메뉴 건너뛰기




Volumn 38, Issue 4, 2006, Pages 755-767

Ros-induced histone modifications and their role in cell survival and cell death

Author keywords

Cell death; Chromatin; DNA damage; Histones; Mitotic catastrophe; Oncotic cell death; Post translational modification; Premature chromatin condensation; Reactive oxygen species; Stress response signaling

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 4 (4 FLUOROPHENYL) 2 (4 HYDROXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; HISTONE; HISTONE H2A; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE INHIBITOR; POLY(ADENOSINE DIPHOSPHATE RIBOSE); REACTIVE OXYGEN METABOLITE;

EID: 33845451723     PISSN: 03602532     EISSN: 10979883     Source Type: Journal    
DOI: 10.1080/03602530600959649     Document Type: Conference Paper
Times cited : (42)

References (63)
  • 1
    • 0021140803 scopus 로고
    • ADP-Ribosylation of nuclear proteins in vivo. Identification of histone H2B as a major acceptor for mono- and poly(ADP-ribose) in dimethyl sulfate-treated hepatoma AH7974 cells
    • Adamietz, P, Rudolph, A. (1984). ADP-Ribosylation of nuclear proteins in vivo. Identification of histone H2B as a major acceptor for mono- and poly(ADP-ribose) in dimethyl sulfate-treated hepatoma AH7974 cells. J. Biol. Chem. 259:6841-6846.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6841-6846
    • Adamietz, P.1    Rudolph, A.2
  • 2
    • 0022350430 scopus 로고
    • Specific site of histone H3 phosphorylation related to the maintenance of premature chromosome condensation. Evidence for catalytically induced interchange of the subunits
    • Ajiro, K., Nishimoto, T. (1985). Specific site of histone H3 phosphorylation related to the maintenance of premature chromosome condensation. Evidence for catalytically induced interchange of the subunits. J. Biol. Chem. 26:15379-15381.
    • (1985) J. Biol. Chem. , vol.26 , pp. 15379-15381
    • Ajiro, K.1    Nishimoto, T.2
  • 3
    • 0020567493 scopus 로고
    • Histone H1 and H3 phosphorylation during premature chromosome condensation in a temperature-sensitive mutant (tsBN2) of baby hamster kidney cells
    • Ajiro, K., Nishimoto, T., Takahashi, T. (1983). Histone H1 and H3 phosphorylation during premature chromosome condensation in a temperature-sensitive mutant (tsBN2) of baby hamster kidney cells. J. Biol. Chem. 258:4534-4538.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4534-4538
    • Ajiro, K.1    Nishimoto, T.2    Takahashi, T.3
  • 4
    • 0030774915 scopus 로고    scopus 로고
    • Disassociation of oxidant-induced ATP depletion and DNA damage from early cytotoxicity in LLC-PK1 cells
    • Andreoli, S. P., Mallett, C. P. (1997). Disassociation of oxidant-induced ATP depletion and DNA damage from early cytotoxicity in LLC-PK1 cells. Am. J. Physiol. 272:F729-735.
    • (1997) Am. J. Physiol. , vol.272
    • Andreoli, S.P.1    Mallett, C.P.2
  • 5
    • 0028793257 scopus 로고
    • Glutamate-induced neuronal death: A succession of necrosis or apoptosis depending on mitochondrial function
    • Ankarcrona, M., Dypbuki, J. M., Bonfoco, E., Zhivotovsky, B., Orrenius, S., Lipton S. A., Nicotera, P. (1995). Glutamate-induced neuronal death: a succession of necrosis or apoptosis depending on mitochondrial function. Neuron 15:961-973.
    • (1995) Neuron , vol.15 , pp. 961-973
    • Ankarcrona, M.1    Dypbuki, J.M.2    Bonfoco, E.3    Zhivotovsky, B.4    Orrenius, S.5    Lipton, S.A.6    Nicotera, P.7
  • 6
    • 0028948871 scopus 로고
    • Relationship between methylation and acetylation of arginine-rich histones in cycling and arrested HeLa cells
    • Annunziato, A. T., Eason, M. B., Perry, C. A. (1995). Relationship between methylation and acetylation of arginine-rich histones in cycling and arrested HeLa cells. Biochemistry 34:2916-2924
    • (1995) Biochemistry , vol.34 , pp. 2916-2924
    • Annunziato, A.T.1    Eason, M.B.2    Perry, C.A.3
  • 7
    • 0032921811 scopus 로고    scopus 로고
    • Hydrogen peroxide activation of multiple mitogen-activated protein kinases in an oligodendrocyte cell line: Role of extracellular signal-regulated kinase in hydrogen peroxide-induced cell death
    • Bhat, N.R., Zhang P. (1999). Hydrogen peroxide activation of multiple mitogen-activated protein kinases in an oligodendrocyte cell line: role of extracellular signal-regulated kinase in hydrogen peroxide-induced cell death. J. Neurochem. 72:112-119.
    • (1999) J. Neurochem. , vol.72 , pp. 112-119
    • Bhat, N.R.1    Zhang, P.2
  • 8
    • 0033011114 scopus 로고    scopus 로고
    • Mice lacking the poly(ADP-ribose) polymerase gene are resistant to pancreatic beta-cell destruction and diabetes development induced by streptozocin
    • Burkart, V., Wang, Z. Q., Radons, J., Heller, B., Herceg, Z., Stingl, L., Wagner, E. F., Kolb, H. (1999). Mice lacking the poly(ADP-ribose) polymerase gene are resistant to pancreatic beta-cell destruction and diabetes development induced by streptozocin. Nat. Med. 5:314-319.
    • (1999) Nat. Med. , vol.5 , pp. 314-319
    • Burkart, V.1    Wang, Z.Q.2    Radons, J.3    Heller, B.4    Herceg, Z.5    Stingl, L.6    Wagner, E.F.7    Kolb, H.8
  • 9
    • 0033609882 scopus 로고    scopus 로고
    • Increased Ser-10 phosphorylation of histone H3 in mitogen-stimulated and oncogene-transformed mouse fibroblasts
    • Chadee, D. N., Hendzel, M. J., Tylipski, C. P., Allis, C. D., Bazett-Jones, D. P., Wright, J. A., Davie, J. R. (1999). Increased Ser-10 phosphorylation of histone H3 in mitogen-stimulated and oncogene-transformed mouse fibroblasts. J. Biol. Chem. 274:24914-24920.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24914-24920
    • Chadee, D.N.1    Hendzel, M.J.2    Tylipski, C.P.3    Allis, C.D.4    Bazett-Jones, D.P.5    Wright, J.A.6    Davie, J.R.7
  • 10
    • 0032852942 scopus 로고    scopus 로고
    • Tempol, a membrane-permeable radical scavenger, reduces oxidant stress-mediated renal dysfunction and injury in the rat
    • Chatterjee, P. K., Cuzzocrea, S., Thiemermann, C. (1999). Tempol, a membrane-permeable radical scavenger, reduces oxidant stress-mediated renal dysfunction and injury in the rat. Kidney Int. 56:973-984.
    • (1999) Kidney Int. , vol.56 , pp. 973-984
    • Chatterjee, P.K.1    Cuzzocrea, S.2    Thiemermann, C.3
  • 11
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung, P., Allis, C.D., Sassone-Corsi, P. (2000). Signaling to chromatin through histone modifications. Cell 103:263-271
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 12
    • 0034679625 scopus 로고    scopus 로고
    • Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation
    • Clayton, Al., Rose, S., Barratt, M. J., Mahadevan, L. C. (2000). Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation. EMBO J. 19:3714-3726.
    • (2000) EMBO J. , vol.19 , pp. 3714-3726
    • Clayton, Al.1    Rose, S.2    Barratt, M.J.3    Mahadevan, L.C.4
  • 14
    • 0030936331 scopus 로고    scopus 로고
    • Detection of radiation-induced chromosome aberrations using fluorescence in situ hybridization in drug-induced premature chromosome condensations of tumour cell lines with different radiosensitivities
    • Coco-Martin, J. M., Begg, A. C. (1997). Detection of radiation-induced chromosome aberrations using fluorescence in situ hybridization in drug-induced premature chromosome condensations of tumour cell lines with different radiosensitivities. Inter. J. Rad. Biol. 71:265-273.
    • (1997) Inter. J. Rad. Biol. , vol.71 , pp. 265-273
    • Coco-Martin, J.M.1    Begg, A.C.2
  • 15
    • 0030512391 scopus 로고    scopus 로고
    • Effect of a poly(ADP-ribose) polymerase inhibitor on DNA breakage and cytotoxicity induced by hydrogen peroxide and gamma-radiation
    • Cristovao L., Rueff, J. (1996). Effect of a poly(ADP-ribose) polymerase inhibitor on DNA breakage and cytotoxicity induced by hydrogen peroxide and gamma-radiation. Terat. Carcinog. Mutagenesis 16:219-227.
    • (1996) Terat. Carcinog. Mutagenesis , vol.16 , pp. 219-227
    • Cristovao, L.1    Rueff, J.2
  • 16
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours, D., Desnoyers, S., D'Silva, I., Poirier, G. G. (1999). Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 342:249-268.
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 17
    • 0031777895 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase pathway contributes to vanadate toxicity in vascular smooth muscle cells
    • Daum, G., Levkau, B., Chamberlain, N. L., Wang, Y., Clowes, A. W. (1998). The mitogen-activated protein kinase pathway contributes to vanadate toxicity in vascular smooth muscle cells. Mol. Cell Biochem. 183:97-103.
    • (1998) Mol. Cell Biochem. , vol.183 , pp. 97-103
    • Daum, G.1    Levkau, B.2    Chamberlain, N.L.3    Wang, Y.4    Clowes, A.W.5
  • 20
    • 0030832874 scopus 로고    scopus 로고
    • Ischemic brain injury is mediated by the activation of poly(ADP-ribose)polymerase
    • Endres, M., Wang, Z. Q., Namura, S., Waeber, C., Moskowitz, M. A. (1997). Ischemic brain injury is mediated by the activation of poly(ADP-ribose) polymerase. J. Cereb. Blood Flow Metab. 17:1143-1151.
    • (1997) J. Cereb. Blood Flow Metab. , vol.17 , pp. 1143-1151
    • Endres, M.1    Wang, Z.Q.2    Namura, S.3    Waeber, C.4    Moskowitz, M.A.5
  • 21
    • 20444386251 scopus 로고    scopus 로고
    • Inhibition of PARP prevents oxidant-induced necrosis but not apoptosis in LLC-PK1 cells
    • Filipovic, D. M., Meng, X., Reeves, W. B. (1999). Inhibition of PARP prevents oxidant-induced necrosis but not apoptosis in LLC-PK1 cells. Am. J. Physiol. 277:F428-436.
    • (1999) Am. J. Physiol. , vol.277
    • Filipovic, D.M.1    Meng, X.2    Reeves, W.B.3
  • 22
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • Frye, R. A. (1999). Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophy. Res. Com. 260:273-279.
    • (1999) Biochem. Biophy. Res. Com. , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 24
    • 0028931408 scopus 로고
    • Chromosome condensation induced by fostriecin does not require p34cdc2 kinase activity and histone H1 hyperphosphorylation, but is associated with enhanced histone H2A and H3 phosphorylation
    • Guo, X. W., Th'ng, J. P. H., Swank, R. A., Anderson, H. J., Tudan, C., Bradbury, E. M., Roberge, M. (1995). Chromosome condensation induced by fostriecin does not require p34cdc2 kinase activity and histone H1 hyperphosphorylation, but is associated with enhanced histone H2A and H3 phosphorylation. EMBO J.14:976-985.
    • (1995) EMBO J. , vol.14 , pp. 976-985
    • Guo, X.W.1    Th'ng, J.P.H.2    Swank, R.A.3    Anderson, H.J.4    Tudan, C.5    Bradbury, E.M.6    Roberge, M.7
  • 25
    • 0017853206 scopus 로고
    • Histone phosphorylation and chromatin structure during mitosis in Chinese hamster cells
    • Gurley, L. R., D'Anna, J. A., Barham, S. S., Deaven, L. L., Tobey, R. A. (1978). Histone phosphorylation and chromatin structure during mitosis in Chinese hamster cells. E. J. Biochem. 84:1-15.
    • (1978) E. J. Biochem. , vol.84 , pp. 1-15
    • Gurley, L.R.1    D'Anna, J.A.2    Barham, S.S.3    Deaven, L.L.4    Tobey, R.A.5
  • 26
    • 0033598713 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion
    • Ha, H. C., Snyder, S. H. (1999). Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion. Proc. Natl. Acad. Sci. 96:13978-13982.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 13978-13982
    • Ha, H.C.1    Snyder, S.H.2
  • 27
    • 0030828073 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation
    • Hendzel, M. J. (1997). Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation. Chromosoma 106:348-360.
    • (1997) Chromosoma , vol.106 , pp. 348-360
    • Hendzel, M.J.1
  • 28
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S., Armstrong, C. M., Kaeberlein, M., Guarente, L. (2000). Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403:795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 29
    • 33745632390 scopus 로고    scopus 로고
    • The epigenetic magic of histone lysine methylation
    • Jenuwein, T. (2006). The epigenetic magic of histone lysine methylation. FEBS J. 273:3121-3135.
    • (2006) FEBS J. , vol.273 , pp. 3121-3135
    • Jenuwein, T.1
  • 30
    • 6344252131 scopus 로고    scopus 로고
    • GRP78/Bip is essential for 11-deoxy-16,16-dimethylprostaglandin mediated cytoprotection in renal epithelial cells
    • Jia, Z., Person, M. D., Shen, J., Hensley, S. C., Stevens, J. L., Monks, T .J., Lau, S. S. (2004). GRP78/Bip is essential for 11-deoxy-16,16- dimethylprostaglandin mediated cytoprotection in renal epithelial cells. Am. J. Physiol. Renal Physiol. 287:F1113-F1122.
    • (2004) Am. J. Physiol. Renal Physiol. , vol.287
    • Jia, Z.1    Person, M.D.2    Shen, J.3    Hensley, S.C.4    Stevens, J.L.5    Monks, T.J.6    Lau, S.S.7
  • 32
    • 0021047749 scopus 로고
    • Transformation of temperature-sensitive growth mutant of BHK21 cell line to wild-type phenotype with hamster and mouse DNA
    • Kai R., Sekiguchi T., Yamashita K., Sekiguchi M., Nishimoto, T. (1983). Transformation of temperature-sensitive growth mutant of BHK21 cell line to wild-type phenotype with hamster and mouse DNA. Somatic Cell Genet. 9:673-680
    • (1983) Somatic Cell Genet. , vol.9 , pp. 673-680
    • Kai, R.1    Sekiguchi, T.2    Yamashita, K.3    Sekiguchi, M.4    Nishimoto, T.5
  • 33
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J. F., Wyllie, A. H., Currie, A. R. (1972). Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26:239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 35
    • 0024455114 scopus 로고
    • Mammalian growth-associated H1 histone kinase: A homolog of cdc2+/CDC28 protein kinases controlling mitotic entry in yeast and frog cells
    • Langan, T. A., Gautier, J., Lohka, M., Hollingsworth, R., Moreno, S., Nurse, P., Maller, J., Sclafani, R. A. (1989). Mammalian growth-associated H1 histone kinase: a homolog of cdc2+/CDC28 protein kinases controlling mitotic entry in yeast and frog cells. Mol. Cell. Biol. 9:3860-3868.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3860-3868
    • Langan, T.A.1    Gautier, J.2    Lohka, M.3    Hollingsworth, R.4    Moreno, S.5    Nurse, P.6    Maller, J.7    Sclafani, R.A.8
  • 36
    • 0030009567 scopus 로고    scopus 로고
    • Uncoupling of M-phase kinase activation from the completion of S-phase by heat shock
    • Mackey, M. A., Zhang, X. F., Hunt, C. R., Sullivan, S. J., Blum, J., Laszlo, A., Roti, J. L. (1996). Uncoupling of M-phase kinase activation from the completion of S-phase by heat shock. Cancer Res. 56:1770-1774.
    • (1996) Cancer Res , vol.56 , pp. 1770-1774
    • Mackey, M.A.1    Zhang, X.F.2    Hunt, C.R.3    Sullivan, S.J.4    Blum, J.5    Laszlo, A.6    Roti, J.L.7
  • 37
    • 0025872683 scopus 로고
    • Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors
    • Mahadevan, L. C., Willis, A. C., Barrah, M. J. (1991). Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors. Cell 65:775-783
    • (1991) Cell , vol.65 , pp. 775-783
    • Mahadevan, L.C.1    Willis, A.C.2    Barrah, M.J.3
  • 38
    • 0020759349 scopus 로고
    • Immunoaffinity fractionation of the polyADP-ribosylated domains of chromatin
    • Malik, N., Miwa, M., Sugimura, T., Thraves, P., Smulson, M. (1983). Immunoaffinity fractionation of the poly(ADP-ribosylated domains of chromatin. Proc. Natl. Acad. Sci. USA 80:2554-2558
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2554-2558
    • Malik, N.1    Miwa, M.2    Sugimura, T.3    Thraves, P.4    Smulson, M.5
  • 40
    • 0030638249 scopus 로고    scopus 로고
    • Neuronal necrosis and apoptosis: Two distinct events induced by exposure to glutamate or oxidatuve stress
    • Nicotera, P., Ankacrona, M., Bonfocco, E., Orrenius, S., Lipton, S. A. (1997). Neuronal necrosis and apoptosis: Two distinct events induced by exposure to glutamate or oxidatuve stress. Adv. Neurol. 72:95-101.
    • (1997) Adv. Neurol. , vol.72 , pp. 95-101
    • Nicotera, P.1    Ankacrona, M.2    Bonfocco, E.3    Orrenius, S.4    Lipton, S.A.5
  • 41
    • 0030787863 scopus 로고    scopus 로고
    • Modeling the control of DNA replication in fission yeast
    • Novak, B., Tyson, J. J. (1997). Modeling the control of DNA replication in fission yeast. Proc. Natl. Acad. Sci. USA 94:9147-9152.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9147-9152
    • Novak, B.1    Tyson, J.J.2
  • 44
    • 0036916586 scopus 로고    scopus 로고
    • Mitogen activated protein kinases contribute to reactive oxygen species-induced cell death in renal proximal tubule epithelial cells
    • Ramachandiran, S., Huang, Q., Dong, J., Lau, S. S., Monks, T. J. (2002). Mitogen activated protein kinases contribute to reactive oxygen species-induced cell death in renal proximal tubule epithelial cells. Chem. Res. Toxicol. 15:1635-1642,.
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 1635-1642
    • Ramachandiran, S.1    Huang, Q.2    Dong, J.3    Lau, S.S.4    Monks, T.J.5
  • 45
    • 0026730009 scopus 로고
    • Histone shuttling by poly(ADP-ribosylation)
    • Realini, C. A., Althaus, F. R. (1992). Histone shuttling by poly(ADP-ribosylation). J. Biol. Chem. 267:18858-18865.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18858-18865
    • Realini, C.A.1    Althaus, F.R.2
  • 46
    • 0027948538 scopus 로고
    • Early morphological and biochemical changes during 2-Br-(diglutathion-S- yl)hydroquinone-induced nephrotoxicity
    • Rivera, M. I., Jones, T. W., Lau, S. S., Monks, T. J. (1994). Early morphological and biochemical changes during 2-Br-(diglutathion-S-yl) hydroquinone-induced nephrotoxicity. Toxicol. Appl. Pharmacol. 128:239-250.
    • (1994) Toxicol. Appl. Pharmacol. , vol.128 , pp. 239-250
    • Rivera, M.I.1    Jones, T.W.2    Lau, S.S.3    Monks, T.J.4
  • 47
    • 0026545414 scopus 로고
    • Chromatin condensation: Does histone H1 dephosphorylation play a role?
    • Roth, S. Y., Allis, C. D.(1992). Chromatin condensation: does histone H1 dephosphorylation play a role? Trends Biochem. Sci. 17:93-98.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 93-98
    • Roth, S.Y.1    Allis, C.D.2
  • 48
    • 0345299208 scopus 로고    scopus 로고
    • Phosphorylation-induced rearrangement of the histone H3 NH2-terminal domain during mitotic chromosome condensation
    • Sauve, D. M., Anderson, H. J., Ray, J. M., James, W. M., Roberge, M. (1999). Phosphorylation-induced rearrangement of the histone H3 NH2-terminal domain during mitotic chromosome condensation. J. Cell Biol. 145:225-235.
    • (1999) J. Cell Biol. , vol.145 , pp. 225-235
    • Sauve, D.M.1    Anderson, H.J.2    Ray, J.M.3    James, W.M.4    Roberge, M.5
  • 49
    • 0029013311 scopus 로고
    • Linker histones are not essential and affect chromatin condensation in vivo
    • Shen, X., Yu, L., Weir, J. W., Gorovsky, M. A., (1995). Linker histones are not essential and affect chromatin condensation in vivo. Cell 82:47-56.
    • (1995) Cell , vol.82 , pp. 47-56
    • Shen, X.1    Yu, L.2    Weir, J.W.3    Gorovsky, M.A.4
  • 51
    • 20444391346 scopus 로고    scopus 로고
    • Chromatin in need of a fix: Phosphorylation of H2AX connects chromatin to DNA repair
    • Thiriet, C., Hayes, J. J. (2005). Chromatin in need of a fix: phosphorylation of H2AX connects chromatin to DNA repair. Molec. Cell 18:617-622.
    • (2005) Molec. Cell , vol.18 , pp. 617-622
    • Thiriet, C.1    Hayes, J.J.2
  • 52
    • 0028284541 scopus 로고
    • Inhibition of histone phosphorylation by staurosporine leads to chromosome decondensation
    • Th'ng, J. P. H., Guo, X.-W., Swank, R. A., Crissman, H. A., Bradbury, E. M. (1994). Inhibition of histone phosphorylation by staurosporine leads to chromosome decondensation. J. Biol. Chem. 269:9568-9573.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9568-9573
    • Th'ng, J.P.H.1    Guo, X.-W.2    Swank, R.A.3    Crissman, H.A.4    Bradbury, E.M.5
  • 53
    • 0034921212 scopus 로고    scopus 로고
    • Histone H3 phosphorylation is coupled to poly(ADP-ribosylation) and reactive oxygen species-induced cell death in renal proximal tubular epithelial cells
    • Tikoo, K., Lau, S. S., Monks, T. J. (2001). Histone H3 phosphorylation is coupled to poly(ADP-ribosylation) and reactive oxygen species-induced cell death in renal proximal tubular epithelial cells. Molec. Pharmacol. 60:394-402.
    • (2001) Molec. Pharmacol. , vol.60 , pp. 394-402
    • Tikoo, K.1    Lau, S.S.2    Monks, T.J.3
  • 54
    • 0033574536 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase pathway is required for activation-induced cell death of T cells
    • van den Brink, M. R., Kapeller, R., Pratt, J. C., Chang, J. H., Burakoff, S. J. (1999). The extracellular signal-regulated kinase pathway is required for activation-induced cell death of T cells. J. Biol. Chem. 274:11178-11185.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11178-11185
    • Van Den Brink, M.R.1    Kapeller, R.2    Pratt, J.C.3    Chang, J.H.4    Burakoff, S.J.5
  • 55
    • 0003903126 scopus 로고
    • New York: Springer-Verlag New York Inc.
    • van Holde, K. E. (1989). Chromatin. New York: Springer-Verlag New York Inc.
    • (1989) Chromatin
    • Van Holde, K.E.1
  • 56
    • 0032442522 scopus 로고    scopus 로고
    • Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation
    • van Hooser, A., Goodrich, D. W., Allis, C. D., Brinkley, B. R., Mancini, M. A. (1998). Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation. J. Cell Sci. 111:3497-3506.
    • (1998) J. Cell Sci. , vol.111 , pp. 3497-3506
    • Van Hooser, A.1    Goodrich, D.W.2    Allis, C.D.3    Brinkley, B.R.4    Mancini, M.A.5
  • 57
    • 0033568205 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase inhibition in oxidant-stressed endothelial cells prevents oncosis and permits caspase activation and apoptosis
    • Walisser, J. A., Thies, R. L. (1999). Poly(ADP-ribose) polymerase inhibition in oxidant-stressed endothelial cells prevents oncosis and permits caspase activation and apoptosis. Expt. Cell Res. 251:401-413.
    • (1999) Expt. Cell Res. , vol.251 , pp. 401-413
    • Walisser, J.A.1    Thies, R.L.2
  • 58
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • Wei, Y., Yu, L., Bowen, J., Gorovsky, M. A., Allis, C. D. (1999). Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell 97:99-109.
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Bowen, J.3    Gorovsky, M.A.4    Allis, C.D.5
  • 59
    • 0033080794 scopus 로고    scopus 로고
    • Chromatin disruption and modification
    • Wolffe, A. P., Hayes J. J. (1999). Chromatin disruption and modification. Nucleic Acid Res. 27:711-720.
    • (1999) Nucleic Acid Res. , vol.27 , pp. 711-720
    • Wolffe, A.P.1    Hayes, J.J.2
  • 60
    • 0033613250 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase kinase activity is required for the G(2)/M transition of the cell cycle in mammalian fibroblasts
    • Wright, J. H., Munar, E., Jameson, D. R., Andreassen, P. R., Margolis, R. L., Seger, R., Krebs, E. G. (1999). Mitogen-activated protein kinase kinase activity is required for the G(2)/M transition of the cell cycle in mammalian fibroblasts. Proc. Natl. Acad. Sci. USA 96:11335-11340.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11335-11340
    • Wright, J.H.1    Munar, E.2    Jameson, D.R.3    Andreassen, P.R.4    Margolis, R.L.5    Seger, R.6    Krebs, E.G.7
  • 61
    • 0019225636 scopus 로고
    • Cell death: The significance of apoptosis
    • Wyllie, A. H., Kerr, J. F., Currie, A. R. (1980). Cell death: the significance of apoptosis. Int. Rev. Cytol. 68:251-306.
    • (1980) Int. Rev. Cytol. , vol.68 , pp. 251-306
    • Wyllie, A.H.1    Kerr, J.F.2    Currie, A.R.3
  • 62
    • 0032514225 scopus 로고    scopus 로고
    • Genetic disruption of poly (ADP-ribose) synthetase inhibits the expression of P-selectin and intercellular adhesion molecule-1 in myocardial ischemia/reperfusion injury
    • Zingarelli, B., Salzman, A. L., Szabo, C. (1998). Genetic disruption of poly (ADP-ribose) synthetase inhibits the expression of P-selectin and intercellular adhesion molecule-1 in myocardial ischemia/reperfusion injury. Cir. Res. 83:85-94.
    • (1998) Cir. Res. , vol.83 , pp. 85-94
    • Zingarelli, B.1    Salzman, A.L.2    Szabo, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.