메뉴 건너뛰기




Volumn 100, Issue , 2016, Pages 257-270

Mitochondrial poly(ADP-ribose) polymerase: The Wizard of Oz at work

Author keywords

Cell death; Mitochondria; Oxidative stress; PARP; Poly(ADP ribose)

Indexed keywords

MITOCHONDRIAL DNA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; MITOCHONDRIAL PROTEIN; PARP1 PROTEIN, HUMAN;

EID: 84960969254     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2016.02.024     Document Type: Review
Times cited : (64)

References (108)
  • 1
    • 0036733355 scopus 로고    scopus 로고
    • The therapeutic potential of poly(ADP-ribose) polymerase inhibitors
    • [1] Virág, L., Szabo, C., The therapeutic potential of poly(ADP-ribose) polymerase inhibitors. Pharmacol. Rev. 54 (2002), 375–429.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 375-429
    • Virág, L.1    Szabo, C.2
  • 2
    • 18944390248 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors
    • [2] Jagtap, P., Szabo, C., Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors. Nat. Rev. Drug Discov. 4 (2005), 421–440.
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 421-440
    • Jagtap, P.1    Szabo, C.2
  • 5
    • 84886723521 scopus 로고    scopus 로고
    • Poly(ADP-ribose): PARadigms and PARadoxes
    • [5] Bürkle, A., Virág, L., Poly(ADP-ribose): PARadigms and PARadoxes. Mol. Asp. Med. 34 (2013), 1046–1065.
    • (2013) Mol. Asp. Med. , vol.34 , pp. 1046-1065
    • Bürkle, A.1    Virág, L.2
  • 6
    • 0002160618 scopus 로고
    • Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme
    • [6] Chambon, P., Weill, J.D., Mandel, P., Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme. Biochem. Biophys. Res. Commun. 11 (1963), 39–43.
    • (1963) Biochem. Biophys. Res. Commun. , vol.11 , pp. 39-43
    • Chambon, P.1    Weill, J.D.2    Mandel, P.3
  • 8
    • 0016784789 scopus 로고
    • Cytoplasmic poly(ADP-ribose) polymerase during the HeLa cell cycle
    • [8] Roberts, J.H., Stard, P., Giri, C.P., Smulson, M., Cytoplasmic poly(ADP-ribose) polymerase during the HeLa cell cycle. Arch. Biochem. Biophys. 171 (1975), 305–315.
    • (1975) Arch. Biochem. Biophys. , vol.171 , pp. 305-315
    • Roberts, J.H.1    Stard, P.2    Giri, C.P.3    Smulson, M.4
  • 9
    • 0017365877 scopus 로고
    • Stimulation of poly(adenosine diphosphate ribose) synthase activity of Xenopus germinal vesicle by progesterone
    • [9] Burzio, L.O., Koide, S.S., Stimulation of poly(adenosine diphosphate ribose) synthase activity of Xenopus germinal vesicle by progesterone. Ann. N. Y. Acad. Sci. 286 (1977), 398–407.
    • (1977) Ann. N. Y. Acad. Sci. , vol.286 , pp. 398-407
    • Burzio, L.O.1    Koide, S.S.2
  • 10
    • 0018800811 scopus 로고
    • ADP ribosylation of rat liver nucleosomal core histones
    • [10] Burzio, L.O., Riquelme, P.T., Koide, S.S., ADP ribosylation of rat liver nucleosomal core histones. J. Biol. Chem. 254 (1979), 3029–3030.
    • (1979) J. Biol. Chem. , vol.254 , pp. 3029-3030
    • Burzio, L.O.1    Riquelme, P.T.2    Koide, S.S.3
  • 11
    • 0019883001 scopus 로고
    • Poly (ADP-ribose) synthetase activity in rat testis mitochondria
    • [11] Burzio, L.O., Sáez, L., Cornejo, R., Poly (ADP-ribose) synthetase activity in rat testis mitochondria. Biochem. Biophys. Res. Commun. 103 (1981), 369–375.
    • (1981) Biochem. Biophys. Res. Commun. , vol.103 , pp. 369-375
    • Burzio, L.O.1    Sáez, L.2    Cornejo, R.3
  • 13
    • 0019575258 scopus 로고
    • Protein-bound polymeric and monomeric ADP-ribose residues in hepatic tissues. Comparative analyses using a new procedure for the quantification of poly(ADP-ribose)
    • [13] Wielckens, K., Bredehorst, R., Adamietz, P., Hilz, H., Protein-bound polymeric and monomeric ADP-ribose residues in hepatic tissues. Comparative analyses using a new procedure for the quantification of poly(ADP-ribose). Eur. J. Biochem. 117 (1981), 69–74.
    • (1981) Eur. J. Biochem. , vol.117 , pp. 69-74
    • Wielckens, K.1    Bredehorst, R.2    Adamietz, P.3    Hilz, H.4
  • 14
    • 84993679801 scopus 로고
    • Mitochondrial ADP-ribosiltransferase system in ADP-ribosylation reactions
    • [14] Kun, E., Kirsten, E., Mitochondrial ADP-ribosiltransferase system in ADP-ribosylation reactions. Curr. Top. Cell. Regul. 21 (1982), 175–187.
    • (1982) Curr. Top. Cell. Regul. , vol.21 , pp. 175-187
    • Kun, E.1    Kirsten, E.2
  • 16
    • 0019590727 scopus 로고
    • ATP prevents both hydroperoxide-induced hydrolysis of pyridine nucleotides and release of calcium in rat liver mitochondria
    • [16] Hofstetter, W., Mühlebach, T., Lötscher, H.R., Winterhalter, K.H., Richter, C., ATP prevents both hydroperoxide-induced hydrolysis of pyridine nucleotides and release of calcium in rat liver mitochondria. Eur. J. Biochem. 117 (1981), 361–367.
    • (1981) Eur. J. Biochem. , vol.117 , pp. 361-367
    • Hofstetter, W.1    Mühlebach, T.2    Lötscher, H.R.3    Winterhalter, K.H.4    Richter, C.5
  • 18
    • 0014424610 scopus 로고
    • Ultrastructure of sonic and digitonin fragments from beef heart mitochondria
    • [18] Malviya, A.N., Parsa, B., Yodaiken, R.E., Elliott, W.B., Ultrastructure of sonic and digitonin fragments from beef heart mitochondria. Biochim. Biophys. Acta 162 (1968), 195–209.
    • (1968) Biochim. Biophys. Acta , vol.162 , pp. 195-209
    • Malviya, A.N.1    Parsa, B.2    Yodaiken, R.E.3    Elliott, W.B.4
  • 19
    • 0023193968 scopus 로고
    • ADP-ribosyl transferase and NAD glycohydrolase activities in rat liver mitochondria
    • [19] Masmoudi, A., Mandel, P., ADP-ribosyl transferase and NAD glycohydrolase activities in rat liver mitochondria. Biochemistry 26 (1987), 1965–1969.
    • (1987) Biochemistry , vol.26 , pp. 1965-1969
    • Masmoudi, A.1    Mandel, P.2
  • 20
    • 0023879129 scopus 로고
    • ADP-ribosylation of highly purified rat brain mitochondria
    • [20] Masmoudi, A., Islam, F., Mandel, P., ADP-ribosylation of highly purified rat brain mitochondria. J. Neurochem. 51 (1988), 188–193.
    • (1988) J. Neurochem. , vol.51 , pp. 188-193
    • Masmoudi, A.1    Islam, F.2    Mandel, P.3
  • 21
    • 0027407185 scopus 로고
    • Association of mitochondrial ADP-ribosyl transferase activity with the DNA-protein complex
    • [21] Masmoudi, A., el-Fetouaki, J., Weltin, D., Belhadj, O., Mandel, P., Association of mitochondrial ADP-ribosyl transferase activity with the DNA-protein complex. Biochem. Mol. Biol. Int. 29 (1993), 77–83.
    • (1993) Biochem. Mol. Biol. Int. , vol.29 , pp. 77-83
    • Masmoudi, A.1    el-Fetouaki, J.2    Weltin, D.3    Belhadj, O.4    Mandel, P.5
  • 22
    • 0030041061 scopus 로고    scopus 로고
    • Nuclear architecture and ultrastructural distribution of poly(ADP-ribosyl)transferase, a multifunctional enzyme
    • [22] Mosgoeller, W., Steiner, M., Hozák, P., Penner, E., Wesierska-Gadek, J., Nuclear architecture and ultrastructural distribution of poly(ADP-ribosyl)transferase, a multifunctional enzyme. J. Cell Sci. 109 (1996), 409–418.
    • (1996) J. Cell Sci. , vol.109 , pp. 409-418
    • Mosgoeller, W.1    Steiner, M.2    Hozák, P.3    Penner, E.4    Wesierska-Gadek, J.5
  • 23
    • 0032524894 scopus 로고    scopus 로고
    • Enzymic, cysteine-specific ADP-ribosylation in bovine liver mitochondria
    • [23] Jorcke, D., Ziegler, M., Herrero-Yraola, A., Schweiger, M., Enzymic, cysteine-specific ADP-ribosylation in bovine liver mitochondria. Biochem. J. 332 (1998), 189–193.
    • (1998) Biochem. J. , vol.332 , pp. 189-193
    • Jorcke, D.1    Ziegler, M.2    Herrero-Yraola, A.3    Schweiger, M.4
  • 24
    • 0019332669 scopus 로고
    • Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes
    • [24] Moss, J., Stanley, S.J., Watkins, P.A., Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 255 (1980), 5838–5840.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5838-5840
    • Moss, J.1    Stanley, S.J.2    Watkins, P.A.3
  • 27
    • 5044232010 scopus 로고    scopus 로고
    • Mitochondrial poly(ADP-ribosylation): from old data to new perspectives
    • [27] Scovassi, A.I., Mitochondrial poly(ADP-ribosylation): from old data to new perspectives. FASEB J. 18 (2004), 1487–1488.
    • (2004) FASEB J. , vol.18 , pp. 1487-1488
    • Scovassi, A.I.1
  • 29
    • 62549134965 scopus 로고    scopus 로고
    • Intra-mitochondrial poly(ADP-ribosyl)ation: potential role for alpha-ketoglutarate dehydrogenase
    • [29] Pankotai, E., Lacza, Z., Murányi, M., Szabo, C., Intra-mitochondrial poly(ADP-ribosyl)ation: potential role for alpha-ketoglutarate dehydrogenase. Mitochondrion 9 (2009), 159–164.
    • (2009) Mitochondrion , vol.9 , pp. 159-164
    • Pankotai, E.1    Lacza, Z.2    Murányi, M.3    Szabo, C.4
  • 30
    • 70450277835 scopus 로고    scopus 로고
    • Mitochondrial localization of PARP-1 requires interaction with mitofilin and is involved in the maintenance of mitochondrial DNA integrity
    • [30] Rossi, M.N., Carbone, M., Mostocotto, C., Mancone, C., Tripodi, M., Maione, R., Amati, P., Mitochondrial localization of PARP-1 requires interaction with mitofilin and is involved in the maintenance of mitochondrial DNA integrity. J. Biol. Chem. 284 (2009), 31616–31624.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31616-31624
    • Rossi, M.N.1    Carbone, M.2    Mostocotto, C.3    Mancone, C.4    Tripodi, M.5    Maione, R.6    Amati, P.7
  • 31
    • 38049010435 scopus 로고
    • Nuclear receptors and other nuclear transcription factors in mitochondria: regulatory molecules in a new environment
    • [31] Psarra, A.M., Sekeris, C.E., Nuclear receptors and other nuclear transcription factors in mitochondria: regulatory molecules in a new environment. Biochim. Biophys. Acta, 1–11, 1783, 2008.
    • (1783) Biochim. Biophys. Acta , vol.1-11 , pp. 2008
    • Psarra, A.M.1    Sekeris, C.E.2
  • 32
    • 84856117760 scopus 로고    scopus 로고
    • Cellular bioenergetics is regulated by PARP1 under resting conditions and during oxidative stress
    • [32] Módis, K., Gero, D., Erdélyi, K., Szoleczky, P., DeWitt, D., Szabo, C., Cellular bioenergetics is regulated by PARP1 under resting conditions and during oxidative stress. Biochem. Pharmacol. 83 (2012), 633–643.
    • (2012) Biochem. Pharmacol. , vol.83 , pp. 633-643
    • Módis, K.1    Gero, D.2    Erdélyi, K.3    Szoleczky, P.4    DeWitt, D.5    Szabo, C.6
  • 33
    • 84907447200 scopus 로고    scopus 로고
    • Regulation of mitochondrial poly(ADP-Ribose) polymerase activation by the β-adrenoceptor/cAMP/protein kinase A axis during oxidative stress
    • [33] Brunyanszki, A., Olah, G., Coletta, C., Szczesny, B., Szabo, C., Regulation of mitochondrial poly(ADP-Ribose) polymerase activation by the β-adrenoceptor/cAMP/protein kinase A axis during oxidative stress. Mol. Pharm. 86 (2014), 450–462.
    • (2014) Mol. Pharm. , vol.86 , pp. 450-462
    • Brunyanszki, A.1    Olah, G.2    Coletta, C.3    Szczesny, B.4    Szabo, C.5
  • 34
    • 84941028477 scopus 로고    scopus 로고
    • Opposing roles of mitochondrial and nuclear PARP1 in the regulation of mitochondrial and nuclear DNA integrity: implications for the regulation of mitochondrial function
    • [34] Szczesny, B., Brunyanszki, A., Olah, G., Mitra, S., Szabo, C., Opposing roles of mitochondrial and nuclear PARP1 in the regulation of mitochondrial and nuclear DNA integrity: implications for the regulation of mitochondrial function. Nucleic Acids Res., 2014, 4213161–4213173.
    • (2014) Nucleic Acids Res. , pp. 4213161-4213173
    • Szczesny, B.1    Brunyanszki, A.2    Olah, G.3    Mitra, S.4    Szabo, C.5
  • 36
    • 20444454999 scopus 로고    scopus 로고
    • Nuclear poly(ADP-ribose) polymerase-1 rapidly triggers mitochondrial dysfunction
    • [36] Cipriani, G., Rapizzi, E., Vannacci, A., Rizzuto, R., Moroni, F., Chiarugi, A., Nuclear poly(ADP-ribose) polymerase-1 rapidly triggers mitochondrial dysfunction. J. Biol. Chem. 280 (2005), 17227–17234.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17227-17234
    • Cipriani, G.1    Rapizzi, E.2    Vannacci, A.3    Rizzuto, R.4    Moroni, F.5    Chiarugi, A.6
  • 37
    • 34547783237 scopus 로고    scopus 로고
    • Spatial and functional relationship between poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in the brain
    • [37] Poitras, M.F., Koh, D.W., Yu, S.W., Andrabi, S.A., Mandir, A.S., Poirier, G.G., Dawson, V.L., Dawson, T.M., Spatial and functional relationship between poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in the brain. Neuroscience 148 (2007), 198–211.
    • (2007) Neuroscience , vol.148 , pp. 198-211
    • Poitras, M.F.1    Koh, D.W.2    Yu, S.W.3    Andrabi, S.A.4    Mandir, A.S.5    Poirier, G.G.6    Dawson, V.L.7    Dawson, T.M.8
  • 38
    • 79956316213 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 is a nuclear epigenetic regulator of mitochondrial DNA repair and transcription
    • [38] Lapucci, A., Pittelli, M., Rapizzi, E., Felici, R., Moroni, F., Chiarugi, A., Poly(ADP-ribose) polymerase-1 is a nuclear epigenetic regulator of mitochondrial DNA repair and transcription. Mol. Pharm. 79 (2011), 932–940.
    • (2011) Mol. Pharm. , vol.79 , pp. 932-940
    • Lapucci, A.1    Pittelli, M.2    Rapizzi, E.3    Felici, R.4    Moroni, F.5    Chiarugi, A.6
  • 40
    • 0346500490 scopus 로고    scopus 로고
    • The 40 kDa carboxy-terminal domain of poly(ADP-ribose) polymerase-1 forms catalytically competent homo- and heterodimers in the absence of DNA
    • [40] Mendoza-Alvarez, H., Alvarez-Gonzalez, R., The 40 kDa carboxy-terminal domain of poly(ADP-ribose) polymerase-1 forms catalytically competent homo- and heterodimers in the absence of DNA. J. Mol. Biol. 336 (2004), 105–114.
    • (2004) J. Mol. Biol. , vol.336 , pp. 105-114
    • Mendoza-Alvarez, H.1    Alvarez-Gonzalez, R.2
  • 41
    • 0035161896 scopus 로고    scopus 로고
    • Purines inhibit poly(ADP-ribose) polymerase activation and modulate oxidant-induced cell death
    • [41] Virág, L., Szabo, C., Purines inhibit poly(ADP-ribose) polymerase activation and modulate oxidant-induced cell death. FASEB J. 15 (2001), 99–107.
    • (2001) FASEB J. , vol.15 , pp. 99-107
    • Virág, L.1    Szabo, C.2
  • 42
    • 27144555760 scopus 로고    scopus 로고
    • Gender differences in the endotoxin-induced inflammatory and vascular responses: potential role of poly(ADP-ribose) polymerase activation
    • [42] Mabley, J.G., Horváth, E.M., Murthy, K.G., Zsengellér, Z., Vaslin, A., Benko, R., Kollai, M., Szabo, C., Gender differences in the endotoxin-induced inflammatory and vascular responses: potential role of poly(ADP-ribose) polymerase activation. J. Pharmacol. Exp. Ther. 315 (2005), 812–820.
    • (2005) J. Pharmacol. Exp. Ther. , vol.315 , pp. 812-820
    • Mabley, J.G.1    Horváth, E.M.2    Murthy, K.G.3    Zsengellér, Z.4    Vaslin, A.5    Benko, R.6    Kollai, M.7    Szabo, C.8
  • 43
    • 0025267542 scopus 로고
    • Inhibition of poly(ADP-ribose) synthetase by unsaturated fatty acids, vitamins and vitamin-like substances
    • [43] Banasik, M., Komura, H., Ueda, K., Inhibition of poly(ADP-ribose) synthetase by unsaturated fatty acids, vitamins and vitamin-like substances. FEBS Lett. 263 (1990), 222–224.
    • (1990) FEBS Lett. , vol.263 , pp. 222-224
    • Banasik, M.1    Komura, H.2    Ueda, K.3
  • 44
    • 84865411082 scopus 로고    scopus 로고
    • The dynamic regulation of NAD metabolism in mitochondria
    • [44] Stein, L.R., Imai, S., The dynamic regulation of NAD metabolism in mitochondria. Trends Endocrinol. Metab. 23 (2012), 420–428.
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 420-428
    • Stein, L.R.1    Imai, S.2
  • 45
    • 37849013404 scopus 로고    scopus 로고
    • Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix
    • [45] Niere, M., Kernstock, S., Koch-Nolte, F., Ziegler, M., Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix. Mol. Cell Biol. 28 (2008), 814–824.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 814-824
    • Niere, M.1    Kernstock, S.2    Koch-Nolte, F.3    Ziegler, M.4
  • 46
    • 84860844237 scopus 로고    scopus 로고
    • ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose)
    • [46] Niere, M., Mashimo, M., Agledal, L., Dölle, C., Kasamatsu, A., Kato, J., Moss, J., Ziegler, M., ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose). J. Biol. Chem. 287 (2012), 16088–160102.
    • (2012) J. Biol. Chem. , vol.287 , pp. 16088-160102
    • Niere, M.1    Mashimo, M.2    Agledal, L.3    Dölle, C.4    Kasamatsu, A.5    Kato, J.6    Moss, J.7    Ziegler, M.8
  • 48
    • 33746806606 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 hyperactivation and impairment of mitochondrial respiratory chain complex I function in reperfused mouse hearts
    • [48] Zhou, H.Z., Swanson, R.A., Simonis, U., Ma, X., Cecchini, G., Gray, M.O., Poly(ADP-ribose) polymerase-1 hyperactivation and impairment of mitochondrial respiratory chain complex I function in reperfused mouse hearts. Am. J. Physiol. Heart Circ.Physiol. 291 (2006), H714–H723.
    • (2006) Am. J. Physiol. Heart Circ.Physiol. , vol.291 , pp. H714-H723
    • Zhou, H.Z.1    Swanson, R.A.2    Simonis, U.3    Ma, X.4    Cecchini, G.5    Gray, M.O.6
  • 51
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: biochemistry, pathophysiology and development of therapeutics
    • [51] Szabo, C., Ischiropoulos, H., Radi, R., Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat. Rev. Drug Discov. 6 (2007), 662–680.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 52
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • [52] Pacher, P., Beckman, J.S., Liaudet, L., Nitric oxide and peroxynitrite in health and disease. Physiol. Rev. 87 (2007), 315–424.
    • (2007) Physiol. Rev. , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 53
    • 0038268052 scopus 로고    scopus 로고
    • Precise determination of mitochondrial DNA copy number in human skeletal and cardiac muscle by a PCR-based assay: lack of change of copy number with age
    • [53] Miller, F.J., Rosenfeldt, F.L., Zhang, C., Linnane, A.W., Nagley, P., Precise determination of mitochondrial DNA copy number in human skeletal and cardiac muscle by a PCR-based assay: lack of change of copy number with age. Nucleic Acids Res., 31, 2003, e61.
    • (2003) Nucleic Acids Res. , vol.31 , pp. e61
    • Miller, F.J.1    Rosenfeldt, F.L.2    Zhang, C.3    Linnane, A.W.4    Nagley, P.5
  • 54
    • 62149086299 scopus 로고    scopus 로고
    • Number matters: control of mammalian mitochondrial DNA copy number
    • [54] Clay Montier, L.L., Deng, J.J., Bai, Y., Number matters: control of mammalian mitochondrial DNA copy number. J. Genet. Genom. 36 (2009), 125–131.
    • (2009) J. Genet. Genom. , vol.36 , pp. 125-131
    • Clay Montier, L.L.1    Deng, J.J.2    Bai, Y.3
  • 55
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • [55] Cadenas, E., Davies, K.J., Mitochondrial free radical generation, oxidative stress, and aging. Free Radic. Biol. Med. 29 (2000), 222–223.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 222-223
    • Cadenas, E.1    Davies, K.J.2
  • 56
    • 0033026606 scopus 로고    scopus 로고
    • Nucleotide substitution rate of mammalian mitochondrial genomes
    • [56] Pesole, G., Gissi, C., De Chirico, A., Saccone, C., Nucleotide substitution rate of mammalian mitochondrial genomes. J. Mol. Evol. 48 (1999), 427–434.
    • (1999) J. Mol. Evol. , vol.48 , pp. 427-434
    • Pesole, G.1    Gissi, C.2    De Chirico, A.3    Saccone, C.4
  • 57
    • 0000825475 scopus 로고
    • The absence of a pyrimidine dimer repair mechanism in mammalian mitochondria
    • [57] Clayton, D.A., Doda, J.N., Friedberg, E.C., The absence of a pyrimidine dimer repair mechanism in mammalian mitochondria. Proc. Natl. Acad. Sci. USA 71 (1974), 2777–2781.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 2777-2781
    • Clayton, D.A.1    Doda, J.N.2    Friedberg, E.C.3
  • 58
    • 0027438888 scopus 로고
    • Repair of oxidative damage within the mitochondrial DNA of RINr 38 cells
    • [58] Driggers, W.J., LeDoux, S.P., Wilson, G.L., Repair of oxidative damage within the mitochondrial DNA of RINr 38 cells. J. Biol. Chem. 268 (1993), 22042–22045.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22042-22045
    • Driggers, W.J.1    LeDoux, S.P.2    Wilson, G.L.3
  • 59
    • 0030881789 scopus 로고    scopus 로고
    • Repair of oxidative damage to nuclear and mitochondrial DNA in mammalian cells
    • [59] Croteau, D.L., Bohr, V.A., Repair of oxidative damage to nuclear and mitochondrial DNA in mammalian cells. J. Biol. Chem. 272 (1997), 25409–25412.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25409-25412
    • Croteau, D.L.1    Bohr, V.A.2
  • 60
    • 0033568311 scopus 로고    scopus 로고
    • Single-nucleotide patch base excision repair of uracil in DNA by mitochondrial protein extracts
    • [60] Stierum, R.H., Dianov, G.L., Bohr, V.A., Single-nucleotide patch base excision repair of uracil in DNA by mitochondrial protein extracts. Nucleic Acids Res. 27 (1999), 3712–3719.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3712-3719
    • Stierum, R.H.1    Dianov, G.L.2    Bohr, V.A.3
  • 61
    • 55049124777 scopus 로고    scopus 로고
    • Long patch base excision repair in mammalian mitochondrial genomes
    • [61] Szczesny, B., Tann, A.W., Longley, M.J., Copeland, W.C., Mitra, S., Long patch base excision repair in mammalian mitochondrial genomes. J. Biol. Chem. 283 (2008), 26349–26356.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26349-26356
    • Szczesny, B.1    Tann, A.W.2    Longley, M.J.3    Copeland, W.C.4    Mitra, S.5
  • 62
    • 40649109989 scopus 로고    scopus 로고
    • Mitochondrial base excision repair of uracil and AP sites takes place by single-nucleotide insertion and long-patch DNA synthesis
    • [62] Akbari, M., Visnes, T., Krokan, H.E., Otterlei, M., Mitochondrial base excision repair of uracil and AP sites takes place by single-nucleotide insertion and long-patch DNA synthesis. DNA Repair 7 (2008), 605–616.
    • (2008) DNA Repair , vol.7 , pp. 605-616
    • Akbari, M.1    Visnes, T.2    Krokan, H.E.3    Otterlei, M.4
  • 64
    • 0017378110 scopus 로고
    • DNA polymerase of mitochondria is a gamma-polymerase
    • [64] Bolden, A., Noy, G.P., Weissbach, A., DNA polymerase of mitochondria is a gamma-polymerase. J. Biol. Chem. 252 (1977), 3351–3356.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3351-3356
    • Bolden, A.1    Noy, G.P.2    Weissbach, A.3
  • 66
    • 33644635644 scopus 로고    scopus 로고
    • DNA polymerase gamma in mitochondrial DNA replication and repair
    • [66] Graziewicz, M.A., Longley, M.J., Copeland, W.C., DNA polymerase gamma in mitochondrial DNA replication and repair. Chem. Rev. 106 (2006), 383–405.
    • (2006) Chem. Rev. , vol.106 , pp. 383-405
    • Graziewicz, M.A.1    Longley, M.J.2    Copeland, W.C.3
  • 67
    • 77953484497 scopus 로고    scopus 로고
    • DNA repair in mammalian mitochondria: Much more than we thought?
    • [67] Liu, P., Demple, B., DNA repair in mammalian mitochondria: Much more than we thought?. Environ. Mol. Mutagen. 51 (2010), 417–426.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 417-426
    • Liu, P.1    Demple, B.2
  • 69
    • 77955365267 scopus 로고    scopus 로고
    • Production and characterization of recombinant protein preparations of Endonuclease G-homologs from yeast, C. elegans and humans
    • [69] Kieper, J., Lauber, C., Gimadutdinow, O., Urbańska, A., Cymerman, I., Ghosh, M., Szczesny, B., Meiss, G., Production and characterization of recombinant protein preparations of Endonuclease G-homologs from yeast, C. elegans and humans. Protein Expr. Purif. 73 (2010), 99–106.
    • (2010) Protein Expr. Purif. , vol.73 , pp. 99-106
    • Kieper, J.1    Lauber, C.2    Gimadutdinow, O.3    Urbańska, A.4    Cymerman, I.5    Ghosh, M.6    Szczesny, B.7    Meiss, G.8
  • 70
    • 80052698492 scopus 로고    scopus 로고
    • Apoptosis induced by persistent single-strand breaks in mitochondrial genome: critical role of EXOG (5'-EXO/endonuclease) in their repair
    • [70] Tann, A.W., Boldogh, I., Meiss, G., Qian, W., Van Houten, B., Mitra, S., Szczesny, B., Apoptosis induced by persistent single-strand breaks in mitochondrial genome: critical role of EXOG (5'-EXO/endonuclease) in their repair. J. Biol. Chem. 286 (2011), 31975–31983.
    • (2011) J. Biol. Chem. , vol.286 , pp. 31975-31983
    • Tann, A.W.1    Boldogh, I.2    Meiss, G.3    Qian, W.4    Van Houten, B.5    Mitra, S.6    Szczesny, B.7
  • 71
    • 0023879129 scopus 로고
    • ADP-ribosylation of highly purified rat brain mitochondria
    • [71] Masmoudi, A., Islam, F., Mandel, P., ADP-ribosylation of highly purified rat brain mitochondria. J. Neurochem. 51 (1988), 188–193.
    • (1988) J. Neurochem. , vol.51 , pp. 188-193
    • Masmoudi, A.1    Islam, F.2    Mandel, P.3
  • 72
    • 0033755242 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase facilitates the repair of N-methylpurines in mitochondrial DNA
    • [72] Druzhyna, N., Smulson, M.E., LeDoux, S.P., Wilson, G.L., Poly(ADP-ribose) polymerase facilitates the repair of N-methylpurines in mitochondrial DNA. Diabetes 49 (2000), 1849–1855.
    • (2000) Diabetes , vol.49 , pp. 1849-1855
    • Druzhyna, N.1    Smulson, M.E.2    LeDoux, S.P.3    Wilson, G.L.4
  • 73
    • 0032924757 scopus 로고    scopus 로고
    • Mitochondrial damage induced by conditions of oxidative stress
    • [73] Kowaltowski, A.J., Vercesi, A.E., Mitochondrial damage induced by conditions of oxidative stress. Free Radic. Biol. Med. 26 (1999), 463–471.
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 463-471
    • Kowaltowski, A.J.1    Vercesi, A.E.2
  • 75
    • 0032193692 scopus 로고    scopus 로고
    • Poly(ADP-ribose) synthetase activation mediates mitochondrial injury during oxidant-induced cell death
    • [75] Virág, L., Salzman, A.L., Szabo, C., Poly(ADP-ribose) synthetase activation mediates mitochondrial injury during oxidant-induced cell death. J. Immunol. 161 (1998), 3753–3759.
    • (1998) J. Immunol. , vol.161 , pp. 3753-3759
    • Virág, L.1    Salzman, A.L.2    Szabo, C.3
  • 78
    • 84857217832 scopus 로고    scopus 로고
    • ER stress and its functional link to mitochondria: role in cell survival and death
    • [78] Malhotra, J.D., Kaufman, R.J., ER stress and its functional link to mitochondria: role in cell survival and death. Cold Spring Harb. Perspect. Biol, 3, 2011, a004424.
    • (2011) Cold Spring Harb. Perspect. Biol , vol.3 , pp. a004424
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 79
    • 33646827842 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 signaling to mitochondria in necrotic cell death requires RIP1/TRAF2-mediated JNK1 activation
    • [79] Xu, Y., Huang, S., Liu, Z.G., Han, J., Poly(ADP-ribose) polymerase-1 signaling to mitochondria in necrotic cell death requires RIP1/TRAF2-mediated JNK1 activation. J. Biol. Chem. 281 (2006), 8788–8795.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8788-8795
    • Xu, Y.1    Huang, S.2    Liu, Z.G.3    Han, J.4
  • 80
    • 84898143711 scopus 로고    scopus 로고
    • Induction of mitochondrial dysfunction by poly(ADP-ribose) polymer: implication for neuronal cell death
    • [80] SH1, Baek, Bae, O.N., Kim, E.K., Yu, S.W., Induction of mitochondrial dysfunction by poly(ADP-ribose) polymer: implication for neuronal cell death. Mol. Cells 36 (2013), 258–266.
    • (2013) Mol. Cells , vol.36 , pp. 258-266
    • SH1, B.1    Bae, O.N.2    Kim, E.K.3    Yu, S.W.4
  • 81
    • 84884379434 scopus 로고    scopus 로고
    • ROS-mediated PARP activity undermines mitochondrial function after permeability transition pore opening during myocardial ischemia-reperfusion
    • [81] JM1, Schriewer, Peek, C.B., Bass, J., Schumacker, P.T., ROS-mediated PARP activity undermines mitochondrial function after permeability transition pore opening during myocardial ischemia-reperfusion. J. Am. Heart Assoc., 2, 2013, e000159.
    • (2013) J. Am. Heart Assoc. , vol.2 , pp. e000159
    • JM1, S.1    Peek, C.B.2    Bass, J.3    Schumacker, P.T.4
  • 82
    • 0020980976 scopus 로고
    • Poly(ADP-ribose) polymerase mediates the suicide response to massive DNA damage: studies in normal and DNA-repair defective cells
    • [82] Berger, N.A., Sims, J.L., Catino, D.M., Berger, S.J., Poly(ADP-ribose) polymerase mediates the suicide response to massive DNA damage: studies in normal and DNA-repair defective cells. Princess Takamatsu Symp. 13 (1983), 219–226.
    • (1983) Princess Takamatsu Symp. , vol.13 , pp. 219-226
    • Berger, N.A.1    Sims, J.L.2    Catino, D.M.3    Berger, S.J.4
  • 83
    • 0022553195 scopus 로고
    • Oxidant injury of cells. DNA strand-breaks activate polyadenosine diphosphate-ribose polymerase and lead to depletion of nicotinamide adenine dinucleotide
    • [83] Schraufstatter, I.U., Hinshaw, D.B., Hyslop, P.A., Spragg, R.G., Cochrane, C.G., Oxidant injury of cells. DNA strand-breaks activate polyadenosine diphosphate-ribose polymerase and lead to depletion of nicotinamide adenine dinucleotide. J. Clin. Invest. 77 (1986), 1312–1320.
    • (1986) J. Clin. Invest. , vol.77 , pp. 1312-1320
    • Schraufstatter, I.U.1    Hinshaw, D.B.2    Hyslop, P.A.3    Spragg, R.G.4    Cochrane, C.G.5
  • 85
    • 0028294246 scopus 로고
    • Nitric oxide activation of poly(ADP-ribose) synthetase in neurotoxicity
    • [85] Zhang, J., Dawson, V.L., Dawson, T.M., Snyder, S.H., Nitric oxide activation of poly(ADP-ribose) synthetase in neurotoxicity. Science 263 (1994), 687–689.
    • (1994) Science , vol.263 , pp. 687-689
    • Zhang, J.1    Dawson, V.L.2    Dawson, T.M.3    Snyder, S.H.4
  • 86
    • 0030000690 scopus 로고    scopus 로고
    • DNA strand breakage, activation of poly (ADP-ribose) synthetase, and Cellular Energy Depletion Are Involved In The Cytotoxicity Of Macrophages And Smooth Muscle Cells Exposed To Peroxynitrite
    • [86] Szabo, C., Zingarelli, B., O'Connor, M., Salzman, A.L., DNA strand breakage, activation of poly (ADP-ribose) synthetase, and Cellular Energy Depletion Are Involved In The Cytotoxicity Of Macrophages And Smooth Muscle Cells Exposed To Peroxynitrite. Proc. Natl. Acad. Sci. USA 93 (1996), 1753–1758.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1753-1758
    • Szabo, C.1    Zingarelli, B.2    O'Connor, M.3    Salzman, A.L.4
  • 88
    • 0032127666 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) synthetase in inflammation and ischaemia-reperfusion
    • [88] Szabo, C., Dawson, V.L., Role of poly(ADP-ribose) synthetase in inflammation and ischaemia-reperfusion. Trends Pharmacol. Sci. 19 (1998), 287–298.
    • (1998) Trends Pharmacol. Sci. , vol.19 , pp. 287-298
    • Szabo, C.1    Dawson, V.L.2
  • 89
    • 84886717487 scopus 로고    scopus 로고
    • Therapeutic applications of PARP inhibitors: anticancer therapy and beyond
    • [89] Curtin, N.J., Szabo, C., Therapeutic applications of PARP inhibitors: anticancer therapy and beyond. Mol. Asp. Med. 34 (2013), 1217–1256.
    • (2013) Mol. Asp. Med. , vol.34 , pp. 1217-1256
    • Curtin, N.J.1    Szabo, C.2
  • 90
    • 2142694340 scopus 로고    scopus 로고
    • Nuclear and mitochondrial conversations in cell death: PARP-1 and AIF signaling
    • [90] Hong, S.J., Dawson, T.M., Dawson, V.L., Nuclear and mitochondrial conversations in cell death: PARP-1 and AIF signaling. Trends Pharmacol. Sci. 25 (2004), 259–264.
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 259-264
    • Hong, S.J.1    Dawson, T.M.2    Dawson, V.L.3
  • 91
    • 10244241834 scopus 로고    scopus 로고
    • Deadly conversations: nuclear-mitochondrial cross-talk
    • [91] Dawson, V.L., Dawson, T.M., Deadly conversations: nuclear-mitochondrial cross-talk. J. Bioenergy Biomembr. 36 (2004), 287–294.
    • (2004) J. Bioenergy Biomembr. , vol.36 , pp. 287-294
    • Dawson, V.L.1    Dawson, T.M.2
  • 93
    • 84908300733 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in cancer chemoresistance
    • [93] Guaragnella, N., Giannattasio, S., Moro, L., Mitochondrial dysfunction in cancer chemoresistance. Biochem. Pharmacol. 92 (2014), 62–72.
    • (2014) Biochem. Pharmacol. , vol.92 , pp. 62-72
    • Guaragnella, N.1    Giannattasio, S.2    Moro, L.3
  • 94
    • 84897442012 scopus 로고    scopus 로고
    • Parthanatos: mitochondrial-linked mechanisms and therapeutic opportunities
    • [94] Fatokun, A.A., Dawson, V.L., Dawson, T.M., Parthanatos: mitochondrial-linked mechanisms and therapeutic opportunities. Br. J. Pharmacol. 171 (2014), 2000–2016.
    • (2014) Br. J. Pharmacol. , vol.171 , pp. 2000-2016
    • Fatokun, A.A.1    Dawson, V.L.2    Dawson, T.M.3
  • 95
    • 84908205819 scopus 로고    scopus 로고
    • Poly(ADP-ribose): a signaling molecule in different paradigms of cell death
    • [95] Aredia, F., Scovassi, A.I., Poly(ADP-ribose): a signaling molecule in different paradigms of cell death. Biochem. Pharmacol. 92 (2014), 157–163.
    • (2014) Biochem. Pharmacol. , vol.92 , pp. 157-163
    • Aredia, F.1    Scovassi, A.I.2
  • 96
    • 84907429451 scopus 로고    scopus 로고
    • Formation and repair of oxidative damage in the mitochondrial DNA
    • [96] Muftuoglu, M., Mori, M.P., de Souza-Pinto, N.C., Formation and repair of oxidative damage in the mitochondrial DNA. Mitochondrion 17 (2014), 164–181.
    • (2014) Mitochondrion , vol.17 , pp. 164-181
    • Muftuoglu, M.1    Mori, M.P.2    de Souza-Pinto, N.C.3
  • 97
    • 84927930923 scopus 로고    scopus 로고
    • PARP-1 involvement in neurodegeneration: A focus on Alzheimer's and Parkinson's diseases
    • [97] Martire, S., Mosca, L., d'Erme, M., PARP-1 involvement in neurodegeneration: A focus on Alzheimer's and Parkinson's diseases. Mech. Ageing Dev. 146–148 (2015), 53–64.
    • (2015) Mech. Ageing Dev. , vol.146-148 , pp. 53-64
    • Martire, S.1    Mosca, L.2    d'Erme, M.3
  • 98
    • 84923080018 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerases as modulators of mitochondrial activity
    • [98] Bai, P., Nagy, L., Fodor, T., Liaudet, L., Pacher, P., Poly(ADP-ribose) polymerases as modulators of mitochondrial activity. Trends Endocrinol. Metab. 26 (2015), 75–83.
    • (2015) Trends Endocrinol. Metab. , vol.26 , pp. 75-83
    • Bai, P.1    Nagy, L.2    Fodor, T.3    Liaudet, L.4    Pacher, P.5
  • 99
    • 84937862063 scopus 로고    scopus 로고
    • Poly(ADP-ribosylation) and neurodegenerative disorders
    • [99] Basello, D.A., Scovassi, A.I., Poly(ADP-ribosylation) and neurodegenerative disorders. Mitochondrion 4 (2015), 56–63.
    • (2015) Mitochondrion , vol.4 , pp. 56-63
    • Basello, D.A.1    Scovassi, A.I.2
  • 100
    • 0026662651 scopus 로고
    • The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity
    • [100] Schreiber, V., Molinete, M., Boeuf, H., de Murcia, G., Ménissier-de Murcia, J., The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity. EMBO J. 11 (1992), 3263–3269.
    • (1992) EMBO J. , vol.11 , pp. 3263-3269
    • Schreiber, V.1    Molinete, M.2    Boeuf, H.3    de Murcia, G.4    Ménissier-de Murcia, J.5
  • 101
    • 38049010435 scopus 로고
    • Nuclear receptors and other nuclear transcription factors in mitochondria: regulatory molecules in a new environment
    • [101] Psarra, A.M., Sekeris, C.E., Nuclear receptors and other nuclear transcription factors in mitochondria: regulatory molecules in a new environment. Biochim. Biophys. Acta, 1–11, 1783, 2008.
    • (1783) Biochim. Biophys. Acta , vol.1-11 , pp. 2008
    • Psarra, A.M.1    Sekeris, C.E.2
  • 102
    • 79961162915 scopus 로고    scopus 로고
    • Cellular and molecular effects of sirtuins in health and disease
    • [102] Horio, Y., Hayashi, T., Kuno, A., Kunimoto, R., Cellular and molecular effects of sirtuins in health and disease. Clin. Sci. (Lond.) 121 (2011), 191–203.
    • (2011) Clin. Sci. (Lond.) , vol.121 , pp. 191-203
    • Horio, Y.1    Hayashi, T.2    Kuno, A.3    Kunimoto, R.4
  • 104
    • 84886717428 scopus 로고    scopus 로고
    • Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes
    • [104] Cantó, C., Sauve, A.A., Bai, P., Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes. Mol. Asp. Med. 34 (2013), 1168–1201.
    • (2013) Mol. Asp. Med. , vol.34 , pp. 1168-1201
    • Cantó, C.1    Sauve, A.A.2    Bai, P.3
  • 105
    • 84880328473 scopus 로고    scopus 로고
    • NAD and ADP-ribose metabolism in mitochondria
    • [105] Dölle, C., Rack, J.G., Ziegler, M., NAD and ADP-ribose metabolism in mitochondria. FEBS J. 280 (2013), 3530–4531.
    • (2013) FEBS J. , vol.280 , pp. 3530-4531
    • Dölle, C.1    Rack, J.G.2    Ziegler, M.3
  • 106
    • 79952353862 scopus 로고    scopus 로고
    • Neuronal Sirt3 protects against excitotoxic injury in mouse cortical neuron culture
    • [106] Kim, S.H., Lu, H.F., Alano, C.C., Neuronal Sirt3 protects against excitotoxic injury in mouse cortical neuron culture. PLoS One, 6, 2011, e14731.
    • (2011) PLoS One , vol.6 , pp. e14731
    • Kim, S.H.1    Lu, H.F.2    Alano, C.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.