메뉴 건너뛰기




Volumn 333, Issue 2, 2004, Pages 256-264

A nonradiometric, high-throughput assay for poly(ADP-ribose) glycohydrolase (PARG): Application to inhibitor identification and evaluation

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CELL DEATH; MOLECULES;

EID: 4644241346     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2004.04.032     Document Type: Article
Times cited : (28)

References (45)
  • 1
    • 0035281786 scopus 로고    scopus 로고
    • The world according to PARP
    • Smith S. The world according to PARP. Trends Biochem. Sci. 26:2001;174-179
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 174-179
    • Smith, S.1
  • 2
    • 0035977206 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase: A guardian angel protecting the genome and suppressing tumorigenesis
    • Tong W.-M., Cortes U., Wang Z.-Q. Poly(ADP-ribose) polymerase: a guardian angel protecting the genome and suppressing tumorigenesis. Biochim. Biophys. Acta. 1552:2001;27-37
    • (2001) Biochim. Biophys. Acta , vol.1552 , pp. 27-37
    • Tong, W.-M.1    Cortes, U.2    Wang, Z.-Q.3
  • 3
    • 0035425899 scopus 로고    scopus 로고
    • Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism
    • Davidovic L., Vodenicharov M., Affar E.B., Poirier G.G. Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism. Exp. Cell Res. 268:2001;7-13
    • (2001) Exp. Cell Res. , vol.268 , pp. 7-13
    • Davidovic, L.1    Vodenicharov, M.2    Affar, E.B.3    Poirier, G.G.4
  • 4
    • 0033080520 scopus 로고    scopus 로고
    • Poly(ADP-ribose) glycohydrolase is present and active in mammalian cells as a 110-kDa protein
    • Winstall E., Affar E.B., Shah R., Bourassa S., Scovassi A.I. Poly(ADP-ribose) glycohydrolase is present and active in mammalian cells as a 110-kDa protein. Exper. Cell Res. 246:1999;395-398
    • (1999) Exper. Cell Res. , vol.246 , pp. 395-398
    • Winstall, E.1    Affar, E.B.2    Shah, R.3    Bourassa, S.4    Scovassi, A.I.5
  • 5
    • 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. 272:1997;11895-11901
    • (1997) J. Biol. Chem. , vol.272 , pp. 11895-11901
    • Lin, W.1    Ame, J.-C.2    Aboul-Ela, N.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 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. 218:1989;67-74
    • (1989) Mutat. Res. , vol.218 , pp. 67-74
    • Alvarez-Gonzalez, R.1    Althaus, F.R.2
  • 9
    • 0036733355 scopus 로고    scopus 로고
    • The therapeutic potential of poly(ADP-ribose) polymerase inhibitors
    • Virag 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
    • Virag, L.1    Szabo, C.2
  • 10
    • 0036447366 scopus 로고    scopus 로고
    • Potential clinical applications of poly(ADP-ribose) polymerase (PARP) inhibitors
    • Tentori L., Portarena I., Graziani G. Potential clinical applications of poly(ADP-ribose) polymerase (PARP) inhibitors. Pharmacol. Res. 45:2002;73-85
    • (2002) Pharmacol. Res. , vol.45 , pp. 73-85
    • Tentori, L.1    Portarena, I.2    Graziani, G.3
  • 11
    • 0037239590 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase inhibitors
    • Southan G.J., Szabo C. Poly(ADP-ribose) polymerase inhibitors. Curr. Med. Chem. 10:2003;321-340
    • (2003) Curr. Med. Chem. , vol.10 , pp. 321-340
    • Southan, G.J.1    Szabo, C.2
  • 13
    • 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. 46:2003;4322-4332
    • (2003) J. Med. Chem. , vol.46 , 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
  • 14
    • 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. 38:1995;389-393
    • (1995) J. Med. Chem. , vol.38 , 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
  • 16
    • 0021913164 scopus 로고
    • Effect of DNA intercalators on poly(ADP-ribose) glycohydrolase activity
    • Tavassoli M., Hajihosaini T., Shall S. Effect of DNA intercalators on poly(ADP-ribose) glycohydrolase activity. Biochim. Biophys. Acta. 827:1985;228-234
    • (1985) Biochim. Biophys. Acta , vol.827 , pp. 228-234
    • Tavassoli, M.1    Hajihosaini, T.2    Shall, S.3
  • 17
    • 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. 267:1992;14436-14442
    • (1992) J. Biol. Chem. , vol.267 , 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
  • 19
    • 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. 38:1995;4332-4336
    • (1995) J. Med. Chem. , vol.38 , pp. 4332-4336
    • Slama, J.-T.1    Aboul-Ela, N.2    Jacobson, M.K.3
  • 20
    • 0031018627 scopus 로고    scopus 로고
    • Analysis of poly(ADP-ribose) glycohydrolase activity in nuclear extracts from mammalian cells
    • Bernardi R., Rossi L., Poirier G.G., Scovassi A.I. Analysis of poly(ADP-ribose) glycohydrolase activity in nuclear extracts from mammalian cells. Biochim. Biophys. Acta. 1338:1997;60-68
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 60-68
    • Bernardi, R.1    Rossi, L.2    Poirier, G.G.3    Scovassi, A.I.4
  • 21
    • 0037756771 scopus 로고    scopus 로고
    • Post-treatment with a novel PARG inhibitor reduces infarct in cerebral ischemia in the rat
    • Lu X.-C.M., Massuda E., Lin Q., Li W., Li J.-H., Zhang J. Post-treatment with a novel PARG inhibitor reduces infarct in cerebral ischemia in the rat. Brain Res. 978:2003;99-103
    • (2003) Brain Res. , vol.978 , pp. 99-103
    • Lu, X.-C.M.1    Massuda, E.2    Lin, Q.3    Li, W.4    Li, J.-H.5    Zhang, J.6
  • 22
    • 0035834146 scopus 로고    scopus 로고
    • Poly(ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death
    • Ying W., Sevigny M.B., Chen Y., Swanson R.A. Poly(ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death. Proc. Natl. Acad. Sci. USA. 98:2001;12227-12232
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12227-12232
    • Ying, W.1    Sevigny, M.B.2    Chen, Y.3    Swanson, R.A.4
  • 23
    • 0034657984 scopus 로고    scopus 로고
    • The poly(ADP-ribose) glycohydrolase inhibitor gallotannin blocks oxidative astrocyte death
    • Ying W.H., Swanson R.A. The poly(ADP-ribose) glycohydrolase inhibitor gallotannin blocks oxidative astrocyte death. Neuroreport. 11:2000;1385-1388
    • (2000) Neuroreport , vol.11 , pp. 1385-1388
    • Ying, W.H.1    Swanson, R.A.2
  • 24
    • 0023375254 scopus 로고
    • Rapid assay of poly(ADP-ribose) glycohydrolase
    • Menard L., Poirier G.G. Rapid assay of poly(ADP-ribose) glycohydrolase. Biochem. Cell Biol. 65:1987;668-673
    • (1987) Biochem. Cell Biol. , vol.65 , pp. 668-673
    • Menard, L.1    Poirier, G.G.2
  • 25
    • 0032891436 scopus 로고    scopus 로고
    • Measurement of poly(ADP-ribose) glycohydrolase activity by high resolution polyacrylamide gel electrophoresis: Specific inhibition by histones and nuclear matrix proteins
    • Pacheco-Rodriguez G., Alvarez-Gonzalez R. Measurement of poly(ADP-ribose) glycohydrolase activity by high resolution polyacrylamide gel electrophoresis: specific inhibition by histones and nuclear matrix proteins. Mol. Cell. Biochem. 193:1999;13-18
    • (1999) Mol. Cell. Biochem. , vol.193 , pp. 13-18
    • Pacheco-Rodriguez, G.1    Alvarez-Gonzalez, R.2
  • 26
    • 0037281168 scopus 로고    scopus 로고
    • Single amino acid substitution enhances bacterial expression of PARP-1 D214A
    • Gagnon S.N., Desnoyers S. Single amino acid substitution enhances bacterial expression of PARP-1 D214A. Mol. Cell. Biochem. 243:2003;15-22
    • (2003) Mol. Cell. Biochem. , vol.243 , pp. 15-22
    • Gagnon, S.N.1    Desnoyers, S.2
  • 27
    • 0842324496 scopus 로고    scopus 로고
    • +: Application to the high-throughput screening of small molecules as potential inhibitors
    • +: application to the high-throughput screening of small molecules as potential inhibitors. Anal. Biochem. 326:2004;78-86
    • (2004) Anal. Biochem. , vol.326 , pp. 78-86
    • Putt, K.S.1    Hergenrother, P.J.2
  • 29
    • 0034355325 scopus 로고    scopus 로고
    • Purpald: A reagent that turns aldehydes purple
    • Hopps H.B. Purpald: a reagent that turns aldehydes purple. Aldrichimica Acta. 33:2000;28-30
    • (2000) Aldrichimica Acta , vol.33 , pp. 28-30
    • Hopps, H.B.1
  • 31
    • 0022255318 scopus 로고
    • Determination of reducing sugars in the nanomole range with tetrazolium blue
    • Jue C.K., Lipke P.N. Determination of reducing sugars in the nanomole range with tetrazolium blue. J. Biochem. Biophys. Meth. 11:1985;109-115
    • (1985) J. Biochem. Biophys. Meth. , vol.11 , pp. 109-115
    • Jue, C.K.1    Lipke, P.N.2
  • 32
    • 0015333650 scopus 로고
    • A new reaction for colorimetric determination of carbohydrates
    • Lever M. A new reaction for colorimetric determination of carbohydrates. Anal. Biochem. 47:1972;273-279
    • (1972) Anal. Biochem. , vol.47 , pp. 273-279
    • Lever, M.1
  • 33
    • 0017736277 scopus 로고
    • Carbohydrate determination with 4-hydroxybenzoic acid hydrazide (PAHBAH): Effect of bismuth on the reaction
    • Lever M. Carbohydrate determination with 4-hydroxybenzoic acid hydrazide (PAHBAH): effect of bismuth on the reaction. Anal. Biochem. 81:1977;21-27
    • (1977) Anal. Biochem. , vol.81 , pp. 21-27
    • Lever, M.1
  • 34
    • 0021240134 scopus 로고
    • Optimal conditions for 4-hydroxybenzoyl- and 2-furoylhydrazine as reagents for the determination of carbohydates, including ketosamines
    • Lever M., Walmsley T.A., Visser R.S., Ryde S.J. Optimal conditions for 4-hydroxybenzoyl- and 2-furoylhydrazine as reagents for the determination of carbohydates, including ketosamines. Anal. Biochem. 139:1984;205-211
    • (1984) Anal. Biochem. , vol.139 , pp. 205-211
    • Lever, M.1    Walmsley, T.A.2    Visser, R.S.3    Ryde, S.J.4
  • 35
    • 0015811338 scopus 로고
    • A convenient ferricyanide estimation of reducing sugars in the nanomole range
    • Kidby D.K., Davidson D.J. A convenient ferricyanide estimation of reducing sugars in the nanomole range. Anal. Biochem. 55:1973;321-325
    • (1973) Anal. Biochem. , vol.55 , pp. 321-325
    • Kidby, D.K.1    Davidson, D.J.2
  • 36
    • 0016379479 scopus 로고
    • Fluorimetric determination of reducing sugars with ethylenediamine sulfate
    • Honda S., Kakimoto K., Sudo K., Kakehi K., Takiura K. Fluorimetric determination of reducing sugars with ethylenediamine sulfate. Anal. Chim. Acta. 70:1974;133-139
    • (1974) Anal. Chim. Acta , vol.70 , pp. 133-139
    • Honda, S.1    Kakimoto, K.2    Sudo, K.3    Kakehi, K.4    Takiura, K.5
  • 37
    • 0343480111 scopus 로고
    • Rapid spectrophotofluorometric method for determining nanogram quantities of carbohydrates
    • Rogers C.J., Chambers C.W., Clarke N.A. Rapid spectrophotofluorometric method for determining nanogram quantities of carbohydrates. Anal. Chem. 38:1966;1851-1853
    • (1966) Anal. Chem. , vol.38 , pp. 1851-1853
    • Rogers, C.J.1    Chambers, C.W.2    Clarke, N.A.3
  • 38
    • 0026716983 scopus 로고
    • An ultraviolet-spectrophotometric method with 2-cyanoacetamide for the determination of the enzymatic degradation of reducing polysaccharides
    • Bach E., Schollmeyer E. An ultraviolet-spectrophotometric method with 2-cyanoacetamide for the determination of the enzymatic degradation of reducing polysaccharides. Anal. Biochem. 203:1992;335-339
    • (1992) Anal. Biochem. , vol.203 , pp. 335-339
    • Bach, E.1    Schollmeyer, E.2
  • 39
    • 0023225795 scopus 로고
    • Fluorometric assay of O-linked glycoproteins by reaction with 2-cyanoacetamide
    • Crowther R.S., Wetmore R.F. Fluorometric assay of O-linked glycoproteins by reaction with 2-cyanoacetamide. Anal. Biochem. 163:1987;170-174
    • (1987) Anal. Biochem. , vol.163 , pp. 170-174
    • Crowther, R.S.1    Wetmore, R.F.2
  • 40
    • 84998335521 scopus 로고
    • Aromatic amidines as fluorogenic reagents for reducing carbohydrates
    • Kai M., Tamura K., Yamaguchi M., Ohkura Y. Aromatic amidines as fluorogenic reagents for reducing carbohydrates. Anal. Sci. 1:1985;59-63
    • (1985) Anal. Sci. , vol.1 , pp. 59-63
    • Kai, M.1    Tamura, K.2    Yamaguchi, M.3    Ohkura, Y.4
  • 41
    • 0025834237 scopus 로고
    • Selective post-column fluorigenic reaction with benzamidine for trace level detection of reducing saccharides in liquid chromatography
    • Coquet A., Veuthey J.L., Haerdi W. Selective post-column fluorigenic reaction with benzamidine for trace level detection of reducing saccharides in liquid chromatography. J. Chromatogr. 553:1991;255-263
    • (1991) J. Chromatogr. , vol.553 , pp. 255-263
    • Coquet, A.1    Veuthey, J.L.2    Haerdi, W.3
  • 42
    • 0037188762 scopus 로고    scopus 로고
    • Simultaneous analysis of monosaccharides and oligosaccharides by high-performance liquid chromatography with postcolumn fluorescence derivatization
    • Kakita H., Kamishima H., Komiya K., Kato Y. Simultaneous analysis of monosaccharides and oligosaccharides by high-performance liquid chromatography with postcolumn fluorescence derivatization. J. Chromatogr. 961:2002;77-82
    • (2002) J. Chromatogr. , vol.961 , pp. 77-82
    • Kakita, H.1    Kamishima, H.2    Komiya, K.3    Kato, Y.4
  • 43
    • 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. 220:1994;369-375
    • (1994) Eur. J. Biochem. , vol.220 , pp. 369-375
    • Braun, S.A.1    Panzeter, P.L.2    Collinge, M.A.3    Althaus, F.R.4
  • 45
    • 0032755520 scopus 로고    scopus 로고
    • Isolation and cloning of rat poly(ADP-ribose) glycohydrolase: Presence of potential nuclear export signal conserved in mammalian orthologs
    • Shimokawa T., Masutani M., Nagasawa S., Nozaki T., Ikota N., Aoki Y., Nakagama H., Sugimura T. Isolation and cloning of rat poly(ADP-ribose) glycohydrolase: presence of potential nuclear export signal conserved in mammalian orthologs. J. Biochem. 126:1999;748-755
    • (1999) J. Biochem. , vol.126 , pp. 748-755
    • Shimokawa, T.1    Masutani, M.2    Nagasawa, S.3    Nozaki, T.4    Ikota, N.5    Aoki, Y.6    Nakagama, H.7    Sugimura, T.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.