메뉴 건너뛰기




Volumn 58, Issue 22, 1998, Pages 5075-5078

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

Author keywords

[No Author keywords available]

Indexed keywords

METHYLNITRONITROSOGUANIDINE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN P53;

EID: 0032533856     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (80)

References (33)
  • 1
    • 0026504147 scopus 로고
    • Social controls on cell survival and cell death
    • Raff, M. C. Social controls on cell survival and cell death. Nature (Lond.) 356: 397-400, 1992.
    • (1992) Nature (Lond.) , vol.356 , pp. 397-400
    • Raff, M.C.1
  • 2
    • 0027247729 scopus 로고
    • The control of apoptosis in mammalian cells
    • Collins, M. K. L., and Rivas, A. L. The control of apoptosis in mammalian cells. Trends Biochem. Sci., 108: 307-309, 1993.
    • (1993) Trends Biochem. Sci. , vol.108 , pp. 307-309
    • Collins, M.K.L.1    Rivas, A.L.2
  • 3
    • 0028929328 scopus 로고
    • Mechanisms and genes in cellular suicide
    • Washington DC
    • Steller, H. Mechanisms and genes in cellular suicide. Science (Washington DC), 275: 1445-1449, 1995.
    • (1995) Science , vol.275 , pp. 1445-1449
    • Steller, H.1
  • 4
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson, M. D., Weil, M., and Raff, M. C. Programmed cell death in animal development. Cell, 88: 347-354, 1997.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 5
    • 0347766480 scopus 로고
    • Apoptosis, the molecular basis of cell death
    • Tomei, L. D., and Cope, F. O. (eds). Apoptosis, the molecular basis of cell death. Curr. Commun. Cell. Mol. Biol., 3: 1-321, 1991.
    • (1991) Curr. Commun. Cell. Mol. Biol. , vol.3 , pp. 1-321
    • Tomei, L.D.1    Cope, F.O.2
  • 7
    • 0027172322 scopus 로고
    • Molecular regulation of apoptosis: Genetic controls of cell death
    • Williams, G. T., and Smith, C. A. Molecular regulation of apoptosis: genetic controls of cell death. Cell, 74: 777-779, 1993.
    • (1993) Cell , vol.74 , pp. 777-779
    • Williams, G.T.1    Smith, C.A.2
  • 11
    • 0031044652 scopus 로고    scopus 로고
    • Mammalian cell-death proteases. A family of highly conserved aspartate-specific cysteine proteases
    • Alnemri, E. S. Mammalian cell-death proteases. A family of highly conserved aspartate-specific cysteine proteases. J. Cell. Biochem., 64: 33-42, 1997.
    • (1997) J. Cell. Biochem. , vol.64 , pp. 33-42
    • Alnemri, E.S.1
  • 13
    • 0024470862 scopus 로고
    • Induction of endonucleolytic DNA cleavage in human acute myelogenous leukemia cells by etoposide, camptothecin, and other cytotoxic anticancer drugs: A cautionary note
    • Kauffman, S. H. Induction of endonucleolytic DNA cleavage in human acute myelogenous leukemia cells by etoposide, camptothecin, and other cytotoxic anticancer drugs: a cautionary note. Cancer Res., 49: 5870-5878, 1989.
    • (1989) Cancer Res. , vol.49 , pp. 5870-5878
    • Kauffman, S.H.1
  • 14
    • 0027255417 scopus 로고
    • Specific proteolytic cleavage of poly(ADP- Ribose)polymerase: An early marker of chemotherapy-induced apoptosis
    • Kauffman, S. H., Desnoyers, S., Ottaviano, Y., Davidson, N. E., and Poirier, G. G. Specific proteolytic cleavage of poly(ADP-ribose)polymerase: an early marker of chemotherapy-induced apoptosis. Cancer Res., 53: 3976-3985, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 3976-3985
    • Kauffman, S.H.1    Desnoyers, S.2    Ottaviano, Y.3    Davidson, N.E.4    Poirier, G.G.5
  • 15
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik, Y. A., Kauffman, S. H., Desnoyers, S., Poirier, G. G., and Earnshaw, W. C. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature (Lond.), 371: 346-347, 1994.
    • (1994) Nature (Lond.) , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kauffman, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 16
    • 0030187244 scopus 로고    scopus 로고
    • Proteolytic cleavage during chemotherapy-induce apoptosis
    • Kauffman, S. H. Proteolytic cleavage during chemotherapy-induce apoptosis. Mol. Med. Today. 2: 298-303, 1996.
    • (1996) Mol. Med. Today , vol.2 , pp. 298-303
    • Kauffman, S.H.1
  • 17
    • 0030605878 scopus 로고    scopus 로고
    • Sequential activation of three distinct ICE-like activities in Fas-ligated Jurkat cells
    • Greidenger, E. L., Miller, D. K., Yamin, T-T., Casciola-Rosen, L., and Rosen, A. Sequential activation of three distinct ICE-like activities in Fas-ligated Jurkat cells. FEBS Lett., 390: 299-303, 1997.
    • (1997) FEBS Lett. , vol.390 , pp. 299-303
    • Greidenger, E.L.1    Miller, D.K.2    Yamin, T.-T.3    Casciola-Rosen, L.4    Rosen, A.5
  • 18
    • 0019321840 scopus 로고
    • ADP-ribosylation in mammalian cell ghosts: Dependence of poly(ADP-ribose) synthesis on strand breakage in DNA
    • Benjamin, R. C., and Gill, D. M. ADP-ribosylation in mammalian cell ghosts: dependence of poly(ADP-ribose) synthesis on strand breakage in DNA. J. Biol. Chem., 255: 10493-10501, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10493-10501
    • Benjamin, R.C.1    Gill, D.M.2
  • 19
    • 0027441894 scopus 로고
    • Poly(ADP- Ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular
    • Mendoza-Alvarez, H., and Alvarez-Gonzalez, R. Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular. J. Biol. Chem., 268: 22575-22580, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22575-22580
    • Mendoza-Alvarez, H.1    Alvarez-Gonzalez, R.2
  • 20
    • 0021140803 scopus 로고
    • ADP-ribosylation of nuclear proteins in vivo
    • Adamietz, P., and Rudolph, A. ADP-ribosylation of nuclear proteins in vivo. J. Biol. Chem., 259: 6841-6848, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6841-6848
    • Adamietz, P.1    Rudolph, A.2
  • 21
    • 0024393978 scopus 로고
    • Poly(ADP-ribosyl)ation of proteins: Processivity of posttranslational modification
    • Naegeli, H. P., Loetscher, P., and Althaus, F. R. Poly(ADP-ribosyl)ation of proteins: processivity of posttranslational modification. J. Biol. Chem., 264: 14382-14385, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14382-14385
    • Naegeli, H.P.1    Loetscher, P.2    Althaus, F.R.3
  • 22
    • 0027500246 scopus 로고
    • Induction of nuclear accumulation of the tumor suppressor protein p53 by DNA-damaging agents
    • Fritsche, M., Haessler, C., and Bradner, G. Induction of nuclear accumulation of the tumor suppressor protein p53 by DNA-damaging agents. Oncogene, 8: 307-318, 1993.
    • (1993) Oncogene , vol.8 , pp. 307-318
    • Fritsche, M.1    Haessler, C.2    Bradner, G.3
  • 23
    • 0029843775 scopus 로고    scopus 로고
    • ADP-ribosylation of p53 tumor suppressor protein: Mutant but no wild type p53 is modified
    • Wesierska-Gadek, J., Bugajaska-Schretter, A., and Cerni, C. ADP-ribosylation of p53 tumor suppressor protein: mutant but no wild type p53 is modified. J. Cell. Biochem., 62: 90-101, 1996.
    • (1996) J. Cell. Biochem. , vol.62 , pp. 90-101
    • Wesierska-Gadek, J.1    Bugajaska-Schretter, A.2    Cerni, C.3
  • 24
    • 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 involving poly(ADP-ribose) polymerase
    • Vaziri, H., West, M. D., Allsopp, R. C., Davison, T. S., Wu, Y. S., Arrowsmith, C. A., Poirier, G. G., and Benchimol, S. ATM-dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the post-translational activation of p53 involving poly(ADP-ribose) polymerase. EMBO J., 16: 6018-6033, 1997.
    • (1997) EMBO J. , vol.16 , pp. 6018-6033
    • Vaziri, H.1    West, M.D.2    Allsopp, R.C.3    Davison, T.S.4    Wu, Y.S.5    Arrowsmith, C.A.6    Poirier, G.G.7    Benchimol, S.8
  • 25
    • 0022549981 scopus 로고
    • Poly(ADP-ribose) biosynthesis and suicidal NAD-depletion following carcinogen exposure of mammalian cells
    • Alvarez-Gonzalez, R., Eichenberger, R., and Althaus, F. R. Poly(ADP-ribose) biosynthesis and suicidal NAD-depletion following carcinogen exposure of mammalian cells. Biochem. Biophys. Res. Commun., 138: 1051-1057, 1986.
    • (1986) Biochem. Biophys. Res. Commun. , vol.138 , pp. 1051-1057
    • Alvarez-Gonzalez, R.1    Eichenberger, R.2    Althaus, F.R.3
  • 26
    • 0024428970 scopus 로고
    • Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents
    • Alvarez-Gonzalez, R., and Althaus, F. R. Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents. Mutat. Res., 218: 67-74, 1989.
    • (1989) Mutat. Res. , vol.218 , pp. 67-74
    • Alvarez-Gonzalez, R.1    Althaus, F.R.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (Lond.), 227: 680-684, 1970.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-684
    • Laemmli, U.K.1
  • 29
  • 30
    • 0021333746 scopus 로고
    • Poly(ADP-ribose) synthetase. Separation and identification of three proteolytic fragments as the substrate-binding domain, the DNA-binding domain, and the automodification domain
    • Kameshita, I., Matsuda, Z., Taniguchi, T., and Shizuta, Y. Poly(ADP-ribose) synthetase. Separation and identification of three proteolytic fragments as the substrate-binding domain, the DNA-binding domain, and the automodification domain. J. Biol. Chem., 259: 4770-4776, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4770-4776
    • Kameshita, I.1    Matsuda, Z.2    Taniguchi, T.3    Shizuta, Y.4
  • 31
    • 0028868288 scopus 로고
    • Identification of domains of poly(ADP-ribose) polymerase for protein binding and self-association
    • Buki, K. G., Bauer, P. I., Hakam, A., and Kun, E. Identification of domains of poly(ADP-ribose) polymerase for protein binding and self-association. J. Biol. Chem., 17: 3370-3377, 1995.
    • (1995) J. Biol. Chem. , vol.17 , pp. 3370-3377
    • Buki, K.G.1    Bauer, P.I.2    Hakam, A.3    Kun, E.4
  • 32
    • 0031007707 scopus 로고    scopus 로고
    • TFIIF, a basal eukaryotic transcription factor, is a substrate for poly(ADP-ribosyl)ation
    • Rawling, J. M., and Alvarez-Gonzalez, R. TFIIF, a basal eukaryotic transcription factor, is a substrate for poly(ADP-ribosyl)ation. Biochem. J., 324: 249-253, 1997.
    • (1997) Biochem. J. , vol.324 , pp. 249-253
    • Rawling, J.M.1    Alvarez-Gonzalez, R.2
  • 33
    • 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. Poly(ADP-ribose) binds to specific domains of p53 and alters its DNA binding functions. J. Biol. Chem., 273: 11839-11843, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11839-11843
    • Malanga, M.1    Pleschke, J.M.2    Kleczkowska, H.E.3    Althaus, F.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.