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Volumn 1799, Issue 1-2, 2010, Pages 28-36

HMG modifications and nuclear function

Author keywords

High mobility group protein; Mass spectrometry; Post translational modification

Indexed keywords

DNA; HIGH MOBILITY GROUP A PROTEIN; HIGH MOBILITY GROUP A1A PROTEIN; HIGH MOBILITY GROUP B1 PROTEIN; HIGH MOBILITY GROUP PROTEIN;

EID: 74549129403     PISSN: 18749399     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2009.11.009     Document Type: Review
Times cited : (63)

References (129)
  • 1
    • 0030358586 scopus 로고    scopus 로고
    • High-mobility-group chromosomal proteins: architectural components that facilitate chromatin function
    • Bustin M., and Reeves R. High-mobility-group chromosomal proteins: architectural components that facilitate chromatin function. Prog. Nucleic Acid Res. Mol. Biol. 54 (1996) 35-100
    • (1996) Prog. Nucleic Acid Res. Mol. Biol. , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 2
    • 0032814140 scopus 로고    scopus 로고
    • Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins
    • Bustin M. Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins. Mol. Cell. Biol. 19 (1999) 5237-5246
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5237-5246
    • Bustin, M.1
  • 3
    • 24344498241 scopus 로고    scopus 로고
    • HMG proteins: dynamic players in gene regulation and differentiation
    • Bianchi M.E., and Agresti A. HMG proteins: dynamic players in gene regulation and differentiation. Curr. Opin. Genet. Dev. 15 (2005) 496-506
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 496-506
    • Bianchi, M.E.1    Agresti, A.2
  • 5
    • 0035282078 scopus 로고    scopus 로고
    • Revised nomenclature for high mobility group (HMG) chromosomal proteins
    • Bustin M. Revised nomenclature for high mobility group (HMG) chromosomal proteins. Trends Biochem. Sci. 26 (2001) 152-153
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 152-153
    • Bustin, M.1
  • 6
    • 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 Nissen M.S. 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 (1990) 8573-8582
    • (1990) J. Biol. Chem. , vol.265 , pp. 8573-8582
    • Reeves, R.1    Nissen, M.S.2
  • 7
    • 0035904395 scopus 로고    scopus 로고
    • Molecular biology of HMGA proteins: hubs of nuclear function
    • Reeves R. Molecular biology of HMGA proteins: hubs of nuclear function. Gene 277 (2001) 63-81
    • (2001) Gene , vol.277 , pp. 63-81
    • Reeves, R.1
  • 8
    • 0035962921 scopus 로고    scopus 로고
    • HMGI/Y proteins: flexible regulators of transcription and chromatin structure
    • Reeves R., and Beckerbauer L. HMGI/Y proteins: flexible regulators of transcription and chromatin structure. Biochim. Biophys. Acta 1519 (2001) 13-29
    • (2001) Biochim. Biophys. Acta , vol.1519 , pp. 13-29
    • Reeves, R.1    Beckerbauer, L.2
  • 11
    • 30544446339 scopus 로고    scopus 로고
    • A new role for the oncogenic high-mobility group A2 transcription factor in myogenesis of embryonic stem cells
    • Caron L., Bost F., Prot M., Hofman P., and Binetruy B. A new role for the oncogenic high-mobility group A2 transcription factor in myogenesis of embryonic stem cells. Oncogene 24 (2005) 6281-6291
    • (2005) Oncogene , vol.24 , pp. 6281-6291
    • Caron, L.1    Bost, F.2    Prot, M.3    Hofman, P.4    Binetruy, B.5
  • 12
    • 36448992338 scopus 로고    scopus 로고
    • Roles of HMGA proteins in cancer
    • Fusco A., and Fedele M. Roles of HMGA proteins in cancer. Nat. Rev., Cancer 7 (2007) 899-910
    • (2007) Nat. Rev., Cancer , vol.7 , pp. 899-910
    • Fusco, A.1    Fedele, M.2
  • 13
    • 0034069653 scopus 로고    scopus 로고
    • In vivo modulation of HMGIC reduces obesity
    • Anand A., and Chada K. In vivo modulation of HMGIC reduces obesity. Nat. Genet. 24 (2000) 377-380
    • (2000) Nat. Genet. , vol.24 , pp. 377-380
    • Anand, A.1    Chada, K.2
  • 16
    • 0029796563 scopus 로고    scopus 로고
    • Calcium-dependent ADP-ribosylation of high-mobility-group I (HMGI) proteins
    • Giancotti V., Bandiera A., Sindici C., Perissin L., and Crane-Robinson C. Calcium-dependent ADP-ribosylation of high-mobility-group I (HMGI) proteins. Biochem. J. 317 Pt 3 (1996) 865-870
    • (1996) Biochem. J. , vol.317 , Issue.PART 3 , pp. 865-870
    • Giancotti, V.1    Bandiera, A.2    Sindici, C.3    Perissin, L.4    Crane-Robinson, C.5
  • 17
    • 0021998631 scopus 로고
    • On the phosphorylation of low molecular mass HMG (high mobility group) proteins in Ehrlich ascites cells
    • Lund T., Holtlund J., and Laland S.G. On the phosphorylation of low molecular mass HMG (high mobility group) proteins in Ehrlich ascites cells. FEBS Lett. 180 (1985) 275-279
    • (1985) FEBS Lett. , vol.180 , pp. 275-279
    • Lund, T.1    Holtlund, J.2    Laland, S.G.3
  • 18
    • 0020577114 scopus 로고
    • On the presence of two new high mobility group-like proteins in HeLa S3 cells
    • Lund T., Holtlund J., Fredriksen M., and Laland S.G. On the presence of two new high mobility group-like proteins in HeLa S3 cells. FEBS Lett. 152 (1983) 163-167
    • (1983) FEBS Lett. , vol.152 , pp. 163-167
    • Lund, T.1    Holtlund, J.2    Fredriksen, M.3    Laland, S.G.4
  • 19
    • 38849089984 scopus 로고    scopus 로고
    • The HMGA proteins: a myriad of functions
    • Cleynen I., and Van de Ven W.J. The HMGA proteins: a myriad of functions. Int. J. Oncol. 32 (2008) 289-305
    • (2008) Int. J. Oncol. , vol.32 , pp. 289-305
    • Cleynen, I.1    Van de Ven, W.J.2
  • 20
    • 0025184587 scopus 로고
    • The metaphase specific phosphorylation of HMG I
    • Lund T., and Laland S.G. The metaphase specific phosphorylation of HMG I. Biochem. Biophys. Res. Commun. 171 (1990) 342-347
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 342-347
    • Lund, T.1    Laland, S.G.2
  • 21
    • 0025724096 scopus 로고
    • Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein
    • Nissen M.S., Langan T.A., and Reeves R. Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein. J. Biol. Chem. 266 (1991) 19945-19952
    • (1991) J. Biol. Chem. , vol.266 , pp. 19945-19952
    • Nissen, M.S.1    Langan, T.A.2    Reeves, R.3
  • 22
    • 0026026024 scopus 로고
    • Phosphorylation of the DNA-binding domain of nonhistone high-mobility group I protein by cdc2 kinase: reduction of binding affinity
    • Reeves R., Langan T.A., and Nissen M.S. Phosphorylation of the DNA-binding domain of nonhistone high-mobility group I protein by cdc2 kinase: reduction of binding affinity. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 1671-1675
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 1671-1675
    • Reeves, R.1    Langan, T.A.2    Nissen, M.S.3
  • 24
    • 38049037736 scopus 로고    scopus 로고
    • Homeodomain-interacting protein kinase-2 (HIPK2) phosphorylates HMGA1a at Ser-35, Thr-52, and Thr-77 and modulates its DNA binding affinity
    • Zhang Q., and Wang Y. Homeodomain-interacting protein kinase-2 (HIPK2) phosphorylates HMGA1a at Ser-35, Thr-52, and Thr-77 and modulates its DNA binding affinity. J. Proteome Res. 6 (2007) 4711-4719
    • (2007) J. Proteome Res. , vol.6 , pp. 4711-4719
    • Zhang, Q.1    Wang, Y.2
  • 25
    • 4444254840 scopus 로고    scopus 로고
    • Dynamic interaction of HMGA1a proteins with chromatin
    • Harrer M., Luhrs H., Bustin M., Scheer U., and Hock R. Dynamic interaction of HMGA1a proteins with chromatin. J. Cell Sci. 117 (2004) 3459-3471
    • (2004) J. Cell Sci. , vol.117 , pp. 3459-3471
    • Harrer, M.1    Luhrs, H.2    Bustin, M.3    Scheer, U.4    Hock, R.5
  • 27
    • 33747057745 scopus 로고    scopus 로고
    • High mobility group A1 (HMGA1) proteins interact with p53 and inhibit its apoptotic activity
    • Pierantoni G.M., Rinaldo C., Esposito F., Mottolese M., Soddu S., and Fusco A. High mobility group A1 (HMGA1) proteins interact with p53 and inhibit its apoptotic activity. Cell Death Differ. 13 (2006) 1554-1563
    • (2006) Cell Death Differ. , vol.13 , pp. 1554-1563
    • Pierantoni, G.M.1    Rinaldo, C.2    Esposito, F.3    Mottolese, M.4    Soddu, S.5    Fusco, A.6
  • 28
    • 0024429562 scopus 로고
    • Identification of sites on chromosomal protein HMG-I phosphorylated by casein kinase II
    • Palvimo J., and Linnala-Kankkunen A. Identification of sites on chromosomal protein HMG-I phosphorylated by casein kinase II. FEBS Lett. 257 (1989) 101-104
    • (1989) FEBS Lett. , vol.257 , pp. 101-104
    • Palvimo, J.1    Linnala-Kankkunen, A.2
  • 29
    • 33745021874 scopus 로고    scopus 로고
    • Acetylation and phosphorylation of high-mobility group A1 proteins in PC-3 human tumor cells
    • Jiang X., and Wang Y. Acetylation and phosphorylation of high-mobility group A1 proteins in PC-3 human tumor cells. Biochemistry 45 (2006) 7194-7201
    • (2006) Biochemistry , vol.45 , pp. 7194-7201
    • Jiang, X.1    Wang, Y.2
  • 30
    • 0026540134 scopus 로고
    • Mass spectrometric analysis of the HMGY protein from Lewis lung carcinoma. Identification of phosphorylation sites
    • Ferranti P., Malorni A., Marino G., Pucci P., Goodwin G.H., Manfioletti G., and Giancotti V. Mass spectrometric analysis of the HMGY protein from Lewis lung carcinoma. Identification of phosphorylation sites. J. Biol. Chem. 267 (1992) 22486-22489
    • (1992) J. Biol. Chem. , vol.267 , pp. 22486-22489
    • Ferranti, P.1    Malorni, A.2    Marino, G.3    Pucci, P.4    Goodwin, G.H.5    Manfioletti, G.6    Giancotti, V.7
  • 31
    • 0029123838 scopus 로고
    • Interleukin 4-inducible phosphorylation of HMG-I(Y) is inhibited by rapamycin
    • Wang D.Z., Ray P., and Boothby M. Interleukin 4-inducible phosphorylation of HMG-I(Y) is inhibited by rapamycin. J. Biol. Chem. 270 (1995) 22924-22932
    • (1995) J. Biol. Chem. , vol.270 , pp. 22924-22932
    • Wang, D.Z.1    Ray, P.2    Boothby, M.3
  • 32
    • 0033957694 scopus 로고    scopus 로고
    • Phosphorylation of HMG-I by protein kinase C attenuates its binding affinity to the promoter regions of protein kinase C gamma and neurogranin/RC3 genes
    • Xiao D.M., Pak J.H., Wang X., Sato T., Huang F.L., Chen H.C., and Huang K.P. Phosphorylation of HMG-I by protein kinase C attenuates its binding affinity to the promoter regions of protein kinase C gamma and neurogranin/RC3 genes. J. Neurochem. 74 (2000) 392-399
    • (2000) J. Neurochem. , vol.74 , pp. 392-399
    • Xiao, D.M.1    Pak, J.H.2    Wang, X.3    Sato, T.4    Huang, F.L.5    Chen, H.C.6    Huang, K.P.7
  • 33
    • 0034682565 scopus 로고    scopus 로고
    • Differential in vivo modifications of the HMGI(Y) nonhistone chromatin proteins modulate nucleosome and DNA interactions
    • Banks G.C., Li Y., and Reeves R. Differential in vivo modifications of the HMGI(Y) nonhistone chromatin proteins modulate nucleosome and DNA interactions. Biochemistry 39 (2000) 8333-8346
    • (2000) Biochemistry , vol.39 , pp. 8333-8346
    • Banks, G.C.1    Li, Y.2    Reeves, R.3
  • 37
    • 15744362782 scopus 로고    scopus 로고
    • Dynamic and differential in vivo modifications of the isoform HMGA1a and HMGA1b chromatin proteins
    • Edberg D.D., Adkins J.N., Springer D.L., and Reeves R. Dynamic and differential in vivo modifications of the isoform HMGA1a and HMGA1b chromatin proteins. J. Biol. Chem. 280 (2005) 8961-8973
    • (2005) J. Biol. Chem. , vol.280 , pp. 8961-8973
    • Edberg, D.D.1    Adkins, J.N.2    Springer, D.L.3    Reeves, R.4
  • 38
    • 34548130666 scopus 로고    scopus 로고
    • A quantitative study on the in-vitro and in-vivo acetylation of high mobility group A1 proteins
    • Zhang Q., Zhang K., Zou Y., Perna A., and Wang Y. A quantitative study on the in-vitro and in-vivo acetylation of high mobility group A1 proteins. J. Am. Soc. Mass Spectrom. 18 (2007) 1569-1578
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1569-1578
    • Zhang, Q.1    Zhang, K.2    Zou, Y.3    Perna, A.4    Wang, Y.5
  • 39
  • 40
    • 0032186185 scopus 로고    scopus 로고
    • Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome
    • Munshi N., Merika M., Yie J., Senger K., Chen G., and Thanos D. Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome. Mol. Cell 2 (1998) 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
  • 41
    • 4444277135 scopus 로고    scopus 로고
    • In vivo posttranslational modifications of the high mobility group A1a proteins in breast cancer cells of differing metastatic potential
    • Edberg D.D., Bruce J.E., Siems W.F., and Reeves R. In vivo posttranslational modifications of the high mobility group A1a proteins in breast cancer cells of differing metastatic potential. Biochemistry 43 (2004) 11500-11515
    • (2004) Biochemistry , vol.43 , pp. 11500-11515
    • Edberg, D.D.1    Bruce, J.E.2    Siems, W.F.3    Reeves, R.4
  • 42
    • 0037621427 scopus 로고    scopus 로고
    • Increase of HMGA1a protein methylation is a distinctive characteristic of leukaemic cells induced to undergo apoptosis
    • Sgarra R., Diana F., Rustighi A., Manfioletti G., and Giancotti V. Increase of HMGA1a protein methylation is a distinctive characteristic of leukaemic cells induced to undergo apoptosis. Cell Death Differ. 10 (2003) 386-389
    • (2003) Cell Death Differ. , vol.10 , pp. 386-389
    • Sgarra, R.1    Diana, F.2    Rustighi, A.3    Manfioletti, G.4    Giancotti, V.5
  • 43
    • 0037378828 scopus 로고    scopus 로고
    • During apoptosis of tumor cells HMGA1a protein undergoes methylation: identification of the modification site by mass spectrometry
    • Sgarra R., Diana F., Bellarosa C., Dekleva V., Rustighi A., Toller M., Manfioletti G., and Giancotti V. During apoptosis of tumor cells HMGA1a protein undergoes methylation: identification of the modification site by mass spectrometry. Biochemistry 42 (2003) 3575-3585
    • (2003) Biochemistry , vol.42 , pp. 3575-3585
    • Sgarra, R.1    Diana, F.2    Bellarosa, C.3    Dekleva, V.4    Rustighi, A.5    Toller, M.6    Manfioletti, G.7    Giancotti, V.8
  • 44
    • 17644367507 scopus 로고    scopus 로고
    • Tandem mass spectrometry for the examination of the posttranslational modifications of high-mobility group A1 proteins: symmetric and asymmetric dimethylation of Arg25 in HMGA1a protein
    • Zou Y., and Wang Y. Tandem mass spectrometry for the examination of the posttranslational modifications of high-mobility group A1 proteins: symmetric and asymmetric dimethylation of Arg25 in HMGA1a protein. Biochemistry 44 (2005) 6293-6301
    • (2005) Biochemistry , vol.44 , pp. 6293-6301
    • Zou, Y.1    Wang, Y.2
  • 45
    • 0035854372 scopus 로고    scopus 로고
    • State of the arg: protein methylation at arginine comes of age
    • McBride A.E., and Silver P.A. State of the arg: protein methylation at arginine comes of age. Cell 106 (2001) 5-8
    • (2001) Cell , vol.106 , pp. 5-8
    • McBride, A.E.1    Silver, P.A.2
  • 46
    • 25144459091 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a
    • Miranda T.B., Webb K.J., Edberg D.D., Reeves R., and Clarke S. Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a. Biochem. Biophys. Res. Commun. 336 (2005) 831-835
    • (2005) Biochem. Biophys. Res. Commun. , vol.336 , pp. 831-835
    • Miranda, T.B.1    Webb, K.J.2    Edberg, D.D.3    Reeves, R.4    Clarke, S.5
  • 47
    • 33645238282 scopus 로고    scopus 로고
    • The AT-hook of the chromatin architectural transcription factor high mobility group A1a is arginine-methylated by protein arginine methyltransferase 6
    • Sgarra R., Lee J., Tessari M.A., Altamura S., Spolaore B., Giancotti V., Bedford M.T., and Manfioletti G. The AT-hook of the chromatin architectural transcription factor high mobility group A1a is arginine-methylated by protein arginine methyltransferase 6. J. Biol. Chem. 281 (2006) 3764-3772
    • (2006) J. Biol. Chem. , vol.281 , pp. 3764-3772
    • Sgarra, R.1    Lee, J.2    Tessari, M.A.3    Altamura, S.4    Spolaore, B.5    Giancotti, V.6    Bedford, M.T.7    Manfioletti, G.8
  • 48
    • 34250851755 scopus 로고    scopus 로고
    • Mass spectrometric analysis of high-mobility group proteins and their post-translational modifications in normal and cancerous human breast tissues
    • Zou Y., and Wang Y. Mass spectrometric analysis of high-mobility group proteins and their post-translational modifications in normal and cancerous human breast tissues. J. Proteome Res. 6 (2007) 2304-2314
    • (2007) J. Proteome Res. , vol.6 , pp. 2304-2314
    • Zou, Y.1    Wang, Y.2
  • 49
    • 34347355449 scopus 로고    scopus 로고
    • A mass spectrometric study on the in vitro methylation of HMGA1a and HMGA1b proteins by PRMTs: methylation specificity, the effect of binding to AT-rich duplex DNA, and the effect of C-terminal phosphorylation
    • Zou Y., Webb K., Perna A.D., Zhang Q., Clarke S., and Wang Y. A mass spectrometric study on the in vitro methylation of HMGA1a and HMGA1b proteins by PRMTs: methylation specificity, the effect of binding to AT-rich duplex DNA, and the effect of C-terminal phosphorylation. Biochemistry 46 (2007) 7896-7906
    • (2007) Biochemistry , vol.46 , pp. 7896-7906
    • Zou, Y.1    Webb, K.2    Perna, A.D.3    Zhang, Q.4    Clarke, S.5    Wang, Y.6
  • 52
    • 0029094755 scopus 로고
    • Mutation responsible for the mouse pygmy phenotype in the developmentally regulated factor HMGI-C
    • Zhou X., Benson K.F., Ashar H.R., and Chada K. Mutation responsible for the mouse pygmy phenotype in the developmentally regulated factor HMGI-C. Nature 376 (1995) 771-774
    • (1995) Nature , vol.376 , pp. 771-774
    • Zhou, X.1    Benson, K.F.2    Ashar, H.R.3    Chada, K.4
  • 54
    • 33747888858 scopus 로고    scopus 로고
    • Misexpression of full-length HMGA2 induces benign mesenchymal tumors in mice
    • Zaidi M.R., Okada Y., and Chada K.K. Misexpression of full-length HMGA2 induces benign mesenchymal tumors in mice. Cancer Res. 66 (2006) 7453-7459
    • (2006) Cancer Res. , vol.66 , pp. 7453-7459
    • Zaidi, M.R.1    Okada, Y.2    Chada, K.K.3
  • 57
    • 0034695478 scopus 로고    scopus 로고
    • Architecture of high mobility group protein I-C.DNA complex and its perturbation upon phosphorylation by Cdc2 kinase
    • Schwanbeck R., Manfioletti G., and Wisniewski J.R. Architecture of high mobility group protein I-C.DNA complex and its perturbation upon phosphorylation by Cdc2 kinase. J. Biol. Chem. 275 (2000) 1793-1801
    • (2000) J. Biol. Chem. , vol.275 , pp. 1793-1801
    • Schwanbeck, R.1    Manfioletti, G.2    Wisniewski, J.R.3
  • 58
    • 0032127306 scopus 로고    scopus 로고
    • The high mobility group protein, HMGI-C, Int
    • Goodwin G. The high mobility group protein, HMGI-C, Int. J. Biochem. Cell Biol. 30 (1998) 761-766
    • (1998) J. Biochem. Cell Biol. , vol.30 , pp. 761-766
    • Goodwin, G.1
  • 59
    • 1542283801 scopus 로고    scopus 로고
    • Phosphorylation of high-mobility group protein A2 by Nek2 kinase during the first meiotic division in mouse spermatocytes
    • Di Agostino S., Fedele M., Chieffi P., Fusco A., Rossi P., Geremia R., and Sette C. Phosphorylation of high-mobility group protein A2 by Nek2 kinase during the first meiotic division in mouse spermatocytes. Mol. Biol. Cell 15 (2004) 1224-1232
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1224-1232
    • Di Agostino, S.1    Fedele, M.2    Chieffi, P.3    Fusco, A.4    Rossi, P.5    Geremia, R.6    Sette, C.7
  • 60
    • 67049117516 scopus 로고    scopus 로고
    • Macroscopic differences in HMGA oncoproteins post-translational modifications: C-terminal phosphorylation of HMGA2 affects its DNA binding properties
    • Sgarra R., Maurizio E., Zammitti S., Lo Sardo A., Giancotti V., and Manfioletti G. Macroscopic differences in HMGA oncoproteins post-translational modifications: C-terminal phosphorylation of HMGA2 affects its DNA binding properties. J. Proteome Res. 8 (2009) 2978-2989
    • (2009) J. Proteome Res. , vol.8 , pp. 2978-2989
    • Sgarra, R.1    Maurizio, E.2    Zammitti, S.3    Lo Sardo, A.4    Giancotti, V.5    Manfioletti, G.6
  • 61
    • 42249109186 scopus 로고    scopus 로고
    • SUMOylation of HMGA2: selective destabilization of promyelocytic leukemia protein via proteasome
    • Cao X., Clavijo C., Li X., Lin H.H., Chen Y., Shih H.M., and Ann D.K. SUMOylation of HMGA2: selective destabilization of promyelocytic leukemia protein via proteasome. Mol. Cancer Ther. 7 (2008) 923-934
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 923-934
    • Cao, X.1    Clavijo, C.2    Li, X.3    Lin, H.H.4    Chen, Y.5    Shih, H.M.6    Ann, D.K.7
  • 62
    • 0035281548 scopus 로고    scopus 로고
    • HMG1 and 2, and related 'architectural' DNA-binding proteins
    • Thomas J.O., and Travers A.A. HMG1 and 2, and related 'architectural' DNA-binding proteins. Trends Biochem. Sci. 26 (2001) 167-174
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 167-174
    • Thomas, J.O.1    Travers, A.A.2
  • 64
    • 0033052037 scopus 로고    scopus 로고
    • The lack of chromosomal protein HMG1 does not disrupt cell growth but causes lethal hypoglycaemia in newborn mice
    • Calogero S., Grassi F., Aguzzi A., Voigtlander T., Ferrier P., Ferrari S., and Bianchi M.E. The lack of chromosomal protein HMG1 does not disrupt cell growth but causes lethal hypoglycaemia in newborn mice. Nat. Genet. 22 (1999) 276-280
    • (1999) Nat. Genet. , vol.22 , pp. 276-280
    • Calogero, S.1    Grassi, F.2    Aguzzi, A.3    Voigtlander, T.4    Ferrier, P.5    Ferrari, S.6    Bianchi, M.E.7
  • 65
    • 4243824006 scopus 로고    scopus 로고
    • The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding
    • Bonaldi T., Langst G., Strohner R., Becker P.B., and Bianchi M.E. The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding. EMBO J. 21 (2002) 6865-6873
    • (2002) EMBO J. , vol.21 , pp. 6865-6873
    • Bonaldi, T.1    Langst, G.2    Strohner, R.3    Becker, P.B.4    Bianchi, M.E.5
  • 66
    • 0037295617 scopus 로고    scopus 로고
    • Priming the nucleosome: a role for HMGB proteins?
    • Travers A.A. Priming the nucleosome: a role for HMGB proteins?. EMBO Rep. 4 (2003) 131-136
    • (2003) EMBO Rep. , vol.4 , pp. 131-136
    • Travers, A.A.1
  • 68
    • 0037062934 scopus 로고    scopus 로고
    • Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
    • Scaffidi P., Misteli T., and Bianchi M.E. Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature 418 (2002) 191-195
    • (2002) Nature , vol.418 , pp. 191-195
    • Scaffidi, P.1    Misteli, T.2    Bianchi, M.E.3
  • 69
    • 0035882102 scopus 로고    scopus 로고
    • New EMBO members' review: the double life of HMGB1 chromatin protein: architectural factor and extracellular signal
    • Muller S., Scaffidi P., Degryse B., Bonaldi T., Ronfani L., Agresti A., Beltrame M., and Bianchi M.E. New EMBO members' review: the double life of HMGB1 chromatin protein: architectural factor and extracellular signal. EMBO J. 20 (2001) 4337-4340
    • (2001) EMBO J. , vol.20 , pp. 4337-4340
    • Muller, S.1    Scaffidi, P.2    Degryse, B.3    Bonaldi, T.4    Ronfani, L.5    Agresti, A.6    Beltrame, M.7    Bianchi, M.E.8
  • 70
    • 50549094596 scopus 로고    scopus 로고
    • HMGB1: a two-headed signal regulating tumor progression and immunity
    • Campana L., Bosurgi L., and Rovere-Querini P. HMGB1: a two-headed signal regulating tumor progression and immunity. Curr. Opin. Immunol. 20 (2008) 518-523
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 518-523
    • Campana, L.1    Bosurgi, L.2    Rovere-Querini, P.3
  • 72
    • 49249127841 scopus 로고    scopus 로고
    • Molecular interactions between dying tumor cells and the innate immune system determine the efficacy of conventional anticancer therapies
    • Apetoh L., Tesniere A., Ghiringhelli F., Kroemer G., and Zitvogel L. Molecular interactions between dying tumor cells and the innate immune system determine the efficacy of conventional anticancer therapies. Cancer Res. 68 (2008) 4026-4030
    • (2008) Cancer Res. , vol.68 , pp. 4026-4030
    • Apetoh, L.1    Tesniere, A.2    Ghiringhelli, F.3    Kroemer, G.4    Zitvogel, L.5
  • 73
    • 0018801554 scopus 로고
    • Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1
    • Sterner R., Vidali G., and Allfrey V.G. Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1. J. Biol. Chem. 254 (1979) 11577-11583
    • (1979) J. Biol. Chem. , vol.254 , pp. 11577-11583
    • Sterner, R.1    Vidali, G.2    Allfrey, V.G.3
  • 74
    • 0035807789 scopus 로고    scopus 로고
    • In vivo acetylation of HMG1 protein enhances its binding affinity to distorted DNA structures
    • Ugrinova I., Pasheva E.A., Armengaud J., and Pashev I.G. In vivo acetylation of HMG1 protein enhances its binding affinity to distorted DNA structures. Biochemistry 40 (2001) 14655-14660
    • (2001) Biochemistry , vol.40 , pp. 14655-14660
    • Ugrinova, I.1    Pasheva, E.A.2    Armengaud, J.3    Pashev, I.G.4
  • 75
    • 42449148710 scopus 로고    scopus 로고
    • A critical role in structure-specific DNA binding for the acetylatable lysine residues in HMGB1
    • Assenberg R., Webb M., Connolly E., Stott K., Watson M., Hobbs J., and Thomas J.O. A critical role in structure-specific DNA binding for the acetylatable lysine residues in HMGB1. Biochem. J. 411 (2008) 553-561
    • (2008) Biochem. J. , vol.411 , pp. 553-561
    • Assenberg, R.1    Webb, M.2    Connolly, E.3    Stott, K.4    Watson, M.5    Hobbs, J.6    Thomas, J.O.7
  • 76
    • 67651123159 scopus 로고    scopus 로고
    • Post-synthetic acetylation of HMGB1 protein modulates its interactions with supercoiled DNA
    • Ugrinova I., Pashev I.G., and Pasheva E.A. Post-synthetic acetylation of HMGB1 protein modulates its interactions with supercoiled DNA. Mol. Biol. Rep. 36 (2009) 1399-1404
    • (2009) Mol. Biol. Rep. , vol.36 , pp. 1399-1404
    • Ugrinova, I.1    Pashev, I.G.2    Pasheva, E.A.3
  • 77
    • 43049124103 scopus 로고    scopus 로고
    • HMGB1 protein inhibits DNA replication in vitro: a role of the acetylation and the acidic tail
    • Topalova D., Ugrinova I., Pashev I.G., and Pasheva E.A. HMGB1 protein inhibits DNA replication in vitro: a role of the acetylation and the acidic tail. Int. J. Biochem. Cell Biol. 40 (2008) 1536-1542
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1536-1542
    • Topalova, D.1    Ugrinova, I.2    Pashev, I.G.3    Pasheva, E.A.4
  • 79
    • 0021690153 scopus 로고
    • Phosphorylation of high-mobility-group proteins by the calcium-phospholipid-dependent protein kinase and the cyclic AMP-dependent protein kinase
    • Ramachandran C., Yau P., Bradbury E.M., Shyamala G., Yasuda H., and Walsh D.A. Phosphorylation of high-mobility-group proteins by the calcium-phospholipid-dependent protein kinase and the cyclic AMP-dependent protein kinase. J. Biol. Chem. 259 (1984) 13495-13503
    • (1984) J. Biol. Chem. , vol.259 , pp. 13495-13503
    • Ramachandran, C.1    Yau, P.2    Bradbury, E.M.3    Shyamala, G.4    Yasuda, H.5    Walsh, D.A.6
  • 80
    • 33751584837 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of HMGB1 is regulated by phosphorylation that redirects it toward secretion
    • Youn J.H., and Shin J.S. Nucleocytoplasmic shuttling of HMGB1 is regulated by phosphorylation that redirects it toward secretion. J. Immunol. 177 (2006) 7889-7897
    • (2006) J. Immunol. , vol.177 , pp. 7889-7897
    • Youn, J.H.1    Shin, J.S.2
  • 81
    • 33646371497 scopus 로고    scopus 로고
    • HMGB-1 as a therapeutic target for infectious and inflammatory disorders
    • Mantell L.L., Parrish W.R., and Ulloa L. HMGB-1 as a therapeutic target for infectious and inflammatory disorders. Shock 25 (2006) 4-11
    • (2006) Shock , vol.25 , pp. 4-11
    • Mantell, L.L.1    Parrish, W.R.2    Ulloa, L.3
  • 83
    • 66949144402 scopus 로고    scopus 로고
    • HMGB1 is phosphorylated by classical protein kinase C and is secreted by a calcium-dependent mechanism
    • Oh Y.J., Youn J.H., Ji Y., Lee S.E., Lim K.J., Choi J.E., and Shin J.S. HMGB1 is phosphorylated by classical protein kinase C and is secreted by a calcium-dependent mechanism. J. Immunol. 182 (2009) 5800-5809
    • (2009) J. Immunol. , vol.182 , pp. 5800-5809
    • Oh, Y.J.1    Youn, J.H.2    Ji, Y.3    Lee, S.E.4    Lim, K.J.5    Choi, J.E.6    Shin, J.S.7
  • 84
    • 58149308833 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase (CaMK) IV mediates nucleocytoplasmic shuttling and release of HMGB1 during lipopolysaccharide stimulation of macrophages
    • Zhang X., Wheeler D., Tang Y., Guo L., Shapiro R.A., Ribar T.J., Means A.R., Billiar T.R., Angus D.C., and Rosengart M.R. Calcium/calmodulin-dependent protein kinase (CaMK) IV mediates nucleocytoplasmic shuttling and release of HMGB1 during lipopolysaccharide stimulation of macrophages. J. Immunol. 181 (2008) 5015-5023
    • (2008) J. Immunol. , vol.181 , pp. 5015-5023
    • Zhang, X.1    Wheeler, D.2    Tang, Y.3    Guo, L.4    Shapiro, R.A.5    Ribar, T.J.6    Means, A.R.7    Billiar, T.R.8    Angus, D.C.9    Rosengart, M.R.10
  • 85
    • 34447523457 scopus 로고    scopus 로고
    • Post-translational methylation of high mobility group box 1 (HMGB1) causes its cytoplasmic localization in neutrophils
    • Ito I., Fukazawa J., and Yoshida M. Post-translational methylation of high mobility group box 1 (HMGB1) causes its cytoplasmic localization in neutrophils. J. Biol. Chem. 282 (2007) 16336-16344
    • (2007) J. Biol. Chem. , vol.282 , pp. 16336-16344
    • Ito, I.1    Fukazawa, J.2    Yoshida, M.3
  • 86
    • 0025323711 scopus 로고
    • Structural features of the HMG chromosomal proteins and their genes
    • Bustin M., Lehn D.A., and Landsman D. Structural features of the HMG chromosomal proteins and their genes. Biochim. Biophys. Acta 1049 (1990) 231-243
    • (1990) Biochim. Biophys. Acta , vol.1049 , pp. 231-243
    • Bustin, M.1    Lehn, D.A.2    Landsman, D.3
  • 87
    • 0019322514 scopus 로고
    • The interaction of high mobility proteins HMG14 and 17 with nucleosomes
    • Sandeen G., Wood W.I., and Felsenfeld G. The interaction of high mobility proteins HMG14 and 17 with nucleosomes. Nucleic Acids Res. 8 (1980) 3757-3778
    • (1980) Nucleic Acids Res. , vol.8 , pp. 3757-3778
    • Sandeen, G.1    Wood, W.I.2    Felsenfeld, G.3
  • 88
    • 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., Scheer U., and Bustin M. Chromosomal proteins HMG-14 and HMG-17 are released from mitotic chromosomes and imported into the nucleus by active transport. J. Cell Biol. 143 (1998) 1427-1436
    • (1998) J. Cell Biol. , vol.143 , pp. 1427-1436
    • Hock, R.1    Scheer, U.2    Bustin, M.3
  • 89
    • 0028791878 scopus 로고
    • Modular structure of chromosomal proteins HMG-14 and HMG-17: definition of a transcriptional enhancement domain distinct from the nucleosomal binding domain
    • Trieschmann L., Postnikov Y.V., Rickers A., and Bustin M. Modular structure of chromosomal proteins HMG-14 and HMG-17: definition of a transcriptional enhancement domain distinct from the nucleosomal binding domain. Mol. Cell. Biol. 15 (1995) 6663-6669
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6663-6669
    • Trieschmann, L.1    Postnikov, Y.V.2    Rickers, A.3    Bustin, M.4
  • 90
    • 0030610561 scopus 로고    scopus 로고
    • Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region in chromosomal protein HMG-14
    • Ding H.F., Bustin M., and Hansen U. Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region in chromosomal protein HMG-14. Mol. Cell. Biol. 17 (1997) 5843-5855
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5843-5855
    • Ding, H.F.1    Bustin, M.2    Hansen, U.3
  • 91
    • 0026676799 scopus 로고
    • Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain
    • Crippa M.P., Alfonso P.J., and Bustin M. Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain. J. Mol. Biol. 228 (1992) 442-449
    • (1992) J. Mol. Biol. , vol.228 , pp. 442-449
    • Crippa, M.P.1    Alfonso, P.J.2    Bustin, M.3
  • 92
    • 0035399963 scopus 로고    scopus 로고
    • Chromatin unfolding and activation by HMGN(*) chromosomal proteins
    • Bustin M. Chromatin unfolding and activation by HMGN(*) chromosomal proteins. Trends Biochem. Sci. 26 (2001) 431-437
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 431-437
    • Bustin, M.1
  • 93
    • 0032401763 scopus 로고    scopus 로고
    • Dynamic relocation of chromosomal protein HMG-17 in the nucleus is dependent on transcriptional activity
    • Hock R., Wilde F., Scheer U., and Bustin M. Dynamic relocation of chromosomal protein HMG-17 in the nucleus is dependent on transcriptional activity. EMBO J. 17 (1998) 6992-7001
    • (1998) EMBO J. , vol.17 , pp. 6992-7001
    • Hock, R.1    Wilde, F.2    Scheer, U.3    Bustin, M.4
  • 94
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair R.D., and Misteli T. High mobility of proteins in the mammalian cell nucleus. Nature 404 (2000) 604-609
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 95
    • 66449110070 scopus 로고    scopus 로고
    • HMGN proteins act in opposition to ATP-dependent chromatin remodeling factors to restrict nucleosome mobility
    • Rattner B.P., Yusufzai T., and Kadonaga J.T. HMGN proteins act in opposition to ATP-dependent chromatin remodeling factors to restrict nucleosome mobility. Mol. Cell 34 (2009) 620-626
    • (2009) Mol. Cell , vol.34 , pp. 620-626
    • Rattner, B.P.1    Yusufzai, T.2    Kadonaga, J.T.3
  • 96
    • 0019789162 scopus 로고
    • Differential phosphorylation of nuclear nonhistone high mobility group proteins HMG 14 and HMG 17 during the cell cycle
    • Bhorjee J.S. Differential phosphorylation of nuclear nonhistone high mobility group proteins HMG 14 and HMG 17 during the cell cycle. Proc. Natl. Acad. Sci. U. S. A. 78 (1981) 6944-6948
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 6944-6948
    • Bhorjee, J.S.1
  • 97
    • 0025803095 scopus 로고
    • Cyclic adenosine 3′,5′-monophosphate-dependent phosphorylation of HMG 14 inhibits its interactions with nucleosomes
    • Spaulding S.W., Fucile N.W., Bofinger D.P., and Sheflin L.G. Cyclic adenosine 3′,5′-monophosphate-dependent phosphorylation of HMG 14 inhibits its interactions with nucleosomes. Mol. Endocrinol. 5 (1991) 42-50
    • (1991) Mol. Endocrinol. , vol.5 , pp. 42-50
    • Spaulding, S.W.1    Fucile, N.W.2    Bofinger, D.P.3    Sheflin, L.G.4
  • 98
    • 0024299063 scopus 로고
    • Binding of high-mobility-group proteins HMG 14 and HMG 17 to DNA and histone H1 as influenced by phosphorylation
    • Palvimo J., and Maenpaa P.H. Binding of high-mobility-group proteins HMG 14 and HMG 17 to DNA and histone H1 as influenced by phosphorylation. Biochim. Biophys. Acta 952 (1988) 172-180
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 172-180
    • Palvimo, J.1    Maenpaa, P.H.2
  • 99
    • 0022396565 scopus 로고
    • Phosphorylation alters the affinity of high mobility group protein HMG 14 for single-stranded DNA
    • Palvimo J., Linnala-Kankkunen A., and Maenpaa P.H. Phosphorylation alters the affinity of high mobility group protein HMG 14 for single-stranded DNA. Biochem. Biophys. Res. Commun. 133 (1985) 343-346
    • (1985) Biochem. Biophys. Res. Commun. , vol.133 , pp. 343-346
    • Palvimo, J.1    Linnala-Kankkunen, A.2    Maenpaa, P.H.3
  • 100
    • 0025784824 scopus 로고
    • Metaphase-specific phosphorylations weaken the association between chromosomal proteins HMG 14 and 17, and DNA
    • Lund T., and Berg K. Metaphase-specific phosphorylations weaken the association between chromosomal proteins HMG 14 and 17, and DNA. FEBS Lett. 289 (1991) 113-116
    • (1991) FEBS Lett. , vol.289 , pp. 113-116
    • Lund, T.1    Berg, K.2
  • 101
    • 0033979602 scopus 로고    scopus 로고
    • Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry
    • Louie D.F., Gloor K.K., Galasinski S.C., Resing K.A., and Ahn N.G. Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry. Protein Sci. 9 (2000) 170-179
    • (2000) Protein Sci. , vol.9 , pp. 170-179
    • Louie, D.F.1    Gloor, K.K.2    Galasinski, S.C.3    Resing, K.A.4    Ahn, N.G.5
  • 102
    • 0020490531 scopus 로고
    • The phosphorylation of high mobility group proteins 14 and 17 and their distribution in chromatin
    • Saffer J.D., and Glazer R.I. The phosphorylation of high mobility group proteins 14 and 17 and their distribution in chromatin. J. Biol. Chem. 257 (1982) 4655-4660
    • (1982) J. Biol. Chem. , vol.257 , pp. 4655-4660
    • Saffer, J.D.1    Glazer, R.I.2
  • 103
    • 0023650335 scopus 로고
    • Phosphorylation of high-mobility-group chromatin proteins by protein kinase C from rat brain
    • Palvimo J., Mahonen A., and Maenpaa P.H. Phosphorylation of high-mobility-group chromatin proteins by protein kinase C from rat brain. Biochim. Biophys. Acta 931 (1987) 376-383
    • (1987) Biochim. Biophys. Acta , vol.931 , pp. 376-383
    • Palvimo, J.1    Mahonen, A.2    Maenpaa, P.H.3
  • 104
    • 0020490525 scopus 로고
    • Phosphorylation of high mobility group 14 protein by cyclic nucleotide-dependent protein kinases
    • Walton G.M., Spiess J., and Gill G.N. Phosphorylation of high mobility group 14 protein by cyclic nucleotide-dependent protein kinases. J. Biol. Chem. 257 (1982) 4661-4668
    • (1982) J. Biol. Chem. , vol.257 , pp. 4661-4668
    • Walton, G.M.1    Spiess, J.2    Gill, G.N.3
  • 105
    • 0020694122 scopus 로고
    • Differential phosphorylation of high mobility group protein hmg 14 from calf thymus and avian erythrocytes by a cyclic gmp-dependent protein kinase
    • Palvimo J., Linnala-Kankkunen A., and Maenpaa P.H. Differential phosphorylation of high mobility group protein hmg 14 from calf thymus and avian erythrocytes by a cyclic gmp-dependent protein kinase. Biochem. Biophys. Res. Commun. 110 (1983) 378-382
    • (1983) Biochem. Biophys. Res. Commun. , vol.110 , pp. 378-382
    • Palvimo, J.1    Linnala-Kankkunen, A.2    Maenpaa, P.H.3
  • 106
    • 0021816430 scopus 로고
    • Phosphorylation of high mobility group protein 14 by casein kinase II
    • Walton G.M., Spiess J., and Gill G.N. Phosphorylation of high mobility group protein 14 by casein kinase II. J. Biol. Chem. 260 (1985) 4745-4750
    • (1985) J. Biol. Chem. , vol.260 , pp. 4745-4750
    • Walton, G.M.1    Spiess, J.2    Gill, G.N.3
  • 108
    • 0033200205 scopus 로고    scopus 로고
    • The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase
    • Thomson S., Clayton A.L., Hazzalin C.A., Rose S., Barratt M.J., and Mahadevan L.C. The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase. EMBO J. 18 (1999) 4779-4793
    • (1999) EMBO J. , vol.18 , pp. 4779-4793
    • Thomson, S.1    Clayton, A.L.2    Hazzalin, C.A.3    Rose, S.4    Barratt, M.J.5    Mahadevan, L.C.6
  • 109
    • 0036668636 scopus 로고    scopus 로고
    • Competition between histone H1 and HMGN proteins for chromatin binding sites
    • Catez F., Brown D.T., Misteli T., and Bustin M. Competition between histone H1 and HMGN proteins for chromatin binding sites. EMBO Rep. 3 (2002) 760-766
    • (2002) EMBO Rep. , vol.3 , pp. 760-766
    • Catez, F.1    Brown, D.T.2    Misteli, T.3    Bustin, M.4
  • 110
    • 2942596544 scopus 로고    scopus 로고
    • Network of dynamic interactions between histone H1 and high-mobility-group proteins in chromatin
    • Catez F., Yang H., Tracey K.J., Reeves R., Misteli T., and Bustin M. Network of dynamic interactions between histone H1 and high-mobility-group proteins in chromatin. Mol. Cell. Biol. 24 (2004) 4321-4328
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4321-4328
    • Catez, F.1    Yang, H.2    Tracey, K.J.3    Reeves, R.4    Misteli, T.5    Bustin, M.6
  • 113
    • 0036785555 scopus 로고    scopus 로고
    • Mitotic phosphorylation of chromosomal protein HMGN1 inhibits nuclear import and promotes interaction with 14.3.3 proteins
    • Prymakowska-Bosak M., Hock R., Catez F., Lim J.H., Birger Y., Shirakawa H., Lee K., and Bustin M. Mitotic phosphorylation of chromosomal protein HMGN1 inhibits nuclear import and promotes interaction with 14.3.3 proteins. Mol. Cell. Biol. 22 (2002) 6809-6819
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6809-6819
    • Prymakowska-Bosak, M.1    Hock, R.2    Catez, F.3    Lim, J.H.4    Birger, Y.5    Shirakawa, H.6    Lee, K.7    Bustin, M.8
  • 114
    • 2442686765 scopus 로고    scopus 로고
    • Identification of novel in vivo phosphorylation sites in high mobility group N1 protein from the MCF-7 human breast cancer cells
    • Zou Y., Jiang X., and Wang Y. Identification of novel in vivo phosphorylation sites in high mobility group N1 protein from the MCF-7 human breast cancer cells. Biochemistry 43 (2004) 6322-6329
    • (2004) Biochemistry , vol.43 , pp. 6322-6329
    • Zou, Y.1    Jiang, X.2    Wang, Y.3
  • 115
    • 0019877270 scopus 로고
    • Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in high mobility group proteins 14 and 17
    • Sterner R., Vidali G., and Allfrey V.G. Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in high mobility group proteins 14 and 17. J. Biol. Chem. 256 (1981) 8892-8895
    • (1981) J. Biol. Chem. , vol.256 , pp. 8892-8895
    • Sterner, R.1    Vidali, G.2    Allfrey, V.G.3
  • 116
    • 0034646638 scopus 로고    scopus 로고
    • Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes
    • Bergel M., Herrera J.E., Thatcher B.J., Prymakowska-Bosak M., Vassilev A., Nakatani Y., Martin B., and Bustin M. Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes. J. Biol. Chem. 275 (2000) 11514-11520
    • (2000) J. Biol. Chem. , vol.275 , pp. 11514-11520
    • Bergel, M.1    Herrera, J.E.2    Thatcher, B.J.3    Prymakowska-Bosak, M.4    Vassilev, A.5    Nakatani, Y.6    Martin, B.7    Bustin, M.8
  • 117
    • 0032933141 scopus 로고    scopus 로고
    • Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes
    • Herrera J.E., Sakaguchi K., Bergel M., Trieschmann L., Nakatani Y., and Bustin M. Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes. Mol. Cell. Biol. 19 (1999) 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
  • 118
    • 33744505921 scopus 로고    scopus 로고
    • Distinct domains in high mobility group N variants modulate specific chromatin modifications
    • Ueda T., Postnikov Y.V., and Bustin M. Distinct domains in high mobility group N variants modulate specific chromatin modifications. J. Biol. Chem. 281 (2006) 10182-10187
    • (2006) J. Biol. Chem. , vol.281 , pp. 10182-10187
    • Ueda, T.1    Postnikov, Y.V.2    Bustin, M.3
  • 119
    • 33845591156 scopus 로고    scopus 로고
    • Chromosomal protein HMGN1 modulates the phosphorylation of serine 1 in histone H2A
    • Postnikov Y.V., Belova G.I., Lim J.H., and Bustin M. Chromosomal protein HMGN1 modulates the phosphorylation of serine 1 in histone H2A. Biochemistry 45 (2006) 15092-15099
    • (2006) Biochemistry , vol.45 , pp. 15092-15099
    • Postnikov, Y.V.1    Belova, G.I.2    Lim, J.H.3    Bustin, M.4
  • 121
    • 25444533582 scopus 로고    scopus 로고
    • Inhibition of nucleotide excision repair by high mobility group protein HMGA1
    • Adair J.E., Kwon Y., Dement G.A., Smerdon M.J., and Reeves R. Inhibition of nucleotide excision repair by high mobility group protein HMGA1. J. Biol. Chem. 280 (2005) 32184-32192
    • (2005) J. Biol. Chem. , vol.280 , pp. 32184-32192
    • Adair, J.E.1    Kwon, Y.2    Dement, G.A.3    Smerdon, M.J.4    Reeves, R.5
  • 122
    • 34547781223 scopus 로고    scopus 로고
    • Gene-specific nucleotide excision repair is impaired in human cells expressing elevated levels of high mobility group A1 nonhistone proteins
    • Maloney S.C., Adair J.E., Smerdon M.J., and Reeves R. Gene-specific nucleotide excision repair is impaired in human cells expressing elevated levels of high mobility group A1 nonhistone proteins. DNA Repair 6 (2007) 1371-1379
    • (2007) DNA Repair , vol.6 , pp. 1371-1379
    • Maloney, S.C.1    Adair, J.E.2    Smerdon, M.J.3    Reeves, R.4
  • 123
    • 34447115716 scopus 로고    scopus 로고
    • High-mobility group A1 proteins inhibit expression of nucleotide excision repair factor xeroderma pigmentosum group A
    • Adair J.E., Maloney S.C., Dement G.A., Wertzler K.J., Smerdon M.J., and Reeves R. High-mobility group A1 proteins inhibit expression of nucleotide excision repair factor xeroderma pigmentosum group A. Cancer Res. 67 (2007) 6044-6052
    • (2007) Cancer Res. , vol.67 , pp. 6044-6052
    • Adair, J.E.1    Maloney, S.C.2    Dement, G.A.3    Wertzler, K.J.4    Smerdon, M.J.5    Reeves, R.6
  • 125
    • 2442705192 scopus 로고    scopus 로고
    • Evidence for involvement of HMGB1 protein in human DNA mismatch repair
    • Yuan F., Gu L., Guo S., Wang C., and Li G.M. Evidence for involvement of HMGB1 protein in human DNA mismatch repair. J. Biol. Chem. 279 (2004) 20935-20940
    • (2004) J. Biol. Chem. , vol.279 , pp. 20935-20940
    • Yuan, F.1    Gu, L.2    Guo, S.3    Wang, C.4    Li, G.M.5
  • 126
    • 0037228781 scopus 로고    scopus 로고
    • A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues
    • Krynetski E.Y., Krynetskaia N.F., Bianchi M.E., and Evans W.E. A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues. Cancer Res. 63 (2003) 100-106
    • (2003) Cancer Res. , vol.63 , pp. 100-106
    • Krynetski, E.Y.1    Krynetskaia, N.F.2    Bianchi, M.E.3    Evans, W.E.4
  • 127
    • 0028117527 scopus 로고
    • HMG-domain proteins specifically inhibit the repair of the major DNA adduct of the anticancer drug cisplatin by human excision nuclease
    • Huang J.C., Zamble D.B., Reardon J.T., Lippard S.J., and Sancar A. HMG-domain proteins specifically inhibit the repair of the major DNA adduct of the anticancer drug cisplatin by human excision nuclease. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 10394-10398
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 10394-10398
    • Huang, J.C.1    Zamble, D.B.2    Reardon, J.T.3    Lippard, S.J.4    Sancar, A.5
  • 128
    • 48749124996 scopus 로고    scopus 로고
    • High mobility group protein B1 enhances DNA repair and chromatin modification after DNA damage
    • Lange S.S., Mitchell D.L., and Vasquez K.M. High mobility group protein B1 enhances DNA repair and chromatin modification after DNA damage. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 10320-10325
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 10320-10325
    • Lange, S.S.1    Mitchell, D.L.2    Vasquez, K.M.3


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