고
    • Ultrastructure of inactive chromatin
    • Woodcock C.L.F. Ultrastructure of inactive chromatin. J. Cell Biol. 59:1973;368a.
    • (1973) J. Cell Biol. , vol.59
    • Woodcock, C.L.F.1
  • 23
    • 0018689205 scopus 로고
    • The temperature and pH dependence of conformational transitions of the chromatin subunit
    • Gordon V.C., Schumaker V.N., Olins D.E., Knobler C.M., Horowitz J. The temperature and pH dependence of conformational transitions of the chromatin subunit. Nucleic Acids Res. 6:1979;3845-3856.
    • (1979) Nucleic Acids Res. , vol.6 , pp. 3845-3856
    • Gordon, V.C.1    Schumaker, V.N.2    Olins, D.E.3    Knobler, C.M.4    Horowitz, J.5
  • 24
    • 0019332887 scopus 로고
    • Salt induced transitions of chromatin core particles studied by tyrosine fluorescence anisotropy
    • Libertini L.J., Small E.W. Salt induced transitions of chromatin core particles studied by tyrosine fluorescence anisotropy. Nucleic Acids Res. 8:1980;3517-3534.
    • (1980) Nucleic Acids Res. , vol.8 , pp. 3517-3534
    • Libertini, L.J.1    Small, E.W.2
  • 25
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K., Mäder A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature. 389:1997;251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 26
    • 84987412245 scopus 로고
    • Proteins as counterions of DNA: A new model of nucleoprotamine structure
    • D. Vasilescu, J. Loz, L. Packer, & B. Pullman. Basel: Birkhauser
    • Subirana J.A. Proteins as counterions of DNA: a new model of nucleoprotamine structure. Vasilescu D., Loz J., Packer L., Pullman B. Advances in Life Sciences. 1990;63-70 Birkhauser, Basel.
    • (1990) Advances in Life Sciences , pp. 63-70
    • Subirana, J.A.1
  • 27
    • 0031737904 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Ausió J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Chemtracts. 11:1998;149-155.
    • (1998) Chemtracts , vol.11 , pp. 149-155
    • Ausió, J.1
  • 28
    • 0018363156 scopus 로고
    • DNA folding by histones: The kinetics of chromatin core particle reassembly and the interaction of nucleosomes with histones
    • Stein A. DNA folding by histones: the kinetics of chromatin core particle reassembly and the interaction of nucleosomes with histones. J. Mol. Biol. 130:1979;103-134.
    • (1979) J. Mol. Biol. , vol.130 , pp. 103-134
    • Stein, A.1
  • 29
    • 0019888373 scopus 로고
    • Hydrodynamic studies of the interaction between nucleosome core particles and core histones
    • Eisenberg H., Felsenfeld G. Hydrodynamic studies of the interaction between nucleosome core particles and core histones. J. Mol. Biol. 150:1981;537-555.
    • (1981) J. Mol. Biol. , vol.150 , pp. 537-555
    • Eisenberg, H.1    Felsenfeld, G.2
  • 30
    • 0018627282 scopus 로고
    • Nucleosome dissociation and transfer in concentrated salt solutions
    • Stacks P.C., Schumaker V.N. Nucleosome dissociation and transfer in concentrated salt solutions. Nucleic Acids Res. 7:1979;2457-2467.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 2457-2467
    • Stacks, P.C.1    Schumaker, V.N.2
  • 31
    • 0019887183 scopus 로고
    • Nucleosome dissociation at physiological ionic strengths
    • Cotton R.W., Hamkalo B.A. Nucleosome dissociation at physiological ionic strengths. Nucleic Acids Res. 9:1981;445-457.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 445-457
    • Cotton, R.W.1    Hamkalo, B.A.2
  • 32
    • 0019763110 scopus 로고
    • Heterogeneity of nucleosomes upon dissociation with salts
    • Vassilev L., Russev G., Tsanev R. Heterogeneity of nucleosomes upon dissociation with salts. Int. J. Biochem. 13:1981;1247-1255.
    • (1981) Int. J. Biochem. , vol.13 , pp. 1247-1255
    • Vassilev, L.1    Russev, G.2    Tsanev, R.3
  • 33
    • 0021352605 scopus 로고
    • Dynamics and equilibria of nucleosomes at elevated ionic strength
    • Yager T.D., van Holde K.E. Dynamics and equilibria of nucleosomes at elevated ionic strength. J. Biol. Chem. 259:1984;4212-4222.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4212-4222
    • Yager, T.D.1    Van Holde, K.E.2
  • 34
    • 0021612542 scopus 로고
    • Nucleosome core particle stability and conformational change. Effect of temperature, particle and NaCl concentrations, and crosslinking of histone H3 sulfhydryl groups
    • Ausió J., Seger D., Eisenberg H. Nucleosome core particle stability and conformational change. Effect of temperature, particle and NaCl concentrations, and crosslinking of histone H3 sulfhydryl groups. J. Mol. Biol. 176:1984;77-104.
    • (1984) J. Mol. Biol. , vol.176 , pp. 77-104
    • Ausió, J.1    Seger, D.2    Eisenberg, H.3
  • 35
    • 0342476280 scopus 로고
    • Histone-histone and histone-DNA interactions in chromatin
    • Sund, & Veeger. Berlin: Walter de Gruyter
    • Ausió J., Haik Y., Seger D., Eisenberg H. Histone-histone and histone-DNA interactions in chromatin. Sund, Veeger Mobility and Recognition in Cell Biology. 1983;195-211 Walter de Gruyter, Berlin.
    • (1983) Mobility and Recognition in Cell Biology , pp. 195-211
    • Ausió, J.1    Haik, Y.2    Seger, D.3    Eisenberg, H.4
  • 36
    • 0017884384 scopus 로고
    • Binding of additional histones to chromatin core particles
    • Voordouw G., Eisenberg H. Binding of additional histones to chromatin core particles. Nature. 273:1978;446-448.
    • (1978) Nature , vol.273 , pp. 446-448
    • Voordouw, G.1    Eisenberg, H.2
  • 37
    • 0028791330 scopus 로고
    • Mechanism of protein access to specific DNA sequences in chromatin: A dynamic equilibrium model for gene regulation
    • Polach K.J., Widom J. Mechanism of protein access to specific DNA sequences in chromatin: a dynamic equilibrium model for gene regulation. J. Mol. Biol. 254:1995;130-149.
    • (1995) J. Mol. Biol. , vol.254 , pp. 130-149
    • Polach, K.J.1    Widom, J.2
  • 38
    • 0022128164 scopus 로고
    • The trajectory of a stiff rod in a curved potential energy trough. An initial result for short nucleosomal rods
    • Manning G.S. The trajectory of a stiff rod in a curved potential energy trough. An initial result for short nucleosomal rods. Cell Biophys. 7:1985;177-184.
    • (1985) Cell Biophys. , vol.7 , pp. 177-184
    • Manning, G.S.1
  • 39
    • 0026253639 scopus 로고
    • The elastic resilience of DNA can induce all-or-none structural transitions in the nucleosome core particle
    • Marky N.L., Manning G.S. The elastic resilience of DNA can induce all-or-none structural transitions in the nucleosome core particle. Biopolymers. 31:1991;1543-1957.
    • (1991) Biopolymers , vol.31 , pp. 1543-1957
    • Marky, N.L.1    Manning, G.S.2
  • 40
    • 0028828894 scopus 로고
    • A theory of DNA dissociation from the nucleosome
    • Marky N.L., Manning G.S. A theory of DNA dissociation from the nucleosome. J. Mol. Biol. 254:1995;50-61.
    • (1995) J. Mol. Biol. , vol.254 , pp. 50-61
    • Marky, N.L.1    Manning, G.S.2
  • 41
    • 0021525315 scopus 로고
    • A 145-base pair DNA sequence that positions itself precisely and asymmetrically on the nucleosome core
    • Ramsay N., Felsenfeld G., Rushton B., McGhee J.D. A 145-base pair DNA sequence that positions itself precisely and asymmetrically on the nucleosome core. EMBO J. 3:1984;2605-2611.
    • (1984) EMBO J. , vol.3 , pp. 2605-2611
    • Ramsay, N.1    Felsenfeld, G.2    Rushton, B.3    McGhee, J.D.4
  • 42
    • 0031148959 scopus 로고    scopus 로고
    • In vitro reconstitution and analysis of mononucleosomes containing defined DNAs and proteins
    • Hayes J.J., Lee K-M. In vitro reconstitution and analysis of mononucleosomes containing defined DNAs and proteins. Methods. 12:1997;2-9.
    • (1997) Methods , vol.12 , pp. 2-9
    • Hayes, J.J.1    Lee, K.-M.2
  • 43
    • 0000153207 scopus 로고
    • The cell nucleus
    • Busch H. New York: Academic Press
    • Isenberg I. The cell nucleus. Busch H. Histones. 4:1978;135-154 Academic Press, New York.
    • (1978) Histones , vol.4 , pp. 135-154
    • Isenberg, I.1
  • 44
    • 0017903383 scopus 로고
    • Assaying histone interactions by sedimentation equilibrium and other methods
    • G. Stein, J. Stein, Kleinscmidt L.J. New York: Academic Press
    • Roark D.E. Assaying histone interactions by sedimentation equilibrium and other methods. Stein G., Stein J., Kleinscmidt L.J. Methods in Cell Biology. 18:1978;417-428 Academic Press, New York.
    • (1978) Methods in Cell Biology , vol.18 , pp. 417-428
    • Roark, D.E.1
  • 47
    • 0018267877 scopus 로고
    • The histone core complex: An octamer assembled by two sets of protein-protein interactions
    • Eickbush T.H., Moudrianakis E.N. The histone core complex: an octamer assembled by two sets of protein-protein interactions. Biochemistry. 17:1978;4955-4964.
    • (1978) Biochemistry , vol.17 , pp. 4955-4964
    • Eickbush, T.H.1    Moudrianakis, E.N.2
  • 49
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3.1 Å resolution: A tripartite protein assembly and a left-handed superhelix
    • Arents G., Burlingame R.W., Wang B.-C., Love W.E., Moudrianakis E.N. The nucleosomal core histone octamer at 3.1 Å resolution: a tripartite protein assembly and a left-handed superhelix. Proc. Natl. Acad. Sci. USA. 88:1991;10148-10152.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.-C.3    Love, W.E.4    Moudrianakis, E.N.5
  • 50
    • 0019197607 scopus 로고
    • Size-dependence of a stable higher-order structure of chromatin
    • Thomas J.O., Butler P.J.G. Size-dependence of a stable higher-order structure of chromatin. J. Mol. Biol. 144:1980;89-93.
    • (1980) J. Mol. Biol. , vol.144 , pp. 89-93
    • Thomas, J.O.1    Butler, P.J.G.2
  • 51
    • 0019130753 scopus 로고
    • Changes of chromatin folding in solution
    • Butler P.J.G., Thomas J.O. Changes of chromatin folding in solution. J. Mol. Biol. 140:1980;505-529.
    • (1980) J. Mol. Biol. , vol.140 , pp. 505-529
    • Butler, P.J.G.1    Thomas, J.O.2
  • 52
    • 0021718495 scopus 로고
    • 2. Solubility and binding studies, transition to and characterization of the higher-order structure
    • 2. Solubility and binding studies, transition to and characterization of the higher-order structure. J. Mol. Biol. 177:1984;373-398.
    • (1984) J. Mol. Biol. , vol.177 , pp. 373-398
    • Ausió, J.1    Borochov, N.2    Seger, D.3    Eisenberg, H.4
  • 54
    • 0021760291 scopus 로고
    • Interaction and conformational changes of chromatin with divalent ions
    • Borochov N., Ausió J., Eisenberg H. Interaction and conformational changes of chromatin with divalent ions. Nucleic Acids Res. 12:1984;3089-3096.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 3089-3096
    • Borochov, N.1    Ausió, J.2    Eisenberg, H.3
  • 56
    • 0023091437 scopus 로고
    • Transition of chromatin from the '10 nm' lower order structure, to the '30 nm' higher order structure as followed by small angle X-ray scattering
    • Greulich K.O., Wachtel E., Ausió J., Seger D., Eisenberg H. Transition of chromatin from the '10 nm' lower order structure, to the '30 nm' higher order structure as followed by small angle X-ray scattering. J. Mol. Biol. 193:1987;709-721.
    • (1987) J. Mol. Biol. , vol.193 , pp. 709-721
    • Greulich, K.O.1    Wachtel, E.2    Ausió, J.3    Seger, D.4    Eisenberg, H.5
  • 57
    • 0343345746 scopus 로고
    • Transition of chromatin from the '10 nm' lower order structure, to the '30 nm' higher order structure as followed by small angle X-ray scattering
    • I. Chaiken, E. Chiacone, A. Fontana, & R. Neri. Clifton, NJ: Humana Press
    • Greulich K.O., Wachtel E., Ausió J., Seger D., Eisenberg H. Transition of chromatin from the '10 nm' lower order structure, to the '30 nm' higher order structure as followed by small angle X-ray scattering. Chaiken I., Chiacone E., Fontana A., Neri R. Macromolecular Recognition Principles and Methods. 1987;153-168 Humana Press, Clifton, NJ.
    • (1987) Macromolecular Recognition Principles and Methods , pp. 153-168
    • Greulich, K.O.1    Wachtel, E.2    Ausió, J.3    Seger, D.4    Eisenberg, H.5
  • 58
    • 0022540365 scopus 로고
    • Biochemical and physiochemical characterization of chromatin fractions with different degrees of solubility isolated from chicken erythrocyte nuclei
    • Ausió J., Sasi R., Fasman G.D. Biochemical and physiochemical characterization of chromatin fractions with different degrees of solubility isolated from chicken erythrocyte nuclei. Biochemistry. 25:1986;1981-1988.
    • (1986) Biochemistry , vol.25 , pp. 1981-1988
    • Ausió, J.1    Sasi, R.2    Fasman, G.D.3
  • 59
    • 0026782131 scopus 로고
    • Role of the histone 'tails' in the folding of oligonucleosomes depleted of histone H1
    • García-Ramírez M., Dong F., Ausió J. Role of the histone 'tails' in the folding of oligonucleosomes depleted of histone H1. J. Biol. Chem. 267:1992;19587-19595.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19587-19595
    • García-Ramírez, M.1    Dong, F.2    Ausió, J.3
  • 60
    • 0027960444 scopus 로고
    • Three-dimensional structure of extended chromatin fibers as revealed by tapping-mode scanning force microscopy
    • Leuba S.H., Yang G., Robert C. et al. Three-dimensional structure of extended chromatin fibers as revealed by tapping-mode scanning force microscopy. Proc. Natl. Acad. USA. 91:1994;11621-11625.
    • (1994) Proc. Natl. Acad. USA , vol.91 , pp. 11621-11625
    • Leuba, S.H.1    Yang, G.2    Robert, C.3
  • 61
    • 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
    • Bednar J., Horowitz R.A., Grigoryev S.A. 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. USA. 95:1998;14173-14178.
    • (1998) Proc. Natl. Acad. USA , vol.95 , pp. 14173-14178
    • Bednar, J.1    Horowitz, R.A.2    Grigoryev, S.A.3
  • 62
    • 0032555763 scopus 로고    scopus 로고
    • Dinucleosomes show compaction by ionic strength, consistent with bending of linker DNA
    • Butler P.J., Thomas J.O. Dinucleosomes show compaction by ionic strength, consistent with bending of linker DNA. J. Mol. Biol. 281:1998;401-407.
    • (1998) J. Mol. Biol. , vol.281 , pp. 401-407
    • Butler, P.J.1    Thomas, J.O.2
  • 63
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • Thoma F., Keller T., Klug A. Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J. Cell Biol. 83:1979;403-427.
    • (1979) J. Cell Biol. , vol.83 , pp. 403-427
    • Thoma, F.1    Keller, T.2    Klug, A.3
  • 64
    • 0029780079 scopus 로고    scopus 로고
    • What determines the folding of the chromatin fiber?
    • van Holde K.E., Zlanatova J. What determines the folding of the chromatin fiber? Proc. Natl. Acad. Sci. USA. 93:1996;10548-10555.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10548-10555
    • Van Holde, K.E.1    Zlanatova, J.2
  • 65
    • 0031416394 scopus 로고    scopus 로고
    • Histone H1 and chromatin higher-order structure
    • Ramakrishnan V. Histone H1 and chromatin higher-order structure. Crit. Rev. Eukaryotic Gene Expr. 7:1997;215-230.
    • (1997) Crit. Rev. Eukaryotic Gene Expr. , vol.7 , pp. 215-230
    • Ramakrishnan, V.1
  • 66
    • 0020131558 scopus 로고
    • Participation of core histone 'tails' in the stabilization of the chromatin solenoid
    • Allan J., Harborne N., Rau D.C., Gould H. Participation of core histone 'tails' in the stabilization of the chromatin solenoid. J. Cell Biol. 93:1982;285-297.
    • (1982) J. Cell Biol. , vol.93 , pp. 285-297
    • Allan, J.1    Harborne, N.2    Rau, D.C.3    Gould, H.4
  • 67
    • 0029046603 scopus 로고
    • Modulation of chromatin folding by histone acetylation
    • García-Ramírez M., Rocchini C., Ausió J. Modulation of chromatin folding by histone acetylation. J. Biol. Chem. 270:1995;17923-17928.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17923-17928
    • García-Ramírez, M.1    Rocchini, C.2    Ausió, J.3
  • 68
    • 0031550233 scopus 로고    scopus 로고
    • Major role of the histones H3-H4 in the folding of the chromatin fiber
    • Moore S.C., Iskandar M., Ausió J. Major role of the histones H3-H4 in the folding of the chromatin fiber. Biochem. Biophys. Res. Commun. 230:1997;136-139.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 136-139
    • Moore, S.C.1    Iskandar, M.2    Ausió, J.3
  • 70
    • 0025327471 scopus 로고
    • Electrostatic mechanism of chromatin folding
    • Clark D.J., Kimura T. Electrostatic mechanism of chromatin folding. J. Mol. Biol. 211:1990;883-896.
    • (1990) J. Mol. Biol. , vol.211 , pp. 883-896
    • Clark, D.J.1    Kimura, T.2
  • 71
    • 36849151400 scopus 로고
    • Analytical ultracentrifugation reborn
    • Schachman H.K. Analytical ultracentrifugation reborn. Nature. 341:1989;259-260.
    • (1989) Nature , vol.341 , pp. 259-260
    • Schachman, H.K.1
  • 72
    • 0031018370 scopus 로고    scopus 로고
    • Advances in sedimentation velocity analysis
    • Laue T.M. Advances in sedimentation velocity analysis. Biophys. J. 72:1997;395-396.
    • (1997) Biophys. J. , vol.72 , pp. 395-396
    • Laue, T.M.1
  • 73
    • 0022234831 scopus 로고
    • Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: A model system for study of higher order structure
    • Simpson T., Thoma F., Brubaker J.M. Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: a model system for study of higher order structure. Cell. 42:1985;799-808.
    • (1985) Cell , vol.42 , pp. 799-808
    • Simpson, T.1    Thoma, F.2    Brubaker, J.M.3
  • 74
    • 0024468871 scopus 로고
    • Homogeneous reconstituted oligonucleosomes, evidence for salt-dependent folding in the absence of histone H1
    • Hansen J.C., Ausió J., Stanik V.H., van Holde K.E. Homogeneous reconstituted oligonucleosomes, evidence for salt-dependent folding in the absence of histone H1. Biochemistry. 28:1989;9129-9136.
    • (1989) Biochemistry , vol.28 , pp. 9129-9136
    • Hansen, J.C.1    Ausió, J.2    Stanik, V.H.3    Van Holde, K.E.4
  • 75
    • 0002480690 scopus 로고
    • The general theory of irreversible processes in solutions of macromolecules
    • Kirkwood J.G. The general theory of irreversible processes in solutions of macromolecules. J. Pol. Sci. 12:1954;1-14.
    • (1954) J. Pol. Sci. , vol.12 , pp. 1-14
    • Kirkwood, J.G.1
  • 76
    • 0000224079 scopus 로고
    • Sedimentation analysis of proteins
    • R. Hill, Neurath H. San Francisco: Academic Press
    • van Holde K.E. Sedimentation analysis of proteins. Hill R., Neurath H. Proteins, 3rd ed. I:1975;225-291 Academic Press, San Francisco.
    • (1975) Proteins, 3rd Ed , vol.1 , pp. 225-291
    • Van Holde, K.E.1
  • 77
    • 0032496272 scopus 로고    scopus 로고
    • Folding of chromatin in the presence of heterogeneous H1 binding to nucleosomes
    • Howe L., Iskandar M., Ausió J. Folding of chromatin in the presence of heterogeneous H1 binding to nucleosomes. J. Biol. Chem. 273:1998;11625-11629.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11625-11629
    • Howe, L.1    Iskandar, M.2    Ausió, J.3
  • 78
    • 0032553013 scopus 로고    scopus 로고
    • Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: Mechanistic ramifications for higher-order chromatin folding
    • Carruthers L.M., Bednar J., Woodcock C.W., Hansen J.C. Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: mechanistic ramifications for higher-order chromatin folding. Biochemistry. 37:1998;14776-14787.
    • (1998) Biochemistry , vol.37 , pp. 14776-14787
    • Carruthers, L.M.1    Bednar, J.2    Woodcock, C.W.3    Hansen, J.C.4
  • 79
    • 0031669634 scopus 로고    scopus 로고
    • Reconstitution of chromatin complexes from high-performance liquid chromatography-purified histones
    • Ausió J., Moore S.C. Reconstitution of chromatin complexes from high-performance liquid chromatography-purified histones. Methods. 15:1998;333.
    • (1998) Methods , vol.15 , pp. 333
    • Ausió, J.1    Moore, S.C.2
  • 80
    • 0030717135 scopus 로고    scopus 로고
    • Reconstitution of native-like nucleosome core particles from reversed-phase-HPLC-fractionated histones
    • Moore S.C., Rice P., Iskandar M., Ausió J. Reconstitution of native-like nucleosome core particles from reversed-phase-HPLC-fractionated histones. Biochem. J. 328:1997;409-414.
    • (1997) Biochem. J. , vol.328 , pp. 409-414
    • Moore, S.C.1    Rice, P.2    Iskandar, M.3    Ausió, J.4
  • 81
    • 0033603302 scopus 로고    scopus 로고
    • Daunomycin-induced unfolding and aggregation of chromatin
    • Rabbani A., Iskandar M., Ausió J. Daunomycin-induced unfolding and aggregation of chromatin. J. Biol. Chem. 274:1999;18401-18406.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18401-18406
    • Rabbani, A.1    Iskandar, M.2    Ausió, J.3
  • 82
    • 0017762802 scopus 로고
    • Reconstitution of chromatin core particles
    • Tatchell K., van Holde K.E. Reconstitution of chromatin core particles. Biochemistry. 16:1977;5295-5303.
    • (1977) Biochemistry , vol.16 , pp. 5295-5303
    • Tatchell, K.1    Van Holde, K.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.