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Volumn 59, Issue 17, 2016, Pages 8019-8029

Identification of Inhibitors for the DEDDh Family of Exonucleases and a Unique Inhibition Mechanism by Crystal Structure Analysis of CRN-4 Bound with 2-Morpholin-4-ylethanesulfonate (MES)

Author keywords

[No Author keywords available]

Indexed keywords

2 MORPHOLIN 4 YLETHANESULFONIC ACID; AURINTRICARBOXYLIC ACID; ENZYME INHIBITOR; MORPHOLINE DERIVATIVE; PONTACYL VIOLET 6R; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG; VIRAL PROTEIN; 2-(N-MORPHOLINO)ETHANESULFONIC ACID; ALKANESULFONIC ACID; CAENORHABDITIS ELEGANS PROTEIN; CRN-4 PROTEIN, C ELEGANS; DEOXYRIBONUCLEASE; EXONUCLEASE; EXORIBONUCLEASE; EXORIBONUCLEASE T; RNA; SINGLE STRANDED DNA;

EID: 84986552439     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.6b00794     Document Type: Article
Times cited : (19)

References (65)
  • 1
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution
    • Zuo, Y.; Deutscher, M. P. Exoribonuclease superfamilies: structural analysis and phylogenetic distribution Nucleic Acids Res. 2001, 29, 1017-1026 10.1093/nar/29.5.1017
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2
  • 2
    • 79951678159 scopus 로고    scopus 로고
    • Nucleases: Diversity of structure, function and mechanism
    • Yang, W. Nucleases: diversity of structure, function and mechanism Q. Rev. Biophys. 2011, 44, 1-93 10.1017/S0033583510000181
    • (2011) Q. Rev. Biophys. , vol.44 , pp. 1-93
    • Yang, W.1
  • 3
    • 84865456858 scopus 로고    scopus 로고
    • Structural basis for the dsRNA specificity of the Lassa virus NP exonuclease
    • Hastie, K. M.; King, L. B.; Zandonatti, M. A.; Saphire, E. O. Structural basis for the dsRNA specificity of the Lassa virus NP exonuclease PLoS One 2012, 7, e44211 10.1371/journal.pone.0044211
    • (2012) PLoS One , vol.7 , pp. e44211
    • Hastie, K.M.1    King, L.B.2    Zandonatti, M.A.3    Saphire, E.O.4
  • 4
    • 58249107985 scopus 로고    scopus 로고
    • Crystal structure of CRN-4: Implications for domain function in apoptotic DNA degradation
    • Hsiao, Y. Y.; Nakagawa, A.; Shi, Z.; Mitani, S.; Xue, D.; Yuan, H. S. Crystal structure of CRN-4: implications for domain function in apoptotic DNA degradation Mol. Cell. Biol. 2009, 29, 448-457 10.1128/MCB.01006-08
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 448-457
    • Hsiao, Y.Y.1    Nakagawa, A.2    Shi, Z.3    Mitani, S.4    Xue, D.5    Yuan, H.S.6
  • 5
    • 84878889200 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli exonuclease i in complex with single-stranded DNA provide insights into the mechanism of processive digestion
    • Korada, S. K.; Johns, T. D.; Smith, C. E.; Jones, N. D.; McCabe, K. A.; Bell, C. E. Crystal structures of Escherichia coli exonuclease I in complex with single-stranded DNA provide insights into the mechanism of processive digestion Nucleic Acids Res. 2013, 41, 5887-5897 10.1093/nar/gkt278
    • (2013) Nucleic Acids Res. , vol.41 , pp. 5887-5897
    • Korada, S.K.1    Johns, T.D.2    Smith, C.E.3    Jones, N.D.4    McCabe, K.A.5    Bell, C.E.6
  • 6
    • 7544228191 scopus 로고    scopus 로고
    • Crystal structure of human ISG20, an interferon-induced antiviral ribonuclease
    • Horio, T.; Murai, M.; Inoue, T.; Hamasaki, T.; Tanaka, T.; Ohgi, T. Crystal structure of human ISG20, an interferon-induced antiviral ribonuclease FEBS Lett. 2004, 577, 111-116 10.1016/j.febslet.2004.09.074
    • (2004) FEBS Lett. , vol.577 , pp. 111-116
    • Horio, T.1    Murai, M.2    Inoue, T.3    Hamasaki, T.4    Tanaka, T.5    Ohgi, T.6
  • 7
    • 84870546369 scopus 로고    scopus 로고
    • How an exonuclease decides where to stop in trimming of nucleic acids: Crystal structures of RNase T-product complexes
    • Hsiao, Y. Y.; Duh, Y.; Chen, Y. P.; Wang, Y. T.; Yuan, H. S. How an exonuclease decides where to stop in trimming of nucleic acids: crystal structures of RNase T-product complexes Nucleic Acids Res. 2012, 40, 8144-8154 10.1093/nar/gks548
    • (2012) Nucleic Acids Res. , vol.40 , pp. 8144-8154
    • Hsiao, Y.Y.1    Duh, Y.2    Chen, Y.P.3    Wang, Y.T.4    Yuan, H.S.5
  • 8
    • 33845264383 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of Drosophila Snipper: A promiscuous member of the metazoan 3′hExo/ERI-1 family of 3′ to 5′ exonucleases
    • Kupsco, J. M.; Wu, M. J.; Marzluff, W. F.; Thapar, R.; Duronio, R. J. Genetic and biochemical characterization of Drosophila Snipper: A promiscuous member of the metazoan 3′hExo/ERI-1 family of 3′ to 5′ exonucleases RNA 2006, 12, 2103-2117 10.1261/rna.186706
    • (2006) RNA , vol.12 , pp. 2103-2117
    • Kupsco, J.M.1    Wu, M.J.2    Marzluff, W.F.3    Thapar, R.4    Duronio, R.J.5
  • 9
    • 42249095447 scopus 로고    scopus 로고
    • A novel mutation of the WRN gene in a Chinese patient with Werner syndrome
    • Zhao, N.; Hao, F.; Qu, T.; Zuo, Y. G.; Wang, B. X. A novel mutation of the WRN gene in a Chinese patient with Werner syndrome Clin. Exp. Dermatol. 2008, 33, 278-281 10.1111/j.1365-2230.2007.02641.x
    • (2008) Clin. Exp. Dermatol. , vol.33 , pp. 278-281
    • Zhao, N.1    Hao, F.2    Qu, T.3    Zuo, Y.G.4    Wang, B.X.5
  • 13
    • 84870946428 scopus 로고    scopus 로고
    • A live, impaired-fidelity coronavirus vaccine protects in an aged, immunocompromised mouse model of lethal disease
    • Graham, R. L.; Becker, M. M.; Eckerle, L. D.; Bolles, M.; Denison, M. R.; Baric, R. S. A live, impaired-fidelity coronavirus vaccine protects in an aged, immunocompromised mouse model of lethal disease Nat. Med. 2012, 18, 1820-1826 10.1038/nm.2972
    • (2012) Nat. Med. , vol.18 , pp. 1820-1826
    • Graham, R.L.1    Becker, M.M.2    Eckerle, L.D.3    Bolles, M.4    Denison, M.R.5    Baric, R.S.6
  • 15
    • 78650132935 scopus 로고    scopus 로고
    • Cap binding and immune evasion revealed by Lassa nucleoprotein structure
    • Qi, X.; Lan, S.; Wang, W.; Schelde, L. M.; Dong, H.; Wallat, G. D.; Ly, H.; Liang, Y.; Dong, C. Cap binding and immune evasion revealed by Lassa nucleoprotein structure Nature 2010, 468, 779-783 10.1038/nature09605
    • (2010) Nature , vol.468 , pp. 779-783
    • Qi, X.1    Lan, S.2    Wang, W.3    Schelde, L.M.4    Dong, H.5    Wallat, G.D.6    Ly, H.7    Liang, Y.8    Dong, C.9
  • 17
    • 77958114725 scopus 로고    scopus 로고
    • The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1
    • Yan, N.; Regalado-Magdos, A. D.; Stiggelbout, B.; Lee-Kirsch, M. A.; Lieberman, J. The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1 Nat. Immunol. 2010, 11, 1005-1013 10.1038/ni.1941
    • (2010) Nat. Immunol. , vol.11 , pp. 1005-1013
    • Yan, N.1    Regalado-Magdos, A.D.2    Stiggelbout, B.3    Lee-Kirsch, M.A.4    Lieberman, J.5
  • 18
    • 33847698212 scopus 로고    scopus 로고
    • Lassa fever in West African sub-region: An overview
    • Ogbu, O.; Ajuluchukwu, E.; Uneke, C. J. Lassa fever in West African sub-region: an overview J. Vector Borne Dis. 2007, 44, 1-11
    • (2007) J. Vector Borne Dis. , vol.44 , pp. 1-11
    • Ogbu, O.1    Ajuluchukwu, E.2    Uneke, C.J.3
  • 19
    • 0032539857 scopus 로고    scopus 로고
    • 3′ exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli
    • Li, Z.; Pandit, S.; Deutscher, M. P. 3′ exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 1998, 95, 2856-2861 10.1073/pnas.95.6.2856
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 2856-2861
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 20
    • 0032951885 scopus 로고    scopus 로고
    • Maturation of 23S ribosomal RNA requires the exoribonuclease RNase T
    • Li, Z.; Pandit, S.; Deutscher, M. P. Maturation of 23S ribosomal RNA requires the exoribonuclease RNase T RNA 1999, 5, 139-146 10.1017/S1355838299981669
    • (1999) RNA , vol.5 , pp. 139-146
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 21
    • 84898958172 scopus 로고    scopus 로고
    • Structural insights into DNA repair by RNase T - An exonuclease processing 3′ end of structured DNA in repair pathways
    • Hsiao, Y. Y.; Fang, W. H.; Lee, C. C.; Chen, Y. P.; Yuan, H. S. Structural insights into DNA repair by RNase T - an exonuclease processing 3′ end of structured DNA in repair pathways PLoS Biol. 2014, 12, e1001803 10.1371/journal.pbio.1001803
    • (2014) PLoS Biol. , vol.12 , pp. e1001803
    • Hsiao, Y.Y.1    Fang, W.H.2    Lee, C.C.3    Chen, Y.P.4    Yuan, H.S.5
  • 22
    • 0038369994 scopus 로고    scopus 로고
    • Functional genomic analysis of apoptotic DNA degradation in C. Elegans
    • Parrish, J. Z.; Xue, D. Functional genomic analysis of apoptotic DNA degradation in C. elegans Mol. Cell 2003, 11, 987-996 10.1016/S1097-2765(03)00095-9
    • (2003) Mol. Cell , vol.11 , pp. 987-996
    • Parrish, J.Z.1    Xue, D.2
  • 24
    • 44249120771 scopus 로고    scopus 로고
    • Characterization of a novel non-specific nuclease from thermophilic bacteriophage GBSV1
    • Song, Q.; Zhang, X. Characterization of a novel non-specific nuclease from thermophilic bacteriophage GBSV1 BMC Biotechnol. 2008, 8, 43 10.1186/1472-6750-8-43
    • (2008) BMC Biotechnol. , vol.8 , pp. 43
    • Song, Q.1    Zhang, X.2
  • 25
    • 0032555658 scopus 로고    scopus 로고
    • Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity
    • Zhang, M.; Stauffacher, C. V.; Lin, D.; Van Etten, R. L. Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity J. Biol. Chem. 1998, 273, 21714-21720 10.1074/jbc.273.34.21714
    • (1998) J. Biol. Chem. , vol.273 , pp. 21714-21720
    • Zhang, M.1    Stauffacher, C.V.2    Lin, D.3    Van Etten, R.L.4
  • 26
    • 0038756863 scopus 로고    scopus 로고
    • Potent inhibition of ribonuclease A by oligo(vinylsulfonic acid)
    • Smith, B. D.; Soellner, M. B.; Raines, R. T. Potent inhibition of ribonuclease A by oligo(vinylsulfonic acid) J. Biol. Chem. 2003, 278, 20934-20938 10.1074/jbc.M301852200
    • (2003) J. Biol. Chem. , vol.278 , pp. 20934-20938
    • Smith, B.D.1    Soellner, M.B.2    Raines, R.T.3
  • 27
    • 0033974843 scopus 로고    scopus 로고
    • Origin of the "inactivation" of ribonuclease A at low salt concentration
    • Park, C.; Raines, R. T. Origin of the "inactivation" of ribonuclease A at low salt concentration FEBS Lett. 2000, 468, 199-202 10.1016/S0014-5793(00)01227-8
    • (2000) FEBS Lett. , vol.468 , pp. 199-202
    • Park, C.1    Raines, R.T.2
  • 28
    • 8844267049 scopus 로고    scopus 로고
    • A novel inhibitor that protects apoptotic DNA fragmentation catalyzed by DNase gamma
    • Sunaga, S.; Kobayashi, T.; Yoshimori, A.; Shiokawa, D.; Tanuma, S. A novel inhibitor that protects apoptotic DNA fragmentation catalyzed by DNase gamma Biochem. Biophys. Res. Commun. 2004, 325, 1292-1297 10.1016/j.bbrc.2004.10.171
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , pp. 1292-1297
    • Sunaga, S.1    Kobayashi, T.2    Yoshimori, A.3    Shiokawa, D.4    Tanuma, S.5
  • 29
    • 0022201114 scopus 로고
    • Effects of phosphatase inhibitors on nuclease activity
    • Prentice, D. A.; Kitos, P. A.; Gurley, L. R. Effects of phosphatase inhibitors on nuclease activity Cell Biol. Int. Rep. 1985, 9, 1027-1034 10.1016/0309-1651(85)90069-4
    • (1985) Cell Biol. Int. Rep. , vol.9 , pp. 1027-1034
    • Prentice, D.A.1    Kitos, P.A.2    Gurley, L.R.3
  • 30
    • 0030029157 scopus 로고    scopus 로고
    • The role of individual cysteine residues in the activity of Escherichia coli RNase T
    • Li, Z. W.; Zhan, L. J.; Deutscher, M. P. The role of individual cysteine residues in the activity of Escherichia coli RNase T J. Biol. Chem. 1996, 271, 1127-1132 10.1074/jbc.271.2.1127
    • (1996) J. Biol. Chem. , vol.271 , pp. 1127-1132
    • Li, Z.W.1    Zhan, L.J.2    Deutscher, M.P.3
  • 32
    • 84867365374 scopus 로고    scopus 로고
    • DNA repair and cancer therapy: Targeting APE1/Ref-1 using dietary agents
    • Raffoul, J. J.; Heydari, A. R.; Hillman, G. G. DNA repair and cancer therapy: targeting APE1/Ref-1 using dietary agents J. Oncol. 2012, 2012, 370481 10.1155/2012/370481
    • (2012) J. Oncol. , vol.2012 , pp. 370481
    • Raffoul, J.J.1    Heydari, A.R.2    Hillman, G.G.3
  • 33
    • 34548276529 scopus 로고    scopus 로고
    • The DNA base excision repair protein Ape1/Ref-1 as a therapeutic and chemopreventive target
    • Fishel, M. L.; Kelley, M. R. The DNA base excision repair protein Ape1/Ref-1 as a therapeutic and chemopreventive target Mol. Aspects Med. 2007, 28, 375-395 10.1016/j.mam.2007.04.005
    • (2007) Mol. Aspects Med. , vol.28 , pp. 375-395
    • Fishel, M.L.1    Kelley, M.R.2
  • 34
    • 0017669601 scopus 로고
    • Use of aurintricarboxylic acid as an inhibitor of nucleases during nucleic-acid isolation
    • Hallick, R. B.; Chelm, B. K.; Gray, P. W.; Orozco, E. M. Use of aurintricarboxylic acid as an inhibitor of nucleases during nucleic-acid isolation Nucleic Acids Res. 1977, 4, 3055-3064 10.1093/nar/4.9.3055
    • (1977) Nucleic Acids Res. , vol.4 , pp. 3055-3064
    • Hallick, R.B.1    Chelm, B.K.2    Gray, P.W.3    Orozco, E.M.4
  • 35
    • 0026063679 scopus 로고
    • Preparation and anti-HIV activities of aurintricarboxylic acid fractions and analogues: Direct correlation of antiviral potency with molecular weight
    • Cushman, M.; Wang, P. L.; Chang, S. H.; Wild, C.; De Clercq, E.; Schols, D.; Goldman, M. E.; Bowen, J. A. Preparation and anti-HIV activities of aurintricarboxylic acid fractions and analogues: direct correlation of antiviral potency with molecular weight J. Med. Chem. 1991, 34, 329-337 10.1021/jm00105a052
    • (1991) J. Med. Chem. , vol.34 , pp. 329-337
    • Cushman, M.1    Wang, P.L.2    Chang, S.H.3    Wild, C.4    De Clercq, E.5    Schols, D.6    Goldman, M.E.7    Bowen, J.A.8
  • 36
    • 0036085386 scopus 로고    scopus 로고
    • Aurintricarboxylic acid protects against cell death caused by lipopolysaccharide in macrophages by decreasing inducible nitric-oxide synthase induction via IkappaB kinase, extracellular signal-regulated kinase, and p38 mitogen-activated protein kinase inhibition
    • Tsi, C. J.; Chao, Y.; Chen, C. W.; Lin, W. W. Aurintricarboxylic acid protects against cell death caused by lipopolysaccharide in macrophages by decreasing inducible nitric-oxide synthase induction via IkappaB kinase, extracellular signal-regulated kinase, and p38 mitogen-activated protein kinase inhibition Mol. Pharmacol. 2002, 62, 90-101 10.1124/mol.62.1.90
    • (2002) Mol. Pharmacol. , vol.62 , pp. 90-101
    • Tsi, C.J.1    Chao, Y.2    Chen, C.W.3    Lin, W.W.4
  • 37
    • 1842846611 scopus 로고    scopus 로고
    • Inhibition of cytokine-induced JAK-STAT signalling pathways by an endonuclease inhibitor aurintricarboxylic acid
    • Chen, C. W.; Chao, Y.; Chang, Y. H.; Hsu, M. J.; Lin, W. W. Inhibition of cytokine-induced JAK-STAT signalling pathways by an endonuclease inhibitor aurintricarboxylic acid Br. J. Pharmacol. 2002, 137, 1011-1020 10.1038/sj.bjp.0704955
    • (2002) Br. J. Pharmacol. , vol.137 , pp. 1011-1020
    • Chen, C.W.1    Chao, Y.2    Chang, Y.H.3    Hsu, M.J.4    Lin, W.W.5
  • 38
    • 77949497846 scopus 로고    scopus 로고
    • Aurintricarboxylic acid is a potent inhibitor of influenza A and B virus neuraminidases
    • Hashem, A. M.; Flaman, A. S.; Farnsworth, A.; Brown, E. G.; Van Domselaar, G.; He, R.; Li, X. Aurintricarboxylic acid is a potent inhibitor of influenza A and B virus neuraminidases PLoS One 2009, 4, e8350 10.1371/journal.pone.0008350
    • (2009) PLoS One , vol.4 , pp. e8350
    • Hashem, A.M.1    Flaman, A.S.2    Farnsworth, A.3    Brown, E.G.4    Van Domselaar, G.5    He, R.6    Li, X.7
  • 40
    • 0345196609 scopus 로고
    • Specific interaction of aurintricarboxylic acid with the human immunodeficiency virus/CD4 cell receptor
    • Schols, D.; Baba, M.; Pauwels, R.; Desmyter, J.; De Clercq, E. Specific interaction of aurintricarboxylic acid with the human immunodeficiency virus/CD4 cell receptor Proc. Natl. Acad. Sci. U. S. A. 1989, 86, 3322-3326 10.1073/pnas.86.9.3322
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 3322-3326
    • Schols, D.1    Baba, M.2    Pauwels, R.3    Desmyter, J.4    De Clercq, E.5
  • 43
    • 33947397199 scopus 로고    scopus 로고
    • Aurintricarboxylic acid inhibits the early stage of vaccinia virus replication by targeting both cellular and viral factors
    • Myskiw, C.; Deschambault, Y.; Jefferies, K.; He, R.; Cao, J. Aurintricarboxylic acid inhibits the early stage of vaccinia virus replication by targeting both cellular and viral factors J. Virol. 2007, 81, 3027-3032 10.1128/JVI.02531-06
    • (2007) J. Virol. , vol.81 , pp. 3027-3032
    • Myskiw, C.1    Deschambault, Y.2    Jefferies, K.3    He, R.4    Cao, J.5
  • 44
    • 20444486621 scopus 로고    scopus 로고
    • Structural analysis of inhibition mechanisms of aurintricarboxylic acid on SARS-CoV polymerase and other proteins
    • Yap, Y.; Zhang, X.; Andonov, A.; He, R. Structural analysis of inhibition mechanisms of aurintricarboxylic acid on SARS-CoV polymerase and other proteins Comput. Biol. Chem. 2005, 29, 212-219 10.1016/j.compbiolchem.2005.04.006
    • (2005) Comput. Biol. Chem. , vol.29 , pp. 212-219
    • Yap, Y.1    Zhang, X.2    Andonov, A.3    He, R.4
  • 45
    • 84884253048 scopus 로고    scopus 로고
    • Aurintricarboxylic acid modulates the affinity of hepatitis C virus NS3 helicase for both nucleic acid and ATP
    • Shadrick, W. R.; Mukherjee, S.; Hanson, A. M.; Sweeney, N. L.; Frick, D. N. Aurintricarboxylic acid modulates the affinity of hepatitis C virus NS3 helicase for both nucleic acid and ATP Biochemistry 2013, 52, 6151-6159 10.1021/bi4006495
    • (2013) Biochemistry , vol.52 , pp. 6151-6159
    • Shadrick, W.R.1    Mukherjee, S.2    Hanson, A.M.3    Sweeney, N.L.4    Frick, D.N.5
  • 46
    • 79951520837 scopus 로고    scopus 로고
    • IGEMDOCK: A graphical environment of enhancing GEMDOCK using pharmacological interactions and post-screening analysis
    • Hsu, K. C.; Chen, Y. F.; Lin, S. R.; Yang, J. M. iGEMDOCK: a graphical environment of enhancing GEMDOCK using pharmacological interactions and post-screening analysis BMC Bioinf. 2011, 12 (Suppl. 1) S33 10.1186/1471-2105-12-S1-S33
    • (2011) BMC Bioinf. , vol.12 , pp. S33
    • Hsu, K.C.1    Chen, Y.F.2    Lin, S.R.3    Yang, J.M.4
  • 47
    • 79952953767 scopus 로고    scopus 로고
    • Structural basis for RNA trimming by RNase T in stable RNA 3′-end maturation
    • Hsiao, Y. Y.; Yang, C. C.; Lin, C. L.; Lin, J. L.; Duh, Y.; Yuan, H. S. Structural basis for RNA trimming by RNase T in stable RNA 3′-end maturation Nat. Chem. Biol. 2011, 7, 236-243 10.1038/nchembio.524
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 236-243
    • Hsiao, Y.Y.1    Yang, C.C.2    Lin, C.L.3    Lin, J.L.4    Duh, Y.5    Yuan, H.S.6
  • 48
    • 34249848019 scopus 로고    scopus 로고
    • The crystal structure of TREX1 explains the 3′ nucleotide specificity and reveals a polyproline II helix for protein partnering
    • de Silva, U.; Choudhury, S.; Bailey, S. L.; Harvey, S.; Perrino, F. W.; Hollis, T. The crystal structure of TREX1 explains the 3′ nucleotide specificity and reveals a polyproline II helix for protein partnering J. Biol. Chem. 2007, 282, 10537-10543 10.1074/jbc.M700039200
    • (2007) J. Biol. Chem. , vol.282 , pp. 10537-10543
    • De Silva, U.1    Choudhury, S.2    Bailey, S.L.3    Harvey, S.4    Perrino, F.W.5    Hollis, T.6
  • 49
    • 0036050539 scopus 로고    scopus 로고
    • Strategies in the design of antiviral drugs
    • De Clercq, E. Strategies in the design of antiviral drugs Nat. Rev. Drug Discovery 2002, 1, 13-25 10.1038/nrd703
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 13-25
    • De Clercq, E.1
  • 50
    • 61449189645 scopus 로고    scopus 로고
    • Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV
    • De Clercq, E. Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV Int. J. Antimicrob. Agents 2009, 33, 307-320 10.1016/j.ijantimicag.2008.10.010
    • (2009) Int. J. Antimicrob. Agents , vol.33 , pp. 307-320
    • De Clercq, E.1
  • 51
    • 82955235541 scopus 로고    scopus 로고
    • Antivirals and resistance: Influenza virus
    • Ison, M. G. Antivirals and resistance: influenza virus Curr. Opin. Virol. 2011, 1, 563-573 10.1016/j.coviro.2011.09.002
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 563-573
    • Ison, M.G.1
  • 52
    • 84876003028 scopus 로고    scopus 로고
    • Influenza virus resistance to neuraminidase inhibitors
    • Samson, M.; Pizzorno, A.; Abed, Y.; Boivin, G. Influenza virus resistance to neuraminidase inhibitors Antiviral Res. 2013, 98, 174-185 10.1016/j.antiviral.2013.03.014
    • (2013) Antiviral Res. , vol.98 , pp. 174-185
    • Samson, M.1    Pizzorno, A.2    Abed, Y.3    Boivin, G.4
  • 53
    • 84878333879 scopus 로고    scopus 로고
    • Emergence of HIV drug resistance during first- and second-line antiretroviral therapy in resource-limited settings
    • Hosseinipour, M. C.; Gupta, R. K.; Van Zyl, G.; Eron, J. J.; Nachega, J. B. Emergence of HIV drug resistance during first- and second-line antiretroviral therapy in resource-limited settings J. Infect. Dis. 2013, 207 (Suppl. 2) S49-S56 10.1093/infdis/jit107
    • (2013) J. Infect. Dis. , vol.207 , pp. S49-S56
    • Hosseinipour, M.C.1    Gupta, R.K.2    Van Zyl, G.3    Eron, J.J.4    Nachega, J.B.5
  • 54
    • 84857363079 scopus 로고    scopus 로고
    • Is there a future for antiviral fusion inhibitors?
    • Berkhout, B.; Eggink, D.; Sanders, R. W. Is there a future for antiviral fusion inhibitors? Curr. Opin. Virol. 2012, 2, 50-59 10.1016/j.coviro.2012.01.002
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 50-59
    • Berkhout, B.1    Eggink, D.2    Sanders, R.W.3
  • 55
    • 84880054656 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase and antiviral drug resistance. Part 1
    • Das, K.; Arnold, E. HIV-1 reverse transcriptase and antiviral drug resistance. Part 1 Curr. Opin. Virol. 2013, 3, 111-118 10.1016/j.coviro.2013.03.012
    • (2013) Curr. Opin. Virol. , vol.3 , pp. 111-118
    • Das, K.1    Arnold, E.2
  • 56
    • 20844460158 scopus 로고    scopus 로고
    • New drug targets for HIV
    • Bean, P. New drug targets for HIV Clin. Infect. Dis. 2005, 41 (Suppl. 1) S96-S100 10.1086/429504
    • (2005) Clin. Infect. Dis. , vol.41 , pp. S96-S100
    • Bean, P.1
  • 60
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, I. N.; Bourne, P. E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path Protein Eng., Des. Sel. 1998, 11, 739-747 10.1093/protein/11.9.739
    • (1998) Protein Eng., Des. Sel. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 61
    • 0028466540 scopus 로고
    • Comparison of Automatic Three-Dimensional Model Builders Using 639 X-ray Structures
    • Sadowski, J.; Gasteiger, J.; Klebe, G. Comparison of Automatic Three-Dimensional Model Builders Using 639 X-ray Structures J. Chem. Inf. Model. 1994, 34, 1000-1008 10.1021/ci00020a039
    • (1994) J. Chem. Inf. Model. , vol.34 , pp. 1000-1008
    • Sadowski, J.1    Gasteiger, J.2    Klebe, G.3
  • 62
    • 1842532062 scopus 로고    scopus 로고
    • GEMDOCK: A generic evolutionary method for molecular docking
    • Yang, J. M.; Chen, C. C. GEMDOCK: a generic evolutionary method for molecular docking Proteins: Struct., Funct., Genet. 2004, 55, 288-304 10.1002/prot.20035
    • (2004) Proteins: Struct., Funct., Genet. , vol.55 , pp. 288-304
    • Yang, J.M.1    Chen, C.C.2
  • 64
    • 0032563164 scopus 로고    scopus 로고
    • Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family
    • Birck, C.; Poch, O.; Romier, C.; Ruff, M.; Mengus, G.; Lavigne, A. C.; Davidson, I.; Moras, D. Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family Cell 1998, 94, 239-249 10.1016/S0092-8674(00)81423-3
    • (1998) Cell , vol.94 , pp. 239-249
    • Birck, C.1    Poch, O.2    Romier, C.3    Ruff, M.4    Mengus, G.5    Lavigne, A.C.6    Davidson, I.7    Moras, D.8
  • 65
    • 0037177882 scopus 로고    scopus 로고
    • Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion
    • Ackerman, S. J.; Liu, L.; Kwatia, M. A.; Savage, M. P.; Leonidas, D. D.; Swaminathan, G. J.; Acharya, K. R. Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion J. Biol. Chem. 2002, 277, 14859-14868 10.1074/jbc.M200221200
    • (2002) J. Biol. Chem. , vol.277 , pp. 14859-14868
    • Ackerman, S.J.1    Liu, L.2    Kwatia, M.A.3    Savage, M.P.4    Leonidas, D.D.5    Swaminathan, G.J.6    Acharya, K.R.7


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