메뉴 건너뛰기




Volumn 304, Issue , 2013, Pages 227-281

Roles of poly(ADP-Ribose) glycohydrolase in DNA damage and apoptosis

Author keywords

Cell death; DNA damage repair; PARG; PARP; PARsylation; Parthanatos; Poly(ADP ribose)

Indexed keywords

DAUNORUBICIN; DNA; ELLIPTICINE; ETHACRIDINE; ETHIDIUM BROMIDE; GLYCOSIDASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 2; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE INHIBITOR; POLY(ADENOSINE DIPHOSPHATE RIBOSE); PROFLAVINE; TANKYRASE; TILORONE;

EID: 84879566553     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-407696-9.00005-1     Document Type: Chapter
Times cited : (56)

References (228)
  • 1
    • 0023514097 scopus 로고
    • Poly(ADP-ribose) synthase is the major endogenous nonhistone acceptor for poly(ADP-ribose) in alkylated rat hepatoma cells
    • Adamietz P. Poly(ADP-ribose) synthase is the major endogenous nonhistone acceptor for poly(ADP-ribose) in alkylated rat hepatoma cells. Eur. J. Biochem. 1987, 169(2):365-372.
    • (1987) Eur. J. Biochem. , vol.169 , Issue.2 , pp. 365-372
    • Adamietz, P.1
  • 3
    • 0034672418 scopus 로고    scopus 로고
    • BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration
    • Aguiar R.C., Yakushijin Y., Kharbanda S., Salgia R., Fletcher J.A., Shipp M.A. BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration. Blood 2000, 96(13):4328-4334.
    • (2000) Blood , vol.96 , Issue.13 , pp. 4328-4334
    • Aguiar, R.C.1    Yakushijin, Y.2    Kharbanda, S.3    Salgia, R.4    Fletcher, J.A.5    Shipp, M.A.6
  • 4
    • 38049064044 scopus 로고    scopus 로고
    • Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins
    • Ahel I., Ahel D., Matsusaka T., Clark A.J., Pines J., Boulton S.J., West S.C. Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Nature 2008, 451(7174):81-85.
    • (2008) Nature , vol.451 , Issue.7174 , pp. 81-85
    • Ahel, I.1    Ahel, D.2    Matsusaka, T.3    Clark, A.J.4    Pines, J.5    Boulton, S.J.6    West, S.C.7
  • 7
    • 0024428970 scopus 로고
    • Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents
    • Alvarez-Gonzalez R., Althaus F.R. Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents. Mutat. Res. 1989, 218(2):67-74.
    • (1989) Mutat. Res. , vol.218 , Issue.2 , pp. 67-74
    • Alvarez-Gonzalez, R.1    Althaus, F.R.2
  • 8
    • 0023191708 scopus 로고
    • Characterization of polymers of adenosine diphosphate ribose generated in vitro and in vivo
    • Alvarez-Gonzalez R., Jacobson M.K. Characterization of polymers of adenosine diphosphate ribose generated in vitro and in vivo. Biochemistry 1987, 26(11):3218-3224.
    • (1987) Biochemistry , vol.26 , Issue.11 , pp. 3218-3224
    • Alvarez-Gonzalez, R.1    Jacobson, M.K.2
  • 14
    • 57649233085 scopus 로고    scopus 로고
    • Mitochondrial and nuclear cross talk in cell death: parthanatos
    • Andrabi S.A., Dawson T.M., Dawson V.L. Mitochondrial and nuclear cross talk in cell death: parthanatos. Ann. N. Y. Acad. Sci. 2008, 1147:233-241.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 233-241
    • Andrabi, S.A.1    Dawson, T.M.2    Dawson, V.L.3
  • 16
    • 0026669916 scopus 로고
    • Effect of short-term egg exclusion diet on infantile atopic dermatitis and its relation to egg allergy: a single-blind test
    • Aoki T., Kojima M., Adachi J., Okano M. Effect of short-term egg exclusion diet on infantile atopic dermatitis and its relation to egg allergy: a single-blind test. Acta Derm. Venereol. Suppl. 1992, 176:99-102.
    • (1992) Acta Derm. Venereol. Suppl. , vol.176 , pp. 99-102
    • Aoki, T.1    Kojima, M.2    Adachi, J.3    Okano, M.4
  • 17
    • 0042237031 scopus 로고    scopus 로고
    • Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization
    • Arnoult D., Gaume B., Karbowski M., Sharpe J.C., Cecconi F., Youle R.J. Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization. EMBO J. 2003, 22(17):4385-4399.
    • (2003) EMBO J. , vol.22 , Issue.17 , pp. 4385-4399
    • Arnoult, D.1    Gaume, B.2    Karbowski, M.3    Sharpe, J.C.4    Cecconi, F.5    Youle, R.J.6
  • 19
    • 11244280890 scopus 로고    scopus 로고
    • Involvement of poly(ADP-ribose) polymerase-1 and XRCC1/DNA ligase III in an alternative route for DNA double-strand breaks rejoining
    • Audebert M., Salles B., Calsou P. Involvement of poly(ADP-ribose) polymerase-1 and XRCC1/DNA ligase III in an alternative route for DNA double-strand breaks rejoining. J. Biol. Chem. 2004, 279(53):55117-55126.
    • (2004) J. Biol. Chem. , vol.279 , Issue.53 , pp. 55117-55126
    • Audebert, M.1    Salles, B.2    Calsou, P.3
  • 21
    • 38049129655 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-2 [corrected] controls adipocyte differentiation and adipose tissue function through the regulation of the activity of the retinoid X receptor/peroxisome proliferator-activated receptor-gamma [corrected] heterodimer
    • Bai P., Houten S.M., Huber A., Schreiber V., Watanabe M., Kiss B., de Murcia G., Auwerx J., Menissier-de Murcia J. Poly(ADP-ribose) polymerase-2 [corrected] controls adipocyte differentiation and adipose tissue function through the regulation of the activity of the retinoid X receptor/peroxisome proliferator-activated receptor-gamma [corrected] heterodimer. J. Biol. Chem. 2007, 282(52):37738-37746.
    • (2007) J. Biol. Chem. , vol.282 , Issue.52 , pp. 37738-37746
    • Bai, P.1    Houten, S.M.2    Huber, A.3    Schreiber, V.4    Watanabe, M.5    Kiss, B.6    de Murcia, G.7    Auwerx, J.8    Menissier-de Murcia, J.9
  • 25
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidere N., Lorenzo H.K., Carmona S., Laforge M., Harper F., Dumont C., Senik A. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J. Biol. Chem. 2003, 278(33):31401-31411.
    • (2003) J. Biol. Chem. , vol.278 , Issue.33 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 28
    • 79952148357 scopus 로고    scopus 로고
    • The ups and downs of tannins as inhibitors of poly(ADP-ribose)glycohydrolase
    • Blenn C., Wyrsch P., Althaus F.R. The ups and downs of tannins as inhibitors of poly(ADP-ribose)glycohydrolase. Molecules 2011, 16(2):1854-1877.
    • (2011) Molecules , vol.16 , Issue.2 , pp. 1854-1877
    • Blenn, C.1    Wyrsch, P.2    Althaus, F.R.3
  • 30
    • 79953651847 scopus 로고    scopus 로고
    • PARP-3, a DNA-dependent PARP with emerging roles in double-strand break repair and mitotic progression
    • Boehler C., Dantzer F. PARP-3, a DNA-dependent PARP with emerging roles in double-strand break repair and mitotic progression. Cell Cycle 2011, 10(7):1023-1024.
    • (2011) Cell Cycle , vol.10 , Issue.7 , pp. 1023-1024
    • Boehler, C.1    Dantzer, F.2
  • 31
    • 0742323811 scopus 로고    scopus 로고
    • Alteration of poly(ADP-ribose) glycohydrolase nucleocytoplasmic shuttling characteristics upon cleavage by apoptotic proteases
    • Bonicalzi M.E., Vodenicharov M., Coulombe M., Gagne J.P., Poirier G.G. Alteration of poly(ADP-ribose) glycohydrolase nucleocytoplasmic shuttling characteristics upon cleavage by apoptotic proteases. Biol. Cell 2003, 95(9):635-644.
    • (2003) Biol. Cell , vol.95 , Issue.9 , pp. 635-644
    • Bonicalzi, M.E.1    Vodenicharov, M.2    Coulombe, M.3    Gagne, J.P.4    Poirier, G.G.5
  • 32
    • 77956145378 scopus 로고    scopus 로고
    • Identification of a regulatory segment of poly(ADP-ribose) glycohydrolase
    • Botta D., Jacobson M.K. Identification of a regulatory segment of poly(ADP-ribose) glycohydrolase. Biochemistry 2010, 49(35):7674-7682.
    • (2010) Biochemistry , vol.49 , Issue.35 , pp. 7674-7682
    • Botta, D.1    Jacobson, M.K.2
  • 33
    • 0028280995 scopus 로고
    • Endoglycosidic cleavage of branched polymers by poly(ADP-ribose) glycohydrolase
    • Braun S.A., Panzeter P.L., Collinge M.A., Althaus F.R. Endoglycosidic cleavage of branched polymers by poly(ADP-ribose) glycohydrolase. Eur. J. Biochem. 1994, 220(2):369-375.
    • (1994) Eur. J. Biochem. , vol.220 , Issue.2 , pp. 369-375
    • Braun, S.A.1    Panzeter, P.L.2    Collinge, M.A.3    Althaus, F.R.4
  • 35
    • 63449092539 scopus 로고    scopus 로고
    • Selective down-regulation of nuclear poly(ADP-ribose) glycohydrolase
    • Burns D.M., Ying W., Kauppinen T.M., Zhu K., Swanson R.A. Selective down-regulation of nuclear poly(ADP-ribose) glycohydrolase. PLoS One 2009, 4(3):e4896.
    • (2009) PLoS One , vol.4 , Issue.3
    • Burns, D.M.1    Ying, W.2    Kauppinen, T.M.3    Zhu, K.4    Swanson, R.A.5
  • 36
    • 0018800811 scopus 로고
    • ADP ribosylation of rat liver nucleosomal core histones
    • Burzio L.O., Riquelme P.T., Koide S.S. ADP ribosylation of rat liver nucleosomal core histones. J. Biol. Chem. 1979, 254(8):3029-3037.
    • (1979) J. Biol. Chem. , vol.254 , Issue.8 , pp. 3029-3037
    • Burzio, L.O.1    Riquelme, P.T.2    Koide, S.S.3
  • 39
    • 34548431366 scopus 로고    scopus 로고
    • Critical role of calpain I in mitochondrial release of apoptosis-inducing factor in ischemic neuronal injury
    • Cao G., Xing J., Xiao X., Liou A.K., Gao Y., Yin X.M., Clark R.S., Graham S.H., Chen J. Critical role of calpain I in mitochondrial release of apoptosis-inducing factor in ischemic neuronal injury. J. Neurosci. 2007, 27(35):9278-9293.
    • (2007) J. Neurosci. , vol.27 , Issue.35 , pp. 9278-9293
    • Cao, G.1    Xing, J.2    Xiao, X.3    Liou, A.K.4    Gao, Y.5    Yin, X.M.6    Clark, R.S.7    Graham, S.H.8    Chen, J.9
  • 40
    • 58149528362 scopus 로고    scopus 로고
    • Gallotannin ameliorates the development of streptozotocin-induced diabetic nephropathy by preventing the activation of PARP
    • Chandak P.G., Gaikwad A.B., Tikoo K. Gallotannin ameliorates the development of streptozotocin-induced diabetic nephropathy by preventing the activation of PARP. Phytother. Res. 2009, 23(1):72-77.
    • (2009) Phytother. Res. , vol.23 , Issue.1 , pp. 72-77
    • Chandak, P.G.1    Gaikwad, A.B.2    Tikoo, K.3
  • 41
    • 10344234720 scopus 로고    scopus 로고
    • Poly(ADP-ribose) is required for spindle assembly and structure
    • Chang P., Jacobson M.K., Mitchison T.J. Poly(ADP-ribose) is required for spindle assembly and structure. Nature 2004, 432(7017):645-649.
    • (2004) Nature , vol.432 , Issue.7017 , pp. 645-649
    • Chang, P.1    Jacobson, M.K.2    Mitchison, T.J.3
  • 42
    • 27444438371 scopus 로고    scopus 로고
    • NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis
    • Chang W., Dynek J.N., Smith S. NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis. Biochem. J. 2005, 391(Pt 2):177-184.
    • (2005) Biochem. J. , vol.391 , Issue.PART 2 , pp. 177-184
    • Chang, W.1    Dynek, J.N.2    Smith, S.3
  • 43
    • 56949083197 scopus 로고    scopus 로고
    • Tannic acid-induced apoptosis and -enhanced sensitivity to arsenic trioxide in human leukemia HL-60 cells
    • Chen K.S., Hsiao Y.C., Kuo D.Y., Chou M.C., Chu S.C., Hsieh Y.S., Lin T.H. Tannic acid-induced apoptosis and -enhanced sensitivity to arsenic trioxide in human leukemia HL-60 cells. Leuk. Res. 2009, 33(2):297-307.
    • (2009) Leuk. Res. , vol.33 , Issue.2 , pp. 297-307
    • Chen, K.S.1    Hsiao, Y.C.2    Kuo, D.Y.3    Chou, M.C.4    Chu, S.C.5    Hsieh, Y.S.6    Lin, T.H.7
  • 44
    • 84855908554 scopus 로고    scopus 로고
    • Activation of mitochondrial mu-calpain increases AIF cleavage in cardiac mitochondria during ischemia-reperfusion
    • Chen Q., Paillard M., Gomez L., Ross T., Hu Y., Xu A., Lesnefsky E.J. Activation of mitochondrial mu-calpain increases AIF cleavage in cardiac mitochondria during ischemia-reperfusion. Biochem. Biophys. Res. Commun. 2011, 415(4):533-538.
    • (2011) Biochem. Biophys. Res. Commun. , vol.415 , Issue.4 , pp. 533-538
    • Chen, Q.1    Paillard, M.2    Gomez, L.3    Ross, T.4    Hu, Y.5    Xu, A.6    Lesnefsky, E.J.7
  • 47
    • 41949083926 scopus 로고    scopus 로고
    • Redox-dependent changes in molecular properties of mitochondrial apoptosis-inducing factor
    • Churbanova I.Y., Sevrioukova I.F. Redox-dependent changes in molecular properties of mitochondrial apoptosis-inducing factor. J. Biol. Chem. 2008, 283(9):5622-5631.
    • (2008) J. Biol. Chem. , vol.283 , Issue.9 , pp. 5622-5631
    • Churbanova, I.Y.1    Sevrioukova, I.F.2
  • 48
    • 0036132673 scopus 로고    scopus 로고
    • Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres
    • Cook B.D., Dynek J.N., Chang W., Shostak G., Smith S. Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres. Mol. Cell. Biol. 2002, 22(1):332-342.
    • (2002) Mol. Cell. Biol. , vol.22 , Issue.1 , pp. 332-342
    • Cook, B.D.1    Dynek, J.N.2    Chang, W.3    Shostak, G.4    Smith, S.5
  • 50
    • 27744476223 scopus 로고    scopus 로고
    • Apoptosis-inducing factor triggered by poly(ADP-ribose) polymerase and Bid mediates neuronal cell death after oxygen-glucose deprivation and focal cerebral ischemia
    • Culmsee C., Zhu C., Landshamer S., Becattini B., Wagner E., Pellecchia M., Blomgren K., Plesnila N. Apoptosis-inducing factor triggered by poly(ADP-ribose) polymerase and Bid mediates neuronal cell death after oxygen-glucose deprivation and focal cerebral ischemia. J. Neurosci. 2005, 25(44):10262-10272.
    • (2005) J. Neurosci. , vol.25 , Issue.44 , pp. 10262-10272
    • Culmsee, C.1    Zhu, C.2    Landshamer, S.3    Becattini, B.4    Wagner, E.5    Pellecchia, M.6    Blomgren, K.7    Plesnila, N.8
  • 53
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours D., Desnoyers S., D'Silva I., Poirier G.G. Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 1999, 342(Pt 2):249-268.
    • (1999) Biochem. J. , vol.342 , Issue.PART 2 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 55
    • 0034617449 scopus 로고    scopus 로고
    • Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis
    • Daugas E., Nochy D., Ravagnan L., Loeffler M., Susin S.A., Zamzami N., Kroemer G. Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis. FEBS Lett. 2000, 476(3):118-123.
    • (2000) FEBS Lett. , vol.476 , Issue.3 , pp. 118-123
    • Daugas, E.1    Nochy, D.2    Ravagnan, L.3    Loeffler, M.4    Susin, S.A.5    Zamzami, N.6    Kroemer, G.7
  • 57
  • 60
    • 84861231399 scopus 로고    scopus 로고
    • The diverse roles and clinical relevance of PARPs in DNA damage repair: current state of the art
    • De Vos M., Schreiber V., Dantzer F. The diverse roles and clinical relevance of PARPs in DNA damage repair: current state of the art. Biochem. Pharmacol. 2012, 84(2):137-146.
    • (2012) Biochem. Pharmacol. , vol.84 , Issue.2 , pp. 137-146
    • De Vos, M.1    Schreiber, V.2    Dantzer, F.3
  • 61
    • 78649901987 scopus 로고    scopus 로고
    • Identification of the aryl hydrocarbon receptor target gene TiPARP as a mediator of suppression of hepatic gluconeogenesis by 2,3,7,8-tetrachlorodibenzo-p-dioxin and of nicotinamide as a corrective agent for this effect
    • Diani-Moore S., Ram P., Li X., Mondal P., Youn D.Y., Sauve A.A., Rifkind A.B. Identification of the aryl hydrocarbon receptor target gene TiPARP as a mediator of suppression of hepatic gluconeogenesis by 2,3,7,8-tetrachlorodibenzo-p-dioxin and of nicotinamide as a corrective agent for this effect. J. Biol. Chem. 2010, 285(50):38801-38810.
    • (2010) J. Biol. Chem. , vol.285 , Issue.50 , pp. 38801-38810
    • Diani-Moore, S.1    Ram, P.2    Li, X.3    Mondal, P.4    Youn, D.Y.5    Sauve, A.A.6    Rifkind, A.B.7
  • 62
    • 79953322962 scopus 로고    scopus 로고
    • Regulatory roles of tankyrase 1 at telomeres and in DNA repair: suppression of T-SCE and stabilization of DNA-PKcs
    • Dregalla R.C., Zhou J., Idate R.R., Battaglia C.L., Liber H.L., Bailey S.M. Regulatory roles of tankyrase 1 at telomeres and in DNA repair: suppression of T-SCE and stabilization of DNA-PKcs. Aging 2010, 2(10):691-708.
    • (2010) Aging , vol.2 , Issue.10 , pp. 691-708
    • Dregalla, R.C.1    Zhou, J.2    Idate, R.R.3    Battaglia, C.L.4    Liber, H.L.5    Bailey, S.M.6
  • 65
    • 23944439186 scopus 로고    scopus 로고
    • Gallotannin inhibits the expression of chemokines and inflammatory cytokines in A549 cells
    • Erdelyi K., Kiss A., Bakondi E., Bai P., Szabo C., Gergely P., Erdodi F., Virag L. Gallotannin inhibits the expression of chemokines and inflammatory cytokines in A549 cells. Mol. Pharmacol. 2005, 68(3):895-904.
    • (2005) Mol. Pharmacol. , vol.68 , Issue.3 , pp. 895-904
    • Erdelyi, K.1    Kiss, A.2    Bakondi, E.3    Bai, P.4    Szabo, C.5    Gergely, P.6    Erdodi, F.7    Virag, L.8
  • 66
    • 70349658096 scopus 로고    scopus 로고
    • Dual role of poly(ADP-ribose) glycohydrolase in the regulation of cell death in oxidatively stressed A549 cells
    • Erdelyi K., Bai P., Kovacs I., Szabo E., Mocsar G., Kakuk A., Szabo C., Gergely P., Virag L. Dual role of poly(ADP-ribose) glycohydrolase in the regulation of cell death in oxidatively stressed A549 cells. FASEB J. 2009, 23(10):3553-3563.
    • (2009) FASEB J. , vol.23 , Issue.10 , pp. 3553-3563
    • Erdelyi, K.1    Bai, P.2    Kovacs, I.3    Szabo, E.4    Mocsar, G.5    Kakuk, A.6    Szabo, C.7    Gergely, P.8    Virag, L.9
  • 67
    • 4143154152 scopus 로고    scopus 로고
    • Poly(ADP-ribose) glycohydrolase as a target for neuroprotective intervention: assessment of currently available pharmacological tools
    • Falsig J., Christiansen S.H., Feuerhahn S., Burkle A., Oei S.L., Keil C., Leist M. Poly(ADP-ribose) glycohydrolase as a target for neuroprotective intervention: assessment of currently available pharmacological tools. Eur. J. Pharmacol. 2004, 497(1):7-16.
    • (2004) Eur. J. Pharmacol. , vol.497 , Issue.1 , pp. 7-16
    • Falsig, J.1    Christiansen, S.H.2    Feuerhahn, S.3    Burkle, A.4    Oei, S.L.5    Keil, C.6    Leist, M.7
  • 68
    • 84857945772 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribose) glycohydrolase (PARG) specifically kills BRCA2-deficient tumor cells
    • Fathers C., Drayton R.M., Solovieva S., Bryant H.E. Inhibition of poly(ADP-ribose) glycohydrolase (PARG) specifically kills BRCA2-deficient tumor cells. Cell Cycle 2012, 11(5):990-997.
    • (2012) Cell Cycle , vol.11 , Issue.5 , pp. 990-997
    • Fathers, C.1    Drayton, R.M.2    Solovieva, S.3    Bryant, H.E.4
  • 69
    • 84863482663 scopus 로고    scopus 로고
    • Silencing poly(ADP-ribose) glycohydrolase (PARG) expression inhibits growth of human colon cancer cells in vitro via PI3K/Akt/NFkappa-B pathway
    • Fauzee N.J., Li Q., Wang Y.L., Pan J. Silencing poly(ADP-ribose) glycohydrolase (PARG) expression inhibits growth of human colon cancer cells in vitro via PI3K/Akt/NFkappa-B pathway. Pathol. Oncol. Res. 2012, 18(2):191-199.
    • (2012) Pathol. Oncol. Res. , vol.18 , Issue.2 , pp. 191-199
    • Fauzee, N.J.1    Li, Q.2    Wang, Y.L.3    Pan, J.4
  • 70
    • 84864258177 scopus 로고    scopus 로고
    • Silencing of apoptosis-inducing factor and poly(ADP-ribose) glycohydrolase reveals novel roles in breast cancer cell death after chemotherapy
    • Feng X., Zhou Y., Proctor A.M., Hopkins M.M., Liu M., Koh D.W. Silencing of apoptosis-inducing factor and poly(ADP-ribose) glycohydrolase reveals novel roles in breast cancer cell death after chemotherapy. Mol. Cancer 2012, 11(1):48.
    • (2012) Mol. Cancer , vol.11 , Issue.1 , pp. 48
    • Feng, X.1    Zhou, Y.2    Proctor, A.M.3    Hopkins, M.M.4    Liu, M.5    Koh, D.W.6
  • 71
    • 0032887710 scopus 로고    scopus 로고
    • Inhibition of PARP prevents oxidant-induced necrosis but not apoptosis in LLC-PK1 cells
    • Filipovic D.M., Meng X., Reeves W.B. Inhibition of PARP prevents oxidant-induced necrosis but not apoptosis in LLC-PK1 cells. Am. J. Physiol. 1999, 277(3 Pt 2):F428-F436.
    • (1999) Am. J. Physiol. , vol.277 , Issue.3 PART 2
    • Filipovic, D.M.1    Meng, X.2    Reeves, W.B.3
  • 73
    • 34547225606 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 accelerates single-strand break repair in concert with poly(ADP-ribose) glycohydrolase
    • Fisher A.E., Hochegger H., Takeda S., Caldecott K.W. Poly(ADP-ribose) polymerase 1 accelerates single-strand break repair in concert with poly(ADP-ribose) glycohydrolase. Mol. Cell. Biol. 2007, 27(15):5597-5605.
    • (2007) Mol. Cell. Biol. , vol.27 , Issue.15 , pp. 5597-5605
    • Fisher, A.E.1    Hochegger, H.2    Takeda, S.3    Caldecott, K.W.4
  • 75
    • 33845292554 scopus 로고    scopus 로고
    • Neither energy collapse nor transcription underlie in vitro neurotoxicity of poly(ADP-ribose) polymerase hyper-activation
    • Fossati S., Cipriani G., Moroni F., Chiarugi A. Neither energy collapse nor transcription underlie in vitro neurotoxicity of poly(ADP-ribose) polymerase hyper-activation. Neurochem. Int. 2007, 50(1):203-210.
    • (2007) Neurochem. Int. , vol.50 , Issue.1 , pp. 203-210
    • Fossati, S.1    Cipriani, G.2    Moroni, F.3    Chiarugi, A.4
  • 76
    • 71749119589 scopus 로고    scopus 로고
    • Global analysis of transcriptional regulation by poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in MCF-7 human breast cancer cells
    • Frizzell K.M., Gamble M.J., Berrocal J.G., Zhang T., Krishnakumar R., Cen Y., Sauve A.A., Kraus W.L. Global analysis of transcriptional regulation by poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in MCF-7 human breast cancer cells. J. Biol. Chem. 2009, 284(49):33926-33938.
    • (2009) J. Biol. Chem. , vol.284 , Issue.49 , pp. 33926-33938
    • Frizzell, K.M.1    Gamble, M.J.2    Berrocal, J.G.3    Zhang, T.4    Krishnakumar, R.5    Cen, Y.6    Sauve, A.A.7    Kraus, W.L.8
  • 77
    • 29644440131 scopus 로고    scopus 로고
    • Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles
    • Gagne J.P., Bonicalzi M.E., Gagne P., Ouellet M.E., Hendzel M.J., Poirier G.G. Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles. Biochem. J. 2005, 392(Pt 3):499-509.
    • (2005) Biochem. J. , vol.392 , Issue.PART 3 , pp. 499-509
    • Gagne, J.P.1    Bonicalzi, M.E.2    Gagne, P.3    Ouellet, M.E.4    Hendzel, M.J.5    Poirier, G.G.6
  • 80
    • 57649167477 scopus 로고    scopus 로고
    • Necroptosis: a specialized pathway of programmed necrosis
    • Galluzzi L., Kroemer G. Necroptosis: a specialized pathway of programmed necrosis. Cell 2008, 135(7):1161-1163.
    • (2008) Cell , vol.135 , Issue.7 , pp. 1161-1163
    • Galluzzi, L.1    Kroemer, G.2
  • 83
    • 33847096037 scopus 로고    scopus 로고
    • Altered poly(ADP-ribose) metabolism impairs cellular responses to genotoxic stress in a hypomorphic mutant of poly(ADP-ribose) glycohydrolase
    • Gao H., Coyle D.L., Meyer-Ficca M.L., Meyer R.G., Jacobson E.L., Wang Z.Q., Jacobson M.K. Altered poly(ADP-ribose) metabolism impairs cellular responses to genotoxic stress in a hypomorphic mutant of poly(ADP-ribose) glycohydrolase. Exp. Cell Res. 2007, 313(5):984-996.
    • (2007) Exp. Cell Res. , vol.313 , Issue.5 , pp. 984-996
    • Gao, H.1    Coyle, D.L.2    Meyer-Ficca, M.L.3    Meyer, R.G.4    Jacobson, E.L.5    Wang, Z.Q.6    Jacobson, M.K.7
  • 84
    • 2942558562 scopus 로고    scopus 로고
    • Treatment with a novel poly(ADP-ribose) glycohydrolase inhibitor reduces development of septic shock-like syndrome induced by zymosan in mice
    • Genovese T., Di Paola R., Catalano P., Li J.H., Xu W., Massuda E., Caputi A.P., Zhang J., Cuzzocrea S. Treatment with a novel poly(ADP-ribose) glycohydrolase inhibitor reduces development of septic shock-like syndrome induced by zymosan in mice. Crit. Care Med. 2004, 32(6):1365-1374.
    • (2004) Crit. Care Med. , vol.32 , Issue.6 , pp. 1365-1374
    • Genovese, T.1    Di Paola, R.2    Catalano, P.3    Li, J.H.4    Xu, W.5    Massuda, E.6    Caputi, A.P.7    Zhang, J.8    Cuzzocrea, S.9
  • 85
    • 84862758175 scopus 로고    scopus 로고
    • New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
    • Gibson B.A., Kraus W.L. New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs. Nat. Rev. Mol. Cell Biol. 2012, 13(7):411-424.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , Issue.7 , pp. 411-424
    • Gibson, B.A.1    Kraus, W.L.2
  • 86
    • 33645243011 scopus 로고    scopus 로고
    • Selective potentiation of Stat-dependent gene expression by collaborator of Stat6 (CoaSt6), a transcriptional cofactor
    • Goenka S., Boothby M. Selective potentiation of Stat-dependent gene expression by collaborator of Stat6 (CoaSt6), a transcriptional cofactor. Proc. Natl. Acad. Sci. U.S.A. 2006, 103(11):4210-4215.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , Issue.11 , pp. 4210-4215
    • Goenka, S.1    Boothby, M.2
  • 88
    • 84864381495 scopus 로고    scopus 로고
    • Herpes simplex virus 1 infection activates poly(ADP-ribose) polymerase and triggers the degradation of poly(ADP-ribose) glycohydrolase
    • Grady S.L., Hwang J., Vastag L., Rabinowitz J.D., Shenk T. Herpes simplex virus 1 infection activates poly(ADP-ribose) polymerase and triggers the degradation of poly(ADP-ribose) glycohydrolase. J. Virol. 2012, 86(15):8259-8268.
    • (2012) J. Virol. , vol.86 , Issue.15 , pp. 8259-8268
    • Grady, S.L.1    Hwang, J.2    Vastag, L.3    Rabinowitz, J.D.4    Shenk, T.5
  • 89
    • 8644267555 scopus 로고    scopus 로고
    • The zinc finger antiviral protein directly binds to specific viral mRNAs through the CCCH zinc finger motifs
    • Guo X., Carroll J.W., Macdonald M.R., Goff S.P., Gao G. The zinc finger antiviral protein directly binds to specific viral mRNAs through the CCCH zinc finger motifs. J. Virol. 2004, 78(23):12781-12787.
    • (2004) J. Virol. , vol.78 , Issue.23 , pp. 12781-12787
    • Guo, X.1    Carroll, J.W.2    Macdonald, M.R.3    Goff, S.P.4    Gao, G.5
  • 91
    • 33644984966 scopus 로고    scopus 로고
    • Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage
    • Haince J.F., Ouellet M.E., McDonald D., Hendzel M.J., Poirier G.G. Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage. Biochim. Biophys. Acta 2006, 1763(2):226-237.
    • (2006) Biochim. Biophys. Acta , vol.1763 , Issue.2 , pp. 226-237
    • Haince, J.F.1    Ouellet, M.E.2    McDonald, D.3    Hendzel, M.J.4    Poirier, G.G.5
  • 93
    • 38449088040 scopus 로고    scopus 로고
    • The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases
    • Hassa P.O., Hottiger M.O. The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases. Front. Biosci. 2008, 13:3046-3082.
    • (2008) Front. Biosci. , vol.13 , pp. 3046-3082
    • Hassa, P.O.1    Hottiger, M.O.2
  • 94
    • 33749260519 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?
    • Hassa P.O., Haenni S.S., Elser M., Hottiger M.O. Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?. Microbiol. Mol. Biol. Rev. 2006, 70(3):789-829.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , Issue.3 , pp. 789-829
    • Hassa, P.O.1    Haenni, S.S.2    Elser, M.3    Hottiger, M.O.4
  • 95
    • 0023020120 scopus 로고
    • Purification and characterization of poly(ADP-ribose) glycohydrolase. Different modes of action on large and small poly(ADP-ribose)
    • Hatakeyama K., Nemoto Y., Ueda K., Hayaishi O. Purification and characterization of poly(ADP-ribose) glycohydrolase. Different modes of action on large and small poly(ADP-ribose). J. Biol. Chem. 1986, 261(32):14902-14911.
    • (1986) J. Biol. Chem. , vol.261 , Issue.32 , pp. 14902-14911
    • Hatakeyama, K.1    Nemoto, Y.2    Ueda, K.3    Hayaishi, O.4
  • 96
    • 25444471892 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase (PARP-1) in homologous recombination and as a target for cancer therapy
    • Helleday T., Bryant H.E., Schultz N. Poly(ADP-ribose) polymerase (PARP-1) in homologous recombination and as a target for cancer therapy. Cell Cycle 2005, 4(9):1176-1178.
    • (2005) Cell Cycle , vol.4 , Issue.9 , pp. 1176-1178
    • Helleday, T.1    Bryant, H.E.2    Schultz, N.3
  • 97
    • 44949183554 scopus 로고    scopus 로고
    • Loss of apoptosis-inducing factor results in cell-type-specific neurogenesis defects
    • Ishimura R., Martin G.R., Ackerman S.L. Loss of apoptosis-inducing factor results in cell-type-specific neurogenesis defects. J. Neurosci. 2008, 28(19):4938-4948.
    • (2008) J. Neurosci. , vol.28 , Issue.19 , pp. 4938-4948
    • Ishimura, R.1    Martin, G.R.2    Ackerman, S.L.3
  • 98
    • 67649855305 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation of heterogeneous nuclear ribonucleoproteins modulates splicing
    • Ji Y., Tulin A.V. Poly(ADP-ribosyl)ation of heterogeneous nuclear ribonucleoproteins modulates splicing. Nucleic Acids Res. 2009, 37(11):3501-3513.
    • (2009) Nucleic Acids Res. , vol.37 , Issue.11 , pp. 3501-3513
    • Ji, Y.1    Tulin, A.V.2
  • 99
    • 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. A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues. Genomics 1999, 57(3):442-445.
    • (1999) Genomics , vol.57 , Issue.3 , pp. 442-445
    • Johansson, M.1
  • 100
    • 67649786599 scopus 로고    scopus 로고
    • Mitochondrial micro-calpain is not involved in the processing of apoptosis-inducing factor
    • Joshi A., Bondada V., Geddes J.W. Mitochondrial micro-calpain is not involved in the processing of apoptosis-inducing factor. Exp. Neurol. 2009, 218(2):221-227.
    • (2009) Exp. Neurol. , vol.218 , Issue.2 , pp. 221-227
    • Joshi, A.1    Bondada, V.2    Geddes, J.W.3
  • 102
    • 0018723423 scopus 로고
    • Poly(ADP-ribose) levels in carcinogen-treated cells
    • Juarez-Salinas H., Sims J.L., Jacobson M.K. Poly(ADP-ribose) levels in carcinogen-treated cells. Nature 1979, 282(5740):740-741.
    • (1979) Nature , vol.282 , Issue.5740 , pp. 740-741
    • Juarez-Salinas, H.1    Sims, J.L.2    Jacobson, M.K.3
  • 104
    • 0027255417 scopus 로고
    • Specific proteolytic cleavage of poly(ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis
    • Kaufmann S.H., Desnoyers S., Ottaviano Y., Davidson N.E., Poirier G.G. Specific proteolytic cleavage of poly(ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis. Cancer Res. 1993, 53(17):3976-3985.
    • (1993) Cancer Res. , vol.53 , Issue.17 , pp. 3976-3985
    • Kaufmann, S.H.1    Desnoyers, S.2    Ottaviano, Y.3    Davidson, N.E.4    Poirier, G.G.5
  • 105
    • 33845931841 scopus 로고    scopus 로고
    • MNNG-induced cell death is controlled by interactions between PARP-1, poly(ADP-ribose) glycohydrolase, and XRCC1
    • Keil C., Grobe T., Oei S.L. MNNG-induced cell death is controlled by interactions between PARP-1, poly(ADP-ribose) glycohydrolase, and XRCC1. J. Biol. Chem. 2006, 281(45):34394-34405.
    • (2006) J. Biol. Chem. , vol.281 , Issue.45 , pp. 34394-34405
    • Keil, C.1    Grobe, T.2    Oei, S.L.3
  • 109
    • 10944227347 scopus 로고    scopus 로고
    • NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1
    • Kim M.Y., Mauro S., Gevry N., Lis J.T., Kraus W.L. NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1. Cell 2004, 119(6):803-814.
    • (2004) Cell , vol.119 , Issue.6 , pp. 803-814
    • Kim, M.Y.1    Mauro, S.2    Gevry, N.3    Lis, J.T.4    Kraus, W.L.5
  • 110
    • 24344454692 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal
    • Kim M.Y., Zhang T., Kraus W.L. Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal. Genes Dev. 2005, 19(17):1951-1967.
    • (2005) Genes Dev. , vol.19 , Issue.17 , pp. 1951-1967
    • Kim, M.Y.1    Zhang, T.2    Kraus, W.L.3
  • 111
    • 84861869442 scopus 로고    scopus 로고
    • Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element
    • Kim I.K., Kiefer J.R., Ho C.M., Stegeman R.A., Classen S., Tainer J.A., Ellenberger T. Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element. Nat. Struct. Mol. Biol. 2012, 19(6):653-656.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , Issue.6 , pp. 653-656
    • Kim, I.K.1    Kiefer, J.R.2    Ho, C.M.3    Stegeman, R.A.4    Classen, S.5    Tainer, J.A.6    Ellenberger, T.7
  • 112
    • 0141538207 scopus 로고    scopus 로고
    • Nicotinamide offers multiple protective mechanisms in stroke as a precursor for NAD+, as a PARP inhibitor and by partial restoration of mitochondrial function
    • Klaidman L., Morales M., Kem S., Yang J., Chang M.L., Adams J.D. Nicotinamide offers multiple protective mechanisms in stroke as a precursor for NAD+, as a PARP inhibitor and by partial restoration of mitochondrial function. Pharmacology 2003, 69(3):150-157.
    • (2003) Pharmacology , vol.69 , Issue.3 , pp. 150-157
    • Klaidman, L.1    Morales, M.2    Kem, S.3    Yang, J.4    Chang, M.L.5    Adams, J.D.6
  • 116
    • 0141792692 scopus 로고    scopus 로고
    • SAR analysis of adenosine diphosphate (hydroxymethyl)pyrrolidinediol inhibition of poly(ADP-ribose) glycohydrolase
    • Koh D.W., Coyle D.L., Mehta N., Ramsinghani S., Kim H., Slama J.T., Jacobson M.K. SAR analysis of adenosine diphosphate (hydroxymethyl)pyrrolidinediol inhibition of poly(ADP-ribose) glycohydrolase. J. Med. Chem. 2003, 46(20):4322-4332.
    • (2003) J. Med. Chem. , vol.46 , Issue.20 , pp. 4322-4332
    • Koh, D.W.1    Coyle, D.L.2    Mehta, N.3    Ramsinghani, S.4    Kim, H.5    Slama, J.T.6    Jacobson, M.K.7
  • 118
    • 30444446344 scopus 로고    scopus 로고
    • Critical role of PI3-kinase/Akt activation in the PARP inhibitor induced heart function recovery during ischemia-reperfusion
    • Kovacs K., Toth A., Deres P., Kalai T., Hideg K., Gallyas F., Sumegi B. Critical role of PI3-kinase/Akt activation in the PARP inhibitor induced heart function recovery during ischemia-reperfusion. Biochem. Pharmacol. 2006, 71(4):441-452.
    • (2006) Biochem. Pharmacol. , vol.71 , Issue.4 , pp. 441-452
    • Kovacs, K.1    Toth, A.2    Deres, P.3    Kalai, T.4    Hideg, K.5    Gallyas, F.6    Sumegi, B.7
  • 119
    • 44649130038 scopus 로고    scopus 로고
    • Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation
    • Kraus W.L. Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation. Curr. Opin. Cell Biol. 2008, 20(3):294-302.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , Issue.3 , pp. 294-302
    • Kraus, W.L.1
  • 120
    • 77954274504 scopus 로고    scopus 로고
    • The PARP side of the nucleus: molecular actions, physiological outcomes, and clinical targets
    • Krishnakumar R., Kraus W.L. The PARP side of the nucleus: molecular actions, physiological outcomes, and clinical targets. Mol. Cell 2010, 39(1):8-24.
    • (2010) Mol. Cell , vol.39 , Issue.1 , pp. 8-24
    • Krishnakumar, R.1    Kraus, W.L.2
  • 121
    • 38949198773 scopus 로고    scopus 로고
    • Reciprocal binding of PARP-1 and histone H1 at promoters specifies transcriptional outcomes
    • Krishnakumar R., Gamble M.J., Frizzell K.M., Berrocal J.G., Kininis M., Kraus W.L. Reciprocal binding of PARP-1 and histone H1 at promoters specifies transcriptional outcomes. Science 2008, 319(5864):819-821.
    • (2008) Science , vol.319 , Issue.5864 , pp. 819-821
    • Krishnakumar, R.1    Gamble, M.J.2    Frizzell, K.M.3    Berrocal, J.G.4    Kininis, M.5    Kraus, W.L.6
  • 122
    • 39749123276 scopus 로고    scopus 로고
    • Apoptosis and necrosis: detection, discrimination and phagocytosis
    • Krysko D.V., Vanden Berghe T., D'Herde K., Vandenabeele P. Apoptosis and necrosis: detection, discrimination and phagocytosis. Methods 2008, 44(3):205-221.
    • (2008) Methods , vol.44 , Issue.3 , pp. 205-221
    • Krysko, D.V.1    Vanden Berghe, T.2    D'Herde, K.3    Vandenabeele, P.4
  • 124
    • 84860806404 scopus 로고    scopus 로고
    • Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1
    • Langelier M.F., Planck J.L., Roy S., Pascal J.M. Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1. Science 2012, 336(6082):728-732.
    • (2012) Science , vol.336 , Issue.6082 , pp. 728-732
    • Langelier, M.F.1    Planck, J.L.2    Roy, S.3    Pascal, J.M.4
  • 125
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik Y.A., Kaufmann S.H., Desnoyers S., Poirier G.G., Earnshaw W.C. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 1994, 371(6495):346-347.
    • (1994) Nature , vol.371 , Issue.6495 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 126
    • 79955957616 scopus 로고    scopus 로고
    • Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm
    • Leung A.K., Vyas S., Rood J.E., Bhutkar A., Sharp P.A., Chang P. Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm. Mol. Cell 2011, 42(4):489-499.
    • (2011) Mol. Cell , vol.42 , Issue.4 , pp. 489-499
    • Leung, A.K.1    Vyas, S.2    Rood, J.E.3    Bhutkar, A.4    Sharp, P.A.5    Chang, P.6
  • 127
    • 84055199304 scopus 로고    scopus 로고
    • Nondegradative ubiquitination of apoptosis inducing factor (AIF) by X-linked inhibitor of apoptosis at a residue critical for AIF-mediated chromatin degradation
    • Lewis E.M., Wilkinson A.S., Davis N.Y., Horita D.A., Wilkinson J.C. Nondegradative ubiquitination of apoptosis inducing factor (AIF) by X-linked inhibitor of apoptosis at a residue critical for AIF-mediated chromatin degradation. Biochemistry 2011, 50(51):11084-11096.
    • (2011) Biochemistry , vol.50 , Issue.51 , pp. 11084-11096
    • Lewis, E.M.1    Wilkinson, A.S.2    Davis, N.Y.3    Horita, D.A.4    Wilkinson, J.C.5
  • 128
    • 0036084912 scopus 로고    scopus 로고
    • Role of ADP-ribose in 11,12-EET-induced activation of K(Ca) channels in coronary arterial smooth muscle cells
    • Li P.L., Zhang D.X., Ge Z.D., Campbell W.B. Role of ADP-ribose in 11,12-EET-induced activation of K(Ca) channels in coronary arterial smooth muscle cells. Am. J. Physiol. Heart Circ. Physiol. 2002, 282(4):H1229-H1236.
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.282 , Issue.4
    • Li, P.L.1    Zhang, D.X.2    Ge, Z.D.3    Campbell, W.B.4
  • 129
    • 84859892610 scopus 로고    scopus 로고
    • RNA interference of PARG could inhibit the metastatic potency of colon carcinoma cells via PI3-kinase/Akt pathway
    • Li Q., Li M., Wang Y.L., Fauzee N.J., Yang Y., Pan J., Yang L., Lazar A. RNA interference of PARG could inhibit the metastatic potency of colon carcinoma cells via PI3-kinase/Akt pathway. Cell. Physiol. Biochem. 2012, 29(3-4):361-372.
    • (2012) Cell. Physiol. Biochem. , vol.29 , Issue.3-4 , pp. 361-372
    • Li, Q.1    Li, M.2    Wang, Y.L.3    Fauzee, N.J.4    Yang, Y.5    Pan, J.6    Yang, L.7    Lazar, A.8
  • 130
    • 0031010494 scopus 로고    scopus 로고
    • Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase
    • Lin W., Ame J.C., Aboul-Ela N., Jacobson E.L., Jacobson M.K. Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 1997, 272(18):11895-11901.
    • (1997) J. Biol. Chem. , vol.272 , Issue.18 , pp. 11895-11901
    • Lin, W.1    Ame, J.C.2    Aboul-Ela, N.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 131
    • 77956646565 scopus 로고    scopus 로고
    • Destruction of a destructor: a new avenue for cancer therapeutics targeting the Wnt pathway
    • Liu C., He X. Destruction of a destructor: a new avenue for cancer therapeutics targeting the Wnt pathway. J. Mol. Cell Biol. 2010, 2(2):70-73.
    • (2010) J. Mol. Cell Biol. , vol.2 , Issue.2 , pp. 70-73
    • Liu, C.1    He, X.2
  • 134
    • 33845637791 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits the nuclear import of apoptosis-inducing factor to avoid DNA fragmentation in TF-1 cells during erythropoiesis
    • Lui J.C., Kong S.K. Heat shock protein 70 inhibits the nuclear import of apoptosis-inducing factor to avoid DNA fragmentation in TF-1 cells during erythropoiesis. FEBS Lett. 2007, 581(1):109-117.
    • (2007) FEBS Lett. , vol.581 , Issue.1 , pp. 109-117
    • Lui, J.C.1    Kong, S.K.2
  • 135
    • 33646946845 scopus 로고    scopus 로고
    • PARP-2 interacts with TTF-1 and regulates expression of surfactant protein-B
    • Maeda Y., Hunter T.C., Loudy D.E., Dave V., Schreiber V., Whitsett J.A. PARP-2 interacts with TTF-1 and regulates expression of surfactant protein-B. J. Biol. Chem. 2006, 281(14):9600-9606.
    • (2006) J. Biol. Chem. , vol.281 , Issue.14 , pp. 9600-9606
    • Maeda, Y.1    Hunter, T.C.2    Loudy, D.E.3    Dave, V.4    Schreiber, V.5    Whitsett, J.A.6
  • 136
    • 0028246305 scopus 로고
    • Poly(ADP-ribose) molecules formed during DNA repair in vivo
    • Malanga M., Althaus F.R. Poly(ADP-ribose) molecules formed during DNA repair in vivo. J. Biol. Chem. 1994, 269(26):17691-17696.
    • (1994) J. Biol. Chem. , vol.269 , Issue.26 , pp. 17691-17696
    • Malanga, M.1    Althaus, F.R.2
  • 137
    • 24744447821 scopus 로고    scopus 로고
    • The role of poly(ADP-ribose) in the DNA damage signaling network
    • Malanga M., Althaus F.R. The role of poly(ADP-ribose) in the DNA damage signaling network. Biochem. Cell Biol. 2005, 83(3):354-364.
    • (2005) Biochem. Cell Biol. , vol.83 , Issue.3 , pp. 354-364
    • Malanga, M.1    Althaus, F.R.2
  • 141
    • 34547153717 scopus 로고    scopus 로고
    • Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose) glycohydrolase (PARG) activity
    • Meyer R.G., Meyer-Ficca M.L., Whatcott C.J., Jacobson E.L., Jacobson M.K. Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose) glycohydrolase (PARG) activity. Exp. Cell Res. 2007, 313(13):2920-2936.
    • (2007) Exp. Cell Res. , vol.313 , Issue.13 , pp. 2920-2936
    • Meyer, R.G.1    Meyer-Ficca, M.L.2    Whatcott, C.J.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 142
    • 2942707644 scopus 로고    scopus 로고
    • Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments
    • Meyer-Ficca M.L., Meyer R.G., Coyle D.L., Jacobson E.L., Jacobson M.K. Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments. Exp. Cell Res. 2004, 297(2):521-532.
    • (2004) Exp. Cell Res. , vol.297 , Issue.2 , pp. 521-532
    • Meyer-Ficca, M.L.1    Meyer, R.G.2    Coyle, D.L.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 143
    • 67649672425 scopus 로고    scopus 로고
    • Disruption of poly(ADP-ribose) homeostasis affects spermiogenesis and sperm chromatin integrity in mice
    • Meyer-Ficca M.L., Lonchar J., Credidio C., Ihara M., Li Y., Wang Z.Q., Meyer R.G. Disruption of poly(ADP-ribose) homeostasis affects spermiogenesis and sperm chromatin integrity in mice. Biol. Reprod. 2009, 81(1):46-55.
    • (2009) Biol. Reprod. , vol.81 , Issue.1 , pp. 46-55
    • Meyer-Ficca, M.L.1    Lonchar, J.2    Credidio, C.3    Ihara, M.4    Li, Y.5    Wang, Z.Q.6    Meyer, R.G.7
  • 144
    • 78649815064 scopus 로고    scopus 로고
    • Deletion of the nuclear isoform of poly(ADP-ribose) glycohydrolase (PARG) reveals its function in DNA repair, genomic stability and tumorigenesis
    • Min W., Cortes U., Herceg Z., Tong W.M., Wang Z.Q. Deletion of the nuclear isoform of poly(ADP-ribose) glycohydrolase (PARG) reveals its function in DNA repair, genomic stability and tumorigenesis. Carcinogenesis 2010, 31(12):2058-2065.
    • (2010) Carcinogenesis , vol.31 , Issue.12 , pp. 2058-2065
    • Min, W.1    Cortes, U.2    Herceg, Z.3    Tong, W.M.4    Wang, Z.Q.5
  • 145
    • 0021099468 scopus 로고
    • Probable helical conformation of poly(ADP-ribose). The effect of cations on spectral properties
    • Minaga T., Kun E. Probable helical conformation of poly(ADP-ribose). The effect of cations on spectral properties. J. Biol. Chem. 1983, 258(9):5726-5730.
    • (1983) J. Biol. Chem. , vol.258 , Issue.9 , pp. 5726-5730
    • Minaga, T.1    Kun, E.2
  • 146
    • 0015240269 scopus 로고
    • Splitting of the ribose-ribose linkage of poly(adenosine diphosphate-robose) by a calf thymus extract
    • Miwa M., Sugimura T. Splitting of the ribose-ribose linkage of poly(adenosine diphosphate-robose) by a calf thymus extract. J. Biol. Chem. 1971, 246(20):6362-6364.
    • (1971) J. Biol. Chem. , vol.246 , Issue.20 , pp. 6362-6364
    • Miwa, M.1    Sugimura, T.2
  • 147
    • 0018346860 scopus 로고
    • Structure of poly(adenosine diphosphate ribose): identification of 2'-[1″-ribosyl-2″-(or 3″-)(1‴-ribosyl)]adenosine-5',5″,5‴-tris(phosphate) as a branch linkage
    • Miwa M., Saikawa N., Yamaizumi Z., Nishimura S., Sugimura T. Structure of poly(adenosine diphosphate ribose): identification of 2'-[1″-ribosyl-2″-(or 3″-)(1‴-ribosyl)]adenosine-5',5″,5‴-tris(phosphate) as a branch linkage. Proc. Natl. Acad. Sci. U.S.A. 1979, 76(2):595-599.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , Issue.2 , pp. 595-599
    • Miwa, M.1    Saikawa, N.2    Yamaizumi, Z.3    Nishimura, S.4    Sugimura, T.5
  • 148
    • 79960206370 scopus 로고    scopus 로고
    • PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-dependent mechanisms
    • Mortusewicz O., Fouquerel E., Ame J.C., Leonhardt H., Schreiber V. PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-dependent mechanisms. Nucleic Acids Res. 2011, 39(12):5045-5056.
    • (2011) Nucleic Acids Res. , vol.39 , Issue.12 , pp. 5045-5056
    • Mortusewicz, O.1    Fouquerel, E.2    Ame, J.C.3    Leonhardt, H.4    Schreiber, V.5
  • 149
    • 34347344991 scopus 로고    scopus 로고
    • Sequential activation of poly(ADP-ribose) polymerase 1, calpains, and Bax is essential in apoptosis-inducing factor-mediated programmed necrosis
    • Moubarak R.S., Yuste V.J., Artus C., Bouharrour A., Greer P.A., Menissier-de Murcia J., Susin S.A. Sequential activation of poly(ADP-ribose) polymerase 1, calpains, and Bax is essential in apoptosis-inducing factor-mediated programmed necrosis. Mol. Cell. Biol. 2007, 27(13):4844-4862.
    • (2007) Mol. Cell. Biol. , vol.27 , Issue.13 , pp. 4844-4862
    • Moubarak, R.S.1    Yuste, V.J.2    Artus, C.3    Bouharrour, A.4    Greer, P.A.5    Menissier-de Murcia, J.6    Susin, S.A.7
  • 150
    • 33845659501 scopus 로고    scopus 로고
    • Tannic acid synergizes the cytotoxicity of chemotherapeutic drugs in human cholangiocarcinoma by modulating drug efflux pathways
    • Naus P.J., Henson R., Bleeker G., Wehbe H., Meng F., Patel T. Tannic acid synergizes the cytotoxicity of chemotherapeutic drugs in human cholangiocarcinoma by modulating drug efflux pathways. J. Hepatol. 2007, 46(2):222-229.
    • (2007) J. Hepatol. , vol.46 , Issue.2 , pp. 222-229
    • Naus, P.J.1    Henson, R.2    Bleeker, G.3    Wehbe, H.4    Meng, F.5    Patel, T.6
  • 151
    • 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)
    • Niere M., Mashimo M., Agledal L., Dolle 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. 2012, 287(20):16088-16102.
    • (2012) J. Biol. Chem. , vol.287 , Issue.20 , pp. 16088-16102
    • Niere, M.1    Mashimo, M.2    Agledal, L.3    Dolle, C.4    Kasamatsu, A.5    Kato, J.6    Moss, J.7    Ziegler, M.8
  • 153
    • 84889476358 scopus 로고    scopus 로고
    • The promises and pitfalls of small-molecule inhibition of poly(ADP-ribose) glycohydrolase (PARG)
    • Wiley & Sons, New York
    • Nottbohm A.C., Hergenrother P.J. The promises and pitfalls of small-molecule inhibition of poly(ADP-ribose) glycohydrolase (PARG). Drug Discovery Research: New Frontiers in the Post-Genomic Era 2007, 163-165. Wiley & Sons, New York.
    • (2007) Drug Discovery Research: New Frontiers in the Post-Genomic Era , pp. 163-165
    • Nottbohm, A.C.1    Hergenrother, P.J.2
  • 154
    • 0034725720 scopus 로고    scopus 로고
    • ATP for the DNA ligation step in base excision repair is generated from poly(ADP-ribose)
    • Oei S.L., Ziegler M. ATP for the DNA ligation step in base excision repair is generated from poly(ADP-ribose). J. Biol. Chem. 2000, 275(30):23234-23239.
    • (2000) J. Biol. Chem. , vol.275 , Issue.30 , pp. 23234-23239
    • Oei, S.L.1    Ziegler, M.2
  • 155
    • 33644849513 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase
    • Oka S., Kato J., Moss J. Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 2006, 281(2):705-713.
    • (2006) J. Biol. Chem. , vol.281 , Issue.2 , pp. 705-713
    • Oka, S.1    Kato, J.2    Moss, J.3
  • 156
    • 0017712939 scopus 로고
    • Purification and properties of poly(adenosine diphosphate ribose) synthetase
    • Okayama H., Edson C.M., Fukushima M., Ueda K., Hayaishi O. Purification and properties of poly(adenosine diphosphate ribose) synthetase. J. Biol. Chem. 1977, 252(20):7000-7005.
    • (1977) J. Biol. Chem. , vol.252 , Issue.20 , pp. 7000-7005
    • Okayama, H.1    Edson, C.M.2    Fukushima, M.3    Ueda, K.4    Hayaishi, O.5
  • 157
    • 76749103351 scopus 로고    scopus 로고
    • Discovery of novel poly(ADP-ribose) glycohydrolase inhibitors by a quantitative assay system using dot-blot with anti-poly(ADP-ribose)
    • Okita N., Ashizawa D., Ohta R., Abe H., Tanuma S. Discovery of novel poly(ADP-ribose) glycohydrolase inhibitors by a quantitative assay system using dot-blot with anti-poly(ADP-ribose). Biochem. Biophys. Res. Commun. 2010, 392(4):485-489.
    • (2010) Biochem. Biophys. Res. Commun. , vol.392 , Issue.4 , pp. 485-489
    • Okita, N.1    Ashizawa, D.2    Ohta, R.3    Abe, H.4    Tanuma, S.5
  • 158
    • 78650527416 scopus 로고    scopus 로고
    • Cell death mechanisms and their implications in toxicology
    • Orrenius S., Nicotera P., Zhivotovsky B. Cell death mechanisms and their implications in toxicology. Toxicol. Sci. 2011, 119(1):3-19.
    • (2011) Toxicol. Sci. , vol.119 , Issue.1 , pp. 3-19
    • Orrenius, S.1    Nicotera, P.2    Zhivotovsky, B.3
  • 159
    • 17844394478 scopus 로고    scopus 로고
    • Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space
    • Otera H., Ohsakaya S., Nagaura Z., Ishihara N., Mihara K. Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space. EMBO J. 2005, 24(7):1375-1386.
    • (2005) EMBO J. , vol.24 , Issue.7 , pp. 1375-1386
    • Otera, H.1    Ohsakaya, S.2    Nagaura, Z.3    Ishihara, N.4    Mihara, K.5
  • 160
    • 0036069642 scopus 로고    scopus 로고
    • Tej defines a role for poly(ADP-ribosyl)ation in establishing period length of the arabidopsis circadian oscillator
    • Panda S., Poirier G.G., Kay S.A. tej defines a role for poly(ADP-ribosyl)ation in establishing period length of the arabidopsis circadian oscillator. Dev. Cell 2002, 3(1):51-61.
    • (2002) Dev. Cell , vol.3 , Issue.1 , pp. 51-61
    • Panda, S.1    Poirier, G.G.2    Kay, S.A.3
  • 161
    • 32944479041 scopus 로고    scopus 로고
    • The Raf inhibitor BAY 43-9006 (Sorafenib) induces caspase-independent apoptosis in melanoma cells
    • Panka D.J., Wang W., Atkins M.B., Mier J.W. The Raf inhibitor BAY 43-9006 (Sorafenib) induces caspase-independent apoptosis in melanoma cells. Cancer Res. 2006, 66(3):1611-1619.
    • (2006) Cancer Res. , vol.66 , Issue.3 , pp. 1611-1619
    • Panka, D.J.1    Wang, W.2    Atkins, M.B.3    Mier, J.W.4
  • 162
    • 17444364433 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 protects excessive DNA strand breaks from deterioration during repair in human cell extracts
    • Parsons J.L., Dianova I.I., Allinson S.L., Dianov G.L. Poly(ADP-ribose) polymerase-1 protects excessive DNA strand breaks from deterioration during repair in human cell extracts. FEBS J. 2005, 272(8):2012-2021.
    • (2005) FEBS J. , vol.272 , Issue.8 , pp. 2012-2021
    • Parsons, J.L.1    Dianova, I.I.2    Allinson, S.L.3    Dianov, G.L.4
  • 163
    • 20544475918 scopus 로고    scopus 로고
    • Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain
    • Patel C.N., Koh D.W., Jacobson M.K., Oliveira M.A. Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain. Biochem. J. 2005, 388(Pt 2):493-500.
    • (2005) Biochem. J. , vol.388 , Issue.PART 2 , pp. 493-500
    • Patel, C.N.1    Koh, D.W.2    Jacobson, M.K.3    Oliveira, M.A.4
  • 166
    • 2542457893 scopus 로고    scopus 로고
    • ATP-dependent selection between single nucleotide and long patch base excision repair
    • Petermann E., Ziegler M., Oei S.L. ATP-dependent selection between single nucleotide and long patch base excision repair. DNA Repair 2003, 2(10):1101-1114.
    • (2003) DNA Repair , vol.2 , Issue.10 , pp. 1101-1114
    • Petermann, E.1    Ziegler, M.2    Oei, S.L.3
  • 167
    • 0018748646 scopus 로고
    • Modification of L1210 cell nuclear proteins by 1-methyl-1-nitrosourea and 1-methyl-3-nitro-1-nitrosoguanidine
    • Pinsky S.D., Tew K.D., Smulson M.E., Woolley P.V. Modification of L1210 cell nuclear proteins by 1-methyl-1-nitrosourea and 1-methyl-3-nitro-1-nitrosoguanidine. Cancer Res. 1979, 39(3):923-928.
    • (1979) Cancer Res. , vol.39 , Issue.3 , pp. 923-928
    • Pinsky, S.D.1    Tew, K.D.2    Smulson, M.E.3    Woolley, P.V.4
  • 168
    • 27644528391 scopus 로고    scopus 로고
    • DNA-induced dimerization of poly(ADP-ribose) polymerase-1 triggers its activation
    • Pion E., Ullmann G.M., Ame J.C., Gerard D., de Murcia G., Bombarda E. DNA-induced dimerization of poly(ADP-ribose) polymerase-1 triggers its activation. Biochemistry 2005, 44(44):14670-14681.
    • (2005) Biochemistry , vol.44 , Issue.44 , pp. 14670-14681
    • Pion, E.1    Ullmann, G.M.2    Ame, J.C.3    Gerard, D.4    de Murcia, G.5    Bombarda, E.6
  • 169
    • 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., Althaus F.R. Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 2000, 275(52):40974-40980.
    • (2000) J. Biol. Chem. , vol.275 , Issue.52 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 171
    • 34547783237 scopus 로고    scopus 로고
    • Spatial and functional relationship between poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in the brain
    • 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 2007, 148(1):198-211.
    • (2007) Neuroscience , vol.148 , Issue.1 , 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
  • 172
    • 14844328621 scopus 로고    scopus 로고
    • Calpain I induces cleavage and release of apoptosis-inducing factor from isolated mitochondria
    • Polster B.M., Basanez G., Etxebarria A., Hardwick J.M., Nicholls D.G. Calpain I induces cleavage and release of apoptosis-inducing factor from isolated mitochondria. J. Biol. Chem. 2005, 280(8):6447-6454.
    • (2005) J. Biol. Chem. , vol.280 , Issue.8 , pp. 6447-6454
    • Polster, B.M.1    Basanez, G.2    Etxebarria, A.3    Hardwick, J.M.4    Nicholls, D.G.5
  • 174
    • 4644241346 scopus 로고    scopus 로고
    • A nonradiometric, high-throughput assay for poly(ADP-ribose) glycohydrolase (PARG): application to inhibitor identification and evaluation
    • Putt K.S., Hergenrother P.J. A nonradiometric, high-throughput assay for poly(ADP-ribose) glycohydrolase (PARG): application to inhibitor identification and evaluation. Anal. Biochem. 2004, 333(2):256-264.
    • (2004) Anal. Biochem. , vol.333 , Issue.2 , pp. 256-264
    • Putt, K.S.1    Hergenrother, P.J.2
  • 175
    • 4844220063 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribose) glycohydrolase by gallotannin selectively up-regulates expression of proinflammatory genes
    • Rapizzi E., Fossati S., Moroni F., Chiarugi A. Inhibition of poly(ADP-ribose) glycohydrolase by gallotannin selectively up-regulates expression of proinflammatory genes. Mol. Pharmacol. 2004, 66(4):890-898.
    • (2004) Mol. Pharmacol. , vol.66 , Issue.4 , pp. 890-898
    • Rapizzi, E.1    Fossati, S.2    Moroni, F.3    Chiarugi, A.4
  • 176
    • 0032539957 scopus 로고    scopus 로고
    • Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from crystal structures and homology modeling
    • Ruf A., de Murcia G., Schulz G.E. Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from crystal structures and homology modeling. Biochemistry 1998, 37(11):3893-3900.
    • (1998) Biochemistry , vol.37 , Issue.11 , pp. 3893-3900
    • Ruf, A.1    de Murcia, G.2    Schulz, G.E.3
  • 177
    • 0032562650 scopus 로고    scopus 로고
    • The mechanism of the elongation and branching reaction of poly(ADP-ribose) polymerase as derived from crystal structures and mutagenesis
    • Ruf A., Rolli V., de Murcia G., Schulz G.E. The mechanism of the elongation and branching reaction of poly(ADP-ribose) polymerase as derived from crystal structures and mutagenesis. J. Mol. Biol. 1998, 278(1):57-65.
    • (1998) J. Mol. Biol. , vol.278 , Issue.1 , pp. 57-65
    • Ruf, A.1    Rolli, V.2    de Murcia, G.3    Schulz, G.E.4
  • 179
    • 33846709501 scopus 로고    scopus 로고
    • Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes
    • Sanders B.D., Zhao K., Slama J.T., Marmorstein R. Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes. Mol. Cell 2007, 25(3):463-472.
    • (2007) Mol. Cell , vol.25 , Issue.3 , pp. 463-472
    • Sanders, B.D.1    Zhao, K.2    Slama, J.T.3    Marmorstein, R.4
  • 180
    • 69249114710 scopus 로고    scopus 로고
    • Involvement of VDAC, Bax and ceramides in the efflux of AIF from mitochondria during curcumin-induced apoptosis
    • Scharstuhl A., Mutsaers H.A., Pennings S.W., Russel F.G., Wagener F.A. Involvement of VDAC, Bax and ceramides in the efflux of AIF from mitochondria during curcumin-induced apoptosis. PLoS One 2009, 4(8):e6688.
    • (2009) PLoS One , vol.4 , Issue.8
    • Scharstuhl, A.1    Mutsaers, H.A.2    Pennings, S.W.3    Russel, F.G.4    Wagener, F.A.5
  • 181
    • 79955542915 scopus 로고    scopus 로고
    • A diverse range of gene products are effectors of the type I interferon antiviral response
    • Schoggins J.W., Wilson S.J., Panis M., Murphy M.Y., Jones C.T., Bieniasz P., Rice C.M. A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 2011, 472(7344):481-485.
    • (2011) Nature , vol.472 , Issue.7344 , pp. 481-485
    • Schoggins, J.W.1    Wilson, S.J.2    Panis, M.3    Murphy, M.Y.4    Jones, C.T.5    Bieniasz, P.6    Rice, C.M.7
  • 183
    • 70349983259 scopus 로고    scopus 로고
    • Tannins: current knowledge of food sources, intake, bioavailability and biological effects
    • Serrano J., Puupponen-Pimia R., Dauer A., Aura A.M., Saura-Calixto F. Tannins: current knowledge of food sources, intake, bioavailability and biological effects. Mol. Nutr. Food Res. 2009, 53(Suppl. 2):S310-S329.
    • (2009) Mol. Nutr. Food Res. , vol.53 , Issue.SUPPL. 2
    • Serrano, J.1    Puupponen-Pimia, R.2    Dauer, A.3    Aura, A.M.4    Saura-Calixto, F.5
  • 185
    • 0021112635 scopus 로고
    • Poly(ADP-ribose) polymerase inhibitors preserve nicotinamide adenine dinucleotide and adenosine 5'-triphosphate pools in DNA-damaged cells: mechanism of stimulation of unscheduled DNA synthesis
    • Sims J.L., Berger S.J., Berger N.A. Poly(ADP-ribose) polymerase inhibitors preserve nicotinamide adenine dinucleotide and adenosine 5'-triphosphate pools in DNA-damaged cells: mechanism of stimulation of unscheduled DNA synthesis. Biochemistry 1983, 22(22):5188-5194.
    • (1983) Biochemistry , vol.22 , Issue.22 , pp. 5188-5194
    • Sims, J.L.1    Berger, S.J.2    Berger, N.A.3
  • 186
    • 72749086075 scopus 로고    scopus 로고
    • Evidence for caspase effects on release of cytochrome c and AIF in a model of ischemia in cortical neurons
    • Singh M.H., Brooke S.M., Zemlyak I., Sapolsky R.M. Evidence for caspase effects on release of cytochrome c and AIF in a model of ischemia in cortical neurons. Neurosci. Lett. 2010, 469(2):179-183.
    • (2010) Neurosci. Lett. , vol.469 , Issue.2 , pp. 179-183
    • Singh, M.H.1    Brooke, S.M.2    Zemlyak, I.3    Sapolsky, R.M.4
  • 188
    • 0029020228 scopus 로고
    • Specific inhibition of poly(ADP-ribose) glycohydrolase by adenosine diphosphate (hydroxymethyl)pyrrolidinediol
    • Slama J.T., Aboul-Ela N., Goli D.M., Cheesman B.V., Simmons A.M., Jacobson M.K. Specific inhibition of poly(ADP-ribose) glycohydrolase by adenosine diphosphate (hydroxymethyl)pyrrolidinediol. J. Med. Chem. 1995, 38(2):389-393.
    • (1995) J. Med. Chem. , vol.38 , Issue.2 , pp. 389-393
    • Slama, J.T.1    Aboul-Ela, N.2    Goli, D.M.3    Cheesman, B.V.4    Simmons, A.M.5    Jacobson, M.K.6
  • 189
    • 0028823239 scopus 로고
    • Mechanism of inhibition of poly(ADP-ribose) glycohydrolase by adenosine diphosphate (hydroxymethyl)pyrrolidinediol
    • Slama J.T., Aboul-Ela N., Jacobson M.K. Mechanism of inhibition of poly(ADP-ribose) glycohydrolase by adenosine diphosphate (hydroxymethyl)pyrrolidinediol. J. Med. Chem. 1995, 38(21):4332-4336.
    • (1995) J. Med. Chem. , vol.38 , Issue.21 , pp. 4332-4336
    • Slama, J.T.1    Aboul-Ela, N.2    Jacobson, M.K.3
  • 190
    • 0032553473 scopus 로고    scopus 로고
    • Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
    • Smith S., Giriat I., Schmitt A., de Lange T. Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. Science 1998, 282(5393):1484-1487.
    • (1998) Science , vol.282 , Issue.5393 , pp. 1484-1487
    • Smith, S.1    Giriat, I.2    Schmitt, A.3    de Lange, T.4
  • 192
    • 79961233161 scopus 로고    scopus 로고
    • Discovery and structure-activity relationships of modified salicylanilides as cell permeable inhibitors of poly(ADP-ribose) glycohydrolase (PARG)
    • Steffen J.D., Coyle D.L., Damodaran K., Beroza P., Jacobson M.K. Discovery and structure-activity relationships of modified salicylanilides as cell permeable inhibitors of poly(ADP-ribose) glycohydrolase (PARG). J. Med. Chem. 2011, 54(15):5403-5413.
    • (2011) J. Med. Chem. , vol.54 , Issue.15 , pp. 5403-5413
    • Steffen, J.D.1    Coyle, D.L.2    Damodaran, K.3    Beroza, P.4    Jacobson, M.K.5
  • 193
    • 84865997511 scopus 로고    scopus 로고
    • Tannic acid, an inhibitor of poly(ADP-ribose) glycohydrolase, sensitizes ovarian carcinoma cells to cisplatin
    • Sun Y., Zhang T., Wang B., Li H., Li P. Tannic acid, an inhibitor of poly(ADP-ribose) glycohydrolase, sensitizes ovarian carcinoma cells to cisplatin. Anticancer Drugs 2012, 23(9):979-990.
    • (2012) Anticancer Drugs , vol.23 , Issue.9 , pp. 979-990
    • Sun, Y.1    Zhang, T.2    Wang, B.3    Li, H.4    Li, P.5
  • 195
    • 0023003512 scopus 로고
    • In vitro poly(ADP-ribosyl)ation of seminal ribonuclease
    • Suzuki H., Quesada P., Farina B., Leone E. In vitro poly(ADP-ribosyl)ation of seminal ribonuclease. J. Biol. Chem. 1986, 261(13):6048-6055.
    • (1986) J. Biol. Chem. , vol.261 , Issue.13 , pp. 6048-6055
    • Suzuki, H.1    Quesada, P.2    Farina, B.3    Leone, E.4
  • 196
    • 0021913164 scopus 로고
    • Effect of DNA intercalators on poly(ADP-ribose) glycohydrolase activity
    • Tavassoli M., Tavassoli M.H., Shall S. Effect of DNA intercalators on poly(ADP-ribose) glycohydrolase activity. Biochim. Biophys. Acta 1985, 827(3):228-234.
    • (1985) Biochim. Biophys. Acta , vol.827 , Issue.3 , pp. 228-234
    • Tavassoli, M.1    Tavassoli, M.H.2    Shall, S.3
  • 197
    • 34247638482 scopus 로고    scopus 로고
    • Differential effects of tannic acid on cisplatin induced nephrotoxicity in rats
    • Tikoo K., Bhatt D.K., Gaikwad A.B., Sharma V., Kabra D.G. Differential effects of tannic acid on cisplatin induced nephrotoxicity in rats. FEBS Lett. 2007, 581(10):2027-2035.
    • (2007) FEBS Lett. , vol.581 , Issue.10 , pp. 2027-2035
    • Tikoo, K.1    Bhatt, D.K.2    Gaikwad, A.B.3    Sharma, V.4    Kabra, D.G.5
  • 198
    • 79952008166 scopus 로고    scopus 로고
    • Tannic acid ameliorates doxorubicin-induced cardiotoxicity and potentiates its anti-cancer activity: potential role of tannins in cancer chemotherapy
    • Tikoo K., Sane M.S., Gupta C. Tannic acid ameliorates doxorubicin-induced cardiotoxicity and potentiates its anti-cancer activity: potential role of tannins in cancer chemotherapy. Toxicol. Appl. Pharmacol. 2011, 251(3):191-200.
    • (2011) Toxicol. Appl. Pharmacol. , vol.251 , Issue.3 , pp. 191-200
    • Tikoo, K.1    Sane, M.S.2    Gupta, C.3
  • 201
    • 0026681651 scopus 로고
    • Mouse mammary tumor virus gene expression is suppressed by oligomeric ellagitannins, novel inhibitors of poly(ADP-ribose) glycohydrolase
    • Tsai Y.J., Aoki T., Maruta H., Abe H., Sakagami H., Hatano T., Okuda T., Tanuma S. Mouse mammary tumor virus gene expression is suppressed by oligomeric ellagitannins, novel inhibitors of poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 1992, 267(20):14436-14442.
    • (1992) J. Biol. Chem. , vol.267 , Issue.20 , pp. 14436-14442
    • Tsai, Y.J.1    Aoki, T.2    Maruta, H.3    Abe, H.4    Sakagami, H.5    Hatano, T.6    Okuda, T.7    Tanuma, S.8
  • 202
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • Tulin A., Spradling A. Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci. Science 2003, 299(5606):560-562.
    • (2003) Science , vol.299 , Issue.5606 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 203
    • 33644777616 scopus 로고    scopus 로고
    • Drosophila poly(ADP-ribose) glycohydrolase mediates chromatin structure and SIR2-dependent silencing
    • Tulin A., Naumova N.M., Menon A.K., Spradling A.C. Drosophila poly(ADP-ribose) glycohydrolase mediates chromatin structure and SIR2-dependent silencing. Genetics 2006, 172(1):363-371.
    • (2006) Genetics , vol.172 , Issue.1 , pp. 363-371
    • Tulin, A.1    Naumova, N.M.2    Menon, A.K.3    Spradling, A.C.4
  • 204
    • 23844434673 scopus 로고    scopus 로고
    • AIF suppresses chemical stress-induced apoptosis and maintains the transformed state of tumor cells
    • Urbano A., Lakshmanan U., Choo P.H., Kwan J.C., Ng P.Y., Guo K., Dhakshinamoorthy S., Porter A. AIF suppresses chemical stress-induced apoptosis and maintains the transformed state of tumor cells. EMBO J. 2005, 24(15):2815-2826.
    • (2005) EMBO J. , vol.24 , Issue.15 , pp. 2815-2826
    • Urbano, A.1    Lakshmanan, U.2    Choo, P.H.3    Kwan, J.C.4    Ng, P.Y.5    Guo, K.6    Dhakshinamoorthy, S.7    Porter, A.8
  • 207
    • 67649794803 scopus 로고    scopus 로고
    • Calcium dysregulation induces apoptosis-inducing factor release: cross-talk between PARP-1- and calpain-signaling pathways
    • Vosler P.S., Sun D., Wang S., Gao Y., Kintner D.B., Signore A.P., Cao G., Chen J. Calcium dysregulation induces apoptosis-inducing factor release: cross-talk between PARP-1- and calpain-signaling pathways. Exp. Neurol. 2009, 218(2):213-220.
    • (2009) Exp. Neurol. , vol.218 , Issue.2 , pp. 213-220
    • Vosler, P.S.1    Sun, D.2    Wang, S.3    Gao, Y.4    Kintner, D.B.5    Signore, A.P.6    Cao, G.7    Chen, J.8
  • 209
    • 35648955118 scopus 로고    scopus 로고
    • The DNA binding and catalytic domains of poly(ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription
    • Wacker D.A., Ruhl D.D., Balagamwala E.H., Hope K.M., Zhang T., Kraus W.L. The DNA binding and catalytic domains of poly(ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription. Mol. Cell. Biol. 2007, 27(21):7475-7485.
    • (2007) Mol. Cell. Biol. , vol.27 , Issue.21 , pp. 7475-7485
    • Wacker, D.A.1    Ruhl, D.D.2    Balagamwala, E.H.3    Hope, K.M.4    Zhang, T.5    Kraus, W.L.6
  • 212
    • 67649491430 scopus 로고    scopus 로고
    • Calpain activation is not required for AIF translocation in PARP-1-dependent cell death (parthanatos)
    • Wang Y., Kim N.S., Li X., Greer P.A., Koehler R.C., Dawson V.L., Dawson T.M. Calpain activation is not required for AIF translocation in PARP-1-dependent cell death (parthanatos). J. Neurochem. 2009, 110(2):687-696.
    • (2009) J. Neurochem. , vol.110 , Issue.2 , pp. 687-696
    • Wang, Y.1    Kim, N.S.2    Li, X.3    Greer, P.A.4    Koehler, R.C.5    Dawson, V.L.6    Dawson, T.M.7
  • 213
  • 215
  • 216
    • 70449716875 scopus 로고    scopus 로고
    • A specific isoform of poly(ADP-ribose) glycohydrolase is targeted to the mitochondrial matrix by a N-terminal mitochondrial targeting sequence
    • Whatcott C.J., Meyer-Ficca M.L., Meyer R.G., Jacobson M.K. A specific isoform of poly(ADP-ribose) glycohydrolase is targeted to the mitochondrial matrix by a N-terminal mitochondrial targeting sequence. Exp. Cell Res. 2009, 315(20):3477-3485.
    • (2009) Exp. Cell Res. , vol.315 , Issue.20 , pp. 3477-3485
    • Whatcott, C.J.1    Meyer-Ficca, M.L.2    Meyer, R.G.3    Jacobson, M.K.4
  • 218
    • 12244267986 scopus 로고    scopus 로고
    • NAD+ as a metabolic link between DNA damage and cell death
    • Ying W., Alano C.C., Garnier P., Swanson R.A. NAD+ as a metabolic link between DNA damage and cell death. J. Neurosci. Res. 2005, 79(1-2):216-223.
    • (2005) J. Neurosci. Res. , vol.79 , Issue.1-2 , pp. 216-223
    • Ying, W.1    Alano, C.C.2    Garnier, P.3    Swanson, R.A.4
  • 221
    • 76049093446 scopus 로고    scopus 로고
    • Outer mitochondrial membrane localization of apoptosis-inducing factor: mechanistic implications for release
    • Yu S.W., Wang Y., Frydenlund D.S., Ottersen O.P., Dawson V.L., Dawson T.M. Outer mitochondrial membrane localization of apoptosis-inducing factor: mechanistic implications for release. ASN Neuro 2009, 1(5):275-281.
    • (2009) ASN Neuro , vol.1 , Issue.5 , pp. 275-281
    • Yu, S.W.1    Wang, Y.2    Frydenlund, D.S.3    Ottersen, O.P.4    Dawson, V.L.5    Dawson, T.M.6
  • 223
    • 77956043225 scopus 로고    scopus 로고
    • Enhanced DNA accessibility and increased DNA damage induced by the absence of poly(ADP-ribose) hydrolysis
    • Zhou Y., Feng X., Koh D.W. Enhanced DNA accessibility and increased DNA damage induced by the absence of poly(ADP-ribose) hydrolysis. Biochemistry 2010, 49(34):7360-7366.
    • (2010) Biochemistry , vol.49 , Issue.34 , pp. 7360-7366
    • Zhou, Y.1    Feng, X.2    Koh, D.W.3
  • 224
    • 79953717442 scopus 로고    scopus 로고
    • Activation of cell death mediated by apoptosis-inducing factor due to the absence of poly(ADP-ribose) glycohydrolase
    • Zhou Y., Feng X., Koh D.W. Activation of cell death mediated by apoptosis-inducing factor due to the absence of poly(ADP-ribose) glycohydrolase. Biochemistry 2011, 50(14):2850-2859.
    • (2011) Biochemistry , vol.50 , Issue.14 , pp. 2850-2859
    • Zhou, Y.1    Feng, X.2    Koh, D.W.3
  • 225
    • 79956021767 scopus 로고    scopus 로고
    • Synergistic cytotoxicity of N-methyl-N'-nitro-N-nitrosoguanidine and absence of poly(ADP-ribose) glycohydrolase involves chromatin decondensation
    • Zhou Y., Feng X., Koh D.W. Synergistic cytotoxicity of N-methyl-N'-nitro-N-nitrosoguanidine and absence of poly(ADP-ribose) glycohydrolase involves chromatin decondensation. Int. J. Oncol. 2011, 39(1):121-127.
    • (2011) Int. J. Oncol. , vol.39 , Issue.1 , pp. 121-127
    • Zhou, Y.1    Feng, X.2    Koh, D.W.3
  • 227
    • 29944438881 scopus 로고    scopus 로고
    • Necrotic death as a cell fate
    • Zong W.X., Thompson C.B. Necrotic death as a cell fate. Genes Dev. 2006, 20(1):1-15.
    • (2006) Genes Dev. , vol.20 , Issue.1 , pp. 1-15
    • Zong, W.X.1    Thompson, C.B.2
  • 228
    • 2642536197 scopus 로고    scopus 로고
    • Alkylating DNA damage stimulates a regulated form of necrotic cell death
    • Zong W.X., Ditsworth D., Bauer D.E., Wang Z.Q., Thompson C.B. Alkylating DNA damage stimulates a regulated form of necrotic cell death. Genes Dev. 2004, 18(11):1272-1282.
    • (2004) Genes Dev. , vol.18 , Issue.11 , pp. 1272-1282
    • Zong, W.X.1    Ditsworth, D.2    Bauer, D.E.3    Wang, Z.Q.4    Thompson, C.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.