메뉴 건너뛰기




Volumn 31, Issue 1-3, 2005, Pages 149-167

Poly(ADP-ribose) polymerase: The nuclear target in signal transduction and its role in brain ischemia-reperfusion injury

Author keywords

Brain; Ischemia; Neuroprotection; NF B; p53; PARP; PARP 1; Reperfusion

Indexed keywords

3 AMINOBENZAMIDE; 3,4 DIHYDRO 5 [4 (1 PIPERIDINYL)BUTOXY] 1(2H) ISOQUINOLINONE; AMPA RECEPTOR; AMYLOID BETA PROTEIN; BENZAMIDE; CHOLINERGIC RECEPTOR; GLUTAMINE; HISTONE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; ISOQUINOLINE DERIVATIVE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE INHIBITOR; NITRIC OXIDE; NUCLEAR PROTEIN; PEROXYNITRITE; PROTEIN P53; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 21044438413     PISSN: 08937648     EISSN: None     Source Type: Journal    
DOI: 10.1385/MN:31:1-3:149     Document Type: Conference Paper
Times cited : (54)

References (108)
  • 1
    • 0023149198 scopus 로고
    • Cellular euthanasia mediated by a nuclear enzyme: A central role for nuclear ADP-ribosylation in cellular methabolism
    • Gaal J.C., Smith K.R., and Pearson C.K. (1987) Cellular euthanasia mediated by a nuclear enzyme: a central role for nuclear ADP-ribosylation in cellular methabolism. Trends Biochem. Sci. 12, 129-130.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 129-130
    • Gaal, J.C.1    Smith, K.R.2    Pearson, C.K.3
  • 2
    • 0026507413 scopus 로고
    • Role of poly(ADP-ribose) formation in DNA repair
    • Satoh M.S. and Lindahl T. (1992) Role of poly(ADP-ribose) formation in DNA repair. Nature 356, 356-358.
    • (1992) Nature , vol.356 , pp. 356-358
    • Satoh, M.S.1    Lindahl, T.2
  • 3
    • 0034985121 scopus 로고    scopus 로고
    • A cellular survival switch: Poly(ADP-ribosyl)ation stimulates DNA repair and silences transcription
    • Ziegler M. and Oei S.L. (2001) A cellular survival switch: poly(ADP-ribosyl)ation stimulates DNA repair and silences transcription. Bioessays 23, 543-548.
    • (2001) Bioessays , vol.23 , pp. 543-548
    • Ziegler, M.1    Oei, S.L.2
  • 4
    • 0035281786 scopus 로고    scopus 로고
    • The world according to PARP
    • Smith S. (2001) The world according to PARP. Trends Biochem. Sci. 26, 174-179.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 174-179
    • Smith, S.1
  • 5
    • 0035796025 scopus 로고    scopus 로고
    • Functions of poly(ADP-ribose) polymerase (PARP) in DNA repair, genomic integrity and cell death
    • Herzeg Z. and Wang Z.Q. (2001) Functions of poly(ADP-ribose) polymerase (PARP) in DNA repair, genomic integrity and cell death. Mutat. Res. 477, 97-110.
    • (2001) Mutat. Res. , vol.477 , pp. 97-110
    • Herzeg, Z.1    Wang, Z.Q.2
  • 6
  • 7
    • 0028113249 scopus 로고
    • Structure and function of poly(ADP-ribose) polymerase
    • de Murcia G., Schreiber V., Molinete M., et al. (1994) Structure and function of poly(ADP-ribose) polymerase. Mol. Cell. Biochem. 138, 15-24.
    • (1994) Mol. Cell. Biochem. , vol.138 , pp. 15-24
    • De Murcia, G.1    Schreiber, V.2    Molinete, M.3
  • 8
    • 0028865245 scopus 로고
    • Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks
    • Lindahl T., Satoh M.S., Poirier G.G., and Klungland A. (1995) Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks. Trends Biochem. Sci. 20, 405-411.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 405-411
    • Lindahl, T.1    Satoh, M.S.2    Poirier, G.G.3    Klungland, A.4
  • 9
    • 0029156632 scopus 로고
    • Poly(ADP-ribose) polymerase: Structure-function relationship
    • Masson M., Rolli V., Dantzer F., et al. (1995) Poly(ADP-ribose) polymerase: structure-function relationship. Biochimie 77, 456-461.
    • (1995) Biochimie , vol.77 , pp. 456-461
    • Masson, M.1    Rolli, V.2    Dantzer, F.3
  • 10
    • 0029618114 scopus 로고
    • Poly(ADP-ribosyl)ation as a fail-safe, transcription-independent, suicide mechanism in acutely DNA-damaged cells: A hypothesis
    • Nagele A. (1995) Poly(ADP-ribosyl)ation as a fail-safe, transcription-independent, suicide mechanism in acutely DNA-damaged cells: a hypothesis. Radiat. Environ. Biophys. 34, 251-254.
    • (1995) Radiat. Environ. Biophys. , vol.34 , pp. 251-254
    • Nagele, A.1
  • 11
    • 0026776003 scopus 로고
    • Poly ADP-ribosylation: A histone shuttle mechanism in DNA excision repair
    • Althaus F.R. (1992) Poly ADP-ribosylation: a histone shuttle mechanism in DNA excision repair. J Cell Sci. 102, 663-670.
    • (1992) J. Cell Sci. , vol.102 , pp. 663-670
    • Althaus, F.R.1
  • 12
    • 0036710459 scopus 로고    scopus 로고
    • The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-kappaB in inflammatory disorders
    • Hassa P.O. and Hottiger M.O. (2002) The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-kappaB in inflammatory disorders. Cell. Mol. Life Sci. 59, 1534-1553.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1534-1553
    • Hassa, P.O.1    Hottiger, M.O.2
  • 13
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours D., Desnoyers S., D'Silva I., and 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
  • 14
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
    • Pleschke J.M., Kleczkowska H.E., Strohm M., and Althaus F.R. (2000) Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275, 40,974-40,980.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 15
    • 0032496235 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains of p53 and alters its DNA binding functions
    • Malanga M., Pleschke J.M., Kleczkowska H.E., and Althaus F.R. (1998) Poly(ADP-ribose) binds to specific domains of p53 and alters its DNA binding functions. J. Biol. Chem. 273, 11,839-11,843.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11839-11843
    • Malanga, M.1    Pleschke, J.M.2    Kleczkowska, H.E.3    Althaus, F.R.4
  • 16
    • 0003908239 scopus 로고
    • ADP-ribosylation reactions biology and medicine
    • (Horecker, B., Kaplan, N., Marmur, J., and Scheraga, A., eds.), Academic Press, New York, London
    • Hayaishi O. and Ueda K. (1982) ADP-ribosylation reactions biology and medicine, in Molecular Biology An Int Series of Monographs. (Horecker, B., Kaplan, N., Marmur, J., and Scheraga, A., eds.), Academic Press, New York, London.
    • (1982) Molecular Biology An Int Series of Monographs
    • Hayaishi, O.1    Ueda, K.2
  • 18
    • 0032863224 scopus 로고    scopus 로고
    • A role of poly (ADP-ribose) polymerase in NF-kappaB transcriptional activation
    • Hassa P.O. and Hottiger M.O. (1999) A role of poly (ADP-ribose) polymerase in NF-kappaB transcriptional activation. Biol. Chem. 380, 953-959.
    • (1999) Biol. Chem. , vol.380 , pp. 953-959
    • Hassa, P.O.1    Hottiger, M.O.2
  • 19
    • 0032518339 scopus 로고    scopus 로고
    • DNA repair: PARP - Another guardian angel?
    • Jeggo P.A. (1998) DNA repair: PARP - another guardian angel? Curr. Biol. 8, R49-R51.
    • (1998) Curr. Biol. , vol.8
    • Jeggo, P.A.1
  • 20
    • 0027081044 scopus 로고
    • Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span
    • Grube K. and Burkle A. (1992) Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span. Proc. Natl. Acad. Sci. USA 89, 11,759-11,763.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11759-11763
    • Grube, K.1    Burkle, A.2
  • 22
    • 0035495529 scopus 로고    scopus 로고
    • PARP-1: A regulator of genomic stability linked with mammalian longevity
    • Burkle A. (2001) PARP-1: a regulator of genomic stability linked with mammalian longevity. Chembiochem 2, 725-728.
    • (2001) Chembiochem , vol.2 , pp. 725-728
    • Burkle, A.1
  • 23
    • 0028107217 scopus 로고
    • Age-associated changes of rat brain neuronal and astroglial poly(ADP-ribose) polymerase activity
    • Messripour M., Weltin D., Rastegar A., et al. (1994) Age-associated changes of rat brain neuronal and astroglial poly(ADP-ribose) polymerase activity. J. Neurochem. 62, 502-506.
    • (1994) J. Neurochem. , vol.62 , pp. 502-506
    • Messripour, M.1    Weltin, D.2    Rastegar, A.3
  • 24
    • 0034569638 scopus 로고    scopus 로고
    • Effect of amyloid beta peptide on poly(ADP-ribose) polymerase activity in adult and aged rat hippocampus
    • Strosznajder J.B., Jesko H., and Strosznajder R.P. (2000) Effect of amyloid beta peptide on poly(ADP-ribose) polymerase activity in adult and aged rat hippocampus. Acta Biochim. Pol. 47, 847-854.
    • (2000) Acta Biochim. Pol. , vol.47 , pp. 847-854
    • Strosznajder, J.B.1    Jesko, H.2    Strosznajder, R.P.3
  • 25
    • 0036499892 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase: Killer or conspirator? the suicide hypothesis revisited
    • Chiarugi A. (2002) Poly(ADP-ribose) polymerase: killer or conspirator? The suicide hypothesis revisited. Trends Pharmacol. Sci. 23(3), 122-129.
    • (2002) Trends Pharmacol. Sci. , vol.23 , Issue.3 , pp. 122-129
    • Chiarugi, A.1
  • 26
    • 0034685885 scopus 로고    scopus 로고
    • Characterization of sPARP-1. An alternative product of PARP-1 gene with poly(ADP-ribose) polymerase activity independent of DNA strand breaks
    • Sallmann F.R., Vodenicharov M.D., Wang Z.Q., and Poirier G.G. (2000) Characterization of sPARP-1. An alternative product of PARP-1 gene with poly(ADP-ribose) polymerase activity independent of DNA strand breaks. J. Biol. Chem. 275, 15,504-15,511.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15504-15511
    • Sallmann, F.R.1    Vodenicharov, M.D.2    Wang, Z.Q.3    Poirier, G.G.4
  • 27
    • 0033580856 scopus 로고    scopus 로고
    • PARP-2, a novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase
    • Ame J.C., Rolli V., Schreiber V., et al. (1999) PARP-2, a novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase. J. Biol. Chem. 274, 17,860-17,868.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17860-17868
    • Ame, J.C.1    Rolli, V.2    Schreiber, V.3
  • 28
    • 10744233161 scopus 로고    scopus 로고
    • Functional interaction between poly (ADP-ribose) polymerase 2 (PARP-2) and TRF2: PARP activity negatively regulates TRF2
    • Dantzer F., Giraud-Panis M.-J., Jaco I., et al. (2004) Functional interaction between poly (ADP-ribose) polymerase 2 (PARP-2) and TRF2: PARP activity negatively regulates TRF2. Mol. Cell. Biol. 24, 1595-1607.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1595-1607
    • Dantzer, F.1    Giraud-Panis, M.-J.2    Jaco, I.3
  • 29
    • 0033135769 scopus 로고    scopus 로고
    • A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues
    • Johansson M. (1999) A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues. Genomics 57, 442-445.
    • (1999) Genomics , vol.57 , pp. 442-445
    • Johansson, M.1
  • 30
    • 0037151051 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC-1
    • Schreiber V., Ame J.-C., Dolle P., et al. (2002) Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC-1. J. Biol. Chem. 277, 23,028-23,036.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23028-23036
    • Schreiber, V.1    Ame, J.-C.2    Dolle, P.3
  • 31
    • 0032553473 scopus 로고    scopus 로고
    • Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
    • Smith S., Giriat I., Schmitt A., and de Lange T. (1998) Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. Science 282, 1484-1487.
    • (1998) Science , vol.282 , pp. 1484-1487
    • Smith, S.1    Giriat, I.2    Schmitt, A.3    De Lange, T.4
  • 32
    • 0034687248 scopus 로고    scopus 로고
    • Tankyrase promotes telomere elongation in human cells
    • Smith S. and de Lange T. (2000) Tankyrase promotes telomere elongation in human cells. Curr. Biol. 10, 1299-1302.
    • (2000) Curr. Biol. , vol.10 , pp. 1299-1302
    • Smith, S.1    De Lange, T.2
  • 33
    • 0034623934 scopus 로고    scopus 로고
    • Tankyrase is a golgi-associated MAP kinase substrate that interacts with IRAP in GLUT4 vesicles
    • Chi N.W. and Lodish H.F. (2000) Tankyrase is a golgi-associated MAP kinase substrate that interacts with IRAP in GLUT4 vesicles. J. Biol. Chem. 275, 38,437-38,444.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38437-38444
    • Chi, N.W.1    Lodish, H.F.2
  • 34
    • 0035907257 scopus 로고    scopus 로고
    • Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14
    • Lyons R.J., Deane R., Lynch D.K., et al. (2001) Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14. J. Biol. Chem. 276, 17,172-17,180.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17172-17180
    • Lyons, R.J.1    Deane, R.2    Lynch, D.K.3
  • 35
    • 0035929591 scopus 로고    scopus 로고
    • TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression
    • Kaminker P.G., Kim S.H., Taylor R.D., et al. (2001) TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression. J. Biol. Chem. 276, 35,891-35,899.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35891-35899
    • Kaminker, P.G.1    Kim, S.H.2    Taylor, R.D.3
  • 36
    • 0032873278 scopus 로고    scopus 로고
    • The 193kD ault protein, VPARP, is a novel poly(ADP-ribose) polymerase
    • Kickhoefer V.A., Siva A.C., Kedersha N.L., et al. (1999) The 193kD ault protein, VPARP, is a novel poly(ADP-ribose) polymerase. J. Cell Biol. 146, 917-928.
    • (1999) J. Cell Biol. , vol.146 , pp. 917-928
    • Kickhoefer, V.A.1    Siva, A.C.2    Kedersha, N.L.3
  • 37
    • 12944332086 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation basally activated by DNA strand breaks reflects glutamate-nitric oxide neurotransmission
    • Pieper A.A., Blackshaw S., Clements E.E., et al. (2000) Poly(ADP-ribosyl)ation basally activated by DNA strand breaks reflects glutamate-nitric oxide neurotransmission. Proc. Natl. Acad. Sci. USA 97, 1845-1850.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1845-1850
    • Pieper, A.A.1    Blackshaw, S.2    Clements, E.E.3
  • 38
    • 0031844311 scopus 로고    scopus 로고
    • XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
    • Masson M., Niedergang C., Schreiber V., Muller S., Menissier-de Murcia J., and de Murcia G. (1998) XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol. Cell. Biol. 18, 3563-3571.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3563-3571
    • Masson, M.1    Niedergang, C.2    Schreiber, V.3    Muller, S.4    Menissier-De Murcia, J.5    De Murcia, G.6
  • 39
    • 0028090317 scopus 로고
    • Inhibitors and activators of ADP-ribosylation reactions
    • Banasik M. and Ueda K. (1994) Inhibitors and activators of ADP-ribosylation reactions. Mol. Cell. Biochem. 138, 185-197.
    • (1994) Mol. Cell. Biochem. , vol.138 , pp. 185-197
    • Banasik, M.1    Ueda, K.2
  • 40
    • 0345824718 scopus 로고    scopus 로고
    • Regulation of enzymatic catalysis of poly(ADP-ribose) polymerase by dsDNA, polyamines, Mg2+, Ca2+, histones H1 and H3 and ATP
    • Kun E., Kirsten E., Mendeleyev J., and Ordahl C.P. (2004) Regulation of enzymatic catalysis of poly(ADP-ribose) polymerase by dsDNA, polyamines, Mg2+, Ca2+, histones H1 and H3 and ATP Biochemistry 43, 210-216.
    • (2004) Biochemistry , vol.43 , pp. 210-216
    • Kun, E.1    Kirsten, E.2    Mendeleyev, J.3    Ordahl, C.P.4
  • 41
    • 0035161896 scopus 로고    scopus 로고
    • Purines inhibit poly(ADP-ribose) polymerase activation and modulate oxidant-induced cell death
    • Virag L. and Szabo C. (2001) Purines inhibit poly(ADP-ribose) polymerase activation and modulate oxidant-induced cell death. FASEB J. 15, 99-107.
    • (2001) FASEB J. , vol.15 , pp. 99-107
    • Virag, L.1    Szabo, C.2
  • 42
    • 0032486256 scopus 로고    scopus 로고
    • Stimulation of the DNA-dependent protein kinase by poly(ADP-ribose) polymerase
    • Ruscetti T., Lehnert B.E., Halbrook J., et al. (1998) Stimulation of the DNA-dependent protein kinase by poly(ADP-ribose) polymerase. J. Biol. Chem. 273, 14,461-14,467.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14461-14467
    • Ruscetti, T.1    Lehnert, B.E.2    Halbrook, J.3
  • 43
    • 1342285197 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase (PARP-1) and p53 independently function in regulating double-strand break repair in primate cells
    • Susse S., Scholz C.J., Burkle A., and Wiesmuller L. (2004) Poly(ADP-ribose) polymerase (PARP-1) and p53 independently function in regulating double-strand break repair in primate cells. Nucleic Acids Res. 32(2), 669-680.
    • (2004) Nucleic Acids Res. , vol.32 , Issue.2 , pp. 669-680
    • Susse, S.1    Scholz, C.J.2    Burkle, A.3    Wiesmuller, L.4
  • 44
    • 0034710285 scopus 로고    scopus 로고
    • A fast signal-induced activation of poly(ADP-ribose) polymerase: A novel downstream target of phospholipase C
    • Homburg S., Visochek L., Moran N., et al. (2000) A fast signal-induced activation of poly(ADP-ribose) polymerase: a novel downstream target of phospholipase C. J. Cell Biol. 150, 293-307.
    • (2000) J. Cell Biol. , vol.150 , pp. 293-307
    • Homburg, S.1    Visochek, L.2    Moran, N.3
  • 45
    • 24644443458 scopus 로고    scopus 로고
    • NMDA receptor mediated PARP activity in hippocampus of adult and aged brain. Effect of amyloid
    • Strosznajder R.P., Jesko H., and Strosznajder J. (1999) NMDA receptor mediated PARP activity in hippocampus of adult and aged brain. Effect of amyloid. Biochimie 81(Suppl. 6), s273.
    • (1999) Biochimie , vol.81 , Issue.6 SUPPL.
    • Strosznajder, R.P.1    Jesko, H.2    Strosznajder, J.3
  • 46
    • 0346511580 scopus 로고    scopus 로고
    • Effect of amyloid beta peptide on cholinergic receptor mediated poly(ADP-ribose)polymerase activity in rat brain
    • Zambrzycka A. and Strosznajder J.B. (2001) Effect of amyloid beta peptide on cholinergic receptor mediated poly(ADP-ribose)polymerase activity in rat brain. Folia Neuropathol. 39(Suppl. A), 51-54.
    • (2001) Folia Neuropathol. , vol.39 , Issue.SUPPL. A , pp. 51-54
    • Zambrzycka, A.1    Strosznajder, J.B.2
  • 47
    • 0030842946 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase gene disruption renders mice resistant to cerebral ischemia
    • Eliasson M.J., Sampei K., Mandir A.S., et al. (1997) Poly(ADP-ribose) polymerase gene disruption renders mice resistant to cerebral ischemia. Nat. Med. 3, 1089-1095.
    • (1997) Nat. Med. , vol.3 , pp. 1089-1095
    • Eliasson, M.J.1    Sampei, K.2    Mandir, A.S.3
  • 48
  • 49
    • 0034329823 scopus 로고    scopus 로고
    • NMDA but not non-NMDA excitotoxicity is mediated by poly(ADP-ribose) polymerase
    • Mandir A.S., Poitras M.F., Berliner A.R., et al. (2000) NMDA but not non-NMDA excitotoxicity is mediated by poly(ADP-ribose) polymerase. J. Neurosci. 20, 8005-8011.
    • (2000) J. Neurosci. , vol.20 , pp. 8005-8011
    • Mandir, A.S.1    Poitras, M.F.2    Berliner, A.R.3
  • 51
    • 0026751781 scopus 로고
    • The dose-response relationship and therapeutic window for dizocilpine (MK-801) in a rat focal ischaemia model
    • Hatfield R.H., Gill R., and Brazell C. (1992) The dose-response relationship and therapeutic window for dizocilpine (MK-801) in a rat focal ischaemia model. Eur. J. Pharmacol. 216, 1-7.
    • (1992) Eur. J. Pharmacol. , vol.216 , pp. 1-7
    • Hatfield, R.H.1    Gill, R.2    Brazell, C.3
  • 52
    • 0032403461 scopus 로고    scopus 로고
    • NMDA receptor-dependent nitric oxide and cGMP synthesis in brain hemispheres and cerebellum during reperfusion after transient forebrain ischemia in gerbils: Effect of 7-nitroindazole
    • Chalimoniuk M. and Strosznajder J. (1998) NMDA receptor-dependent nitric oxide and cGMP synthesis in brain hemispheres and cerebellum during reperfusion after transient forebrain ischemia in gerbils: effect of 7-nitroindazole. J. Neurosci. Res. 54, 681-690.
    • (1998) J. Neurosci. Res. , vol.54 , pp. 681-690
    • Chalimoniuk, M.1    Strosznajder, J.2
  • 53
    • 0031946532 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribose) polymerase - Reduction of ischemic injury and attenuation of N-methyl-D-aspartate-induced neurotransmitter dysregulation
    • Lo E.H., Bosque-Hamilton P., and Meng W. (1998) Inhibition of poly(ADP-ribose) polymerase - reduction of ischemic injury and attenuation of N-methyl-D-aspartate-induced neurotransmitter dysregulation Stroke 29, 830-836.
    • (1998) Stroke , vol.29 , pp. 830-836
    • Lo, E.H.1    Bosque-Hamilton, P.2    Meng, W.3
  • 54
    • 0032127666 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) synthetase in inflammation and ischaemia-reperfusion
    • Szabo C. and Dawson V.L. (1998) Role of poly(ADP-ribose) synthetase in inflammation and ischaemia-reperfusion. Trends Pharmacol. Sci. 19(7), 287-298.
    • (1998) Trends Pharmacol. Sci. , vol.19 , Issue.7 , pp. 287-298
    • Szabo, C.1    Dawson, V.L.2
  • 55
    • 0027280338 scopus 로고
    • Pathological implications of nitric oxide, superoxide and peroxynitrite formation
    • Beckman J.S. and Crow J.P. (1993) Pathological implications of nitric oxide, superoxide and peroxynitrite formation. Biochem. Soc. Trans. 21, 330-334.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 330-334
    • Beckman, J.S.1    Crow, J.P.2
  • 56
    • 0032557410 scopus 로고    scopus 로고
    • Role of peroxynitrite and neuronal nitric oxide synthase in the activation of poly(ADP-ribose) synthetase in a murine model of cerebral ischemia-reperfusion
    • Endres M., Scott G., Namura S., et al. (1998) Role of peroxynitrite and neuronal nitric oxide synthase in the activation of poly(ADP-ribose) synthetase in a murine model of cerebral ischemia-reperfusion. Neurosci. Lett. 248, 41-44.
    • (1998) Neurosci. Lett. , vol.248 , pp. 41-44
    • Endres, M.1    Scott, G.2    Namura, S.3
  • 57
    • 0348109491 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 and apoptosis inducing factor in neurotoxicity
    • Yu S.W., Wang H., Dawson T.M., and Dawson V.L. (2003) Poly(ADP-ribose) polymerase-1 and apoptosis inducing factor in neurotoxicity. Neurobiol. Dis. 14(3), 303-317.
    • (2003) Neurobiol. Dis. , vol.14 , Issue.3 , pp. 303-317
    • Yu, S.W.1    Wang, H.2    Dawson, T.M.3    Dawson, V.L.4
  • 58
    • 0037067317 scopus 로고    scopus 로고
    • Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor
    • Yu S.W., Wang H., Poitras M.F., et al. (2002) Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor. Science. 297(5579), 259-263.
    • (2002) Science , vol.297 , Issue.5579 , pp. 259-263
    • Yu, S.W.1    Wang, H.2    Poitras, M.F.3
  • 59
    • 0037067597 scopus 로고    scopus 로고
    • PARP-1 - A perpetrator of apoptotic cell death?
    • Chiarugi A. and Moskowitz M.A. (2002) PARP-1 - a perpetrator of apoptotic cell death? Science 297, 200-201.
    • (2002) Science , vol.297 , pp. 200-201
    • Chiarugi, A.1    Moskowitz, M.A.2
  • 60
    • 0030862138 scopus 로고    scopus 로고
    • Neuroprotective effects of inhibiting poly(ADP-ribose) synthetase on focal cerebral ischemia in rats
    • Takahashi K., Greenberg J.H., Jackson P., Maclin K., and Zhang J. (1997) Neuroprotective effects of inhibiting poly(ADP-ribose) synthetase on focal cerebral ischemia in rats. J. Cereb. Blood Flow Metab. 17, 1137-1142.
    • (1997) J. Cereb. Blood Flow Metab. , vol.17 , pp. 1137-1142
    • Takahashi, K.1    Greenberg, J.H.2    Jackson, P.3    Maclin, K.4    Zhang, J.5
  • 61
    • 0033551597 scopus 로고    scopus 로고
    • The effect of reperfusion on neuroprotection using an inhibitor of poly(ADP-ribose) polymerase
    • Takahashi K. and Greenberg J.H. (1999) The effect of reperfusion on neuroprotection using an inhibitor of poly(ADP-ribose) polymerase. Neuroreport 10, 2017-2022.
    • (1999) Neuroreport , vol.10 , pp. 2017-2022
    • Takahashi, K.1    Greenberg, J.H.2
  • 62
    • 0031281259 scopus 로고    scopus 로고
    • Protection against myocardial ischemia and reperfusion injury by 3-aminobenzamide, an inhibitor of poly(ADP-ribose) synthetase
    • Zingarelli B., Cuzzocrea S., Zsengeller Z., Salzman A.L., and Szabo C. (1997) Protection against myocardial ischemia and reperfusion injury by 3-aminobenzamide, an inhibitor of poly(ADP-ribose) synthetase. Cardiovasc. Res. 36, 205-215.
    • (1997) Cardiovasc. Res. , vol.36 , pp. 205-215
    • Zingarelli, B.1    Cuzzocrea, S.2    Zsengeller, Z.3    Salzman, A.L.4    Szabo, C.5
  • 63
    • 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., and 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. Circ. Res. 83, 85-94.
    • (1998) Circ. Res. , vol.83 , pp. 85-94
    • Zingarelli, B.1    Salzman, A.L.2    Szabo, C.3
  • 64
    • 0034697060 scopus 로고    scopus 로고
    • The neuroprotective effect of cerebral poly(ADP-ribose) polymerase inhibition in a rat model of global ischemia
    • Plaschke K., Kopitz J., Weigand M.A., Martin E., and Bardenheuer H.J. (2000) The neuroprotective effect of cerebral poly(ADP-ribose) polymerase inhibition in a rat model of global ischemia. Neurosci. Lett. 284(1-2), 109-112.
    • (2000) Neurosci. Lett. , vol.284 , Issue.1-2 , pp. 109-112
    • Plaschke, K.1    Kopitz, J.2    Weigand, M.A.3    Martin, E.4    Bardenheuer, H.J.5
  • 65
    • 0034068520 scopus 로고    scopus 로고
    • Activation of poly(ADP-ribose) polymerase in the rat hippocampus may contribute to cellular recovery following sublethal transient global ischemia
    • Nagayama T., Simon R.P., Chen D., et al. (2000) Activation of poly(ADP-ribose) polymerase in the rat hippocampus may contribute to cellular recovery following sublethal transient global ischemia. J. Neurochem. 74(4), 1636-1645.
    • (2000) J. Neurochem. , vol.74 , Issue.4 , pp. 1636-1645
    • Nagayama, T.1    Simon, R.P.2    Chen, D.3
  • 66
    • 0034868256 scopus 로고    scopus 로고
    • Poly(ADP-ribose)polymerase inhibitors attenuate necrotic but not apoptotic neuronal death in experimental models of cerebral ischemia
    • Moroni F., Meli E., Peruginelli F., et al. (2001) Poly(ADP-ribose) polymerase inhibitors attenuate necrotic but not apoptotic neuronal death in experimental models of cerebral ischemia. Cell Death Differ. 8(9), 921-932.
    • (2001) Cell Death Differ. , vol.8 , Issue.9 , pp. 921-932
    • Moroni, F.1    Meli, E.2    Peruginelli, F.3
  • 67
    • 0037304954 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase during reperfusion after transient forebrain ischemia: Its role in brain edema and cell death
    • Strosznajder R.P., Gadamski R., Czapski G.A., Jesko H., and Strosznajder J.B. (2003) Poly(ADP-ribose) polymerase during reperfusion after transient forebrain ischemia: its role in brain edema and cell death. J. Mol. Neurosci. 20, 61-72.
    • (2003) J. Mol. Neurosci. , vol.20 , pp. 61-72
    • Strosznajder, R.P.1    Gadamski, R.2    Czapski, G.A.3    Jesko, H.4    Strosznajder, J.B.5
  • 68
    • 0031020434 scopus 로고    scopus 로고
    • Inhibition of the activity of poly (ADP-ribose) synthetase reduces ischemia-reperfusion injury in the heart and skeletal muscle
    • Thiemermann C., Bowes J., Myint F.P., and Vane J.R. (1997) Inhibition of the activity of poly (ADP-ribose) synthetase reduces ischemia-reperfusion injury in the heart and skeletal muscle. Proc. Natl. Acad. Sci. USA 94, 679-683.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 679-683
    • Thiemermann, C.1    Bowes, J.2    Myint, F.P.3    Vane, J.R.4
  • 70
    • 0021340281 scopus 로고
    • Inhibitors of poly(adenosine diphosphate-ribose) synthesis: Effect on other metabolic processes
    • Milam K.M. and Cleaver J.E. (1984) Inhibitors of poly(adenosine diphosphate-ribose) synthesis: effect on other metabolic processes. Science 223, 589-591.
    • (1984) Science , vol.223 , pp. 589-591
    • Milam, K.M.1    Cleaver, J.E.2
  • 71
    • 0000528542 scopus 로고
    • Benzamide and its derivatives inhibit nicotinamide methylation as well as ADP-ribosylation
    • Johnson G.S. (1981) Benzamide and its derivatives inhibit nicotinamide methylation as well as ADP-ribosylation. Biochem. Int. 2, 611-617.
    • (1981) Biochem. Int. , vol.2 , pp. 611-617
    • Johnson, G.S.1
  • 72
    • 24644481214 scopus 로고    scopus 로고
    • Effect of 3-aminobenzamide on ultrastructural alteration in CA1 layer of hippocampus after global ischemia in gerbils
    • Strosznajder R.P. and Walski M. (2004) Effect of 3-aminobenzamide on ultrastructural alteration in CA1 layer of hippocampus after global ischemia in gerbils. J. Physiol. Pharmacol., 55, Suppl. 3, 127-133.
    • (2004) J. Physiol. Pharmacol. , vol.55 , Issue.3 SUPPL. , pp. 127-133
    • Strosznajder, R.P.1    Walski, M.2
  • 73
    • 0032125488 scopus 로고    scopus 로고
    • Neurodegeneration in excitotoxicity global cerebral ischemia, and target deprivation: A perspective on the contributions of apoptosis and necrosis
    • Martin L.J., Al-Abdulla N.A., Brambrink A.M., Kirsch J.R., Sieber F.E., and Portera-Cailliau C. (1998) Neurodegeneration in excitotoxicity global cerebral ischemia, and target deprivation: A perspective on the contributions of apoptosis and necrosis. Brain Res. Bull. 46, 281-309.
    • (1998) Brain Res. Bull. , vol.46 , pp. 281-309
    • Martin, L.J.1    Al-Abdulla, N.A.2    Brambrink, A.M.3    Kirsch, J.R.4    Sieber, F.E.5    Portera-Cailliau, C.6
  • 74
    • 0032845121 scopus 로고    scopus 로고
    • Ischemic cell death in brain neurons
    • Lipton P. (1999) Ischemic cell death in brain neurons. Physiol. Rev. 79, 1431-1568.
    • (1999) Physiol. Rev. , vol.79 , pp. 1431-1568
    • Lipton, P.1
  • 75
    • 0033083559 scopus 로고    scopus 로고
    • Neuronal cell death: A demise with different shapes
    • Nicotera P., Leist M., and Manzo L. (1999) Neuronal cell death: a demise with different shapes. Trends Pharmacol. Sci. 20, 46-51.
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 46-51
    • Nicotera, P.1    Leist, M.2    Manzo, L.3
  • 76
    • 0034233751 scopus 로고    scopus 로고
    • Effects of transient global ischemia and kainate on poly(ADP-ribose) polymerase (PARP) gene expression and proteolytic cleavage in gerbil and rat brains
    • Liu J., Ying W., Massa S., et al. (2000) Effects of transient global ischemia and kainate on poly(ADP-ribose) polymerase (PARP) gene expression and proteolytic cleavage in gerbil and rat brains. Brain Res. Mol. Brain Res. 80, 7-16.
    • (2000) Brain Res. Mol. Brain Res. , vol.80 , pp. 7-16
    • Liu, J.1    Ying, W.2    Massa, S.3
  • 77
    • 0032979742 scopus 로고    scopus 로고
    • Novel non-apoptotic morphological changes in neurons of the mouse hippocampus following transient hypoxic-ischemia
    • Fukuda T., Wang H., Nakanishi H., Yamamoto K., and Kosaka T. (1999) Novel non-apoptotic morphological changes in neurons of the mouse hippocampus following transient hypoxic-ischemia. Neurosci. Res. 33, 49-55.
    • (1999) Neurosci. Res. , vol.33 , pp. 49-55
    • Fukuda, T.1    Wang, H.2    Nakanishi, H.3    Yamamoto, K.4    Kosaka, T.5
  • 78
    • 0842277725 scopus 로고    scopus 로고
    • 3-Aminobenzamide reduces brain infarction and neutrophil infiltration after transient focal cerebral ischemia in mice
    • Couturier J.Y., Ding-Zhou L., Croci N., Plotkine M., and Margaill I. (2003) 3-Aminobenzamide reduces brain infarction and neutrophil infiltration after transient focal cerebral ischemia in mice. Exp. Neurol. 184(2), 973-980.
    • (2003) Exp. Neurol. , vol.184 , Issue.2 , pp. 973-980
    • Couturier, J.Y.1    Ding-Zhou, L.2    Croci, N.3    Plotkine, M.4    Margaill, I.5
  • 79
    • 0031946532 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribose) polymerase: Reduction of ischemic injury and attenuation of N-methyl-D-aspartate-induced neurotransmitter dysregulation
    • Lo E.H., Bosque-Hamilton P., and Meng W. (1998) Inhibition of poly(ADP-ribose) polymerase: reduction of ischemic injury and attenuation of N-methyl-D-aspartate-induced neurotransmitter dysregulation. Stroke 29(4), 830-836.
    • (1998) Stroke , vol.29 , Issue.4 , pp. 830-836
    • Lo, E.H.1    Bosque-Hamilton, P.2    Meng, W.3
  • 80
    • 0035850884 scopus 로고    scopus 로고
    • Long-term neuroprotective effect of inhibiting poly(ADP-ribose) polymerase in rats with middle cerebral artery occlusion using a behavioral assessment
    • Ding Y., Zhou Y., Lai Q., Li J., Gordon V., and Diaz F.G. (2001) Long-term neuroprotective effect of inhibiting poly(ADP-ribose) polymerase in rats with middle cerebral artery occlusion using a behavioral assessment. Brain Res. 915(2), 210-217.
    • (2001) Brain Res. , vol.915 , Issue.2 , pp. 210-217
    • Ding, Y.1    Zhou, Y.2    Lai, Q.3    Li, J.4    Gordon, V.5    Diaz, F.G.6
  • 81
    • 0033594743 scopus 로고    scopus 로고
    • Post-treatment with an inhibitor of poly(ADP-ribose) polymerase attenuates cerebral damage in focal ischemia
    • Takahashi K., Pieper A.A., Croul S.E., Zhang J., Snyder S.H., and Greenberg J.H. (1999) Post-treatment with an inhibitor of poly(ADP-ribose) polymerase attenuates cerebral damage in focal ischemia. Brain Res. 829(1-2), 46-54.
    • (1999) Brain Res. , vol.829 , Issue.1-2 , pp. 46-54
    • Takahashi, K.1    Pieper, A.A.2    Croul, S.E.3    Zhang, J.4    Snyder, S.H.5    Greenberg, J.H.6
  • 82
    • 0344721492 scopus 로고    scopus 로고
    • Resistance to endotoxic shock as a consequence of defective NF-kappaB activation in poly(ADP-ribose) polymerase-1 deficient mice
    • Oliver F.J., Menissier-de Murcia J., Nacci C., et al. (1999) Resistance to endotoxic shock as a consequence of defective NF-kappaB activation in poly(ADP-ribose) polymerase-1 deficient mice. EMBO J. 18, 4446-4454.
    • (1999) EMBO J. , vol.18 , pp. 4446-4454
    • Oliver, F.J.1    Menissier-De Murcia, J.2    Nacci, C.3
  • 83
    • 0030842791 scopus 로고    scopus 로고
    • Defective induction but normal activation and function of p53 in mouse cells lacking poly-ADP-ribose polymerase
    • Agarwal M.L., Agarwal A., Taylor W.R., Wang Z.Q., Wagner E.F., and Stark G.R. (1997) Defective induction but normal activation and function of p53 in mouse cells lacking poly-ADP-ribose polymerase. Oncogene 15, 1035-1041.
    • (1997) Oncogene , vol.15 , pp. 1035-1041
    • Agarwal, M.L.1    Agarwal, A.2    Taylor, W.R.3    Wang, Z.Q.4    Wagner, E.F.5    Stark, G.R.6
  • 84
    • 0033573886 scopus 로고    scopus 로고
    • Compensatory expression of p73 in PARP-deficient mouse fibroblasts as response to a reduced level of regularly spliced wild-type p53 protein
    • Schmid G., Wang Z.Q., and Wesierska-Gadek J. (1999) Compensatory expression of p73 in PARP-deficient mouse fibroblasts as response to a reduced level of regularly spliced wild-type p53 protein. Biochem. Biophys. Res. Commun. 255, 399-405.
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 399-405
    • Schmid, G.1    Wang, Z.Q.2    Wesierska-Gadek, J.3
  • 85
    • 0026753708 scopus 로고
    • Mechanism of c-fos induction by active oxygen
    • Amstad P.A., Krupitza G., and Cerutti P.A. (1992) Mechanism of c-fos induction by active oxygen. Cancer Res. 52, 3952-3960.
    • (1992) Cancer Res. , vol.52 , pp. 3952-3960
    • Amstad, P.A.1    Krupitza, G.2    Cerutti, P.A.3
  • 86
    • 0037022627 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 dependence of stress-induced transcription factors and associated gene expression in glia
    • Ha H.C., Hester L.D., and Snyder S.H. (2002) Poly(ADP-ribose) polymerase-1 dependence of stress-induced transcription factors and associated gene expression in glia. Proc. Natl. Acad. Sci. USA 99, 3270-3275.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3270-3275
    • Ha, H.C.1    Hester, L.D.2    Snyder, S.H.3
  • 87
    • 0037387772 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 activity promotes NF-κB-driven transcription and microglial activation: Implication for neurodegenerative disorders
    • Chiarugi A. and Moskowitz M.A. (2003) Poly(ADP-ribose) polymerase-1 activity promotes NF-κB-driven transcription and microglial activation: implication for neurodegenerative disorders. J. Neurochem. 85, 306-317.
    • (2003) J. Neurochem. , vol.85 , pp. 306-317
    • Chiarugi, A.1    Moskowitz, M.A.2
  • 88
    • 0035824647 scopus 로고    scopus 로고
    • The enzymatic and DNA binding activity of PARP-1 are not required for NF-kappa B coactivator function
    • Hassa P.O., Covic M., Hasan S., Imhof R., and Hottiger M.O. (2001) The enzymatic and DNA binding activity of PARP-1 are not required for NF-kappa B coactivator function. J. Biol. Chem. 276, 45,588-45,597.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45588-45597
    • Hassa, P.O.1    Covic, M.2    Hasan, S.3    Imhof, R.4    Hottiger, M.O.5
  • 89
    • 0034654055 scopus 로고    scopus 로고
    • Evidence for regulation of NF-kappaB by poly(ADP-ribose) polymerase
    • Kameoka M., Ota K., Tetsuka T., et al. (2000) Evidence for regulation of NF-kappaB by poly(ADP-ribose) polymerase. Biochem. J. 346, 641-649.
    • (2000) Biochem. J. , vol.346 , pp. 641-649
    • Kameoka, M.1    Ota, K.2    Tetsuka, T.3
  • 90
    • 0043125662 scopus 로고    scopus 로고
    • Phosphorylation regulates the interaction and complex formation between wt p53 protein and PARP-1
    • Wesierska-Gadek J., Wojciechowski J., and Schmid G. (2003) Phosphorylation regulates the interaction and complex formation between wt p53 protein and PARP-1. J. Cell Biochem. 89(6), 1260-1284.
    • (2003) J. Cell Biochem. , vol.89 , Issue.6 , pp. 1260-1284
    • Wesierska-Gadek, J.1    Wojciechowski, J.2    Schmid, G.3
  • 91
    • 0034891887 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation of p53 in vitro and in vivo modulates binding to its DNA consensus sequence
    • Simbulan-Rosenthal C.M., Rosenthal D.S., Luo R.B., et al. (2001) Poly(ADP-ribosyl)ation of p53 in vitro and in vivo modulates binding to its DNA consensus sequence. Neoplasia 3, 179-188.
    • (2001) Neoplasia , vol.3 , pp. 179-188
    • Simbulan-Rosenthal, C.M.1    Rosenthal, D.S.2    Luo, R.B.3
  • 92
    • 0035965257 scopus 로고    scopus 로고
    • Regulation of p53 sequence-specific DNA-binding by covalent poly(ADP-ribosyl)ation
    • Mendoza-Alvarez H. and Alvarez-Gonzalez R. (2001) Regulation of p53 sequence-specific DNA-binding by covalent poly(ADP-ribosyl)ation. J. Biol. Chem. 276(39), 36,425-36,430.
    • (2001) J. Biol. Chem. , vol.276 , Issue.39 , pp. 36425-36430
    • Mendoza-Alvarez, H.1    Alvarez-Gonzalez, R.2
  • 93
    • 0033759112 scopus 로고    scopus 로고
    • Overexpressed poly(ADP-ribose) polymerase delays the release of rat cells from p53-mediated G(1) checkpoint
    • Wesierska-Gadek J. and Schmid G. (2000) Overexpressed poly(ADP-ribose) polymerase delays the release of rat cells from p53-mediated G(1) checkpoint. J. Cell Biochem. 80(1), 85-103.
    • (2000) J. Cell Biochem. , vol.80 , Issue.1 , pp. 85-103
    • Wesierska-Gadek, J.1    Schmid, G.2
  • 94
    • 0034961678 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 regulates the stability of the wild-type p53 protein
    • Wesierska-Gadek J. and Schmid G. (2001) Poly(ADP-ribose) polymerase-1 regulates the stability of the wild-type p53 protein. Cell. Mol. Biol. Lett. 6(2), 117-140.
    • (2001) Cell. Mol. Biol. Lett. , vol.6 , Issue.2 , pp. 117-140
    • Wesierska-Gadek, J.1    Schmid, G.2
  • 95
    • 0036788183 scopus 로고    scopus 로고
    • A novel in vivo post-translational modification of p53 by PARP-1 in MPTP-induced parkinsonism
    • Mandir A.S., Simbulan-Rosenthal C.M., Poitras M.F., et al. (2002) A novel in vivo post-translational modification of p53 by PARP-1 in MPTP-induced parkinsonism. J. Neurochem. 83(1), 186-192.
    • (2002) J. Neurochem. , vol.83 , Issue.1 , pp. 186-192
    • Mandir, A.S.1    Simbulan-Rosenthal, C.M.2    Poitras, M.F.3
  • 96
    • 0032919454 scopus 로고    scopus 로고
    • Reduced stability of regularly spliced but not alternatively spliced p53 protein in PARP-deficient mouse fibroblasts
    • Wesierska-Gadek J., Wang Z.Q., and Schmid G. (1999) Reduced stability of regularly spliced but not alternatively spliced p53 protein in PARP-deficient mouse fibroblasts. Cancer Res. 59(1), 28-34.
    • (1999) Cancer Res. , vol.59 , Issue.1 , pp. 28-34
    • Wesierska-Gadek, J.1    Wang, Z.Q.2    Schmid, G.3
  • 97
    • 0038034413 scopus 로고    scopus 로고
    • Central and carboxy-terminal regions of human p53 protein are essential for interaction and complex formation with PARP-1
    • Wesierska-Gadek J., Wojciechowski J., and Schmid G. (2003) Central and carboxy-terminal regions of human p53 protein are essential for interaction and complex formation with PARP-1. J. Cell. Biochem. 89(2), 220-232.
    • (2003) J. Cell. Biochem. , vol.89 , Issue.2 , pp. 220-232
    • Wesierska-Gadek, J.1    Wojciechowski, J.2    Schmid, G.3
  • 98
    • 85047697499 scopus 로고    scopus 로고
    • PARP-1 modifies the effectiveness of p53-mediated DNA damage response
    • Valenzuela M.T., Guerrero R., Núnez M.I., et al. (2002) PARP-1 modifies the effectiveness of p53-mediated DNA damage response. Oncogene 21(7), 1108-1116.
    • (2002) Oncogene , vol.21 , Issue.7 , pp. 1108-1116
    • Valenzuela, M.T.1    Guerrero, R.2    Núnez, M.I.3
  • 99
    • 0030761351 scopus 로고    scopus 로고
    • ATM-dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the post-translational activation of p53 protein involving poly(ADP-ribose) polymerase
    • Vaziri H., West M.D., Allsopp R.C., et al. (1997) ATM-dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the post-translational activation of p53 protein involving poly(ADP-ribose) polymerase. EMBO J. 16(19), 6018-6033.
    • (1997) EMBO J. , vol.16 , Issue.19 , pp. 6018-6033
    • Vaziri, H.1    West, M.D.2    Allsopp, R.C.3
  • 100
    • 0032481112 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation is required for p53-dependent signal transduction induced by radiation
    • Wang X., Ohnishi K., Takahashi A., and Ohnishi T. (1998) Poly(ADP-ribosyl)ation is required for p53-dependent signal transduction induced by radiation. Oncogene 17(22), 2819-2825.
    • (1998) Oncogene , vol.17 , Issue.22 , pp. 2819-2825
    • Wang, X.1    Ohnishi, K.2    Takahashi, A.3    Ohnishi, T.4
  • 101
    • 0029099358 scopus 로고
    • Involvement of NAD-poly(ADP-ribose) metabolism in p53 regulation and its consequences
    • Whitacre C.M., Hashimoto H., Tsai M.L., Chatterjee S., Berger S.J., and Berger N.A. (1995) Involvement of NAD-poly(ADP-ribose) metabolism in p53 regulation and its consequences. Cancer Res. 55(17), 3697-3701.
    • (1995) Cancer Res. , vol.55 , Issue.17 , pp. 3697-3701
    • Whitacre, C.M.1    Hashimoto, H.2    Tsai, M.L.3    Chatterjee, S.4    Berger, S.J.5    Berger, N.A.6
  • 102
    • 0037805627 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 is a positive regulator of the p53-mediated G1 arrest response following ionizing radiation
    • Wieler S., Gagné J.P, Vaziri H., Poirier G.G., and Benchimol S. (2003) Poly(ADP-ribose) polymerase-1 is a positive regulator of the p53-mediated G1 arrest response following ionizing radiation. J. Biol. Chem. 278(21), 18,914-18,921.
    • (2003) J. Biol. Chem. , vol.278 , Issue.21 , pp. 18914-18921
    • Wieler, S.1    Gagné, J.P.2    Vaziri, H.3    Poirier, G.G.4    Benchimol, S.5
  • 103
    • 0032981214 scopus 로고    scopus 로고
    • Activation of p53 and its target genes p21(WAF1/Cip1) and PAG608/Wig-1 in ischemic preconditioning
    • Tomasevic G., Shamloo M., Israeli D., and Wieloch T. (1999) Activation of p53 and its target genes p21(WAF1/Cip1) and PAG608/Wig-1 in ischemic preconditioning. Brain Res. Mol. Brain Res. 70, 304-313.
    • (1999) Brain Res. Mol. Brain Res. , vol.70 , pp. 304-313
    • Tomasevic, G.1    Shamloo, M.2    Israeli, D.3    Wieloch, T.4
  • 104
    • 0033135756 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation of p53 during apoptosis in human osteosarcoma cells
    • Simbulan-Rosenthal C.M., Rosenthal D.S., Luo R., and Smulson M.E. (1999) Poly(ADP-ribosyl)ation of p53 during apoptosis in human osteosarcoma cells. Cancer Res. 59(9), 2190-2194.
    • (1999) Cancer Res. , vol.59 , Issue.9 , pp. 2190-2194
    • Simbulan-Rosenthal, C.M.1    Rosenthal, D.S.2    Luo, R.3    Smulson, M.E.4
  • 105
    • 0032533856 scopus 로고    scopus 로고
    • Functional interactions of p53 with poly(ADP-ribose) polymerase (PARP) during apoptosis following DNA damage: Covalent poly(ADP-ribosyl)ation of p53 by exogenous PARP and noncovalent binding of p53 to the M(r) 85,000 proteolytic fragment
    • Kumari S.R., Mendoza-Alvarez H., and Alvarez-Gonzalez R. (1998) Functional interactions of p53 with poly(ADP-ribose) polymerase (PARP) during apoptosis following DNA damage: covalent poly(ADP-ribosyl)ation of p53 by exogenous PARP and noncovalent binding of p53 to the M(r) 85,000 proteolytic fragment. Cancer Res. 58(22), 5075-5078.
    • (1998) Cancer Res. , vol.58 , Issue.22 , pp. 5075-5078
    • Kumari, S.R.1    Mendoza-Alvarez, H.2    Alvarez-Gonzalez, R.3
  • 106
    • 0038682011 scopus 로고    scopus 로고
    • PARP goes transcription
    • Kraus W.L. and Lis J.T. (2003) PARP goes transcription. Cell 113, 677-683.
    • (2003) Cell , vol.113 , pp. 677-683
    • Kraus, W.L.1    Lis, J.T.2
  • 107
    • 0027275493 scopus 로고
    • The US-1 element from the gene encoding rat poly(ADP-ribose) polymerase binds the transcription factor Sp1
    • Potvin F., Roy R.J., Poirier G.G., and Guerin S.L. (1993) The US-1 element from the gene encoding rat poly(ADP-ribose) polymerase binds the transcription factor Sp1. Eur. J. Biochem. 215, 73-80.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 73-80
    • Potvin, F.1    Roy, R.J.2    Poirier, G.G.3    Guerin, S.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.