The Nuclear Matrix: A Structural Milieu for Genomic Function

International Review of Cytology

Volumn 162, Issue C, 1996, Pages 1-12

  Berezney, Ronald ^a   Mortillaro, Michael J ^a   Ma, Hong ^a   Wei, Xiangyun ^a   Samarabandu, Jagath ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

Cell nucleus; Chromatin; Chromosome painting; Clustersomes; DNA polymerase ; DNA primase; DNA replication; DNA replication sites; Fluorescence in situ hybridization (FISH); Interchromatin granules (ICGs); Interchromatinic regions; Laser scanning confocal microscopy; Matrin 3; Matrin cyp (cyclophilin); Matrin p250; Matrix protein filaments (MPFs); Multidimensional computer image analysis; Nuclear lamina; Nuclear matrins; Nuclear matrix; Nuclear pore complexes; Nucleolus; RNA splicing; RNP (ribonucleoproteins); Transcription

Indexed keywords

MATRILYSIN; MATRIX PROTEIN; NUCLEAR PROTEIN; RNA POLYMERASE II;

CELL NUCLEUS; CELL NUCLEUS MATRIX; CELL ULTRASTRUCTURE; COMPUTER ANALYSIS; DNA REPLICATION; GENE EXPRESSION REGULATION; GENE FUNCTION; GENE REPLICATION; GENETIC TRANSCRIPTION; HUMAN; IMAGE ANALYSIS; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; REVIEW;

ANIMALS; ANTIGENS, NUCLEAR; CHROMATIN; GENOME; HUMANS; NUCLEAR MATRIX; NUCLEAR PROTEINS; PROTEIN STRUCTURE, TERTIARY; RIBONUCLEOPROTEINS;

EID: 0029620266     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(08)61228-0     Document Type: Article

References (234)

1. Aaronson, R.P., Blobel, G., Isolation of nuclear pore complexes in association with a lamina. Proc. Natl. Acad. Sci. U.S.A. 72 (1975), 1007–1011.
2. Adolph, K.W., Cheng, S.M., Paulson, J.R., Laemmli, U.K., Isolation of protein scaffold from mitotic HeLa cell chromosomes. Proc. Natl. Acad. Sci. U.S.A. 74 (1977), 4937–4941.
3. Allen, S.L., Berezney, R., Coffey, D.S., Phosphorylation of nuclear matrix proteins in isolated regenerating rat liver nuclei. Biochem. Biophys. Res. Commun. 75 (1977), 111–116.
4. Altieri, F., Maras, B., Eufemi, M., Ferraro, A., Turano, C., Purification of a 57 kDa nuclear matrix protein associated with thiol: protein-disulfide oxidoreductase and phospholipase C activities. Biochem. Biophys. Res. Commun. 194 (1993), 992–1000.
5. Aten, J.A., Bakker, P.J.M., Stap, J., Boschman, G.A., Veenhof, C.H.N., DNA double labelling with IdUrd and CldUrd for spatial and temporal analysis of cell proliferation and DNA replication. Histochem. J. 24 (1992), 251–259.
6. Bachs, O., Carafoli, E., Calmodulin and calmodulin binding proteins in liver cell nuclei. J. Biol. Chem. 262 (1987), 10786–10790.
7. Ballard, D.H., Brown, C.M., “Computer Vision”, 1982, Prentice-Hall, Englewood Cliffs, NJ.
8. Bastos, R., Parte, N., Burke, B., Nuclear pore complex proteins. Berezney, R., Jeon, K., (eds.) “International Review of Cytology”, 162, 1995, Academic Press, San Diego in press.
9. Belgrader, P., Siegel, A.J., Berezney, R., A comprehensive study on the isolation and characterization of the HeLa S3 nuclear matrix. J. Cell Sci. 98 (1991), 281–291.
10. Belgrader, P., Dey, R., Berezney, R., Molecular cloning of matrin 3: A 125-kilodalton protein of the nuclear matrix contains an extensive acidic domain. J. Biol. Chem. 266 (1991), 9893–9899.
11. Berezney, R., Large scale isolation of nuclear membranes from bovine liver. Methods Cell Biol. 7 (1974), 205–228.
12. Berezney, R., Dynamic properties of the nuclear matrix. Busch, H., (eds.) “The Cell Nucleus”, 7, 1979, Academic Press, New York, 413–456.
13. Berezney, R., Fractionation of the nuclear matrix. J. Cell Biol. 85 (1980), 641–650.
14. Berezney, R., Organization and functions of the nuclear matrix. Hnilica, L.S., (eds.) “Chromosomal Nonhistone Proteins”, 4, 1984, CRC Press, Boca Raton, FL, 119–180.
15. Berezney, R., Replicating the mammalian genome in 3D. J. Cell. Biochem. Suppl., 21B, 1995, 118.
16. Berezney, R., Basler, J., Hughes, B.B., Kaplan, S.C., Isolation and characterization of the nuclear matrix from zajdela ascites hepatoma cells. Cancer Res. 39 (1979), 3031–3039.
17. Berezney, R., Basler, J., Kaplan, S.C., Hughes, B.B., The nuclear matrix of slowly and rapidly proliferating liver cells. Eur. J. Cell Biol. 20 (1979), 139–142.
18. Berezney, R., Buchholtz, L.B., Isolation and characterization of rat liver nuclear matrices containing high molecular weight deoxyribonucleic acid. Biochemistry 20 (1981), 4995–5002.
19. Berezney, R., Buchholtz, L.B., Dynamic association of replicating DNA fragments with the nuclear matrix of regenerating liver. Exp. Cell Res. 132 (1981), 1–13.
20. Berezney, R., Coffey, D.S., Identification of a nuclear protein matrix. Biochem. Biophys. Res. Commun. 60 (1974), 1410–1417.
21. Berezney, R., Coffey, D.S., The nuclear protein matrix: Association with newly synthesized DNA. Science 189 (1975), 291–293.
22. Berezney, R., Coffey, D.S., The nuclear protein matrix: Isolation, structure, and functions. Weber, G., (eds.) “Advances in Enzyme Regulation”, 14, 1976, Pergamon Press, New York, 63–100.
23. Berezney, R., Coffey, D.S., Nuclear matrix: Isolation and characterization of a framework structure from rat liver nuclei. J. Cell. Biol. 73 (1977), 616–637.
24. Berezney, R., Ma, H., Wei, X., Meng, C., Samarabandu, J.K., Cheng, P.C., Elucidating the higher order assembly of replicating sites in mouse 3T3 cells. J. Cell. Biochem., 21B, 1995, 137.
25. Berezney, R., Macaulay, L.K., Crane, F.L., The purification and biochemical characterization of bovine nuclear membranes. J. Biol. Chem. 247 (1972), 5549–5561.
26. Berger, N.A., Petzold, S.J., Johnson, E.S., High molecular weight DNA intermediates synthesized by permeabilized L cells. Biochim. Biophys. Acta 478 (1977), 44–58.
27. Bernhard, W., A new staining procedure for electron microscopical cytology. J. Ultrastruct. Res. 27 (1969), 250–265.
28. Bernhard, W., Granboulan, N., The fine structure of the cancer cell nucleus. Exp. Cell Res. 9:Suppl. (1963), 19–53.
29. Bidwell, J.P., Fey, E.G., van Wijnen, A.J., Penman, S., Stein, J.L., Lian, J.B., Stein, G.S., Nuclear matrix proteins distinguish normal diploid osteoblasts from osteosarcoma cells. Cancer Res. 54 (1994), 28–32.
30. Blencowe, B., Nickerson, J.A., Issner, R., Penman, S., Sharp, P.A., Association of nuclear matrix antigens with exon-containing splicing complexes. J. Cell Biol. 127 (1994), 593–607.
31. Blobel, G., Gene gating: A hypothesis. Proc. Natl. Acad. Sci. U.S.A. 83 (1985), 8527–8529.
32. Blobel, G., Potter, V.R., Nuclei from rat liver: Isolation method that combines purity with high yield. Science 154 (1966), 1662–1664.
33. Blow, J.J., Laskey, R.A., Initiation of DNA replication in nuclei and purified DNA by a cell-free extract of Xenopus eggs. Cell (Cambridge, Mass.) 47 (1986), 577–587.
34. Bode, J., Schlake, T., Rios-Ramirez, M., Meike, C., Stengert, M., Kay, V., Klenk-Wirth, D., Scaffold/matrix-attached regions (S/MARS): Structural properties of transcriptionally active loci. Berezney, R., Jeon, K., (eds.) “International Review of Cytology”, 162, 1995, Academic Press, San Diego in press.
35. Boulikas, T., Chromatin domains and prediction of MAR sequences. Berezney, R., Jeon, K., (eds.) “International Review of Cytology”, 162, 1995, Academic Press, San Diego in press.
36. Bregman, D.B., Du, L., Zee, S., Warren, S., Transcription-dependent redistribution of the large subunit of RNA polymerase II to discrete nuclear domains. J. Cell Biol. 129:2 (1995), 287–296.
37. Bridger, J.M., Kill, I.R., O'Farrel, M., Hutchison, C.J., Internal lamin structures with Gl nuclei of human fibroblasts. J. Cell Sci. 104 (1993), 297–306.
38. Capco, D.G., Wan, K.M., Penman, S., The nuclear matrix: Three-dimensional architecture and protein composition. Cell (Cambridge, Mass.) 29 (1982), 847–858.
39. Capitani, S., Girard, P.R., Mazzei, G.J., Kuo, J.F., Berezney, R., Manzoli, F.A., Immunochemical characterization of protein kinase C in rat liver nuclei and subnuclear fractions. Biochem. Biophys. Res. Commun. 142 (1987), 367–375.
40. Cardenas-Corona, M.E., Jacobson, E.L., Jacobson, M.K., Endogenous polymers of ADP-ribose are associated with the nuclear matrix. J. Biol. Chem. 262 (1987), 14863–14866.
41. Chaly, N., Bladon, T., Setterfield, G., Little, J.E., Kaplan, J.G., Brown, D.L., Changes in distribution of nuclear matrix antigens during the miotic cell cycle. J. Cell Biol. 99 (1984), 661–671.
42. Ciejek, E.M., Nordstro, J.L., Tsai, M.J., O'Malley, B.W., Ribonucleic acid precursors are associated with the chick oviduct nuclear matrix. Biochemistry 21 (1982), 4945–4953.
43. Coghlan, V.M., Langeberg, L.K., Fernandez, A., Lamb, N.J.C., Scott, J.D., Cloning and characterization of AKAP 95, a nuclear protein that associates with the regulatory subunit of type II cAMP-dependent protein kinase. J. Biol. Chem. 269 (1994), 7658–7665.
44. Collins, J.M., Chu, A.K., Binding of the DNA polymerase α-DNA primase complex to the nuclear matrix in HeLa cells. Biochemistry 26 (1987), 5600–5607.
45. Comings, D.E., Okada, T.A., Nuclear proteins. III. The fibrillar nature of the nuclear matrix. Exp. Cell Res. 103 (1976), 341–360.
46. Compton, D.A., Cleveland, D.W., NuMA, a nuclear protein involved in mitosis and nuclear reformation. Curr. Opin. Cell Biol. 6:3 (1994), 343–346.
47. Compton, D.A., Szilak, I., Cleveland, D.W., Primary structure of NuMA, an intranuclear protein that defines a novel pathway for segregation of proteins at mitosis. J. Cell Biol. 116 (1992), 1395–1408.
48. Covey, L., Choi, Y., Prives, C., Association of simian virus 40 T antigen with the nuclear matrix of infected and transformed monkey cells. Mol. Cell. Biol. 4 (1984), 1384–1392.
49. Cremer, T., Kurz, A., Zirbel, R., Dietzel, S., Rinke, B., Schröck, E., Speicher, M.R., Mathieu, U., Jauch, A., Emmerich, P., Scherthan, H., Ried, T., Cremer, C., Lichter, P., Role of chromosome territories in the functional compartmentalization of cell nucleus. Cold Spring Harbor Symp. Quant. Biol. 53 (1993), 777–792.
50. Davie, J.R., The nuclear matrix and the regulation of chromatin organization and function. Berezney, R., Jeon, K., (eds.) “International Review of Cytology”, 162, 1995, Academic Press, San Diego in press.
51. Derenzini, M., Lorenzoni, E., Marinozzi, V., Barsotti, P., Ultrastructural cytochemistry of active chromatin in regenerating rat hepatocytes. J. Ultrastruct. Res. 59 (1977), 250–262.
52. Derenzini, M., Novello, F., Pession-Brizzi, A., Perichromatin fibrils and chromatin ultrastructural pattern. Exp. Cell Res. 112 (1978), 443–454.
53. Detke, S., Keller, J.M., Comparison of the protein present in HeLa cell interphase nucleoskeletons and metaphase chromosome scaffolds. J. Biol. Chem. 257 (1982), 3905–3911.
54. Dijkwel, P.A., Mullenders, L.H.F., Wanka, F., Analysis of the attachment of replicating DNA to a nuclear matrix in mammalian interphase nuclei. Nucleic Acids Res. 6 (1979), 219–230.
55. Dijkwel, P.A., Wenink, P.W., Poddighe, J., Permanent attachment of replication origins to the nuclear matrix in BHK-cells. Nucleic Acids Res. 14 (1986), 3241–3249.
56. Dworetzky, S.I., Fey, E.G., Penman, S., Lian, J.B., Stein, J.L., Stein, C.S., Progressive changes in the protein composition of the nuclear matrix during rat osteoblast differentiation. Proc. Natl. Acad. Sci. U.S.A. 87 (1990), 4605–4609.
57. Duda, R.O., Hart, P.E., “Pattern Classification and Scene Analysis”, 1973, Wiley, New York.
58. Eisenman, R.N., Tachibana, C.Y., Abrams, H.D., Hann, S.R., v-myc and c-myc-encoded proteins are associated with the nuclear matrix. Mol. Cell. Biol. 5 (1985), 114–126.
59. Faiferman, I., Pogo, A.O., Isolation of a nuclear ribonucleoprotein network that contains heterogeneous RNA and is bound to the nuclear envelope. Biochemistry 14 (1975), 3808–3816.
60. Fakan, S., Bernhard, W., Localization of rapidly and slowly labeled nuclear RNA as visualized by high resolution autoradiography. Exp. Cell Res. 67 (1971), 129–141.
61. Fakan, S., Bernhard, W., Nuclear labeling after prolonged 3H-uridine incorporation as visualized by high resolution autoradiography. Exp. Cell Res. 79 (1973), 431–444.
62. Fakan, S., Puvion, E., Sphor, G., Localization and characterization of newly synthesized nuclear RNA in isolated rat hepatocytes. Exp. Cell Res. 99 (1976), 155–164.
63. Fawcett, D.W., An atlas of fine structure. “The Cell, Its Organelles and Inclusions”, 1966, Saunders, Philadelphia, PA.
64. Feldman, L.T., Nevins, J.R., Localization of the adenovirus E1 A protein, a positive-acting transcriptional factor, in infected cells. Mol. Cell. Biol. 3 (1983), 829–838.
65. Fernandes, D.J., Catapano, C.V., Nuclear matrix targets for anticancer agents. Cancer Cells 3 (1991), 134–140.
66. Fey, E., Krochmalnic, C., Penman, S., The nonchromatin substructures of the nucleus: the ribonucleoprotein (RNP) containing and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy. J. Cell Biol. 102 (1986), 1654–1665.
67. Fey, E., Penman, S., Nuclear matrix proteins reflect cell type of origin in cultured human cells. Proc. Natl. Acad. Sci. U.S.A. 85 (1988), 121–125.
68. Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T., Schmid, F.X., Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature (London) 337 (1989), 476–478.
69. Foisner, R., Gerace, L., Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell (Cambridge, Mass.) 73 (1993), 1267–1279.
70. Foster, K.A., Collins, J.M., The interrelation between DNA synthesis rates and DNA polymerases bound to the nuclear matrix in synchronzied HeLa cells. J. Biol. Chem. 260 (1988), 4229–4235.
71. Fox, M.H., Arndt-Jovin, D.J., Jovin, T.M., Baumann, P.H., Robert-Nicaud, M., Spatial and temporal distribution of DNA replication sites localized by immunofluorescence and confocal microscopy. J. Cell Sci. 99 (1991), 247–255.
72. Franke, W.W., Falk, H., Appearance of nuclear pore complexes after Bernhard's staining procedure. Histochemie 24 (1970), 266–278.
73. Gasser, S.M., Laemmli, U.K., A glimpse at chromosomal order. Trends Genet. 3 (1987), 16–22.
74. Gerace, L., Blobel, G., The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell (Cambridge, Mass.) 19 (1980), 277–287.
75. Gerace, L., Comeau, C., Benson, M., Organization and modulation of nuclear lamina structure. J. Cell Sci. 1:Suppl. (1984), 137–160.
76. Gerber, U.F., Gerace, L., Depletion of calcium from the lumen of endoplasmic reticulum reversibly inhibits passive diffusion and signal-mediated transport into the nucleus. The J. Cell Biol. 128 (1995), 5–14.
77. Gething, M-J., Sambrook, J., Protein folding in the cell. Nature (London) 355 (1992), 33–45.
78. Getzenberg, R.H., Coffey, D.S., Tissue specificity of the hormonal response in sex accessory tissue is associated with nuclear matrix protein patterns. Mol. Endocrinol. 4 (1990), 1336–1342.
79. Getzenberg, R.H., Pienta, K.J., Huang, E.Y., Coffey, D.S., Identification of nuclear matrix proteins in the cancer and normal rat prostate. Cancer Res. 51 (1991), 6514–6520.
80. Goldman, M.A., Holmquist, G.P., Gray, M.C., Caston, L., Nag, A., Replication timing of genes and middle repetitive sequences. Science 224 (1984), 686–692.
81. Goldman, A.E., Moir, R.D., Montag-Lowy, M., Goldman, R.D., Pathway of incorporation of microinjected lamin A into the nuclear envelope. J. Cell Biol. 119 (1992), 725–735.
82. Graham, C.F., Arms, K., Gurdon, J.B., The induction of DNA synthesis by egg cytoplasm. Dev. Biol. 14 (1966), 349–359.
83. Greenleaf, A.L., Positive patches and negative noodles: linking RNA processing to transcription?. Trends Biochem. Sci. 18:4 (1993), 117–122.
84. Gui, J-F., Lane, W.S., Fu, X-D., A serine kinase regulates intracellular localization of splicing factors in the cell cycle. Nature (London) 369 (1994), 678–682.
85. Gupta, R.C., Dighe, N.R., Randerath, K., Smith, H.C., Distribution of initial and persistent 2-acetylaminofluorene-induced DNA adducts within DNA loops. Proc. Natl. Acad. Sci. U.S.A. 82 (1985), 6605–6608.
86. Hadlaczky, G., Went, M., Ringertz, N.R., Direct evidence for the non-random localization of mammalian chromosomes in the interphase nucleus. Exp. Cell Res. 167 (1986), 1–15.
87. Hakes, D.J., Berezney, R., DNA-binding properties of the nuclear matrix and individual nuclear matrix proteins: Evidence for salt resistant DNA binding sites. J. Biol. Chem. 266 (1991), 11131–11140.
88. Halikowski, M.J., Liew, C., Identification of a phosphoprotein in the nuclear matrix by monoclonal antibodies. Biochem. J. 241 (1987), 693–697.
89. Hand, R., Regulation of DNA replication on subchromosomal units of mammalian cells. J. Cell Biol. 64 (1975), 89–97.
90. Hand, R., Eucaryotic DNA: Organization of the genome for replication. Cell (Cambridge, Mass.) 15 (1978), 315–325.
91. Harris, H., “Nucleus and Cytoplasm”, 1968, Clarendon Press, Oxford.
92. Harris, H., “Cell Fusion”, 1970, Clarendon Press, Oxford.
93. Harris, S.G., Smith, H.C., SnRNP core protein enrichment in the nuclear matrix. Biochem. Biophys. Res. Commun. 152 (1988), 1383–1387.
94. Hassan, A.B., Cook, P.R., Visualization of replication sites in unfixed human cells. J. Cell Sci. 105 (1993), 541–550.
95. Hatton, K.S., Dhar, V., Gahn, T.A., Brown, E.H., Mager, D., Schildkraut, C.L., Temporal order of replication of multigene families reflects chromosomal location and transcriptional activity. Cancer Cells 6 (1988), 335–340.
96. He, D., Nickerson, J.A., Penman, S., Core filaments of the nuclear matrix. J. Cell Biol. 110 (1990), 569–580.
97. He, D., Zheng, C., Brinkley, B.R., Nuclear matrix proteins as structural and functional components of the mitotic apparatus. Berezney, R., Jeon, K., (eds.) “International Review of Cytology”, 162, 1995, Academic Press, San Diego in press.
98. Hendzel, M.J., Delcuve, G.P., Davie, J.R., Histone deacetylase is a component of the internal matrix. J. Biol. Chem. 266 (1991), 21936–21942.
99. Hendzel, M.J., Sun, J-M., Chen, H.Y., Rattner, J.B., Davie, J.R., Histone acetyltransferase is associated with the nuclear matrix. J. Biol. Chem. 269 (1994), 22894–22901.
100. Henry, S.M., Hodge, L.D., Nuclear matrix: A cell-cycle-dependent site of increased intranuclear protein phosphorylation. Eur. J. Biochem. 133 (1983), 23–29.
101. Herlan, G., Eckert, W.A., Kaffenberger, W., Wunderlich, F., Isolation and characterization of an RNA-containing nuclear matrix from retrahymena macronuclei. Biochemistry 18 (1979), 1782–1788.
102. Herman, R., Weymouth, L., Penman, S., Heterogeneous nuclear RNA-protein fibers in chromatin-depleted nuclei. J. Cell Biol. 78 (1978), 663–674.
103. Herman, R., Zieve, G., Williams, J., Lenk, R., Penman, S., Cellular skeletons and RNA messages. Proc. Nucleic Acid Res. Mol. Biol. 19 (1976), 379–401.
104. Hisatake, K., Hasegawa, S., Takada, R., Nakatani, Y., Hirikoshi, M., Roeder, R.G., The p250 subunit of native TATA box-binding factor TFIID is the cell-cycle regulatory protein CCG1. Nature (London) 362 (1993), 179–181.
105. Hozák, P., Hassan, A.B., Jackson, D.A., Cook, P.R., Visualization of replication factories attached to a nucleoskeleton. Cell (Cambridge, Mass.) 73 (1993), 361–373.
106. Huang, S., Spector, D.L., Nascent pre-mRNA transcripts are associated with nuclear regions enriched in splicing factors. Genes Dev. 5 (1991), 2288–2302.
107. Ingber, D.E., Dike, L., Hansen, L., Karp, S., Liley, H., Maniotis, A., McNamee, H., Mooney, D., Plopper, G., Sims, J., Cellular tensegrity: exploring how mechanical charges in the cytoskeleton regulate cell growth, migration, and tissue pattern during morphogenesis. Int. Rev. Cytol. 150 (1994), 173–224.
108. Jackson, D.A., Cook, P.R., A general method for preparing chromatin containing intact DNA. EMBO J. 14 (1985), 913–918.
109. Jackson, D.A., Cook, P.R., Replication occurs at a nucleoskeleton. EMBO J. 5 (1986), 1403–1410.
110. Jackson, D.A., Cook, P.R., A cell cycle-dependent DNA polymerase activity that replicates intact DNA in chromatin. J. Mol. Biol. 192 (1986), 65–67.
111. Jackson, D.A., Cook, P.R., Different populations of DNA polymerase α in HeLa cells. J. Mol. Biol. 192 (1986), 77–86.
112. Jackson, D.A., Cook, P.R., Visualization of a filamentous nucleoskeleton with a 23 nm axial repeat. EMBO J. 7 (1988), 3667–3677.
113. Jackson, D.A., Hassan, A.B., Errington, R.J., Cook, P.R., Visualization of focal sites of transcription within human nuclei. EMBO J. 12 (1993), 1059–1065.
114. Jiménez-García, L.F., Spector, D.L., In vivo evidence that transcription and splicing are coordinated by a recruiting mechanism. Cell (Cambridge, Mass.) 73 (1993), 47–59.
115. Jones, C., Su, R.T., DNA polymerase α from the nuclear matrix of cells infected with simian virus 40. Nucleic Acids Res. 10 (1982), 5517–5582.
116. Kaufmann, S.H., Coffey, D.S., Shaper, J.H., Considerations in the isolation of rat liver nuclear matrix, nuclear envelope, and pore complex lamina. Exp. Cell Res. 132 (1981), 105–123.
117. Keesee, S.K., Meneghini, M.D., Szaro, R.P., Wu, Y.J., Nuclear matrix proteins in human colon cancer. Proc. Natl. Acad. Sci. U.S.A. 91 (1994), 1913–1916.
118. Khanuja, P.S., Lehr, J.E., Soule, H.D., Gehani, S.K., Noto, A.C., Choudhury, S., Chen, R., Pienta, K.J., Nuclear matrix proteins in normal and breast cancer cells. Cancer Res. 53 (1993), 3394–3398.
119. Kill, I.R., Bridger, J.M., Campbell, K.H.S., Maldonado-codina, G., Hutchison, C.J., The timing of the formation and usage of replicase cluster in S-phase nuclei of human dipoid fibroblasts. J. Cell Sci. 100 (1991), 869–876.
120. Konstantinovic, M., Sevaljevic, L., Nuclear matrix from resting and concanavalin A-stimulated human lymphocytes. Biochim. Biophys. Acta 762 (1983), 1–8.
121. Lao, Y.F., Arrighi, F.F., Studies of mammalian chromosome replication. II. Evidence for the existence of defined chromosome replicating units. Chromosoma 83 (1981), 721–741.
122. Lawrence, J.B., Singer, R.H., Marselle, L.M., Highly localized tracks of specific transcripts within interphase nuclei visualized by in situ hybridization. Cell (Cambridge, Mass.) 57 (1989), 493–502.
123. Lebkowski, J.S., Laemmli, U., Non-histone proteins and long-range organization of HeLa interphase DNA. J. Mol. Biol. 156 (1982), 325–344.
124. Lehner, C.F., Eppenberger, H.M., Fakan, S., Nigg, E.A., Nuclear substructure antigens monoclonal antibodies against components of nuclear matrix preparations. Exp. Cell Res. 162 (1986), 205–219.
125. Lewis, C.D., Lebkowski, J.S., Daly, A.K., Laemmli, U.K., Interphase nuclear matrix and metaphase scaffolding structures. J. Cell Sci 1:Suppl. (1984), 103–122.
126. Li, H., Bingham, P.M., Arginine/serine-rich domains of the su(wa) and tra RNA processing regulators target proteins to a subnuclear compartment implicated in splicing. Cell 67 (1991), 335–342.
127. Loidl, P., Eberharter, A., Nuclear matrix and the cell cycle. Berezney, R., Jeon, K., (eds.) “International Review of Cytology”, 162, 1995, Academic Press, San Diego in press.
128. Mancini, M.A., Shan, B., Nickerson, J.A., Penman, S., Lee, W., The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein. Proc. Natl. Acad. Sci. U.S.A. 91 (1994), 418–422.
129. Manders, E.M.M., Stap, J., Brakenhoff, G.J., Van Driel, R., Aten, J.A., Dynamics of three dimensional replication patterns during the S-phase, analyzed by double labeling and confocal microscopy. J. Cell Sci. 103 (1992), 857–862.
130. Manuelidis, L., Individual interphase chromosome domains revealed by in situ hybridization. Hum. Genet. 71 (1985), 288–293.
131. Manuelidis, L., Individual interphase chromosomes. Science 250 (1990), 1533–1540.
132. Mariman, E.C.M., van Eckelen, C.A.G., Reinders, R.J., Berns, A.J.M., van Venrooij, W.J., Adenoviral heterogeneous nuclear RNA is associated with the host nuclear matrix during splicing. J. Mol. Biol. 154 (1982), 103–119.
133. Maul, G.G., Maul, H.M., Scogna, J.E., Liebermann, M.W., Stein, G.S., Hsu, B.Y.I., Borun, T.W., Time sequence of nuclear pore formation in phytohemagglutinin-stimulated lymphocytes and HeLa cells during the cell cycle. J. Cell Biol. 5 (1972), 433–442.
134. McCready, S.J., Godwin, J., Mason, D.W., Brazell, I.A., Cook, P.R., DNA is replicated at the nuclear cage. J. Cell Sci. 46 (1980), 365–386.
135. McKeon, F.D., Kirschner, M.W., Caput, D., Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature (London) 319 (1986), 463–468.
136. Meier, U.T., Blobel, G., Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell 70 (1992), 127–138.
137. Meng, C., Berezney, R., Replication cluster domains persist throughout the cell cycle of mouse 3T3 cells. J. Cell Biol., 115, 1991, 95a.
138. Milavetz, B.I., Edwards, D.R., Synthesis and stability of nuclear matrix proteins in resting and serum-stimulated Swiss 3T3 cells. J. Cell. Physiol. 127 (1986), 388–396.
139. Miller, T.E., Huang, C.Y., Pogo, A.O., Rat liver nuclear skeleton and ribonucleo-protein complexes containing hnRNA. J. Cell Biol. 76 (1978), 675–691.
140. Mirkovitch, J., Mirault, M.F., Laemmli, U.K., Organization of the higher-order chromatin loop: Specific attachment sites on nuclear scaffold. Cell (Cambridge, Mass.) 39 (1984), 223–232.
141. Moir, R.D., Montag-Lowy, M., Goldman, R.D., Dynamic properties of nuclear lamins: lamin B is associated with sites of DNA replication. J. Cell Biol. 125 (1994), 1201–1212.
142. Moir, R.D., Spann, T.P., Goldman, R.D., The dynamic properties and possible functions of nuclear lamins. Berezney, R., Jeon, K., (eds.) “International Review of Cytology”, Vol 162, 1995, Academic Press, San Diego in press.
143. Monneron, A., Bernhard, W., Fine structural organization of the interphase nucleus in some mammalian cells. J. Ultrastruct. Res. 27 (1969), 266–288.
144. Moreno Diaz de la Espina, S., Nuclear matrix proteins isolated from plant cells. Berezney, R., Jeon, K., (eds.) “International Review of Cytology”, Vol 162, 1995, Academic Press, San Diego in press.
145. Mortillaro, M.J., Berezney, R., Association of a nuclear matrix cyclophilin with splicing factors. J. Cell. Biochem. Suppl., 21B, 1995, 142.
146. Mortillaro, M.J., Vijayaraghavan, S., Berezney, R., Evidence that matrin 3 is a member of a complex gene family. Mol. Biol. Cell, 4, 1993, 81S.
147. Nakamura, H., Morita, T., Sato, C., Structural organization of replication domains during DNA synthetic phase in the mammalian nucleus. Exp. Cell Res. 165 (1986), 291–297.
148. Nakayasu, H., Berezney, R., Identification of two high molecular weight internal nuclear matrix proteins with monoclonal antibodies. J. Cell Biol., 105, 1987, 70a.
149. Nakayasu, H., Berezney, R., Mapping replicational sites in the eucaryotic cell nucleus. J. Cell Biol. 108 (1989), 1–11.
150. Nakayasu, H., Berezney, R., Nuclear matrins: Identification of the major nuclear matrix proteins. Proc. Natl. Acad. Sci. U.S.A. 88 (1991), 10312–10316.
151. Nash, R.E., Puvion, E., Bernhard, W., Perichromatin fibrils as components of rapidly labeled extranucleolar RNA. J. Ultrastruct. Res. 53 (1975), 395–405.
152. Neri, L.M., Mazzotti, G., Capitani, S., Maraldi, N.M., Cinti, C., Baldini, N., Rana, R., Martelli, A.M., Nuclear matrix-bound replicational sites detected in situ by 5-bromodeoxyuridine. Histochemistry 98 (1992), 19–32.
153. Nickerson, J.A., He, D., Fey, F.G., Penman, S., The nuclear matrix. Strauss, P.R., Wilson, S.H., (eds.) “The Eukaryotic Nucleus. Molecular Biochemistry and Macromolecular Assemblies”, 2, 1990, Telford Press, Caldwell, NJ, 763–782.
154. Nickerson, J.A., Krockmalnic, G., Wan, K.M., Turner, C.D., Penman, S., A normally masked nuclear matrix antigen that appears at mitosis on cytoskeleton filaments adjoining chromosomes, centrioles and midbodies. J. Cell Biol. 116 (1992), 977–987.
155. Noaillac-Depeyre, J., Azum, M., Geraud, M., Mathieu, C., Gas, N., Distribution of nuclear matrix proteins in interphase CHO cells and rearrangements during the cell cycle: An ultrastructural study. Biol. Cell 61 (1987), 23–32.
156. Ochs, R., Smetana, K., Detection of fibrillarin in nucleolar remnants and the nucleolar matrix. Exp. Cell Res. 197 (1991), 183–190.
157. O'Keefe, R.T., Henderson, S.C., Spector, D.L., Dynamic organization of DNA replication in mammalian cell nuclei: Spatially and temporally defined replication of chromosome-specific α-satellite DNA sequences. J. Cell Biol. 116 (1992), 1095–1110.
158. Olson, M.O., Thompson, B.A., Distribution of proteins among chromatin components of nucleoli. Biochemistry 22 (1983), 3187–3193.
159. Olson, M.O., Wallace, M.O., Herrera, A.H., Marshall-Carlson, L., Hunt, R.C., Preribosomal ribonucleoprotein particles are a major component of a nucleolar matrix fraction. Biochemistry 25 (1986), 484–491.
160. Paff, M.T., Fernandes, D.J., Synthesis and distribution of primer RNA in nuclei of CCRF-CEM leukemia cells. Biochemistry 29 (1990), 3442–3450.
161. Painter, R.B., Young, B.R., Formation of nascent DNA molecules during inhibition of replicon initiation in mammalian cells. Biochim. Biophys. Acta 418 (1976), 146–153.
162. Pardoll, D.M., Vogelstein, B., Coffey, D.S., A fixed site of DNA replication in eucaryotic cells. Cell 19 (1980), 527–536.
163. Park, M.K., D'Onofrio, M., Willingham, M.C., Hanover, J.A., A monoclonal antibody against a family of nuclear pore proteins (nucleoporins): O-linked N-acetylglucosamine is part of the immunodeterminant. Proc. Natl. Acad. Sci. U.S.A. 84 (1987), 6462–6466.
164. Partin, A.W., Getzenberg, R.H., Carmichael, M.J., Vindivich, D., Yoo, J., Epstein, J.I., Coffey, D.S., Nuclear matrix protein patterns in human benign prostate hyperplasia and prostate cancer. Cancer Res. 53 (1993), 744–746.
165. Paulson, J.R., Laemmli, U.K., The structure of histone-depleted metaphase chromosomes. Cell (Cambridge, Mass.) 12 (1977), 817–828.
166. Payrastre, B., Nievers, M., Boonstra, J., Breton, M., Verkleji, A.J., Van Bergen en Henegouwen, P.M.P., A differential location of phosphoinositide kinases, diacylglycerol kinase, and phospholipase C in the nuclear matrix. J. Biol. Chem. 267 (1992), 5078–5084.
167. Peick, A.C., van der Velden, H.M., Rijken, A.A., Neis, J.M., Wanka, F., Protein composition of the chromosomal scaffold and interphase nuclear matrix. Chromosoma 91 (1985), 137–144.
168. Perret, C., Lomri, N., Thomasset, M., Evolution of the EF-hand calcium-binding protein family: Evidence for exon shuffling and intron insertion. J. Mol. Evol. 27 (1988), 351–364.
169. Peters, K.E., Comings, D.E., Two-dimensional gel electrophoresis of rat liver nuclear washes, nuclear matrix and hnRNA proteins. J. Cell Biol. 86 (1980), 135–155.
170. Peters, K.F., Okada, T.A., Comings, D.F., Chinese hamster nuclear proteins. An electrophoretic analysis of interphase, metaphase and nuclear matrix preparations. Eur. J. Biochem. 129 (1982), 221–232.
171. Pienta, K.J., Lehr, J.E., A common set of nuclear matrix proteins in prostate cancer cells. Prostate 23 (1993), 61–67.
172. Pienta, K.J., Lehr, J.E., Inhibition of prostate cancer growth by estramustine and etoposide: Evidence for interaction at the nuclear matrix. J. Urol. 149 (1993), 1622–1625.
173. Puvion, E., Moyne, G., In situ localization of RNA structures. Busch, H., (eds.) “The Cell Nucleus”, 8, 1981, Academic Press, New York, 59–115.
174. Razin, S.V., Gronova, I.T., Iarovaia, O.V., Specificity and functional significance of DNA interaction with the nuclear matrix: new approaches to clarify the old questions. Berezney, R., Jeon, K., (eds.) “International Review of Cytology”, Vol 162, 1995, Academic Press, San Diego in press.
175. Reeves, R., Chang, D., Investigations of the possible functions for glycosylation in the high mobility group proteins: Evidence for a role in nuclear matrix association. J. Biol. Chem. 258 (1983), 679–687.
176. Reiter, T., Penman, S., ‘Prompt’ heat shock proteins: Translationally regulated synthesis of new proteins associated with the nuclear matrix-intermediate filaments as an early response to heat shock. Proc. Natl. Acad. Sci. U.S.A. 80 (1983), 4737–4741.
177. Rennie, P.S., Bruchovsky, N., Cheng, H., Isolation of 3 S androgen receptors from salt resistant fractions and nuclear matrices of prostatic nuclei after mild trypsin digestion. J. Biol. Chem. 258 (1983), 7623–7630.
178. Rout, M.P., Blobel, G., Isolation of the yeast nuclear pore complex. J. Cell Biol. 123 (1993), 771–783.
179. Sahyoun, N., LeVine, H., Bronson, D., Cuatrecasas, P., Ca(2+)-calmodulin-dependent protein kinase in neuronal nuclei. J. Biol. Chem. 269 (1984), 9341–9344.
180. Samarabandu, J.K., Cheng, P.C., Berezney, R., Application of three-dimensional image analysis to the mammalian cell nucleus. Proc. IEEE Southeastcon 94 (1994), 98–100.
181. Samarabandu, J.K., Ma, H., Cheng, P.C., Berezney, R., Computer aided analysis of DNA replication sites in the mammalian cell. J. Cell. Biochem. Suppl., 21B, 1995, 137.
182. Sevaljevic, L., Petrovic, M., Konstantinovic, M., Krtolica, K., Comparative studies of rat liver and sea urchin embryo nuclear matrices: pertial fractional and protein kinase activity distribution. J. Cell Sci. 55 (1982), 189–198.
183. Shan, X., Xue, Z., Melese, T., Yeast NPI46 encodes a novel prolyl cis-trans isomerase that is located in the nucleolus. J. Cell Biol. 126 (1994), 853–862.
184. Shaper, J.H., Pardoll, D.M., Kaufmann, S.H., Barrack, F.R., Vogelstein, B., Coffey, D.S., The relationship of nuclear matrix to cellular structure and function. Adv. Enzyme Regul. 17 (1978), 213–248.
185. Shiomi, Y., Powers, J., Bolla, R.I., Nguyen, T.V., Schlessinger, D., Proteins and RNA in mouse L cell core nucleoli and nucleolar matrix. Biochemistry 25 (1986), 5745–5751.
186. Sikorska, M., Whitfield, J.F., Walker, P.R., The regulatory and catalytic subunits of cAMP-dependent protein kinases are associated with transcriptional active chromatin during changes in gene expression. J. Biol. Chem. 263 (1988), 3005–3011.
187. Smetana, K., Lejnar, J., Vlastiborova, A., Busch, H., On interchromatinic dense granules of mature human neutrophil granulocytes. Exp. Cell Res. 64 (1971), 105–112.
188. Smith, H.C., Berezney, R., DNA polymerase α is tightly bound to the nuclear matrix of actively replicating liver. Biochem. Biophys. Res. Commun. 97 (1980), 1541–1547.
189. Smith, H.C., Berezney, R., Nuclear matrix-bound DNA synthesis: An in vitro system. Biochemistry 21 (1982), 6751–6761.
190. Smith, H.C., Berezney, R., Dynamic domains of DNA polymerase α in regenerating rat liver. Biochemistry 22 (1983), 3042–3046.
191. Smith, H.C., Berezney, R., Brewster, J.M., Rekosh, D., Properties of adenoviral DNA bound to the nuclear matrix. Biochemistry 24 (1985), 1197–1202.
192. Smith, H.C., Harris, S.G., Zillmann, M., Berget, S.M., Evidence that a nuclear matrix protein participates in pre-mRNA splicing. Exp. Cell Res. 182 (1989), 521–533.
193. Smith, H.C., Puvion, F., Buchholtz, L.A., Berezney, R., Spatial distribution of DNA loop attachment and replication sites in the nuclear matrix. J. Cell Biol. 99 (1984), 1794–1802.
194. Somanathan, S., Mortillaro, M.J., Berezney, R., Identifying members of the matrin 3 gene family. J. Cell. Biochem. Suppl., 21B, 1995, 146.
195. Song, M.H., Adolph, K.W., Phosphorylation of nonhistone proteins during the HeLa cell cycle. J. Biol. Chem. 258 (1983), 3309–3319.
196. Sorimachi, H., Ishiura, S., Suzuki, K., A novel tissue-specific calpain species expressed predominantly in the stomach comprises two alternatively spliced products with and without Ca(2+)-binding domain. J. Biol. Chem. 268 (1993), 19476–19482.
197. Sparuoli, E., Levi, M., Rossi, E., Replicon clusters may form structurally stable complexes of chromatin and chromosomes. J. Cell Sci. 107 (1994), 3097–3103.
198. Spector, D., Colocalization of U1 and U2 small nuclear RNPs by immunocytochemistry. Biol. Cell 51 (1984), 109–112.
199. Spector, D.L., Macromolecular domains within the cell nucleus. Annu. Rev. Cell Biol. 9 (1993), 265–315.
200. Spector, D.L., Schrier, W.H., Busch, H., Immunoelectron microscopic localization of SnRNPs. Bio. Cell 49 (1983), 1–10.
201. Staufenbiel, M., Deppert, W., Nuclear matrix preparations from liver tissue and from cultured vertebrate cells: Differences in major polypeptides. Eur. J. Cell Biol. 31 (1983), 341–348.
202. Staufenbiel, M., Deppert, W., Preparation of nuclear matrices from cultured cells: subfractionation of nuclei in situ. J. Cell Biol. 98 (1984), 1886–1894.
203. Steele, W.J., Busch, H., Studies on the acidic nuclear proteins of the Walker tumor and the liver. Cancer Res. 23 (1963), 1153–1163.
204. Stuurman, N., van Driel, L., De Jong, A.M.L., van Renswoude, J., The protein composition of the nuclear matrix of murine P19 embryonal carcinoma cells is differentiation-state dependent. Exp. Cell Res. 180 (1989), 460–466.
205. Stuurman, N., Meijne, A.M.L., van der Pol, A.J., de Jong, L., van Driel, R., van Renswoude, J., The nuclear matrix from cells of different origin: Evidence for a common set of matrix proteins. J. Biol. Chem. 265 (1990), 5460–5465.
206. Tawfic, S., Ahmed, K., Association of casien kinase 2 with nuclear matrix. J. Biol. Chem. 269 (1994), 7489–7493.
207. Tubo, R.A., Berezney, R., Pre-replicative association of multiple replicative enzyme activities with the nuclear matrix during rat liver regeneration. J. Biol. Chem. 262 (1987), 1148–1154.
208. Tubo, R.A., Berezney, R., Identification of 100 and 150S DNA polymerase α-primase megacomplexes solubilized from the nuclear matrix of regenerating rat liver. J. Biol. Chem. 263 (1987), 5857–5865.
209. Tubo, R.A., Berezney, R., Nuclear matrix-bound DNA primase: Elucidation of an RNA primase system in nuclear matrix isolation from regenerating rat liver. J. Biol. Chem. 262 (1987), 6637–6642.
210. Tubo, R.A., Martelli, A.M., Berezney, R., Enhanced processivity of nuclear matrix bound DNA polymerase α from regenerating rat liver. Biochemistry 26 (1987), 5710–5718.
211. Tubo, R.A., Smith, H.C., Berezney, R., The nuclear matrix continues DNA synthesis at in vivo replicational forks. Biochim. Biophys. Acta 825 (1985), 326–334.
212. Turner, B.M., Franchi, L., Identification of protein antigens associated with the nuclear matrix and with clusters of interchromatin granules in both interphase and miotic cells. J. Cell Sci. 87 (1987), 269–282.
213. van der Velden, H.M.W., Wanka, F., The nuclear matrix—Its role in the spatial organization and replication of eukaryotic DNA. Mol. Biol. Rep. 12 (1987), 69–77.
214. van Eekelen, C.A.G., Salden, M.H.L., Habets, W.J.A., van de Putte, L.B.A., van Venrjooij, W.J., On the existence of an internal nuclear protein structure in HeLa cells. Exp. Cell Res. 141 (1982), 181–190.
215. van Wijnen, A.J., Bidwell, J.P., Fey, E.G., Penman, S., Lian, J.B., Stein, J.L., Stein, G.S., Nuclear matrix association of multiple sequence specific DNA binding activities related to SP-1, ATF, CCAAT, C/EBP, Oct-1 and AP-1. Biochemistry 32 (1993), 8397–8402.
216. Verheijen, R., Kuijpers, H., Vooijs, P., van Venrooij, W., Ramaekers, F., Protein composition of nuclear matrix preparations from HeLa cells: An immunochemical approach. J. Cell Sci. 80 (1986), 103–122.
217. Verheijen, R., van Venrooij, W.J., Ramaekers, F., The nuclear matrix: structure and composition. J. Cell Sci. 90 (1988), 11–36.
218. von Bertalanffy, L., “Problems of Life”, 1952, C. A. Watts & Co., London.
219. Wan, K., Nickerson, J.A., Krockmalnic, G., Penman, S., The B1C8 protein is in the dense assemblies of the nuclear matrix and relocates to the spindle and pericentriolar filaments at mitosis. Proc. Natl. Acad. Sci. U.S.A. 91 (1994), 594–598.
220. Wansink, D.G., Schul, W., van der Kraan, I., van Steensel, B., van Driel, R., de Long, L., Fluorescent labeling of nascent RNA reveals transcription by RNA polymerase II in domains scattered throughout the nucleus. J. Cell Biol. 122 (1993), 283–293.
221. Wei, X., Mortillaro, M.J., Kim, S., Frego, L., Buchholtz, L., Nakayasu, H., Berezney, R., p250 is a novel nuclear matrix protein that colocalizes with splicing factors. J. Cell. Biochem. Suppl., 21B, 1995, 142.
222. Wu, J.Y., Maniatis, T., Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell (Cambridge, Mass.) 75 (1993), 1061–1070.
223. Wunderlich, F., Herlan, G., A reversibly contractile nuclear matrix. J. Cell Biol. 73 (1977), 271–278.
224. Xing, Y., Johnson, C.V., Dobner, P.R., Lawrence, J.B., Higher level organization of individual gene transcription and RNA splicing. Science 259 (1993), 1326–1330.
225. Xing, Y., Lawrence, J.B., Preservation of specific RNA distribution within the chromatin-depleted nuclear substructure demonstrated by in situ hybridization coupled with biochemical fractionation. J. Cell Biol. 112 (1991), 1055–1063.
226. Yang, C.H., Lambie, E.J., Snyder, M., NuMA: An unusually long coiled-coil related protein in the mammalian nucleus. J. Cell Biol. 116 (1992), 1303–1317.
227. Zahler, A.M., Neugebauer, K.M., Stolk, J.A., Roth, M.B., Human SR proteins and isolation of a cDNA encoding SRp75. Mol. Cell Biol. 13 (1993), 4023–4028.
228. Zbarsky, I.B., Nuclear skeleton structures in some normal and tumor cells. Mol. Biol. Rep. 7 (1981), 139–148.
229. Zehnbauer, B., Vogelstein, B., Supercoiled loops in the organization of replication and transcription in eukaryotes. BioEssays 2 (1985), 52–54.
230. Zeitlin, S., Parent, A., Silverstein, S., Efstratiades, A., Pre-mRNA splicing and the nuclear matrix. Mol. Cell. Biol. 7 (1987), 111–120.
231. Zeitlin, S., Wilson, R.C., Efstratiadis, A., Autonomous splicing and complementation of in vivo-assembled spliceosomes. J. Cell Biol. 108 (1989), 765–777.
232. Zeng, C., He, D., Brinkley, B.R., Localization of NuMA proteins isoforms in the nuclear matrix of mammalian cells. Cell Motil. Cytoskel. 29 (1994), 167–176.
233. Zeng, C., He, D., Berget, S.M., Brinkley, B.R., Nuclear mitotic aparatus proteins: A structural protein interphase between the nucleoskeletons and RNA splicing. Proc. Natl. Acad. Sci. U.S.A. 91 (1994), 1505–1509.
234. Zhelev, N.Z., Todorov, I.T., Philipova, R.N., Hadjiolov, A.A., Phosphorylation-related accumulation of the 125K nuclear matrix protein mitotin in human mitotic cells. J. Cell Sci. 95 (1990), 59–64.