메뉴 건너뛰기




Volumn 7, Issue 3, 2012, Pages 563-570

Selective small molecule inhibition of poly(ADP-ribose) glycohydrolase (PARG)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE (HYDROXYMETHYL) PYRROLIDINEDIOL; ADENOSINE DIPHOSPHATE RIBOSYLHYDROLASE 3; GLYCOSIDASE; GLYCOSIDASE INHIBITOR; HYDROLASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; POLY(ADENOSINE DIPHOSPHATE RIBOSE); POLY(ADENOSINE DIPHOSPHATE RIBOSE) GLYCOHYDROLASE; PYRROLIDINE DERIVATIVE; RHODANINE BASED POLY(ADENOSINE DIPHOSPHATE RIBOSE) GLYCOHYDROLASE INHIBITOR; SALICYLANILIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84858631473     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb200506t     Document Type: Article
Times cited : (49)

References (66)
  • 2
    • 0032842477 scopus 로고    scopus 로고
    • Functions of poly(ADP-ribose) polymerase in controlling telomere length and chromosomal stability
    • DOI 10.1038/12680
    • dAdda di Fagagna, F., Hande, M. P., Tong, W. M., Lansdorp, P. M., Wang, Z. Q., and Jackson, S. P. (1999) Functions of poly(ADP-ribose) polymerase in controlling telomere length and chromosomal stability Nat. Genet. 23, 76-80 (Pubitemid 29418792)
    • (1999) Nature Genetics , vol.23 , Issue.1 , pp. 76-80
    • Di Fagagna, F.D.1    Hande, M.P.2    Tong, W.-M.3    Lansdorp, P.M.4    Wang, Z.-Q.5    Jackson, S.P.6
  • 4
    • 0035425899 scopus 로고    scopus 로고
    • Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism
    • DOI 10.1006/excr.2001.5263
    • Davidovic, L., Vodenicharov, M., Affar, E. B., and Poirier, G. G. (2001) Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism Exp. Cell Res. 268, 7-13 (Pubitemid 32678855)
    • (2001) Experimental Cell Research , vol.268 , Issue.1 , pp. 7-13
    • Davidovic, L.1    Vodenicharov, M.2    Affar, E.B.3    Poirier, G.G.4
  • 5
    • 0028246305 scopus 로고
    • Poly(ADP-ribose) molecules formed during DNA repair in vivo
    • Malanga, M. and Althaus, F. R. (1994) Poly(ADP-ribose) molecules formed during DNA repair in vivo J. Biol. Chem. 269, 17691-17696 (Pubitemid 24218056)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.26 , pp. 17691-17696
    • Malanga, M.1    Althaus, F.R.2
  • 6
    • 19444362951 scopus 로고    scopus 로고
    • Clinical perspectives of PARP inhibitors
    • DOI 10.1016/j.phrs.2005.02.013, PII S1043661805000460
    • Graziani, G. and Szabo, C. (2005) Clinical perspectives of PARP inhibitors Pharmacol. Res. 52, 109-118 (Pubitemid 40725605)
    • (2005) Pharmacological Research , vol.52 , Issue.1 SPEC. ISS. , pp. 109-118
    • Graziani, G.1    Szabo, C.2
  • 7
    • 70249091814 scopus 로고    scopus 로고
    • PARP inhibitors blaze a trail in difficult-to-treat cancers
    • Kling, J. (2009) PARP inhibitors blaze a trail in difficult-to-treat cancers Nat. Biotechnol. 27, 784-786
    • (2009) Nat. Biotechnol. , vol.27 , pp. 784-786
    • Kling, J.1
  • 8
    • 25444498338 scopus 로고    scopus 로고
    • The road to survival goes through PARG
    • Koh, D. W., Dawson, V. L., and Dawson, T. M. (2005) The road to survival goes through PARG Cell Cycle 4, 397-399 (Pubitemid 41359723)
    • (2005) Cell Cycle , vol.4 , Issue.3 , pp. 397-399
    • Koh, D.W.1    Dawson, V.L.2    Dawson, T.M.3
  • 9
    • 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., and Koh, D. W. (2011) Activation of cell death mediated by apoptosis-inducing factor due to the absence of poly(ADP-ribose) glycohydrolase Biochemistry 50, 2850-2859
    • (2011) Biochemistry , vol.50 , pp. 2850-2859
    • Zhou, Y.1    Feng, X.2    Koh, D.W.3
  • 10
    • 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., and Hayaishi, O. (1986) Purification and characterization of poly(ADP-ribose) glycohydrolase. Different modes of action on large and small poly(ADP-ribose) J. Biol. Chem. 261, 14902-14911 (Pubitemid 17218047)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.32 , pp. 14902-14911
    • Hatakeyama, K.1    Nemoto, Y.2    Ueda, K.3    Hayaishi, O.4
  • 11
    • 2942707644 scopus 로고    scopus 로고
    • Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments
    • DOI 10.1016/j.yexcr.2004.03.050, PII S0014482704001843
    • Meyer-Ficca, M. L., Meyer, R. G., Coyle, D. L., Jacobson, E. L., and Jacobson, M. K. (2004) Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments Exp. Cell Res. 297, 521-532 (Pubitemid 38798412)
    • (2004) Experimental Cell Research , 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
  • 12
    • 33744986316 scopus 로고    scopus 로고
    • 2-induced cell death
    • DOI 10.1042/BJ20051696
    • Blenn, C., Althaus, F. R., and Malanga, M. (2006) Poly(ADP-ribose) glycohydrolase silencing protects against H2O2-induced cell death Biochem. J. 396, 419-429 (Pubitemid 44228157)
    • (2006) Biochemical Journal , vol.396 , Issue.3 , pp. 419-429
    • Blenn, C.1    Althaus, F.R.2    Malanga, M.3
  • 13
    • 33847313804 scopus 로고    scopus 로고
    • Altered DNA damage response in Caenorhabditis elegans with impaired poly(ADP-ribose) glycohydrolases genes expression
    • DOI 10.1016/j.dnarep.2006.10.027, PII S1568786406003582
    • St-Laurent, J. F., Gagnon, S. N., Dequen, F., Hardy, I., and Desnoyers, S. (2007) Altered DNA damage response in Caenorhabditis elegans with impaired poly(ADP-ribose) glycohydrolases genes expression DNA Repair 6, 329-343 (Pubitemid 46329615)
    • (2007) DNA Repair , vol.6 , Issue.3 , pp. 329-343
    • St-Laurent, J.-F.1    Gagnon, S.N.2    Dequen, F.3    Hardy, I.4    Desnoyers, S.5
  • 16
    • 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., and Koh, D. W. (2010) Enhanced DNA accessibility and increased DNA damage induced by the absence of poly(ADP-ribose) hydrolysis Biochemistry 49, 7360-7366
    • (2010) Biochemistry , vol.49 , pp. 7360-7366
    • Zhou, Y.1    Feng, X.2    Koh, D.W.3
  • 17
    • 84889476358 scopus 로고    scopus 로고
    • The Promises and Pitfalls of Small-Molecule Inhibition of Poly(ADP-Ribose) Glycohydrolase (PARG)
    • Wiley & Sons, Ltd. New York
    • Nottbohm, A. C. and Hergenrother, P. J. (2007) The Promises and Pitfalls of Small-Molecule Inhibition of Poly(ADP-Ribose) Glycohydrolase (PARG), in Drug Discovery Research: New Frontiers in the Post-Genomic Era, pp 163-185, Wiley & Sons, Ltd., New York.
    • (2007) Drug Discovery Research: New Frontiers in the Post-Genomic Era , pp. 163-185
    • Nottbohm, A.C.1    Hergenrother, P.J.2
  • 18
    • 79952148357 scopus 로고    scopus 로고
    • The ups and downs of tannins as inhibitors of poly(ADP-ribose) glycohydrolase
    • Blenn, C., Wyrsch, P., and Althaus, F. R. (2011) The ups and downs of tannins as inhibitors of poly(ADP-ribose)glycohydrolase Molecules 16, 1854-1877
    • (2011) Molecules , vol.16 , pp. 1854-1877
    • Blenn, C.1    Wyrsch, P.2    Althaus, F.R.3
  • 19
    • 4143154152 scopus 로고    scopus 로고
    • Poly(ADP-ribose) glycohydrolase as a target for neuroprotective intervention: Assessment of currently available pharmacological tools
    • DOI 10.1016/j.ejphar.2004.06.042, PII S001429990400665X
    • Falsig, J., Christiansen, S. H., Feuerhahn, S., Burkle, A., Oei, S. L., Keil, C., and Leist, M. (2004) Poly(ADP-ribose) glycohydrolase as a target for neuroprotective intervention: assessment of currently available pharmacological tools Eur. J. Pharmacol. 497, 7-16 (Pubitemid 39092421)
    • (2004) European Journal of Pharmacology , 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
  • 20
    • 0028823239 scopus 로고
    • Mechanism of inhibition of poly(ADP-ribose) glycohydrolase by adenosine diphosphate (hydroxymethyl)pyrrolidinediol
    • Slama, J. T., Aboul-Ela, N., and Jacobson, M. K. (1995) Mechanism of inhibition of poly(ADP-ribose) glycohydrolase by adenosine diphosphate (hydroxymethyl)pyrrolidinediol J. Med. Chem. 38, 4332-4336
    • (1995) J. Med. Chem. , vol.38 , pp. 4332-4336
    • Slama, J.T.1    Aboul-Ela, N.2    Jacobson, M.K.3
  • 21
    • 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., and Jacobson, M. K. (1995) Specific inhibition of poly(ADP-ribose) glycohydrolase by adenosine diphosphate (hydroxymethyl)pyrrolidinediol J. Med. Chem. 38, 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
  • 22
    • 0028452871 scopus 로고
    • Synthesis of (2R,3R,4S)-2-hydroxymethylpyrrolidine-3,4-diol from (2S)-3,4-dehydroproline derivatives
    • Goli, D. M., Cheesman, B. V., Hassan, M. E., Lodaya, R., and Slama, J. T. (1994) Synthesis of (2R,3R,4S)-2-hydroxymethylpyrrolidine-3,4-diol from (2S)-3,4-dehydroproline derivatives Carbohydr. Res. 259, 219-241
    • (1994) Carbohydr. Res. , vol.259 , pp. 219-241
    • Goli, D.M.1    Cheesman, B.V.2    Hassan, M.E.3    Lodaya, R.4    Slama, J.T.5
  • 23
    • 19444366619 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) glycohydrolase (PARG) in shock, ischemia and reperfusion
    • DOI 10.1016/j.phrs.2005.02.009, PII S1043661805000411
    • Cuzzocrea, S. and Wang, Z. Q. (2005) Role of poly(ADP-ribose) glycohydrolase (PARG) in shock, ischemia and reperfusion Pharmacol. Res. 52, 100-108 (Pubitemid 40725604)
    • (2005) Pharmacological Research , vol.52 , Issue.1 SPEC. ISS. , pp. 100-108
    • Cuzzocrea, S.1    Wang, Z.-Q.2
  • 25
    • 20544475918 scopus 로고    scopus 로고
    • Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: Determining the PARG catalytic domain
    • DOI 10.1042/BJ20040942
    • Patel, C. N., Koh, D. W., Jacobson, M. K., and Oliveira, M. A. (2005) Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain Biochem. J. 388, 493-500 (Pubitemid 40839926)
    • (2005) Biochemical Journal , vol.388 , Issue.2 , pp. 493-500
    • Patel, C.N.1    Koh, D.W.2    Jacobson, M.K.3    Oliveira, M.A.4
  • 26
    • 85047693635 scopus 로고    scopus 로고
    • Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function
    • Chang, P., Coughlin, M., and Mitchison, T. J. (2005) Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function Nat. Cell Biol. 7, 1133-1139
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1133-1139
    • Chang, P.1    Coughlin, M.2    Mitchison, T.J.3
  • 27
    • 77954829745 scopus 로고    scopus 로고
    • Recognition of platinum-DNA damage by poly(ADP-ribose) polymerase-1
    • Zhu, G., Chang, P., and Lippard, S. J. (2010) Recognition of platinum-DNA damage by poly(ADP-ribose) polymerase-1 Biochemistry 49, 6177-6183
    • (2010) Biochemistry , vol.49 , pp. 6177-6183
    • Zhu, G.1    Chang, P.2    Lippard, S.J.3
  • 28
    • 77956627087 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 participates in the phase entrainment of circadian clocks to feeding
    • Asher, G., Reinke, H., Altmeyer, M., Gutierrez-Arcelus, M., Hottiger, M. O., and Schibler, U. (2010) Poly(ADP-ribose) polymerase 1 participates in the phase entrainment of circadian clocks to feeding Cell 142, 943-953
    • (2010) Cell , vol.142 , pp. 943-953
    • Asher, G.1    Reinke, H.2    Altmeyer, M.3    Gutierrez-Arcelus, M.4    Hottiger, M.O.5    Schibler, U.6
  • 29
    • 34250198661 scopus 로고    scopus 로고
    • Haploinsufficiency of poly(ADP-ribose) polymerase-1-mediated poly(ADP-ribosyl)ation for centrosome duplication
    • DOI 10.1016/j.bbrc.2007.05.108, PII S0006291X07010728
    • Kanai, M., Tong, W. M., Wang, Z. Q., and Miwa, M. (2007) Haploinsufficiency of poly(ADP-ribose) polymerase-1-mediated poly(ADP-ribosyl)ation for centrosome duplication Biochem. Biophys. Res. Commun. 359, 426-430 (Pubitemid 46898968)
    • (2007) Biochemical and Biophysical Research Communications , vol.359 , Issue.3 , pp. 426-430
    • Kanai, M.1    Tong, W.-M.2    Wang, Z.-Q.3    Miwa, M.4
  • 30
    • 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., and Chang, P. (2011) Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm Mol. Cell 42, 489-499
    • (2011) Mol. Cell , vol.42 , pp. 489-499
    • Leung, A.K.1    Vyas, S.2    Rood, J.E.3    Bhutkar, A.4    Sharp, P.A.5    Chang, P.6
  • 31
    • 10344234720 scopus 로고    scopus 로고
    • Poly(ADP-ribose) is required for spindle assembly and structure
    • DOI 10.1038/nature03061
    • Chang, P., Jacobson, M. K., and Mitchison, T. J. (2004) Poly(ADP-ribose) is required for spindle assembly and structure Nature 432, 645-649 (Pubitemid 39626273)
    • (2004) Nature , vol.432 , Issue.7017 , pp. 645-649
    • Chang, P.1    Jacobson, M.K.2    Mitchison, T.J.3
  • 32
    • 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., and Bailey, S. M. (2010) Regulatory roles of tankyrase 1 at telomeres and in DNA repair: suppression of T-SCE and stabilization of DNA-PKcs Aging 2, 691-708
    • (2010) Aging , vol.2 , 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
  • 33
    • 33846709501 scopus 로고    scopus 로고
    • Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes
    • DOI 10.1016/j.molcel.2006.12.022, PII S1097276507000068
    • Sanders, B. D., Zhao, K., Slama, J. T., and Marmorstein, R. (2007) Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes Mol. Cell 25, 463-472 (Pubitemid 46199287)
    • (2007) Molecular Cell , vol.25 , Issue.3 , pp. 463-472
    • Sanders, B.D.1    Zhao, K.2    Slama, J.T.3    Marmorstein, R.4
  • 35
    • 84858645528 scopus 로고    scopus 로고
    • Replacing the Irreplaceable: Cyclic Compounds as Novel Phosphate Mimics
    • T. P. Begley, ed. John Wiley & Sons
    • Nottbohm, A. C. and Hergenrother, P. J. (2008) Replacing the Irreplaceable: Cyclic Compounds as Novel Phosphate Mimics, in Wiley Encyclopedia of Chemical Biology, T. P. Begley, ed., John Wiley & Sons.
    • (2008) Wiley Encyclopedia of Chemical Biology
    • Nottbohm, A.C.1    Hergenrother, P.J.2
  • 39
    • 2642555622 scopus 로고    scopus 로고
    • Identification of selective inhibitors for the glycosyltransferase murg via high-throughput screening
    • DOI 10.1016/j.chembiol.2004.02.024, PII S1074552104001103
    • Hu, Y., Helm, J. S., Chen, L., Ginsberg, C., Gross, B., Kraybill, B., Tiyanont, K., Fang, X., Wu, T., and Walker, S. (2004) Identification of selective inhibitors for the glycosyltransferase MurG via high-throughput screening Chem. Biol. 11, 703-711 (Pubitemid 38708839)
    • (2004) Chemistry and Biology , vol.11 , Issue.5 , pp. 703-711
    • Hu, Y.1    Helm, J.S.2    Chen, L.3    Ginsberg, C.4    Gross, B.5    Kraybill, B.6    Tiyanont, K.7    Fang, X.8    Wu, T.9    Walker, S.10
  • 41
    • 77949484597 scopus 로고    scopus 로고
    • The bioisosteric similarity of the tetrazole and carboxylate anions: Clues from the topologies of the electrostatic potential and of the electron density
    • Matta, C. F., Arabi, A. A., and Weaver, D. F. (2010) The bioisosteric similarity of the tetrazole and carboxylate anions: clues from the topologies of the electrostatic potential and of the electron density Eur. J. Med. Chem. 45, 1868-1872
    • (2010) Eur. J. Med. Chem. , vol.45 , pp. 1868-1872
    • Matta, C.F.1    Arabi, A.A.2    Weaver, D.F.3
  • 44
    • 72249122328 scopus 로고    scopus 로고
    • Design, synthesis, and structure-activity relationship of a novel series of 2-aryl 5-(4-oxo-3-phenethyl-2-thioxothiazolidinylidenemethyl)furans as HIV-1 entry inhibitors
    • Katritzky, A. R., Tala, S. R., Lu, H., Vakulenko, A. V., Chen, Q. Y., Sivapackiam, J., Pandya, K., Jiang, S., and Debnath, A. K. (2009) Design, synthesis, and structure-activity relationship of a novel series of 2-aryl 5-(4-oxo-3-phenethyl-2-thioxothiazolidinylidenemethyl)furans as HIV-1 entry inhibitors J. Med. Chem. 52, 7631-7639
    • (2009) J. Med. Chem. , vol.52 , pp. 7631-7639
    • Katritzky, A.R.1    Tala, S.R.2    Lu, H.3    Vakulenko, A.V.4    Chen, Q.Y.5    Sivapackiam, J.6    Pandya, K.7    Jiang, S.8    Debnath, A.K.9
  • 49
    • 42949097094 scopus 로고    scopus 로고
    • Epalrestat: An aldose reductase inhibitor for the treatment of diabetic neuropathy
    • DOI 10.1592/phco.28.5.646
    • Ramirez, M. A. and Borja, N. L. (2008) Epalrestat: an aldose reductase inhibitor for the treatment of diabetic neuropathy Pharmacotherapy 28, 646-655 (Pubitemid 351620031)
    • (2008) Pharmacotherapy , vol.28 , Issue.5 PART 1 , pp. 646-655
    • Ramirez, M.A.1    Borja, N.L.2
  • 50
    • 33746456027 scopus 로고    scopus 로고
    • Long-term clinical effects of epalrestat, an aldose reductase inhibitor, on diabetic peripheral neuropathy: The 3-year, multicenter, comparative aldose reductase inhibitor-diabetes complications trial
    • DOI 10.2337/dc05-2370
    • Hotta, N., Akanuma, Y., Kawamori, R., Matsuoka, K., Oka, Y., Shichiri, M., Toyota, T., Nakashima, M., Yoshimura, I., Sakamoto, N., and Shigeta, Y. (2006) Long-term clinical effects of epalrestat, an aldose reductase inhibitor, on diabetic peripheral neuropathy: the 3-year, multicenter, comparative Aldose Reductase Inhibitor-Diabetes Complications Trial Diabetes Care 29, 1538-1544 (Pubitemid 44127578)
    • (2006) Diabetes Care , vol.29 , Issue.7 , pp. 1538-1544
    • Hotta, N.1    Akanuma, Y.2    Kawamori, R.3    Matsuoka, K.4    Oka, Y.5    Shichiri, M.6    Toyota, T.7    Nakashima, M.8    Yoshimura, I.9    Sakamoto, N.10    Shigeta, Y.11
  • 51
    • 0030152978 scopus 로고    scopus 로고
    • Clinical investigation of epalrestat, an aldose reductase inhibitor, on diabetic neuropathy in Japan: Multicenter study
    • Hotta, N., Sakamoto, N., Shigeta, Y., Kikkawa, R., and Goto, Y. (2006) Clinical investigation of epalrestat, an aldose reductase inhibitor, on diabetic neuropathy in Japan: Multicenter study J. Diabetes Complicat. 10, 168-172
    • (2006) J. Diabetes Complicat. , vol.10 , pp. 168-172
    • Hotta, N.1    Sakamoto, N.2    Shigeta, Y.3    Kikkawa, R.4    Goto, Y.5
  • 52
    • 77950571108 scopus 로고    scopus 로고
    • New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays
    • Baell, J. B. and Holloway, G. A. (2010) New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays J. Med. Chem. 53, 2719-2740
    • (2010) J. Med. Chem. , vol.53 , pp. 2719-2740
    • Baell, J.B.1    Holloway, G.A.2
  • 53
    • 33751321865 scopus 로고    scopus 로고
    • A detergent-based assay for the detection of promiscuous inhibitors
    • Feng, B. Y. and Shoichet, B. K. (2006) A detergent-based assay for the detection of promiscuous inhibitors Nat. Protoc. 1, 550-553
    • (2006) Nat. Protoc. , vol.1 , pp. 550-553
    • Feng, B.Y.1    Shoichet, B.K.2
  • 54
    • 33845491449 scopus 로고    scopus 로고
    • Interpreting steep dose-response curves in early inhibitor discovery
    • DOI 10.1021/jm061103g
    • Shoichet, B. K. (2006) Interpreting steep dose-response curves in early inhibitor discovery J. Med. Chem. 49, 7274-7277 (Pubitemid 44913388)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.25 , pp. 7274-7277
    • Shoichet, B.K.1
  • 55
    • 33745188660 scopus 로고    scopus 로고
    • Screening in a spirit haunted world
    • Shoichet, B. K. (2006) Screening in a spirit haunted world Drug Discovery Today 11, 607-615
    • (2006) Drug Discovery Today , vol.11 , pp. 607-615
    • Shoichet, B.K.1
  • 57
    • 33847094111 scopus 로고    scopus 로고
    • Stability and equilibria of promiscuous aggregates in high protein milieus
    • DOI 10.1039/b616314a
    • Coan, K. E. and Shoichet, B. K. (2007) Stability and equilibria of promiscuous aggregates in high protein milieus Mol. Biosyst. 3, 208-213 (Pubitemid 46293327)
    • (2007) Molecular BioSystems , vol.3 , Issue.3 , pp. 208-213
    • Coan, K.E.D.1    Shoichet, B.K.2
  • 58
    • 0141923641 scopus 로고    scopus 로고
    • Identification and prediction of promiscuous aggregating inhibitors among known drugs
    • DOI 10.1021/jm030191r
    • Seidler, J., McGovern, S. L., Doman, T. N., and Shoichet, B. K. (2003) Identification and prediction of promiscuous aggregating inhibitors among known drugs J. Med. Chem. 46, 4477-4486 (Pubitemid 37238749)
    • (2003) Journal of Medicinal Chemistry , vol.46 , Issue.21 , pp. 4477-4486
    • Seidler, J.1    McGovern, S.L.2    Doman, T.N.3    Shoichet, B.K.4
  • 59
    • 33644849513 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase
    • Oka, S., Kato, J., and Moss, J. (2006) Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase J. Biol. Chem. 281, 705-713
    • (2006) J. Biol. Chem. , vol.281 , pp. 705-713
    • Oka, S.1    Kato, J.2    Moss, J.3
  • 60
    • 33750940806 scopus 로고    scopus 로고
    • The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases
    • DOI 10.1073/pnas.0607911103
    • Ono, T., Kasamatsu, A., Oka, S., and Moss, J. (2006) The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases Proc. Natl. Acad. Sci. U.S.A. 103, 16687-16691 (Pubitemid 44737314)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.45 , pp. 16687-16691
    • Ono, T.1    Kasamatsu, A.2    Oka, S.3    Moss, J.4
  • 61
    • 37849013404 scopus 로고    scopus 로고
    • Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix
    • Niere, M., Kernstock, S., Koch-Nolte, F., and Ziegler, M. (2007) Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix Mol. Cell. Biol. 28, 814-824
    • (2007) Mol. Cell. Biol. , vol.28 , pp. 814-824
    • Niere, M.1    Kernstock, S.2    Koch-Nolte, F.3    Ziegler, M.4
  • 63
    • 0035289536 scopus 로고    scopus 로고
    • Protective effects of PJ34, a novel, potent inhibitor of poly(ADP-ribose) polymerase (PARP) in in vitro and in vivo models of stroke
    • Abdelkarim, G. E., Gertz, K., Harms, C., Katchanov, J., Dirnagl, U., Szabo, C., and Endres, M. (2001) Protective effects of PJ34, a novel, potent inhibitor of poly(ADP-ribose) polymerase (PARP) in in vitro and in vivo models of stroke Int. J. Mol. Med. 7, 255-260
    • (2001) Int. J. Mol. Med. , vol.7 , pp. 255-260
    • Abdelkarim, G.E.1    Gertz, K.2    Harms, C.3    Katchanov, J.4    Dirnagl, U.5    Szabo, C.6    Endres, M.7
  • 64
    • 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., and Jacobson, M. K. (2011) Discovery and structure-activity relationships of modified salicylanilides as cell permeable inhibitors of poly(ADP-ribose) glycohydrolase (PARG) J. Med. Chem. 54, 5403-5413
    • (2011) J. Med. Chem. , vol.54 , pp. 5403-5413
    • Steffen, J.D.1    Coyle, D.L.2    Damodaran, K.3    Beroza, P.4    Jacobson, M.K.5
  • 65
    • 33747335931 scopus 로고    scopus 로고
    • Chemical Probes of UDP-Galactopyranose Mutase
    • DOI 10.1016/j.chembiol.2006.06.007, PII S1074552106002171
    • Carlson, E. E., May, J. F., and Kiessling, L. L. (2006) Chemical probes of UDP-galactopyranose mutase Chem. Biol. 13, 825-837 (Pubitemid 44247773)
    • (2006) Chemistry and Biology , vol.13 , Issue.8 , pp. 825-837
    • Carlson, E.E.1    May, J.F.2    Kiessling, L.L.3
  • 66
    • 0023375254 scopus 로고
    • Rapid assay of poly(ADP-ribose) glycohydrolase
    • Menard, L. and Poirier, G. G. (1987) Rapid assay of poly(ADP-ribose) glycohydrolase Biochem. Cell Biol. 65, 668-673
    • (1987) Biochem. Cell Biol. , vol.65 , pp. 668-673
    • Menard, L.1    Poirier, G.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.