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Volumn 19, Issue 8, 1999, Pages 5237-5246

Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins

Author keywords

[No Author keywords available]

Indexed keywords

CHROMOSOME PROTEIN; CURVED DNA; DNA; NUCLEAR PROTEIN;

EID: 0032814140     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.8.5237     Document Type: Short Survey
Times cited : (779)

References (132)
  • 1
    • 0028580511 scopus 로고
    • Stimulation of transcription in cultured cells by high mobility group protein 1: Essential role of the acidic carboxyl-terminal region
    • Aizawa, S., H. Nishino, K. Saito, K. Kimura, H. Shirakawa, and Y. Yoshida. 1994. Stimulation of transcription in cultured cells by high mobility group protein 1: essential role of the acidic carboxyl-terminal region. Biochemistry 33:14690-14695.
    • (1994) Biochemistry , vol.33 , pp. 14690-14695
    • Aizawa, S.1    Nishino, H.2    Saito, K.3    Kimura, K.4    Shirakawa, H.5    Yoshida, Y.6
  • 2
    • 0028274720 scopus 로고
    • The footprint of chromosomal proteins HMG-14 and HMG-17 on chromatin subunits
    • Alfonso, P. J., M. P. Crippa, J. J. Hayes, and M. Bustin. 1994. The footprint of chromosomal proteins HMG-14 and HMG-17 on chromatin subunits. J. Mol. Biol. 236:189-198.
    • (1994) J. Mol. Biol. , vol.236 , pp. 189-198
    • Alfonso, P.J.1    Crippa, M.P.2    Hayes, J.J.3    Bustin, M.4
  • 3
    • 0032190230 scopus 로고    scopus 로고
    • AT-hook motifs identified in a wide variety of DNA-binding proteins
    • Aravind, L., and D. Landsman. 1998. AT-hook motifs identified in a wide variety of DNA-binding proteins. Nucleic Acids Res. 26:4413-4421.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4413-4421
    • Aravind, L.1    Landsman, D.2
  • 5
    • 0030059342 scopus 로고    scopus 로고
    • Genomic characterization of human HMGIC, a member of the accessory transcription factor family found at translocation breakpoints in lipomas
    • Ashar, H. R., L. Cherath, K. M. Przybysz, and K. Chada. 1996. Genomic characterization of human HMGIC, a member of the accessory transcription factor family found at translocation breakpoints in lipomas. Genomics 31:207-214.
    • (1996) Genomics , vol.31 , pp. 207-214
    • Ashar, H.R.1    Cherath, L.2    Przybysz, K.M.3    Chada, K.4
  • 6
    • 0031001394 scopus 로고    scopus 로고
    • An HMG I/Y-containing repressor complex and supercoiled DNA topology are critical for long-range enhancer-dependent transcription in vitro
    • Bagga, R., and B. M. Emerson. 1997. An HMG I/Y-containing repressor complex and supercoiled DNA topology are critical for long-range enhancer-dependent transcription in vitro. Genes Dev. 11:629-639.
    • (1997) Genes Dev. , vol.11 , pp. 629-639
    • Bagga, R.1    Emerson, B.M.2
  • 7
    • 0028943520 scopus 로고
    • Homology model building of the HMG-1 box structural domain
    • Baxevanis, A. D., S. H. Bryant, and D. Landsman. 1995. Homology model building of the HMG-1 box structural domain. Nucleic Acids Res. 23:1019-1029.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1019-1029
    • Baxevanis, A.D.1    Bryant, S.H.2    Landsman, D.3
  • 8
    • 0029070956 scopus 로고
    • The HMG-1 box protein family: Classification and functional relationship
    • Baxevanis, A. D., and D. Landsman. 1995. The HMG-1 box protein family: classification and functional relationship. Nucleic Acids Res. 23:1604-1613.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1604-1613
    • Baxevanis, A.D.1    Landsman, A.D.2
  • 9
    • 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., R. A. Horowitz, S. A. Grigoryev, L. M. Carruthers, J. C. Hansen, A. J. Koster, and C. L. Woodcock. 1998. 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. USA 95:14173-14178.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14173-14178
    • Bednar, J.1    Horowitz, R.A.2    Grigoryev, S.A.3    Carruthers, L.M.4    Hansen, J.C.5    Koster, A.J.6    Woodcock, C.L.7
  • 12
    • 0025323711 scopus 로고
    • Structural features of the HMG chromosomal proteins and their genes
    • Bustin, M., D. A. Lehn, and D. Landsman. 1990. Structural features of the HMG chromosomal proteins and their genes. Biochim. Biophys. Acta 1049: 231-243.
    • (1990) Biochim. Biophys. Acta , vol.1049 , pp. 231-243
    • Bustin, M.1    Lehn, D.A.2    Landsman, D.3
  • 13
    • 0018381702 scopus 로고
    • Antibodies against chromosomal HMG protein stain the cytoplasm of mammalian cells
    • Bustin, M., and N. Neihart 1979. Antibodies against chromosomal HMG protein stain the cytoplasm of mammalian cells. Cell 16:181-189.
    • (1979) Cell , vol.16 , pp. 181-189
    • Bustin, M.1    Neihart, N.2
  • 14
    • 0030358586 scopus 로고    scopus 로고
    • High mobility group chromosomal proteins: Architectural components that facilitate chromatin function
    • Bustin, M., and R. Reeves. 1996. High mobility group chromosomal proteins: architectural components that facilitate chromatin function. Prog. Nucleic Acid Res. Mol. Biol. 54:35-100.
    • (1996) Prog. Nucleic Acid Res. Mol. Biol. , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 15
    • 0029348071 scopus 로고
    • The HMG-14/-17 chromosomal protein family: Architectural elements that enhance transcription from chromatin templates
    • Bustin, M., L. Trieschmann, and Y. V. Postnikov. 1995. The HMG-14/-17 chromosomal protein family: architectural elements that enhance transcription from chromatin templates. Semin. Cell Biol. 6:247-255.
    • (1995) Semin. Cell Biol. , vol.6 , pp. 247-255
    • Bustin, M.1    Trieschmann, L.2    Postnikov, Y.V.3
  • 16
    • 85038163388 scopus 로고    scopus 로고
    • The lack of chromosomal protein HMG1 does not disrupt cell growth, but causes lethal hypoglycaemia in newborn mice
    • in press
    • 15a. Calogero, S., F. Grassi, A. Aguzzi, T. Voigtlander, P. Ferrier, and M. Blanchi. The lack of chromosomal protein HMG1 does not disrupt cell growth, but causes lethal hypoglycaemia in newborn mice. Nat. Genet., in press.
    • Nat. Genet.
    • Calogero, S.1    Grassi, F.2    Aguzzi, A.3    Voigtlander, T.4    Ferrier, P.5    Blanchi, M.6
  • 18
    • 0032540334 scopus 로고    scopus 로고
    • Enhancement of serum-response factor-dependent transcription and DNA binding by the architectural transcription factor HMG-I(Y)
    • Chin, M. T., A. Pellacani, H. Wang, S. S. Lin, M. K. Jain, M. A. Perrella, and M. E. Lee. 1998. Enhancement of serum-response factor-dependent transcription and DNA binding by the architectural transcription factor HMG-I(Y). J. Biol. Chem. 273:9755-9760.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9755-9760
    • Chin, M.T.1    Pellacani, A.2    Wang, H.3    Lin, S.S.4    Jain, M.K.5    Perrella, M.A.6    Lee, M.E.7
  • 19
    • 0026092475 scopus 로고
    • Protein motifs that recognize structural features of DNA
    • Churchill, M. E., and A. A. Travers. 1991. Protein motifs that recognize structural features of DNA. Trends Biochem. Sci. 16:92-97.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 92-97
    • Churchill, M.E.1    Travers, A.A.2
  • 20
    • 0030868737 scopus 로고    scopus 로고
    • High mobility group chromosomal protein 1 binds to the adeno-associated virus replication protein (Rep) and promotes Rep-mediated site-specific cleavage of DNA, ATPase activity and transcriptional repression
    • Costello, E., P. Saudan, E. Winocour, L. Pizer, and P. Beard. 1997. High mobility group chromosomal protein 1 binds to the adeno-associated virus replication protein (Rep) and promotes Rep-mediated site-specific cleavage of DNA, ATPase activity and transcriptional repression. EMBO J. 16:5943-5954.
    • (1997) EMBO J. , vol.16 , pp. 5943-5954
    • Costello, E.1    Saudan, P.2    Winocour, E.3    Pizer, L.4    Beard, P.5
  • 21
    • 0031706629 scopus 로고    scopus 로고
    • High-mobility group 1/2 proteins are essential for initiating rolling-circle-type DNA replication at a parvo-virus hairpin origin
    • Cotmore, S. F., and P. Tattersall. 1998. High-mobility group 1/2 proteins are essential for initiating rolling-circle-type DNA replication at a parvo-virus hairpin origin. J. Virol. 72:8477-8884.
    • (1998) J. Virol. , vol.72 , pp. 8477-8884
    • Cotmore, S.F.1    Tattersall, A.P.2
  • 22
    • 0026676799 scopus 로고
    • Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain
    • Crippa, M. P., P. J. Alfonso, and M. Bustin. 1992. Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain. J. Mol. Biol. 228:442-449.
    • (1992) J. Mol. Biol. , vol.228 , pp. 442-449
    • Crippa, M.P.1    Alfonso, P.J.2    Bustin, M.3
  • 23
    • 0027296065 scopus 로고
    • Deposition of chromosomal protein HMG-17 during replication affects the nucleosomal ladder and transcriptional potential of nascent chromatin
    • Crippa, M. P., L. Trieschmann, P. J. Alfonso, A. P. Wolffe, and M. Bustin. 1993. Deposition of chromosomal protein HMG-17 during replication affects the nucleosomal ladder and transcriptional potential of nascent chromatin. EMBO J. 12:3855-3864.
    • (1993) EMBO J. , vol.12 , pp. 3855-3864
    • Crippa, M.P.1    Trieschmann, L.2    Alfonso, P.J.3    Wolffe, A.P.4    Bustin, M.5
  • 25
    • 0026047748 scopus 로고
    • Characterization and chromatin distribution of the H1 histones and high-mobility-group non-histone chromosomal proteins of trout liver and hepatocellular carcinoma
    • Davie, J. R., and G. P. Delcuve. 1991. Characterization and chromatin distribution of the H1 histones and high-mobility-group non-histone chromosomal proteins of trout liver and hepatocellular carcinoma. Biochem. J. 280:491-497.
    • (1991) Biochem. J. , vol.280 , pp. 491-497
    • Davie, J.R.1    Delcuve, A.G.P.2
  • 26
    • 0029856861 scopus 로고    scopus 로고
    • Remodeling somatic nuclei in Xenopus laevis egg extracts: Molecular mechanisms for the selective release of histone H1 and H1(0) from chromatin and the acquisition of transcriptional competence
    • Dimitrov, S., and A. P. Wolffe. 1996. Remodeling somatic nuclei in Xenopus laevis egg extracts: molecular mechanisms for the selective release of histone H1 and H1(0) from chromatin and the acquisition of transcriptional competence. EMBO J. 15:5897-5906.
    • (1996) EMBO J. , vol.15 , pp. 5897-5906
    • Dimitrov, S.1    Wolffe, A.A.P.2
  • 27
    • 0030610561 scopus 로고    scopus 로고
    • Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region of chromosomal protein HMG-14
    • Ding, H. F., M. Bustin, and U. Hansen. 1997. Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region of chromosomal protein HMG-14. Mol. Cell. Biol. 17:5843-5855.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5843-5855
    • Ding, H.F.1    Bustin, M.2    Hansen, U.3
  • 28
    • 0028000720 scopus 로고
    • Stimulation of RNA polymerase II elongation by chromosomal protein HMG-14
    • Ding, H. F., S. Rimsky, S. C. Batson, M. Bustin, and U. Hansen. 1994. Stimulation of RNA polymerase II elongation by chromosomal protein HMG-14. Science 265:796-799.
    • (1994) Science , vol.265 , pp. 796-799
    • Ding, H.F.1    Rimsky, S.2    Batson, S.C.3    Bustin, M.4    Hansen, U.5
  • 29
    • 0021969964 scopus 로고
    • The intracellular distribution and function of the high mobility group chromosomal proteins
    • Einck, L., and M. Bustin. 1985. The intracellular distribution and function of the high mobility group chromosomal proteins. Exp. Cell Res. 156:295-310.
    • (1985) Exp. Cell Res. , vol.156 , pp. 295-310
    • Einck, L.1    Bustin, M.2
  • 30
    • 0028355759 scopus 로고
    • Mutational analysis of the DNA binding domain a of chromosomal protein HMG1
    • Falciola, L., A. I. Murchle, D. M. Lilley, and M. Bianchi. 1994. Mutational analysis of the DNA binding domain A of chromosomal protein HMG1. Nucleic Acids Res. 22:285-292.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 285-292
    • Falciola, L.1    Murchle, A.I.2    Lilley, D.M.3    Bianchi, M.4
  • 31
    • 0030908902 scopus 로고    scopus 로고
    • High mobility group 1 protein is not stably associated with the chromosomes of somatic cells
    • Falciola, L., F. Spada, S. Calogero, G. Langst, R. Viot, I. Grummt, and M. Bianchi. 1997. High mobility group 1 protein is not stably associated with the chromosomes of somatic cells. J. Cell Biol. 137:19-26.
    • (1997) J. Cell Biol. , vol.137 , pp. 19-26
    • Falciola, L.1    Spada, F.2    Calogero, S.3    Langst, G.4    Viot, R.5    Grummt, I.6    Bianchi, M.7
  • 32
    • 0029619641 scopus 로고
    • Reversal of intrinsic DNA bends in the IFN beta gene enhancer by transcription factors and the architectural protein HMG I(Y)
    • Falvo, J. V., D. Thanos, T. Maniatis. 1995. Reversal of intrinsic DNA bends in the IFN beta gene enhancer by transcription factors and the architectural protein HMG I(Y). Cell 83:1101-1111.
    • (1995) Cell , vol.83 , pp. 1101-1111
    • Falvo, J.V.1    Thanos, D.2    Maniatis, T.3
  • 33
    • 0031004162 scopus 로고    scopus 로고
    • HIV-1 cDNA integration: Requirement of HMG I(Y) protein for function of preintegration complexes in vitro
    • Farnet, C. M, and F. D. Bushman. 1997. HIV-1 cDNA integration: requirement of HMG I(Y) protein for function of preintegration complexes in vitro. Cell 88:483-492.
    • (1997) Cell , vol.88 , pp. 483-492
    • Farnet, C.M.1    Bushman, F.D.2
  • 35
    • 0000878535 scopus 로고
    • Solenoidal model for superstructure in chromatin
    • Finch, J. T., and A. Klug. 1976. Solenoidal model for superstructure in chromatin. Proc. Natl. Acad. Sci. USA 73:1897-1901.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 1897-1901
    • Finch, J.T.1    Klug, A.2
  • 36
    • 0032493632 scopus 로고    scopus 로고
    • Protein footprinting reveals specific binding modes of a high mobility group protein I to DNAs of different conformation
    • Frank, O., R. Schwanbeck, and J. R. Wisnlewski. 1998. Protein footprinting reveals specific binding modes of a high mobility group protein I to DNAs of different conformation. J. Biol. Chem. 273:20015-20020.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20015-20020
    • Frank, O.1    Schwanbeck, R.2    Wisnlewski, J.R.3
  • 37
    • 85038164034 scopus 로고    scopus 로고
    • Personal communication.
    • Fusco, A. Personal communication.
    • Fusco, A.1
  • 38
    • 0028303884 scopus 로고
    • The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein
    • Ge, H., and R. G. Roeder. 1994. The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein. J. Biol. Chem. 269:17136-17140.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17136-17140
    • Ge, H.1    Roeder, R.G.2
  • 39
    • 0022410391 scopus 로고
    • Changes in nuclear proteins on transformation of rat epithelial thyroid cells by a murine sarcoma retrovirus
    • Giancotti, V., M. T. Berlingieri, P. P. DiFlore, A. Fusco, G. Vecchio, and C. Crane-Robinson. 1985. Changes in nuclear proteins on transformation of rat epithelial thyroid cells by a murine sarcoma retrovirus. Cancer Res. 45:6051-6057.
    • (1985) Cancer Res. , vol.45 , pp. 6051-6057
    • Giancotti, V.1    Berlingieri, M.T.2    DiFlore, P.P.3    Fusco, A.4    Vecchio, G.5    Crane-Robinson, C.6
  • 40
    • 0023377879 scopus 로고
    • Elevated levels of a specific class of nuclear phosphoproteins in cells transformed with v-ras and v-mos oncogenes and by cotransfection with c-myc and polyoma middle T genes
    • Giancotti, V., B. Pani, P. D'Andrea, M. T. Berlingieri, F. P. Di, A. Fusco, and G. Vecchio, R. Philp, R. C. Crane, R. H. Nicolas, et al. 1987. Elevated levels of a specific class of nuclear phosphoproteins in cells transformed with v-ras and v-mos oncogenes and by cotransfection with c-myc and polyoma middle T genes. EMBO J. 6:1981-1987.
    • (1987) EMBO J. , vol.6 , pp. 1981-1987
    • Giancotti, V.1    Pani, B.2    D'Andrea, P.3    Berlingieri, M.T.4    Di, F.P.5    Fusco, A.6    Vecchio, G.7    Philp, R.8    Crane, R.C.9    Nicolas, R.H.10
  • 41
    • 0028986250 scopus 로고
    • Assembly and function of a TCR alpha enhancer complex is dependent on LEF-1-induced DNA bending and multiple protein-protein interactions
    • Giese, K., C, Kingsley, J. R. Kirshner, and R. Grosschedl. 1995. Assembly and function of a TCR alpha enhancer complex is dependent on LEF-1-induced DNA bending and multiple protein-protein interactions. Genes Dev. 9:995-1008.
    • (1995) Genes Dev. , vol.9 , pp. 995-1008
    • Giese, K.1    Kingsley, C.2    Kirshner, J.R.3    Grosschedl, R.4
  • 42
    • 0028201316 scopus 로고
    • Distinct DNA-binding properties of the high mobility group domain of murine and human SRY sex-determining factors
    • Giese, K., J. Pagel, and R. Grosschedl. 1994. Distinct DNA-binding properties of the high mobility group domain of murine and human SRY sex-determining factors. Proc. Natl. Acad. Sci. USA 91:3368-3372.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3368-3372
    • Giese, K.1    Pagel, J.2    Grosschedl, R.3
  • 43
    • 0030717552 scopus 로고    scopus 로고
    • Functional analysis of DNA bending and unwinding by the high mobility group domain of LEF-1
    • Giese, K., J. Pagel, and R. Grosschedl. 1997. Functional analysis of DNA bending and unwinding by the high mobility group domain of LEF-1. Proc. Natl. Acad. Sci. USA 94:12845-12850.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12845-12850
    • Giese, K.1    Pagel, J.2    Grosschedl, R.3
  • 44
    • 0032055120 scopus 로고    scopus 로고
    • In vivo analysis of scaffold-associated regions in drosophila: A synthetic high-affinity SAR binding protein suppresses position effect variegation
    • Girard, F., B. Bello, U. K. Laemmli, and W. J. Gehring. 1998. In vivo analysis of scaffold-associated regions in drosophila: a synthetic high-affinity SAR binding protein suppresses position effect variegation. EMBO J. 17: 2079-2085.
    • (1998) EMBO J. , vol.17 , pp. 2079-2085
    • Girard, F.1    Bello, B.2    Laemmli, U.K.3    Gehring, W.J.4
  • 45
    • 0032127306 scopus 로고    scopus 로고
    • The high mobility group protein, HMGI-C
    • Goodwin, G. 1998. The high mobility group protein, HMGI-C. Int. J. Biochem. Cell Biol. 30:761-766.
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 761-766
    • Goodwin, G.1
  • 47
    • 0028197368 scopus 로고
    • HMG domain proteins: Architectural elements in the assembly of nucleoprotein structures
    • Grosschedl, R., K. Giese, and J. Pagel. 1994. HMG domain proteins: architectural elements in the assembly of nucleoprotein structures. Trends Genet. 10:94-100.
    • (1994) Trends Genet. , vol.10 , pp. 94-100
    • Grosschedl, R.1    Giese, K.2    Pagel, J.3
  • 48
    • 0032191345 scopus 로고    scopus 로고
    • Facilitation of chromatin dynamics by SARs
    • Hart, C. M., and U. K. Laemmli. 1998. Facilitation of chromatin dynamics by SARs. Curr. Opin. Genet. Dev. 8:519-525.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 519-525
    • Hart, C.M.1    Laemmli, U.K.2
  • 49
    • 0032933141 scopus 로고    scopus 로고
    • Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes
    • Herrera, J. E., K. Sakaguchi, M. Bergel, L. Trieschmann, Y. Nakatani, and M. Bustin. 1999. Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes. Mol. Cell. Biol. 19:3466-3473.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3466-3473
    • Herrera, J.E.1    Sakaguchi, K.2    Bergel, M.3    Trieschmann, L.4    Nakatani, Y.5    Bustin, M.6
  • 50
    • 0030835937 scopus 로고    scopus 로고
    • Competition between HMG-I(Y), HMG-1 and histone H1 on four way junction DNA
    • Hill, D. A., and R. Reeves. 1997. Competition between HMG-I(Y), HMG-1 and histone H1 on four way junction DNA. Nucleic Acids Res. 25:3523-3531.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3523-3531
    • Hill, D.A.1    Reeves, R.2
  • 51
    • 0032517829 scopus 로고    scopus 로고
    • Chromosomal proteins HMG-14 and HMG-17 are released from mitotic chromosomes and imported into the nucleus by active transport
    • Hock, R., U. Scheer, and M. Bustin. 1998. Chromosomal proteins HMG-14 and HMG-17 are released from mitotic chromosomes and imported into the nucleus by active transport. J. Cell Biol. 143:1427-1436.
    • (1998) J. Cell Biol. , vol.143 , pp. 1427-1436
    • Hock, R.1    Scheer, U.2    Bustin, M.3
  • 52
    • 0032401763 scopus 로고    scopus 로고
    • Dynamic relocation of chromosomal protein HMG-17 in the nucleus is dependent on transcriptional activity
    • Hock, R., F. Wilde, U. Scheer, and M. Bustin. 1998. Dynamic relocation of chromosomal protein HMG-17 in the nucleus is dependent on transcriptional activity. EMBO J. 17:6992-7001.
    • (1998) EMBO J. , vol.17 , pp. 6992-7001
    • Hock, R.1    Wilde, F.2    Scheer, U.3    Bustin, M.4
  • 54
    • 0019160714 scopus 로고
    • High mobility group chromosomal protein isolated from nuclei and cytosol of cultured hepatoma cells are similar
    • Isackson, P., J. Bidney, G. Reeck, N. Niehart, and M. Bustin. 1980. High mobility group chromosomal protein isolated from nuclei and cytosol of cultured hepatoma cells are similar. Biochemistry 19:4466-4471.
    • (1980) Biochemistry , vol.19 , pp. 4466-4471
    • Isackson, P.1    Bidney, J.2    Reeck, G.3    Niehart, N.4    Bustin, M.5
  • 57
    • 0031903569 scopus 로고    scopus 로고
    • Involvement of Sox 1, 2, and 3 in the early and subsequent molecular events of lens induction
    • Kamachi, Y., M. Uchikawa, J. Collignon, R. Lovell-Badge, and H. Kondoh. 1998. Involvement of Sox 1, 2, and 3 in the early and subsequent molecular events of lens induction. Development 125:2521-2532.
    • (1998) Development , vol.125 , pp. 2521-2532
    • Kamachi, Y.1    Uchikawa, M.2    Collignon, J.3    Lovell-Badge, R.4    Kondoh, H.5
  • 58
    • 0032085514 scopus 로고    scopus 로고
    • Intron 3 of HMGIC is the most frequent target of chromosomal aberrations in human tumors and has been conserved basically for at least 30 million years
    • Letter
    • Kazmierczak, B., J. Bullerdiek, K. H. Pham. S. Bartnitzke, and H. Wiesner. 1998. Intron 3 of HMGIC is the most frequent target of chromosomal aberrations in human tumors and has been conserved basically for at least 30 million years. Cancer Genet. Cytogenet. 103:175-177. (Letter.)
    • (1998) Cancer Genet. Cytogenet. , vol.103 , pp. 175-177
    • Kazmierczak, B.1    Bullerdiek, J.2    Pham, K.H.3    Bartnitzke, S.4    Wiesner, H.5
  • 61
    • 0028047506 scopus 로고
    • Functional differences between the two splice variants of the nucleolar transcription factor UBF: The second HMG box determines specificity of DNA binding and transcriptional activity
    • Kuhn, A., R. Voit, V. Stefanovsky, R. Evers, M. Bianchi, and I. Grummt. 1994. Functional differences between the two splice variants of the nucleolar transcription factor UBF: the second HMG box determines specificity of DNA binding and transcriptional activity. EMBO J. 13:416-424.
    • (1994) EMBO J. , vol.13 , pp. 416-424
    • Kuhn, A.1    Voit, R.2    Stefanovsky, V.3    Evers, R.4    Bianchi, M.5    Grummt, I.6
  • 62
    • 0032239155 scopus 로고    scopus 로고
    • Accessibility of nucleosomal DNA to V(D)J cleavage is modulated by RSS positioning and HMG1
    • Kwon, J., A. N. Imbalzano, A. Matthews, and M. A. Oettinger. 1998. Accessibility of nucleosomal DNA to V(D)J cleavage is modulated by RSS positioning and HMG1. Mol. Cell 2:829-839.
    • (1998) Mol. Cell , vol.2 , pp. 829-839
    • Kwon, J.1    Imbalzano, A.N.2    Matthews, A.3    Oettinger, M.A.4
  • 63
    • 0027646025 scopus 로고
    • A signature for the HMG-1 box proteins
    • Landsman, D., and M. Bustin. 1993. A signature for the HMG-1 box proteins. Bioessays 15:539-546.
    • (1993) Bioessays , vol.15 , pp. 539-546
    • Landsman, D.1    Bustin, M.2
  • 64
    • 0022489573 scopus 로고
    • Exchange of proteins during immunofractionation of chromatin
    • Landsman, D., E. Mendelson, S. Druckmann, and M. Bustin. 1986. Exchange of proteins during immunofractionation of chromatin. Exp. Cell Res. 163:95-102.
    • (1986) Exp. Cell Res. , vol.163 , pp. 95-102
    • Landsman, D.1    Mendelson, E.2    Druckmann, S.3    Bustin, M.4
  • 65
    • 0027287821 scopus 로고
    • Ancestry and diversity of the HMG box superfamily
    • Laudet, V., D. Stehelin, and H. Clevers. 1993. Ancestry and diversity of the HMG box superfamily. Nucleic Acids Res. 21:2493-2501.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2493-2501
    • Laudet, V.1    Stehelin, D.2    Clevers, H.3
  • 66
    • 0028876893 scopus 로고
    • Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with thyroid hormone receptor
    • Lee, J. W., H. S. Choi, J. Gyuris, R. Brent, and D. D. Moore. 1995. Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with thyroid hormone receptor. Mol. Endocrinol. 9:243-254.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 243-254
    • Lee, J.W.1    Choi, H.S.2    Gyuris, J.3    Brent, R.4    Moore, D.D.5
  • 67
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin, J. A., K. R. Yamamoto. 1998. Allosteric effects of DNA on transcriptional regulators. Nature 392:885-888.
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 68
    • 0032560469 scopus 로고    scopus 로고
    • Chromatin components as part of a putative transcriptional repressing complex
    • Lehming, N., A. Le Saux, J. Schuller, and M. Ptashne. 1998. Chromatin components as part of a putative transcriptional repressing complex. Proc. Natl. Acad. Sci. USA 95:7322-7326.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7322-7326
    • Lehming, N.1    Le Saux, A.2    Schuller, J.3    Ptashne, M.4
  • 69
    • 0031936603 scopus 로고    scopus 로고
    • Modulation of activity of Moloney murine leukemia virus preintegration complexes by host factors in vitro
    • Li, L., C. M. Farnet. W. F. Anderson, and F. D. Bushman. 1998. Modulation of activity of Moloney murine leukemia virus preintegration complexes by host factors in vitro. J. Virol. 72:2125-2131.
    • (1998) J. Virol. , vol.72 , pp. 2125-2131
    • Li, L.1    Farnet, C.M.2    Anderson, W.F.3    Bushman, F.D.4
  • 70
    • 0030000761 scopus 로고    scopus 로고
    • The DNA bend angle and binding affinity of an HMG box increased by the presence of short terminal arms
    • Lnenicek-Allen, M., C. M. Read, and C. Crane-Robinson. 1996. The DNA bend angle and binding affinity of an HMG box increased by the presence of short terminal arms. Nucleic Acids Res. 24:1047-1051.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1047-1051
    • Lnenicek-Allen, M.1    Read, C.M.2    Crane-Robinson, C.3
  • 71
    • 0029131298 scopus 로고
    • Structural basis for DNA bending by the architectural transcription factor LEF-1
    • Love, J. J., X. Li, D. A. Case, K. Giese, R. Grosschedl, and P. E. Wright. 1995. Structural basis for DNA bending by the architectural transcription factor LEF-1. Nature 376:791-795.
    • (1995) Nature , vol.376 , pp. 791-795
    • Love, J.J.1    Li, X.2    Case, D.A.3    Giese, K.4    Grosschedl, R.5    Wright, P.E.6
  • 72
    • 85045828288 scopus 로고
    • The HMG family of proteins
    • Lovell-Badge, R 1995. The HMG family of proteins. Nature 376:725.
    • (1995) Nature , vol.376 , pp. 725
    • Lovell-Badge, R.1
  • 74
    • 0030011231 scopus 로고    scopus 로고
    • Multivalent DNA-binding properties of the HMG-I protein
    • Maher, J. F., and D. Nathans. 1996. Multivalent DNA-binding properties of the HMG-I protein. Proc. Natl. Acad. Sci. USA 93:6716-6720.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6716-6720
    • Maher, J.F.1    Nathans, A.D.2
  • 76
    • 0032186185 scopus 로고    scopus 로고
    • Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome
    • Munshi, N., M. Merika, J. Yie, K. Senger, G. Chen, and D. Thanos. 1998. Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome. Mol. Cell 2:457-467.
    • (1998) Mol. Cell , vol.2 , pp. 457-467
    • Munshi, N.1    Merika, M.2    Yie, J.3    Senger, K.4    Chen, G.5    Thanos, D.6
  • 77
    • 0028211484 scopus 로고
    • HMG-D, the Drosophila melanogaster homologue of HMG 1 protein, is associated with early embryonic chromatin in the absence of histone H1
    • Ner, S. S., and A. A. Travers. 1994. HMG-D, the Drosophila melanogaster homologue of HMG 1 protein, is associated with early embryonic chromatin in the absence of histone H1. EMBO J. 13:1817-1822.
    • (1994) EMBO J. , vol.13 , pp. 1817-1822
    • Ner, S.S.1    Travers, A.A.2
  • 78
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., K. A. Sharp, and B. Honig. 1991. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 79
    • 0030064348 scopus 로고    scopus 로고
    • Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin
    • Nightingale, K., S. Dimitrov, R. Reeves, and A. P. Wolffe. 1996. Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin. EMBO J. 15:548-561.
    • (1996) EMBO J. , vol.15 , pp. 548-561
    • Nightingale, K.1    Dimitrov, S.2    Reeves, R.3    Wolffe, A.P.4
  • 81
    • 0029131613 scopus 로고
    • HMG17 is a chromatin-specific transcriptional coactivator that increases the efficiency of transcription initiation
    • Paranjape, S. M., A. Krumm, and J. T. Kadonaga. 1995. HMG17 is a chromatin-specific transcriptional coactivator that increases the efficiency of transcription initiation. Genes Dev. 9:1978-1991.
    • (1995) Genes Dev. , vol.9 , pp. 1978-1991
    • Paranjape, S.M.1    Krumm, A.2    Kadonaga, J.T.3
  • 82
    • 0033556402 scopus 로고    scopus 로고
    • Induction of high mobility group-I(Y) protein by endotoxin and interleukin-1β in vascular smooth muscle cells: Role in activation of inducible nitric oxide synthetase
    • Pellacani, A., M. Chin, P. Wiesel, M. Ibanez, L. Foster, A. Patel, S. Yet, C. Hsieh, J. Paulauskis, R. Reeves, M. Lee, and M. Perrella. 1999. Induction of high mobility group-I(Y) protein by endotoxin and interleukin-1β in vascular smooth muscle cells: role in activation of inducible nitric oxide synthetase. J. Biol. Chem. 274:1525-1532.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1525-1532
    • Pellacani, A.1    Chin, M.2    Wiesel, P.3    Ibanez, M.4    Foster, L.5    Patel, A.6    Yet, S.7    Hsieh, C.8    Paulauskis, J.9    Reeves, R.10    Lee, M.11    Perrella, M.12
  • 83
    • 0041092343 scopus 로고    scopus 로고
    • HMG box proteins bind to four-way DNA junctions in their open conformation
    • Pohler, J., D. G. Norman, J. Bramham, M. E. Bianchi, and D. M. Lilley. 1998. HMG box proteins bind to four-way DNA junctions in their open conformation. EMBO J. 17:817-826.
    • (1998) EMBO J. , vol.17 , pp. 817-826
    • Pohler, J.1    Norman, D.G.2    Bramham, J.3    Bianchi, M.E.4    Lilley, D.M.5
  • 84
    • 0030709378 scopus 로고    scopus 로고
    • The interaction of HMG-box proteins with the four-way DNA junction
    • Pohler, J. R., and D. M. Lilley. 1997. The interaction of HMG-box proteins with the four-way DNA junction. Biochem. Soc. Trans. 25:S647.
    • (1997) Biochem. Soc. Trans. , vol.25
    • Pohler, J.R.1    Lilley, D.M.2
  • 86
    • 0028945006 scopus 로고
    • Evolutionary conservation in the DNA-binding and -bending properties of HMG-boxes from SRY proteins of primates
    • Pontiggia, A., S. Whitfield, P. N. Goodfellow, R. Lovell-Badge, and M. E. Bianchi. 1995. Evolutionary conservation in the DNA-binding and -bending properties of HMG-boxes from SRY proteins of primates. Gene 154:277-280.
    • (1995) Gene , vol.154 , pp. 277-280
    • Pontiggia, A.1    Whitfield, S.2    Goodfellow, P.N.3    Lovell-Badge, R.4    Bianchi, M.E.5
  • 87
    • 0031565914 scopus 로고    scopus 로고
    • Clusters of nucleosomes containing chromosomal protein HMG-17 in chromatin
    • Postnikov, Y. V., J. E. Herrera, R. Hock, U. Scheer, and M. Bustin. 1997. Clusters of nucleosomes containing chromosomal protein HMG-17 in chromatin. J. Mol. Biol. 274:454-465.
    • (1997) J. Mol. Biol. , vol.274 , pp. 454-465
    • Postnikov, Y.V.1    Herrera, J.E.2    Hock, R.3    Scheer, U.4    Bustin, M.5
  • 88
    • 0029126965 scopus 로고
    • Homodimers of chromosomal proteins HMG-14 and HMG-17 in nucleosome cores
    • Postnikov, Y. V., L. Trieschmann, A. Rickers, and M. Bustin. 1995. Homodimers of chromosomal proteins HMG-14 and HMG-17 in nucleosome cores. J. Mol. Biol. 252:423-432.
    • (1995) J. Mol. Biol. , vol.252 , pp. 423-432
    • Postnikov, Y.V.1    Trieschmann, L.2    Rickers, A.3    Bustin, M.4
  • 90
    • 0029418485 scopus 로고
    • Cell cycle regulation and functions of HMG-I(Y)
    • Reeves, R., and M. Nissen. 1995. Cell cycle regulation and functions of HMG-I(Y). Prog. Cell Cycle Res. 1:339-349.
    • (1995) Prog. Cell Cycle Res. , vol.1 , pp. 339-349
    • Reeves, R.1    Nissen, M.2
  • 91
    • 0025196283 scopus 로고
    • The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure
    • Reeves, R., and M. S. Nissen. 1990. The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure. J. Biol. Chem. 265:8573-8582.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8573-8582
    • Reeves, R.1    Nissen, M.S.2
  • 92
    • 0028289026 scopus 로고
    • Metaphase chromosome structure: Bands arise from a differential folding path of the highly AT-rich scaffold
    • Saitoh, Y., and U. Laemmli. 1994. Metaphase chromosome structure: bands arise from a differential folding path of the highly AT-rich scaffold. Cell 76:609-622.
    • (1994) Cell , vol.76 , pp. 609-622
    • Saitoh, Y.1    Laemmli, U.2
  • 93
    • 0030980386 scopus 로고    scopus 로고
    • V(D)J recombination: Modulation of RAG1 and RAG2 cleavage activity on 12/23 substrates by whole cell extract and DNA-bending proteins
    • Sawchuk, D. J., F. Weis-Garcia, S. Malik, E. Besmer, M. Bustin, M. C. Nussenzweig, and P. Cortes. 1997. V(D)J recombination: modulation of RAG1 and RAG2 cleavage activity on 12/23 substrates by whole cell extract and DNA-bending proteins. J. Exp. Med. 185:2025-2032.
    • (1997) J. Exp. Med. , vol.185 , pp. 2025-2032
    • Sawchuk, D.J.1    Weis-Garcia, F.2    Malik, S.3    Besmer, E.4    Bustin, M.5    Nussenzweig, M.C.6    Cortes, P.7
  • 94
    • 1842333246 scopus 로고    scopus 로고
    • Cdc2 and mitogen-activated protein kinases modulate DNA binding properties of the putative transcriptional regulator Chironomus high mobility group protein I
    • Schwanbeck, R., and J. R. Wisniewski. 1997. Cdc2 and mitogen-activated protein kinases modulate DNA binding properties of the putative transcriptional regulator Chironomus high mobility group protein I. J. Biol. Chem. 272:27476-27483.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27476-27483
    • Schwanbeck, R.1    Wisniewski, J.R.2
  • 95
    • 0028147923 scopus 로고
    • Architectural elements in nucleoprotein complexes: Interchangeability of specific and non-specific DNA binding proteins
    • Segall, A. C., S. D. Goodman, and H. A. Nash. 1994. Architectural elements in nucleoprotein complexes: interchangeability of specific and non-specific DNA binding proteins. EMBO J. 13:4536-4548.
    • (1994) EMBO J. , vol.13 , pp. 4536-4548
    • Segall, A.C.1    Goodman, S.D.2    Nash, H.A.3
  • 96
    • 0030922526 scopus 로고    scopus 로고
    • Nuclear accumulation of HMG2 is mediated by a basic region interspaced with a long DNA-binding sequence, and retention within the nucleus requires the acidic carboxyl terminus
    • Shirakawa, H., T. Tanigawa, S. Sugyama, M. Kobayashi, T. Terashima, K. Yoshida, T. Aral, and M. Yoshida. 1997. Nuclear accumulation of HMG2 is mediated by a basic region interspaced with a long DNA-binding sequence, and retention within the nucleus requires the acidic carboxyl terminus. Biochemistry 36:5992-5999.
    • (1997) Biochemistry , vol.36 , pp. 5992-5999
    • Shirakawa, H.1    Tanigawa, T.2    Sugyama, S.3    Kobayashi, M.4    Terashima, T.5    Yoshida, K.6    Aral, T.7    Yoshida, M.8
  • 97
    • 0032143150 scopus 로고    scopus 로고
    • High mobility group 1 (HMG1) protein in mouse preimplantation embryos
    • Spada, F., A. Brunet, Y. Mercier, M. E. Bianchi, and E. M. Thompson. 1998. High mobility group 1 (HMG1) protein in mouse preimplantation embryos. Mech. Dev. 76:57-66.
    • (1998) Mech. Dev. , vol.76 , pp. 57-66
    • Spada, F.1    Brunet, A.2    Mercier, Y.3    Bianchi, M.E.4    Thompson, E.M.5
  • 98
    • 0028365309 scopus 로고
    • Repression of basal transcription by HMG2 is counteracted by TFIIH-associated factors in an ATP-dependent process
    • Stelzer, G., A. Goppelt, F. Lottspeich, and M. Meisterernst. 1994. Repression of basal transcription by HMG2 is counteracted by TFIIH-associated factors in an ATP-dependent process. Mol. Cell. Biol. 14:4712-4721.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4712-4721
    • Stelzer, G.1    Goppelt, A.2    Lottspeich, F.3    Meisterernst, M.4
  • 99
    • 0033555550 scopus 로고    scopus 로고
    • HMG-1 interacts species-specifically with the core domain of human TBP and interferes with TFIIB within the pre-initiation complex
    • Sutrias-Grau, M., M. E. Bianchi, and J. Bernues. 1999. HMG-1 interacts species-specifically with the core domain of human TBP and interferes with TFIIB within the pre-initiation complex. J. Biol. Chem. 274:1628-1634.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1628-1634
    • Sutrias-Grau, M.1    Bianchi, M.E.2    Bernues, J.3
  • 100
    • 0028999513 scopus 로고
    • Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY
    • Teo, S. H., K. D. Grasser, and J. O. Thomas. 1995. Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY. Eur. J. Biochem. 230:943-950.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 943-950
    • Teo, S.H.1    Grasser, K.D.2    Thomas, J.O.3
  • 101
    • 0028986193 scopus 로고
    • NF-λB: A lesson in family values
    • Thanos, D., and T. Maniatis. 1995. NF-λB: a lesson in family values. Cell 80:529-532.
    • (1995) Cell , vol.80 , pp. 529-532
    • Thanos, D.1    Maniatis, T.2
  • 102
    • 0029617947 scopus 로고
    • Virus induction of IFN(beta) gene expression requires the assembly of an enhanceosome
    • Thanos, D., and T. Maniatis 1995. Virus induction of IFN(beta) gene expression requires the assembly of an enhanceosome. Cell 83:1091-1100.
    • (1995) Cell , vol.83 , pp. 1091-1100
    • Thanos, D.1    Maniatis, T.2
  • 103
    • 0028337542 scopus 로고
    • Transcriptional activation: A complex puzzle with few easy pieces
    • Tjian, R., and T. Maniatis. 1994. Transcriptional activation: a complex puzzle with few easy pieces. Cell 77:5-8.
    • (1994) Cell , vol.77 , pp. 5-8
    • Tjian, R.1    Maniatis, T.2
  • 104
    • 0030975144 scopus 로고    scopus 로고
    • Misexpression of disrupted HMGI architectural factors activates alternative pathways of tumorigenesis
    • Tkachenko, A., H. R. Ashar, A. M. Meloni, A. A. Sandberg, and K. K. Chada. 1997. Misexpression of disrupted HMGI architectural factors activates alternative pathways of tumorigenesis. Cancer Res. 57:2276-2280.
    • (1997) Cancer Res. , vol.57 , pp. 2276-2280
    • Tkachenko, A.1    Ashar, H.R.2    Meloni, A.M.3    Sandberg, A.A.4    Chada, K.K.5
  • 105
    • 17544363212 scopus 로고    scopus 로고
    • High mobility group proteins 14 and 17 can prevent the close packing of nucleosomes by increasing the strength of protein contacts in the linker DNA
    • Tremethick, D. J., and L. Hyman. 1996. High mobility group proteins 14 and 17 can prevent the close packing of nucleosomes by increasing the strength of protein contacts in the linker DNA. J. Biol. Chem. 271:12009-12016.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12009-12016
    • Tremethick, D.J.1    Hyman, A.L.2
  • 106
    • 0028958663 scopus 로고
    • Incorporation of chromosomal proteins HMG-14/-17 into nascent nucleosomes induces an extended chromatin conformation and enhances the utilization of active transcription complexes
    • Trieschmann, L., P. J. Alfonso, M. P. Crippa, A. P. Wolffe, and M. Bustin. 1995. Incorporation of chromosomal proteins HMG-14/-17 into nascent nucleosomes induces an extended chromatin conformation and enhances the utilization of active transcription complexes. EMBO J. 14:1478-1489.
    • (1995) EMBO J. , vol.14 , pp. 1478-1489
    • Trieschmann, L.1    Alfonso, P.J.2    Crippa, M.P.3    Wolffe, A.P.4    Bustin, M.5
  • 107
    • 0032510746 scopus 로고    scopus 로고
    • The chromatin unfolding domain of chromosomal protein HMG-14 targets the N-terminal tail of histone H3 in nucleosomes
    • Trieschmann, L., B. Martin, and M. Bustin. 1998. The chromatin unfolding domain of chromosomal protein HMG-14 targets the N-terminal tail of histone H3 in nucleosomes. Proc. Natl. Acad. Sci. USA 95:5468-5473.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5468-5473
    • Trieschmann, L.1    Martin, B.2    Bustin, M.3
  • 108
    • 0028791878 scopus 로고
    • Modular structure of chromosomal proteins HMG-14/-17: Definition of a transcriptional activation domain distinct from the nucleosomal binding domain
    • Trieschmann, L., Y. Postnikov, A. Rickers, and M. Bustin. 1995. Modular structure of chromosomal proteins HMG-14/-17: definition of a transcriptional activation domain distinct from the nucleosomal binding domain. Mol. Cell. Biol. 15:6663-6669.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6663-6669
    • Trieschmann, L.1    Postnikov, Y.2    Rickers, A.3    Bustin, M.4
  • 109
  • 110
    • 0030994385 scopus 로고    scopus 로고
    • Stimulation of V(D)J cleavage by high mobility group proteins
    • van Gent, D. C., K. Hiom, T. T. Paull, and M. Gellert. 1997. Stimulation of V(D)J cleavage by high mobility group proteins. EMBO J. 16:2665-2670.
    • (1997) EMBO J. , vol.16 , pp. 2665-2670
    • Van Gent, D.C.1    Hiom, K.2    Paull, T.T.3    Gellert, M.4
  • 111
    • 0030959071 scopus 로고    scopus 로고
    • High-mobility group (HMG) protein HMG-1 and TATA-binding protein-associated factor TAF(II)30 affect estrogen receptor-mediated transcriptional activation
    • Verrier, C. S., N. Roodi, C. J. Yee, L. R. Bailey, R. A. Jensen, M. Bustin, and F. F. Parl. 1997. High-mobility group (HMG) protein HMG-1 and TATA-binding protein-associated factor TAF(II)30 affect estrogen receptor-mediated transcriptional activation. Mol. Endocrinol. 11:1009-1019.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1009-1019
    • Verrier, C.S.1    Roodi, N.2    Yee, C.J.3    Bailey, L.R.4    Jensen, R.A.5    Bustin, M.6    Parl, F.F.7
  • 112
    • 0032540235 scopus 로고    scopus 로고
    • Stimulation of replication efficiency of a chromatin template by chromosomal protein HMG-17
    • Vestner, B., M. Bustin, and C. Gruss. 1998. Stimulation of replication efficiency of a chromatin template by chromosomal protein HMG-17. J. Biol. Chem. 273:9409-9414.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9409-9414
    • Vestner, B.1    Bustin, M.2    Gruss, C.3
  • 113
    • 0031790607 scopus 로고    scopus 로고
    • Location and function of linker histones
    • Vignali, M., and J. L. Workman. 1998. Location and function of linker histones. Nat. Struct. Biol. 5:1025-1028.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1025-1028
    • Vignali, M.1    Workman, J.L.2
  • 115
    • 0029075461 scopus 로고
    • Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
    • Werner, M. H., J. R. Huth, A. M. Gronenborn, and G. M. Clore. 1995. Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell 81:705-714.
    • (1995) Cell , vol.81 , pp. 705-714
    • Werner, M.H.1    Huth, J.R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 116
    • 0031059134 scopus 로고    scopus 로고
    • HMGI(Y) expression in human uterine leiomyomata. Involvement of another high-mobility group architectural factor in a benign neoplasm
    • Williams, A. J., W. L. Powell, T. Collins, and C. C. Morton. 1997. HMGI(Y) expression in human uterine leiomyomata. Involvement of another high-mobility group architectural factor in a benign neoplasm. Am. J. Pathol. 150:911-918.
    • (1997) Am. J. Pathol. , vol.150 , pp. 911-918
    • Williams, A.J.1    Powell, W.L.2    Collins, T.3    Morton, C.C.4
  • 117
    • 0028036514 scopus 로고
    • DNA binding and nuclear translocation of insect HMG-1 proteins are inhibited by phosphorylation
    • Wisniewski, J., E. Schultze, and B. Sapetto. 1994. DNA binding and nuclear translocation of insect HMG-1 proteins are inhibited by phosphorylation. Eur. J. Biochem. 225:687-693.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 687-693
    • Wisniewski, J.1    Schultze, E.2    Sapetto, B.3
  • 118
    • 0029985743 scopus 로고    scopus 로고
    • Structural and functional properties of linker histones and high mobility group proteins in polytene chromosomes
    • Wisniewski, J. R., and U. Grossbach. 1996. Structural and functional properties of linker histones and high mobility group proteins in polytene chromosomes. Int. J. Dev. Biol. 40:177-187.
    • (1996) Int. J. Dev. Biol. , vol.40 , pp. 177-187
    • Wisniewski, J.R.1    Grossbach, U.2
  • 119
    • 0031030055 scopus 로고    scopus 로고
    • Structural and functional consequences of mutations within the hydrophobic cores of the HMG1-box domain of the Chironomus high-mobility-group protein 1a
    • Wisniewski, J. R., K. Hessler, P. Claus, and K. Zechel. 1997. Structural and functional consequences of mutations within the hydrophobic cores of the HMG1-box domain of the Chironomus high-mobility-group protein 1a. Eur. J. Biochem. 243:151-159.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 151-159
    • Wisniewski, J.R.1    Hessler, K.2    Claus, P.3    Zechel, K.4
  • 121
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman, J. L., and R. E. Kingston. 1998. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem. 67:545-579.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 122
    • 0030695332 scopus 로고    scopus 로고
    • Chromatin remodeling and the control of gene expression
    • Wu, C. 1997. Chromatin remodeling and the control of gene expression. J. Biol. Chem. 272:28171-28174.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28171-28174
    • Wu, C.1
  • 124
    • 0031458832 scopus 로고    scopus 로고
    • The major chromatin protein histone H1 binds preferentially to cis-platinum-damaged DNA
    • Yaneva, J., S. H. Leuba, K. van Holde, and J. Zlatanova. 1997. The major chromatin protein histone H1 binds preferentially to cis-platinum-damaged DNA. Proc. Natl. Acad. Sci. USA 94:13448-13451.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13448-13451
    • Yaneva, J.1    Leuba, S.H.2    Van Holde, K.3    Zlatanova, J.4
  • 125
    • 0030998258 scopus 로고    scopus 로고
    • Intra- and intermolecular cooperative binding of high-mobility-group protein I(Y) to the beta-interferon promoter
    • Yie, J., S. Liang, M. Merika, and D. Thanos. 1997. Intra- and intermolecular cooperative binding of high-mobility-group protein I(Y) to the beta-interferon promoter. Mol. Cell. Biol. 17:3649-3662.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3649-3662
    • Yie, J.1    Liang, S.2    Merika, M.3    Thanos, D.4
  • 127
    • 0029811475 scopus 로고    scopus 로고
    • HMG-1 interacts with HOX proteins and enhances their DNA binding and transcription activation
    • Zappavigna, V., L. Falciola, M. H. Citterich, F. Mavillo, and M. E. Bianchi. 1996. HMG-1 interacts with HOX proteins and enhances their DNA binding and transcription activation. EMBO J. 15:4981-4988.
    • (1996) EMBO J. , vol.15 , pp. 4981-4988
    • Zappavigna, V.1    Falciola, L.2    Citterich, M.H.3    Mavillo, F.4    Bianchi, M.E.5
  • 128
    • 0027306750 scopus 로고
    • SAR-dependent mobilization of histone H1 by HMG-I/Y in vitro: HMG-I/Y is enriched in H1-depleted chromatin
    • Zhao, K., E. Kas, E. Gonzalez, and U. Laemmli. 1993. SAR-dependent mobilization of histone H1 by HMG-I/Y in vitro: HMG-I/Y is enriched in H1-depleted chromatin. EMBO J. 12:3237-3247.
    • (1993) EMBO J. , vol.12 , pp. 3237-3247
    • Zhao, K.1    Kas, E.2    Gonzalez, E.3    Laemmli, U.4
  • 129
    • 0032088139 scopus 로고    scopus 로고
    • HMGI family proteins: Architectural transcription factors in mammalian development and cancer
    • Zhou, X., and K. Chada. 1998. HMGI family proteins: architectural transcription factors in mammalian development and cancer. Keio J. Med. 47:73-77.
    • (1998) Keio J. Med. , vol.47 , pp. 73-77
    • Zhou, X.1    Chada, A.K.2
  • 130
    • 0029094755 scopus 로고
    • Mutation responsible for the mouse pygmy phenotype in the developmentally regulated factor HMGI-C
    • Zhou, X. J., K. F. Benson, H. R. Ashar, and K. Chada. 1995. Mutation responsible for the mouse pygmy phenotype in the developmentally regulated factor HMGI-C. Nature 376:771-774.
    • (1995) Nature , vol.376 , pp. 771-774
    • Zhou, X.J.1    Benson, K.F.2    Ashar, H.R.3    Chada, K.4
  • 131
    • 0032128361 scopus 로고    scopus 로고
    • Linker histones versus HMG1/2: A struggle for dominance?
    • Zlatanova, J., and K. van Holde. 1998. Linker histones versus HMG1/2: a struggle for dominance? Bioessays 20:584-588.
    • (1998) Bioessays , vol.20 , pp. 584-588
    • Zlatanova, J.1    Van Holde, K.2
  • 132
    • 0028921810 scopus 로고
    • High mobility group protein 2 functionally interacts with the POU domains of octamer transcription factors
    • Zwilling, S., H. Koenig, and T. Wirth. 1995. High mobility group protein 2 functionally interacts with the POU domains of octamer transcription factors. EMBO J. 14:1198-1208
    • (1995) EMBO J. , vol.14 , pp. 1198-1208
    • Zwilling, S.1    Koenig, H.2    Wirth, T.3


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