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Volumn 60, Issue 9, 2017, Pages 3533-3551

Inhibitors of Influenza Virus Polymerase Acidic (PA) Endonuclease: Contemporary Developments and Perspectives

Author keywords

[No Author keywords available]

Indexed keywords

2,3 DIHYDROXYBENZOIC ACID; ANTIVIRUS AGENT; CATECHOL DERIVATIVE; DIKETO ACID DERIVATIVE; ENDONUCLEASE; ESTERASE INHIBITOR; FLUTIMIDE DERIVATIVE; HETEROCYCLIC COMPOUND; POLYMERASE ACIDIC ENDONUCLEASE; POLYMERASE ACIDIC ENDONUCLEASE INHIBITOR; UNCLASSIFIED DRUG; VIRUS ENZYME; ENZYME INHIBITOR;

EID: 85018868773     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.6b01227     Document Type: Article
Times cited : (62)

References (109)
  • 1
    • 85018930010 scopus 로고    scopus 로고
    • Centers for Disease Control and Prevention, National Center for Immunization and Respiratory Diseases (NCIRD) Website; October 31
    • Centers for Disease Control and Prevention, National Center for Immunization and Respiratory Diseases (NCIRD) Website; October 31, 2016. https://www.cdc.gov/flu/about/disease/.
    • (2016)
  • 3
    • 84941642281 scopus 로고    scopus 로고
    • Clinical implications of antiviral resistance in influenza
    • Li, T. C.; Chan, M. C.; Lee, N. Clinical implications of antiviral resistance in influenza Viruses 2015, 7, 4929-4944 10.3390/v7092850
    • (2015) Viruses , vol.7 , pp. 4929-4944
    • Li, T.C.1    Chan, M.C.2    Lee, N.3
  • 4
    • 84975796039 scopus 로고    scopus 로고
    • Current and novel antiviral strategies for influenza infection
    • Yen, H. L. Current and novel antiviral strategies for influenza infection Curr. Opin. Virol. 2016, 18, 126-134 10.1016/j.coviro.2016.05.004
    • (2016) Curr. Opin. Virol. , vol.18 , pp. 126-134
    • Yen, H.L.1
  • 5
    • 84866740262 scopus 로고    scopus 로고
    • Recent progress in structure-based anti-influenza drug design
    • Du, J.; Cross, T. A.; Zhou, H. X. Recent progress in structure-based anti-influenza drug design Drug Discovery Today 2012, 17, 1111-1120 10.1016/j.drudis.2012.06.002
    • (2012) Drug Discovery Today , vol.17 , pp. 1111-1120
    • Du, J.1    Cross, T.A.2    Zhou, H.X.3
  • 6
    • 33750286032 scopus 로고    scopus 로고
    • Vaccines for seasonal and pandemic influenza
    • Nichol, K. L.; Treanor, J. J. Vaccines for seasonal and pandemic influenza J. Infect. Dis. 2006, 194 ( Suppl. 2 ) S111-S118 10.1086/507544
    • (2006) J. Infect. Dis. , vol.194 , pp. S111-S118
    • Nichol, K.L.1    Treanor, J.J.2
  • 7
    • 33947590474 scopus 로고    scopus 로고
    • Scientific barriers to developing vaccines against avian influenza viruses
    • Subbarao, K.; Joseph, T. Scientific barriers to developing vaccines against avian influenza viruses Nat. Rev. Immunol. 2007, 7, 267-278 10.1038/nri2054
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 267-278
    • Subbarao, K.1    Joseph, T.2
  • 8
    • 77951976539 scopus 로고    scopus 로고
    • Structures of influenza A proteins and insights into antiviral drug targets
    • Das, K.; Aramini, J. M.; Ma, L. C.; Krug, R. M.; Arnold, E. Structures of influenza A proteins and insights into antiviral drug targets Nat. Struct. Mol. Biol. 2010, 17, 530-538 10.1038/nsmb.1779
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 530-538
    • Das, K.1    Aramini, J.M.2    Ma, L.C.3    Krug, R.M.4    Arnold, E.5
  • 10
    • 84922726229 scopus 로고    scopus 로고
    • International severe acute respiratory and emerging infection consortium (ISARIC). antiviral combinations for severe influenza
    • Dunning, J.; Baillie, J. K.; Cao, B.; Hayden, F. G. International severe acute respiratory and emerging infection consortium (ISARIC). antiviral combinations for severe influenza Lancet Infect. Dis. 2014, 14, 1259-1270 10.1016/S1473-3099(14)70821-7
    • (2014) Lancet Infect. Dis. , vol.14 , pp. 1259-1270
    • Dunning, J.1    Baillie, J.K.2    Cao, B.3    Hayden, F.G.4
  • 11
    • 0036016097 scopus 로고    scopus 로고
    • Peramivir (BCX-1812, RWJ-270201): potential new therapy for influenza
    • Smee, D. F.; Sidwell, R. W. Peramivir (BCX-1812, RWJ-270201): potential new therapy for influenza Expert Opin. Invest. Drugs 2002, 11, 859-869 10.1517/13543784.11.6.859
    • (2002) Expert Opin. Invest. Drugs , vol.11 , pp. 859-869
    • Smee, D.F.1    Sidwell, R.W.2
  • 12
    • 84903183021 scopus 로고    scopus 로고
    • From neuraminidase inhibitors to conjugates: a step towards better anti-influenza drugs?
    • Cheng, C. K.; Tsai, C. H.; Shie, J. J.; Fang, J. M. From neuraminidase inhibitors to conjugates: a step towards better anti-influenza drugs? Future Med. Chem. 2014, 6, 757-774 10.4155/fmc.14.30
    • (2014) Future Med. Chem. , vol.6 , pp. 757-774
    • Cheng, C.K.1    Tsai, C.H.2    Shie, J.J.3    Fang, J.M.4
  • 14
    • 33644536465 scopus 로고    scopus 로고
    • Adamantane resistance among influenza A viruses isolated early during the 2005-2006 influenza season in the United States
    • Bright, R. A.; Shay, D. K.; Shu, B.; Cox, N. J.; Klimov, A. I. Adamantane resistance among influenza A viruses isolated early during the 2005-2006 influenza season in the United States JAMA 2006, 295, 891-894 10.1001/jama.295.8.joc60020
    • (2006) JAMA , vol.295 , pp. 891-894
    • Bright, R.A.1    Shay, D.K.2    Shu, B.3    Cox, N.J.4    Klimov, A.I.5
  • 15
    • 85026249393 scopus 로고    scopus 로고
    • Anti-influenza treatment: Drugs currently used and under development
    • Amarelle, L.; Lecuona, E.; Sznajder, J. I. Anti-influenza treatment: Drugs currently used and under development Arch. Bronconeumol. 2017, 53, 19-26 10.1016/j.arbr.2016.11.020
    • (2017) Arch. Bronconeumol. , vol.53 , pp. 19-26
    • Amarelle, L.1    Lecuona, E.2    Sznajder, J.I.3
  • 18
    • 61849118968 scopus 로고    scopus 로고
    • Global transmission of oseltamivir-resistant influenza
    • Moscona, A. Global transmission of oseltamivir-resistant influenza N. Engl. J. Med. 2009, 360, 953-956 10.1056/NEJMp0900648
    • (2009) N. Engl. J. Med. , vol.360 , pp. 953-956
    • Moscona, A.1
  • 19
    • 0037286318 scopus 로고    scopus 로고
    • The treatment of influenza with antiviral drugs
    • Stiver, G. The treatment of influenza with antiviral drugs Can. Med. Assoc. J. 2003, 168, 49-56
    • (2003) Can. Med. Assoc. J. , vol.168 , pp. 49-56
    • Stiver, G.1
  • 20
    • 85018912705 scopus 로고    scopus 로고
    • U.S. Food and Drug Administration. Tamiflu pediatric adverse events: questions and answers; December 07
    • U.S. Food and Drug Administration. Tamiflu pediatric adverse events: questions and answers; December 07, 2015. http://www.fda.gov/Drugs/DrugSafety/PostmarketDrugSafetyInformationforPatientsandProviders/ucm107840.htm.
    • (2015)
  • 21
    • 84983604572 scopus 로고    scopus 로고
    • Antiviral therapies on the horizon for influenza
    • Naesens, L.; Stevaert, A.; Vanderlinden, E. Antiviral therapies on the horizon for influenza Curr. Opin. Pharmacol. 2016, 30, 106-115 10.1016/j.coph.2016.08.003
    • (2016) Curr. Opin. Pharmacol. , vol.30 , pp. 106-115
    • Naesens, L.1    Stevaert, A.2    Vanderlinden, E.3
  • 22
    • 84991769513 scopus 로고    scopus 로고
    • The influenza virus polymerase complex: an update on its structure, functions, and significance for antiviral drug design
    • Stevaert, A.; Naesens, L. The influenza virus polymerase complex: an update on its structure, functions, and significance for antiviral drug design Med. Res. Rev. 2016, 36, 1127-1173 10.1002/med.21401
    • (2016) Med. Res. Rev. , vol.36 , pp. 1127-1173
    • Stevaert, A.1    Naesens, L.2
  • 23
    • 77956536783 scopus 로고    scopus 로고
    • Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms
    • Boivin, S.; Cusack, S.; Ruigrok, R. W.; Hart, D. J. Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms J. Biol. Chem. 2010, 285, 28411-28417 10.1074/jbc.R110.117531
    • (2010) J. Biol. Chem. , vol.285 , pp. 28411-28417
    • Boivin, S.1    Cusack, S.2    Ruigrok, R.W.3    Hart, D.J.4
  • 24
    • 84922257981 scopus 로고    scopus 로고
    • Structure of influenza A polymerase bound to the viral RNA promoter
    • Pflug, A.; Guilligay, D.; Reich, S.; Cusack, S. Structure of influenza A polymerase bound to the viral RNA promoter Nature 2014, 516, 355-360 10.1038/nature14008
    • (2014) Nature , vol.516 , pp. 355-360
    • Pflug, A.1    Guilligay, D.2    Reich, S.3    Cusack, S.4
  • 25
    • 67249130012 scopus 로고    scopus 로고
    • The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit
    • Dias, A.; Bouvier, D.; Crépin, T.; McCarthy, A. A.; Hart, D. J.; Baudin, F.; Cusack, S.; Ruigrok, R. W. The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit Nature 2009, 458, 914-918 10.1038/nature07745
    • (2009) Nature , vol.458 , pp. 914-918
    • Dias, A.1    Bouvier, D.2    Crépin, T.3    McCarthy, A.A.4    Hart, D.J.5    Baudin, F.6    Cusack, S.7    Ruigrok, R.W.8
  • 29
    • 84925326407 scopus 로고    scopus 로고
    • Learning from structure-based drug design and new antivirals targeting the ribonucleoprotein complex for the treatment of influenza
    • Monod, A.; Swale, C.; Tarus, B.; Tissot, A.; Delmas, B.; Ruigrok, R. W.; Crépin, T.; Slama-Schwok, A. Learning from structure-based drug design and new antivirals targeting the ribonucleoprotein complex for the treatment of influenza Expert Opin. Drug Discovery 2015, 10, 345-371 10.1517/17460441.2015.1019859
    • (2015) Expert Opin. Drug Discovery , vol.10 , pp. 345-371
    • Monod, A.1    Swale, C.2    Tarus, B.3    Tissot, A.4    Delmas, B.5    Ruigrok, R.W.6    Crépin, T.7    Slama-Schwok, A.8
  • 31
    • 84893487875 scopus 로고    scopus 로고
    • The N-terminal domain of PA from bat-derived influenza-like virus H17N10 has endonuclease activity
    • Tefsen, B.; Lu, G.; Zhu, Y.; Haywood, J.; Zhao, L.; Deng, T.; Qi, J.; Gao, G. F. The N-terminal domain of PA from bat-derived influenza-like virus H17N10 has endonuclease activity J. Virol. 2014, 88, 1935-1941 10.1128/JVI.03270-13
    • (2014) J. Virol. , vol.88 , pp. 1935-1941
    • Tefsen, B.1    Lu, G.2    Zhu, Y.3    Haywood, J.4    Zhao, L.5    Deng, T.6    Qi, J.7    Gao, G.F.8
  • 32
    • 84866146827 scopus 로고    scopus 로고
    • Structural and biochemical basis for development of influenza virus inhibitors targeting the PA endonuclease
    • DuBois, R. M.; Slavish, P. J.; Baughman, B. M.; Yun, M. K.; Bao, J.; Webby, R. J.; Webb, T. R.; White, S. W. Structural and biochemical basis for development of influenza virus inhibitors targeting the PA endonuclease PLoS Pathog. 2012, 8, e1002830 10.1371/journal.ppat.1002830
    • (2012) PLoS Pathog. , vol.8 , pp. e1002830
    • DuBois, R.M.1    Slavish, P.J.2    Baughman, B.M.3    Yun, M.K.4    Bao, J.5    Webby, R.J.6    Webb, T.R.7    White, S.W.8
  • 33
    • 69449096816 scopus 로고    scopus 로고
    • Nucleoside monophosphate complex structures of the endonuclease domain from the influenza virus polymerase PA subunit reveal the substrate binding site inside the catalytic center
    • Zhao, C.; Lou, Z.; Guo, Y.; Ma, M.; Chen, Y.; Liang, S.; Zhang, L.; Chen, S.; Li, X.; Liu, Y.; Bartlam, M.; Rao, Z. Nucleoside monophosphate complex structures of the endonuclease domain from the influenza virus polymerase PA subunit reveal the substrate binding site inside the catalytic center J. Virol. 2009, 83, 9024-9030 10.1128/JVI.00911-09
    • (2009) J. Virol. , vol.83 , pp. 9024-9030
    • Zhao, C.1    Lou, Z.2    Guo, Y.3    Ma, M.4    Chen, Y.5    Liang, S.6    Zhang, L.7    Chen, S.8    Li, X.9    Liu, Y.10    Bartlam, M.11    Rao, Z.12
  • 34
    • 84976254609 scopus 로고    scopus 로고
    • New insight into metal ion-driven catalysis of nucleic acids by influenza PA-Nter
    • Kotlarek, D.; Worch, R. New insight into metal ion-driven catalysis of nucleic acids by influenza PA-Nter PLoS One 2016, 11, e0156972 10.1371/journal.pone.0156972
    • (2016) PLoS One , vol.11 , pp. e0156972
    • Kotlarek, D.1    Worch, R.2
  • 35
    • 84866177810 scopus 로고    scopus 로고
    • Structural analysis of specific metal chelating inhibitor binding to the endonuclease domain of influenza pH1N1 (2009) polymerase
    • Kowalinski, E.; Zubieta, C.; Wolkerstorfer, A.; Szolar, O. H.; Ruigrok, R. W.; Cusack, S. Structural analysis of specific metal chelating inhibitor binding to the endonuclease domain of influenza pH1N1 (2009) polymerase PLoS Pathog. 2012, 8, e1002831 10.1371/journal.ppat.1002831
    • (2012) PLoS Pathog. , vol.8 , pp. e1002831
    • Kowalinski, E.1    Zubieta, C.2    Wolkerstorfer, A.3    Szolar, O.H.4    Ruigrok, R.W.5    Cusack, S.6
  • 36
    • 34249307213 scopus 로고    scopus 로고
    • Avian influenza A (H5N1) infection: targets and strategies for chemotherapeutic intervention
    • De Clercq, E.; Neyts, J. Avian influenza A (H5N1) infection: targets and strategies for chemotherapeutic intervention Trends Pharmacol. Sci. 2007, 28, 280-285 10.1016/j.tips.2007.04.005
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 280-285
    • De Clercq, E.1    Neyts, J.2
  • 37
    • 67849116495 scopus 로고    scopus 로고
    • Structure-function studies of the influenza virus RNA polymerase PA subunit
    • Liu, Y.; Lou, Z.; Bartlam, M.; Rao, Z. Structure-function studies of the influenza virus RNA polymerase PA subunit Sci. China, Ser. C: Life Sci. 2009, 52, 450-458 10.1007/s11427-009-0060-1
    • (2009) Sci. China, Ser. C: Life Sci. , vol.52 , pp. 450-458
    • Liu, Y.1    Lou, Z.2    Bartlam, M.3    Rao, Z.4
  • 40
    • 84903710585 scopus 로고    scopus 로고
    • "Old friends in new guise": exploiting privileged structures for scaffold re-evolution/refining
    • Song, Y.; Chen, W.; Kang, D.; Zhang, Q.; Zhan, P.; Liu, X. "Old friends in new guise": exploiting privileged structures for scaffold re-evolution/refining Comb. Chem. High Throughput Screening 2014, 17, 536-553 10.2174/1386207317666140122101631
    • (2014) Comb. Chem. High Throughput Screening , vol.17 , pp. 536-553
    • Song, Y.1    Chen, W.2    Kang, D.3    Zhang, Q.4    Zhan, P.5    Liu, X.6
  • 41
  • 42
    • 84878962146 scopus 로고    scopus 로고
    • Binding mode prediction and inhibitor design of anti-influenza virus diketo acids targeting metalloenzyme RNA polymerase by molecular docking
    • Ishikawa, Y.; Fujii, S. Binding mode prediction and inhibitor design of anti-influenza virus diketo acids targeting metalloenzyme RNA polymerase by molecular docking Bioinformation 2011, 6, 221-225 10.6026/97320630006221
    • (2011) Bioinformation , vol.6 , pp. 221-225
    • Ishikawa, Y.1    Fujii, S.2
  • 43
    • 84884683675 scopus 로고    scopus 로고
    • Mutational analysis of the binding pockets of the diketo acid inhibitor L-742,001 in the influenza virus PA endonuclease
    • Stevaert, A.; Dallocchio, R.; Dessì, A.; Pala, N.; Rogolino, D.; Sechi, M.; Naesens, L. Mutational analysis of the binding pockets of the diketo acid inhibitor L-742,001 in the influenza virus PA endonuclease J. Virol. 2013, 87, 10524-10538 10.1128/JVI.00832-13
    • (2013) J. Virol. , vol.87 , pp. 10524-10538
    • Stevaert, A.1    Dallocchio, R.2    Dessì, A.3    Pala, N.4    Rogolino, D.5    Sechi, M.6    Naesens, L.7
  • 44
    • 84969582328 scopus 로고    scopus 로고
    • Two distinctive binding modes of endonuclease inhibitors to the N-terminal region of influenza virus polymerase acidic subunit
    • Fudo, S.; Yamamoto, N.; Nukaga, M.; Odagiri, T.; Tashiro, M.; Hoshino, T. Two distinctive binding modes of endonuclease inhibitors to the N-terminal region of influenza virus polymerase acidic subunit Biochemistry 2016, 55, 2646-2660 10.1021/acs.biochem.5b01087
    • (2016) Biochemistry , vol.55 , pp. 2646-2660
    • Fudo, S.1    Yamamoto, N.2    Nukaga, M.3    Odagiri, T.4    Tashiro, M.5    Hoshino, T.6
  • 47
    • 0035838857 scopus 로고    scopus 로고
    • Synthesis of natural flutimide and analogous fully substituted pyrazine-2,6-diones, endonuclease inhibitors of influenza virus
    • Singh, S. B.; Tomassini, J. E. Synthesis of natural flutimide and analogous fully substituted pyrazine-2,6-diones, endonuclease inhibitors of influenza virus J. Org. Chem. 2001, 66, 5504-5516 10.1021/jo015665d
    • (2001) J. Org. Chem. , vol.66 , pp. 5504-5516
    • Singh, S.B.1    Tomassini, J.E.2
  • 51
    • 84907886581 scopus 로고    scopus 로고
    • Phenyl substituted 4-hydroxypyridazin-3(2H)-ones and 5-hydroxypyrimidin-4(3H)-ones: inhibitors of influenza A endonuclease
    • Sagong, H. Y.; Bauman, J. D.; Patel, D.; Das, K.; Arnold, E.; LaVoie, E. J. Phenyl substituted 4-hydroxypyridazin-3(2H)-ones and 5-hydroxypyrimidin-4(3H)-ones: inhibitors of influenza A endonuclease J. Med. Chem. 2014, 57, 8086-8098 10.1021/jm500958x
    • (2014) J. Med. Chem. , vol.57 , pp. 8086-8098
    • Sagong, H.Y.1    Bauman, J.D.2    Patel, D.3    Das, K.4    Arnold, E.5    LaVoie, E.J.6
  • 52
    • 84924040633 scopus 로고    scopus 로고
    • Advantages of crystallographic fragment screening: functional and mechanistic insights from a powerful platform for efficient drug discovery
    • Patel, D.; Bauman, J. D.; Arnold, E. Advantages of crystallographic fragment screening: functional and mechanistic insights from a powerful platform for efficient drug discovery Prog. Biophys. Mol. Biol. 2014, 116, 92-100 10.1016/j.pbiomolbio.2014.08.004
    • (2014) Prog. Biophys. Mol. Biol. , vol.116 , pp. 92-100
    • Patel, D.1    Bauman, J.D.2    Arnold, E.3
  • 53
    • 84858140219 scopus 로고    scopus 로고
    • Fragment screening using X-ray crystallography
    • Davies, T. G.; Tickle, I. J. Fragment screening using X-ray crystallography Top. Curr. Chem. 2011, 317, 33-59 10.1007/128_2011_179
    • (2011) Top. Curr. Chem. , vol.317 , pp. 33-59
    • Davies, T.G.1    Tickle, I.J.2
  • 54
    • 35348922285 scopus 로고    scopus 로고
    • Fragment-based screening using X-ray crystallography and NMR spectroscopy
    • Jhoti, H.; Cleasby, A.; Verdonk, M.; Williams, G. Fragment-based screening using X-ray crystallography and NMR spectroscopy Curr. Opin. Chem. Biol. 2007, 11, 485-493 10.1016/j.cbpa.2007.07.010
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 485-493
    • Jhoti, H.1    Cleasby, A.2    Verdonk, M.3    Williams, G.4
  • 57
    • 84948569632 scopus 로고    scopus 로고
    • Fragment-based approaches to anti-HIV drug discovery: state of the art and future opportunities
    • Huang, B.; Kang, D.; Zhan, P.; Liu, X. Fragment-based approaches to anti-HIV drug discovery: state of the art and future opportunities Expert Opin. Drug Discovery 2015, 10, 1271-1281 10.1517/17460441.2015.1083007
    • (2015) Expert Opin. Drug Discovery , vol.10 , pp. 1271-1281
    • Huang, B.1    Kang, D.2    Zhan, P.3    Liu, X.4
  • 58
    • 84978648980 scopus 로고    scopus 로고
    • Fragment-based identification of influenza endonuclease inhibitors
    • Credille, C. V.; Chen, Y.; Cohen, S. M. Fragment-based identification of influenza endonuclease inhibitors J. Med. Chem. 2016, 59, 6444-6454 10.1021/acs.jmedchem.6b00628
    • (2016) J. Med. Chem. , vol.59 , pp. 6444-6454
    • Credille, C.V.1    Chen, Y.2    Cohen, S.M.3
  • 62
    • 27644518720 scopus 로고    scopus 로고
    • Antiviral effect of catechins in green tea on influenza virus
    • Song, J. M.; Lee, K. H.; Seong, B. L. Antiviral effect of catechins in green tea on influenza virus Antiviral Res. 2005, 68, 66-74 10.1016/j.antiviral.2005.06.010
    • (2005) Antiviral Res. , vol.68 , pp. 66-74
    • Song, J.M.1    Lee, K.H.2    Seong, B.L.3
  • 63
    • 83755177949 scopus 로고    scopus 로고
    • Green tea catechins inhibit the endonuclease activity of influenza A virus RNA polymerase
    • Kuzuhara, T.; Iwai, Y.; Takahashi, H.; Hatakeyama, D.; Echigo, N. Green tea catechins inhibit the endonuclease activity of influenza A virus RNA polymerase PLoS Curr. 2009, 1, RRN1052 10.1371/currents.RRN1052
    • (2009) PLoS Curr. , vol.1 , pp. RRN1052
    • Kuzuhara, T.1    Iwai, Y.2    Takahashi, H.3    Hatakeyama, D.4    Echigo, N.5
  • 64
    • 47149112921 scopus 로고    scopus 로고
    • Enhanced anti-influenza A virus activity of (−)-epigallocatechin-3-O-gallate fatty acid monoester derivatives: effect of alkyl chain length
    • Mori, S.; Miyake, S.; Kobe, T.; Nakaya, T.; Fuller, S. D.; Kato, N.; Kaihatsu, K. Enhanced anti-influenza A virus activity of (−)-epigallocatechin-3-O-gallate fatty acid monoester derivatives: effect of alkyl chain length Bioorg. Med. Chem. Lett. 2008, 18, 4249-4252 10.1016/j.bmcl.2008.02.020
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 4249-4252
    • Mori, S.1    Miyake, S.2    Kobe, T.3    Nakaya, T.4    Fuller, S.D.5    Kato, N.6    Kaihatsu, K.7
  • 65
  • 67
    • 84946489954 scopus 로고    scopus 로고
    • Structural and computational study on inhibitory compounds for endonuclease activity of influenza virus polymerase
    • Fudo, S.; Yamamoto, N.; Nukaga, M.; Odagiri, T.; Tashiro, M.; Neya, S.; Hoshino, T. Structural and computational study on inhibitory compounds for endonuclease activity of influenza virus polymerase Bioorg. Med. Chem. 2015, 23, 5466-5475 10.1016/j.bmc.2015.07.046
    • (2015) Bioorg. Med. Chem. , vol.23 , pp. 5466-5475
    • Fudo, S.1    Yamamoto, N.2    Nukaga, M.3    Odagiri, T.4    Tashiro, M.5    Neya, S.6    Hoshino, T.7
  • 69
    • 11844255399 scopus 로고    scopus 로고
    • Bioisosterism: a useful strategy for molecular modification and drug design
    • Lima, L. M.; Barreiro, E. J. Bioisosterism: a useful strategy for molecular modification and drug design Curr. Med. Chem. 2005, 12, 23-49 10.2174/0929867053363540
    • (2005) Curr. Med. Chem. , vol.12 , pp. 23-49
    • Lima, L.M.1    Barreiro, E.J.2
  • 70
    • 0033608967 scopus 로고    scopus 로고
    • Metal ion catalysis of RNA cleavage by the influenza virus endonuclease
    • Doan, L.; Handa, B.; Roberts, N. A.; Klumpp, K. Metal ion catalysis of RNA cleavage by the influenza virus endonuclease Biochemistry 1999, 38, 5612-5619 10.1021/bi9828932
    • (1999) Biochemistry , vol.38 , pp. 5612-5619
    • Doan, L.1    Handa, B.2    Roberts, N.A.3    Klumpp, K.4
  • 74
    • 84960487693 scopus 로고    scopus 로고
    • A novel small-molecule inhibitor of influenza A virus acts by suppressing PA endonuclease activity of the viral polymerase
    • Yuan, S.; Chu, H.; Singh, K.; Zhao, H.; Zhang, K.; Kao, R. Y.; Chow, B.; Zhou, J.; Zheng, B. J. A novel small-molecule inhibitor of influenza A virus acts by suppressing PA endonuclease activity of the viral polymerase Sci. Rep. 2016, 6, 22880 10.1038/srep22880
    • (2016) Sci. Rep. , vol.6 , pp. 22880
    • Yuan, S.1    Chu, H.2    Singh, K.3    Zhao, H.4    Zhang, K.5    Kao, R.Y.6    Chow, B.7    Zhou, J.8    Zheng, B.J.9
  • 75
    • 84903780807 scopus 로고    scopus 로고
    • "Old dogs with new tricks": exploiting alternative mechanisms of action and new drug design strategies for clinically validated HIV targets
    • Kang, D.; Song, Y.; Chen, W.; Zhan, P.; Liu, X. "Old dogs with new tricks": exploiting alternative mechanisms of action and new drug design strategies for clinically validated HIV targets Mol. BioSyst. 2014, 10, 1998-2022 10.1039/C4MB00147H
    • (2014) Mol. BioSyst. , vol.10 , pp. 1998-2022
    • Kang, D.1    Song, Y.2    Chen, W.3    Zhan, P.4    Liu, X.5
  • 76
    • 85018891651 scopus 로고    scopus 로고
    • 1st Half of Fiscal 2015. Financial Results; October 30
    • 1st Half of Fiscal 2015. Financial Results; October 30, 2015. http://www.shionogi.co.jp/en/ir/pdf/e_p151030.pdf.
    • (2015)
  • 77
    • 85018910890 scopus 로고    scopus 로고
    • ClinicalTrials.gov processed this record on January 19
    • https://clinicaltrials.gov/ct2/show/NCT02588521. ClinicalTrials.gov processed this record on January 19, 2017.
    • (2017)
  • 78
    • 78751661570 scopus 로고    scopus 로고
    • Identifying chelators for metalloprotein inhibitors using a fragment-based approach
    • Jacobsen, J. A.; Fullagar, J. L.; Miller, M. T.; Cohen, S. M. Identifying chelators for metalloprotein inhibitors using a fragment-based approach J. Med. Chem. 2011, 54, 591-602 10.1021/jm101266s
    • (2011) J. Med. Chem. , vol.54 , pp. 591-602
    • Jacobsen, J.A.1    Fullagar, J.L.2    Miller, M.T.3    Cohen, S.M.4
  • 79
    • 84960203206 scopus 로고    scopus 로고
    • Discovery of bioactive molecules from CuAAC click-chemistry-based combinatorial libraries
    • Wang, X.; Huang, B.; Liu, X.; Zhan, P. Discovery of bioactive molecules from CuAAC click-chemistry-based combinatorial libraries Drug Discovery Today 2016, 21, 118-132 10.1016/j.drudis.2015.08.004
    • (2016) Drug Discovery Today , vol.21 , pp. 118-132
    • Wang, X.1    Huang, B.2    Liu, X.3    Zhan, P.4
  • 80
    • 84898913565 scopus 로고    scopus 로고
    • DNA-encoded chemical libraries: advancing beyond conventional small-molecule libraries
    • Franzini, R. M.; Neri, D.; Scheuermann, J. DNA-encoded chemical libraries: advancing beyond conventional small-molecule libraries Acc. Chem. Res. 2014, 47, 1247-1255 10.1021/ar400284t
    • (2014) Acc. Chem. Res. , vol.47 , pp. 1247-1255
    • Franzini, R.M.1    Neri, D.2    Scheuermann, J.3
  • 81
    • 85018478467 scopus 로고    scopus 로고
    • Journal of medicinal chemistry, Technological advances: highlights 2015-2016
    • Djuric, S. W.; Meanwell, N. A. Journal of medicinal chemistry, Technological advances: highlights 2015-2016 J. Med. Chem. 2017, 60, 1-3 10.1021/acs.jmedchem.6b01600
    • (2017) J. Med. Chem. , vol.60 , pp. 1-3
    • Djuric, S.W.1    Meanwell, N.A.2
  • 82
    • 84922211861 scopus 로고    scopus 로고
    • Beware of docking!
    • Chen, Y. C. Beware of docking! Trends Pharmacol. Sci. 2015, 36, 78-95 10.1016/j.tips.2014.12.001
    • (2015) Trends Pharmacol. Sci. , vol.36 , pp. 78-95
    • Chen, Y.C.1
  • 83
    • 84906874907 scopus 로고    scopus 로고
    • Exploring the influence of the protein environment on metal-binding pharmacophores
    • Martin, D. P.; Blachly, P. G.; McCammon, J. A.; Cohen, S. M. Exploring the influence of the protein environment on metal-binding pharmacophores J. Med. Chem. 2014, 57, 7126-7135 10.1021/jm500984b
    • (2014) J. Med. Chem. , vol.57 , pp. 7126-7135
    • Martin, D.P.1    Blachly, P.G.2    McCammon, J.A.3    Cohen, S.M.4
  • 84
    • 84893407575 scopus 로고    scopus 로고
    • Docking ligands into flexible and solvated macromolecules. 6. Development and application to the docking of HDACs and other zinc metalloenzymes inhibitors
    • Pottel, J.; Therrien, E.; Gleason, J. L.; Moitessier, N. Docking ligands into flexible and solvated macromolecules. 6. Development and application to the docking of HDACs and other zinc metalloenzymes inhibitors J. Chem. Inf. Model. 2014, 54, 254-265 10.1021/ci400550m
    • (2014) J. Chem. Inf. Model. , vol.54 , pp. 254-265
    • Pottel, J.1    Therrien, E.2    Gleason, J.L.3    Moitessier, N.4
  • 85
    • 24944529911 scopus 로고    scopus 로고
    • Virtual screening against metalloenzymes for inhibitors and substrates
    • Irwin, J. J.; Raushel, F. M.; Shoichet, B. K. Virtual screening against metalloenzymes for inhibitors and substrates Biochemistry 2005, 44, 12316-12328 10.1021/bi050801k
    • (2005) Biochemistry , vol.44 , pp. 12316-12328
    • Irwin, J.J.1    Raushel, F.M.2    Shoichet, B.K.3
  • 87
    • 84981249200 scopus 로고    scopus 로고
    • Identification of a novel complex between the nucleoprotein and PA(1-27) of influenza A virus polymerase
    • Vidic, J.; Noiray, M.; Bagchi, A.; Slama-Schwok, A. Identification of a novel complex between the nucleoprotein and PA(1-27) of influenza A virus polymerase Biochemistry 2016, 55, 4259-4262 10.1021/acs.biochem.6b00514
    • (2016) Biochemistry , vol.55 , pp. 4259-4262
    • Vidic, J.1    Noiray, M.2    Bagchi, A.3    Slama-Schwok, A.4
  • 88
    • 77649220192 scopus 로고    scopus 로고
    • Current trends in ligand-based virtual screening: Molecular representations, data mining methods, new application areas, and performance evaluation
    • Geppert, H.; Vogt, M.; Bajorath, J. Current trends in ligand-based virtual screening: Molecular representations, data mining methods, new application areas, and performance evaluation J. Chem. Inf. Model. 2010, 50, 205-216 10.1021/ci900419k
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 205-216
    • Geppert, H.1    Vogt, M.2    Bajorath, J.3
  • 89
    • 12144254795 scopus 로고    scopus 로고
    • Beta-diketo acid pharmacophore hypothesis. 1. Discovery of a novel class of HIV-1 integrase inhibitors
    • Dayam, R.; Sanchez, T.; Clement, O.; Shoemaker, R.; Sei, S.; Neamati, N. Beta-diketo acid pharmacophore hypothesis. 1. Discovery of a novel class of HIV-1 integrase inhibitors J. Med. Chem. 2005, 48, 111-120 10.1021/jm0496077
    • (2005) J. Med. Chem. , vol.48 , pp. 111-120
    • Dayam, R.1    Sanchez, T.2    Clement, O.3    Shoemaker, R.4    Sei, S.5    Neamati, N.6
  • 90
    • 29144509688 scopus 로고    scopus 로고
    • Diketo acid pharmacophore. 2. Discovery of structurally diverse inhibitors of HIV-1 integrase
    • Dayam, R.; Sanchez, T.; Neamati, N. Diketo acid pharmacophore. 2. Discovery of structurally diverse inhibitors of HIV-1 integrase J. Med. Chem. 2005, 48, 8009-8015 10.1021/jm050837a
    • (2005) J. Med. Chem. , vol.48 , pp. 8009-8015
    • Dayam, R.1    Sanchez, T.2    Neamati, N.3
  • 93
    • 79961170232 scopus 로고    scopus 로고
    • Design of HIV-1 integrase inhibitors targeting the catalytic domain as well as its interaction with LEDGF/p75: A scaffold hopping approach using salicylate and catechol groups
    • Fan, X.; Zhang, F. H.; Al-Safi, R. I.; Zeng, L. F.; Shabaik, Y.; Debnath, B.; Sanchez, T. W.; Odde, S.; Neamati, N.; Long, Y. Q. Design of HIV-1 integrase inhibitors targeting the catalytic domain as well as its interaction with LEDGF/p75: A scaffold hopping approach using salicylate and catechol groups Bioorg. Med. Chem. 2011, 19, 4935-4952 10.1016/j.bmc.2011.06.058
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 4935-4952
    • Fan, X.1    Zhang, F.H.2    Al-Safi, R.I.3    Zeng, L.F.4    Shabaik, Y.5    Debnath, B.6    Sanchez, T.W.7    Odde, S.8    Neamati, N.9    Long, Y.Q.10
  • 95
    • 78149353044 scopus 로고    scopus 로고
    • Bunyaviridae RNA polymerases (L-protein) have an N-terminal, influenza-like endonuclease domain, essential for viral cap-dependent transcription
    • Reguera, J.; Weber, F.; Cusack, S. Bunyaviridae RNA polymerases (L-protein) have an N-terminal, influenza-like endonuclease domain, essential for viral cap-dependent transcription PLoS Pathog. 2010, 6, e1001101 10.1371/journal.ppat.1001101
    • (2010) PLoS Pathog. , vol.6 , pp. e1001101
    • Reguera, J.1    Weber, F.2    Cusack, S.3
  • 97
    • 84938517033 scopus 로고    scopus 로고
    • Repurposing of HDAC inhibitors toward anti-hepatitis C virus drug discovery: teaching an old dog new tricks
    • Zhao, F.; Liu, N.; Zhan, P.; Liu, X. Repurposing of HDAC inhibitors toward anti-hepatitis C virus drug discovery: teaching an old dog new tricks Future Med. Chem. 2015, 7, 1367-1371 10.4155/fmc.15.76
    • (2015) Future Med. Chem. , vol.7 , pp. 1367-1371
    • Zhao, F.1    Liu, N.2    Zhan, P.3    Liu, X.4
  • 98
    • 84902185122 scopus 로고    scopus 로고
    • Discovery and characterization of novel imidazopyridine derivative CHEQ-2 as a potent CDC25 inhibitor and promising anticancer drug candidate
    • Song, Y.; Lin, X.; Kang, D.; Li, X.; Zhan, P.; Liu, X.; Zhang, Q. Discovery and characterization of novel imidazopyridine derivative CHEQ-2 as a potent CDC25 inhibitor and promising anticancer drug candidate Eur. J. Med. Chem. 2014, 82, 293-307 10.1016/j.ejmech.2014.05.063
    • (2014) Eur. J. Med. Chem. , vol.82 , pp. 293-307
    • Song, Y.1    Lin, X.2    Kang, D.3    Li, X.4    Zhan, P.5    Liu, X.6    Zhang, Q.7
  • 99
    • 84971671274 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluations of hydroxypyridonecarboxylic acids as inhibitors of HIV reverse transcriptase associated RNase H
    • Kankanala, J.; Kirby, K. A.; Liu, F.; Miller, L.; Nagy, E.; Wilson, D. J.; Parniak, M. A.; Sarafianos, S. G.; Wang, Z. Design, synthesis, and biological evaluations of hydroxypyridonecarboxylic acids as inhibitors of HIV reverse transcriptase associated RNase H J. Med. Chem. 2016, 59, 5051-5062 10.1021/acs.jmedchem.6b00465
    • (2016) J. Med. Chem. , vol.59 , pp. 5051-5062
    • Kankanala, J.1    Kirby, K.A.2    Liu, F.3    Miller, L.4    Nagy, E.5    Wilson, D.J.6    Parniak, M.A.7    Sarafianos, S.G.8    Wang, Z.9
  • 100
    • 84921450614 scopus 로고    scopus 로고
    • Design, synthesis, biochemical, and antiviral evaluations of C6 benzyl and C6 biarylmethyl substituted 2-hydroxylisoquinoline-1,3-diones: dual inhibition against HIV reverse transcriptase-associated RNase H and polymerase with antiviral activities
    • Vernekar, S. K.; Liu, Z.; Nagy, E.; Miller, L.; Kirby, K. A.; Wilson, D. J.; Kankanala, J.; Sarafianos, S. G.; Parniak, M. A.; Wang, Z. Design, synthesis, biochemical, and antiviral evaluations of C6 benzyl and C6 biarylmethyl substituted 2-hydroxylisoquinoline-1,3-diones: dual inhibition against HIV reverse transcriptase-associated RNase H and polymerase with antiviral activities J. Med. Chem. 2015, 58, 651-664 10.1021/jm501132s
    • (2015) J. Med. Chem. , vol.58 , pp. 651-664
    • Vernekar, S.K.1    Liu, Z.2    Nagy, E.3    Miller, L.4    Kirby, K.A.5    Wilson, D.J.6    Kankanala, J.7    Sarafianos, S.G.8    Parniak, M.A.9    Wang, Z.10
  • 101
    • 84962144439 scopus 로고    scopus 로고
    • 3-Hydroxypyrimidine-2,4-diones as selective active site inhibitors of HIV reverse transcriptase-associated RNase H: Design, synthesis, and biochemical evaluations
    • Tang, J.; Liu, F.; Nagy, E.; Miller, L.; Kirby, K. A.; Wilson, D. J.; Wu, B.; Sarafianos, S. G.; Parniak, M. A.; Wang, Z. 3-Hydroxypyrimidine-2,4-diones as selective active site inhibitors of HIV reverse transcriptase-associated RNase H: Design, synthesis, and biochemical evaluations J. Med. Chem. 2016, 59, 2648-2659 10.1021/acs.jmedchem.5b01879
    • (2016) J. Med. Chem. , vol.59 , pp. 2648-2659
    • Tang, J.1    Liu, F.2    Nagy, E.3    Miller, L.4    Kirby, K.A.5    Wilson, D.J.6    Wu, B.7    Sarafianos, S.G.8    Parniak, M.A.9    Wang, Z.10
  • 103
    • 84887128203 scopus 로고    scopus 로고
    • Metalloprotein-inhibitor binding: human carbonic anhydrase II as a model for probing metal-ligand interactions in a metalloprotein active site
    • Martin, D. P.; Hann, Z. S.; Cohen, S. M. Metalloprotein-inhibitor binding: human carbonic anhydrase II as a model for probing metal-ligand interactions in a metalloprotein active site Inorg. Chem. 2013, 52, 12207-12215 10.1021/ic400295f
    • (2013) Inorg. Chem. , vol.52 , pp. 12207-12215
    • Martin, D.P.1    Hann, Z.S.2    Cohen, S.M.3
  • 104
    • 84943779677 scopus 로고    scopus 로고
    • Strategies for the discovery of target-specific or isoform-selective modulators
    • Zhan, P.; Itoh, Y.; Suzuki, T.; Liu, X. Strategies for the discovery of target-specific or isoform-selective modulators J. Med. Chem. 2015, 58, 7611-7633 10.1021/acs.jmedchem.5b00229
    • (2015) J. Med. Chem. , vol.58 , pp. 7611-7633
    • Zhan, P.1    Itoh, Y.2    Suzuki, T.3    Liu, X.4
  • 105
    • 84920380487 scopus 로고    scopus 로고
    • 8-Hydroxyquinoline: a privileged structure with a broad-ranging pharmacological potential
    • Song, Y.; Xu, H.; Chen, W.; Zhan, P.; Liu, X. 8-Hydroxyquinoline: a privileged structure with a broad-ranging pharmacological potential MedChemComm 2015, 6, 61-74 10.1039/C4MD00284A
    • (2015) MedChemComm , vol.6 , pp. 61-74
    • Song, Y.1    Xu, H.2    Chen, W.3    Zhan, P.4    Liu, X.5
  • 106
    • 70450184400 scopus 로고    scopus 로고
    • Design strategies of novel NNRTIs to overcome drug resistance
    • Zhan, P.; Liu, X.; Li, Z.; Pannecouque, C.; De Clercq, E. Design strategies of novel NNRTIs to overcome drug resistance Curr. Med. Chem. 2009, 16, 3903-3917 10.2174/092986709789178019
    • (2009) Curr. Med. Chem. , vol.16 , pp. 3903-3917
    • Zhan, P.1    Liu, X.2    Li, Z.3    Pannecouque, C.4    De Clercq, E.5
  • 107
    • 84907677397 scopus 로고    scopus 로고
    • Recent advances in the structure-based rational design of TNKSIs
    • Zhan, P.; Song, Y.; Itoh, Y.; Suzuki, T.; Liu, X. Recent advances in the structure-based rational design of TNKSIs Mol. BioSyst. 2014, 10, 2783-2799 10.1039/C4MB00385C
    • (2014) Mol. BioSyst. , vol.10 , pp. 2783-2799
    • Zhan, P.1    Song, Y.2    Itoh, Y.3    Suzuki, T.4    Liu, X.5
  • 108
    • 35748934487 scopus 로고    scopus 로고
    • The influence of drug-like concepts on decision-making in medicinal chemistry
    • Leeson, P. D.; Springthorpe, B. The influence of drug-like concepts on decision-making in medicinal chemistry Nat. Rev. Drug Discovery 2007, 6, 881-890 10.1038/nrd2445
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 881-890
    • Leeson, P.D.1    Springthorpe, B.2
  • 109
    • 84911948004 scopus 로고    scopus 로고
    • Novel HIV-1 non-nucleoside reverse transcriptase inhibitors: a patent review (2011-2014)
    • Li, X.; Zhang, L.; Tian, Y.; Song, Y.; Zhan, P.; Liu, X. Novel HIV-1 non-nucleoside reverse transcriptase inhibitors: a patent review (2011-2014) Expert Opin. Ther. Pat. 2014, 24, 1199-1227 10.1517/13543776.2014.964685
    • (2014) Expert Opin. Ther. Pat. , vol.24 , pp. 1199-1227
    • Li, X.1    Zhang, L.2    Tian, Y.3    Song, Y.4    Zhan, P.5    Liu, X.6


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