메뉴 건너뛰기




Volumn , Issue , 2013, Pages 143-172

Ribonuclease H inhibitors: Structural and molecular biology

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84902502321     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4614-7291-9_7     Document Type: Chapter
Times cited : (3)

References (86)
  • 2
    • 0037059743 scopus 로고    scopus 로고
    • Mutational analysis of Tyr-501 of HIV-1 reverse transcriptase. Effects on ribonuclease H activity and inhibition of this activity by N-acylhydrazones
    • Arion D, Sluis-Cremer N, Min KL, Abram ME, Fletcher RS, Parniak MA (2002) Mutational analysis of Tyr-501 of HIV-1 reverse transcriptase. Effects on ribonuclease H activity and inhibition of this activity by N-acylhydrazones. J Biol Chem 277(2):1370-1374
    • (2002) J Biol Chem , vol.277 , Issue.2 , pp. 1370-1374
    • Arion, D.1    Sluis-Cremer, N.2    Min, K.L.3    Abram, M.E.4    Fletcher, R.S.5    Parniak, M.A.6
  • 3
    • 84866325636 scopus 로고    scopus 로고
    • Antiviral drug resistance and the need for development of new HIV-1 reverse transcriptase inhibitors
    • Asahchop EL, Wainberg MA, Sloan RD, Tremblay CL (2012) Antiviral drug resistance and the need for development of new HIV-1 reverse transcriptase inhibitors. Antimicrob Agents Chemother. doi: 10.1128/AAC.00591-12
    • (2012) Antimicrob Agents Chemother
    • Asahchop, E.L.1    Wainberg, M.A.2    Sloan, R.D.3    Tremblay, C.L.4
  • 4
    • 64649098298 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase can simultaneously engage its DNA/RNA substrate at both DNA polymerase and RNase H active sites: Implications for RNase H inhibition
    • Beilhartz GL, Wendeler M, Baichoo N, Rausch J, Le Grice S, Gotte M (2009) HIV-1 reverse transcriptase can simultaneously engage its DNA/RNA substrate at both DNA polymerase and RNase H active sites: implications for RNase H inhibition. J Mol Biol 388(3):462-474
    • (2009) J Mol Biol , vol.388 , Issue.3 , pp. 462-474
    • Beilhartz, G.L.1    Wendeler, M.2    Baichoo, N.3    Rausch, J.4    Le Grice, S.5    Gotte, M.6
  • 5
    • 0031000566 scopus 로고    scopus 로고
    • Inhibition of the ribonuclease H and DNA polymerase activities of HIV-1 reverse transcriptase by N-(4-tert-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone
    • Borkow G, Fletcher RS, Barnard J, Arion D, Motakis D, Dmitrienko GI, Parniak MA (1997) Inhibition of the ribonuclease H and DNA polymerase activities of HIV-1 reverse transcriptase by N-(4-tert-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone. Biochemistry 36(11): 3179-3185
    • (1997) Biochemistry , vol.36 , Issue.11 , pp. 3179-3185
    • Borkow, G.1    Fletcher, R.S.2    Barnard, J.3    Arion, D.4    Motakis, D.5    Dmitrienko, G.I.6    Parniak, M.A.7
  • 6
    • 20044387576 scopus 로고    scopus 로고
    • Selective inhibition of HIV-1 reverse transcriptase-associated ribonuclease H activity by hydroxylated tropolones
    • Budihas SR, Gorshkova I, Gaidamakov S, Wamiru A, Bona MK, Parniak MA et al (2005) Selective inhibition of HIV-1 reverse transcriptase-associated ribonuclease H activity by hydroxylated tropolones. Nucleic Acids Res 33(4):1249-1256
    • (2005) Nucleic Acids Res , vol.33 , Issue.4 , pp. 1249-1256
    • Budihas, S.R.1    Gorshkova, I.2    Gaidamakov, S.3    Wamiru, A.4    Bona, M.K.5    Parniak, M.A.6
  • 7
    • 61349157313 scopus 로고    scopus 로고
    • Ribonuclease H: Properties, substrate specificity and roles in retroviral reverse transcription
    • Champoux JJ, Schultz SJ (2009) Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription. FEBS J 276(6):1506-1516. doi: 10.1111/j.1742-4658.2009.06909.x
    • (2009) FEBS J , vol.276 , Issue.6 , pp. 1506-1516
    • Champoux, J.J.1    Schultz, S.J.2
  • 8
    • 77956131587 scopus 로고    scopus 로고
    • Structure-activity analysis of vinylogous urea inhibitors of human immunodeficiency virus-encoded ribonuclease H
    • Chung S, Wendeler M, Rausch JW, Beilhartz G, Gotte M, O'Keefe BR et al (2010) Structure-activity analysis of vinylogous urea inhibitors of human immunodeficiency virus-encoded ribonuclease H. Antimicrob Agents Chemother 54(9):3913-3921. doi: 10.1128/AAC.00434-10
    • (2010) Antimicrob Agents Chemother , vol.54 , Issue.9 , pp. 3913-3921
    • Chung, S.1    Wendeler, M.2    Rausch, J.W.3    Beilhartz, G.4    Gotte, M.5    O'Keefe, B.R.6
  • 9
    • 79960189034 scopus 로고    scopus 로고
    • Synthesis, activity, and structural analysis of novel alpha-hydroxytropolone inhibitors of human immunodeficiency virus reverse transcriptase-associated ribonuclease H
    • Chung S, Himmel DM, Jiang JK, Wojtak K, Bauman JD, Rausch JW et al (2011) Synthesis, activity, and structural analysis of novel alpha-hydroxytropolone inhibitors of human immunodeficiency virus reverse transcriptase-associated ribonuclease H. J Med Chem 54(13):4462-4473. doi: 10.1021/jm2000757
    • (2011) J Med Chem , vol.54 , Issue.13 , pp. 4462-4473
    • Chung, S.1    Himmel, D.M.2    Jiang, J.K.3    Wojtak, K.4    Bauman, J.D.5    Rausch, J.W.6
  • 10
    • 84863025474 scopus 로고    scopus 로고
    • Mutagenesis of human immunodeficiency virus reverse transcriptase p51 subunit defines residues contributing to vinylogous urea inhibition of ribonuclease H activity
    • Chung S, Miller JT, Johnson BC, Hughes SH, Le Grice SF (2012) Mutagenesis of human immunodeficiency virus reverse transcriptase p51 subunit defines residues contributing to vinylogous urea inhibition of ribonuclease H activity. J Biol Chem 287(6):4066-4075. doi: 10.1074/jbc.M111.314781
    • (2012) J Biol Chem , vol.287 , Issue.6 , pp. 4066-4075
    • Chung, S.1    Miller, J.T.2    Johnson, B.C.3    Hughes, S.H.4    Le Grice, S.F.5
  • 11
    • 0027244668 scopus 로고
    • Fluorimetric analysis of recombinant p15 HIV-1 ribonuclease H
    • Cirino NM, Kalayjian RC, Jentoft JE, Le Grice SF (1993) Fluorimetric analysis of recombinant p15 HIV-1 ribonuclease H. J Biol Chem 268(20):14743-14749
    • (1993) J Biol Chem , vol.268 , Issue.20 , pp. 14743-14749
    • Cirino, N.M.1    Kalayjian, R.C.2    Jentoft, J.E.3    Le Grice, S.F.4
  • 12
    • 0034002794 scopus 로고    scopus 로고
    • Metal-ion stoichiometry of the HIV-1 RT ribonuclease H domain: Evidence for two mutually exclusive sites leads to new mechanistic insights on metal-mediated hydrolysis in nucleic acid biochemistry
    • Cowan JA, Ohyama T, Howard K, Rausch JW, Cowan SM, Le Grice SF (2000) Metal-ion stoichiometry of the HIV-1 RT ribonuclease H domain: evidence for two mutually exclusive sites leads to new mechanistic insights on metal-mediated hydrolysis in nucleic acid biochemistry. J Biol Inorg Chem JBIC A Publ Soc Biol Inorg Chem 5(1):67-74
    • (2000) J Biol Inorg Chem JBIC A Publ Soc Biol Inorg Chem , vol.5 , Issue.1 , pp. 67-74
    • Cowan, J.A.1    Ohyama, T.2    Howard, K.3    Rausch, J.W.4    Cowan, S.M.5    Le Grice, S.F.6
  • 13
    • 85081861640 scopus 로고    scopus 로고
    • Curran DP, Parniak MA, Gabarda A (2004) USA Patent no. US 2004/0058948 A1. United States Patent Application Publication: U. S. P. Office
    • Curran DP, Parniak MA, Gabarda A (2004) USA Patent no. US 2004/0058948 A1. United States Patent Application Publication: U. S. P. Office
  • 14
    • 2342566918 scopus 로고    scopus 로고
    • The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus
    • Das D, Georgiadis MM (2004) The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus. Structure 12(5):819-829. doi: 10.1016/j.str.2004.02.032
    • (2004) Structure , vol.12 , Issue.5 , pp. 819-829
    • Das, D.1    Georgiadis, M.M.2
  • 15
    • 40349091258 scopus 로고    scopus 로고
    • High-resolution structures of HIV-1 reverse transcriptase/TMC278 complexes: Strategic flexibility explains potency against resistance mutations
    • Das K, Bauman JD, Clark AD Jr, Frenkel YV, Lewi PJ, Shatkin AJ et al (2008) High-resolution structures of HIV-1 reverse transcriptase/TMC278 complexes: strategic flexibility explains potency against resistance mutations. Proc Natl Acad Sci USA 105(5):1466-1471. doi: 10.1073/pnas.0711209105
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.5 , pp. 1466-1471
    • Das, K.1    Bauman, J.D.2    Clark, A.D.3    Frenkel, Y.V.4    Lewi, P.J.5    Shatkin, A.J.6
  • 16
    • 84856711380 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase complex with DNA and nevirapine reveals non-nucleoside inhibition mechanism
    • Das K, Martinez SE, Bauman JD, Arnold E (2012) HIV-1 reverse transcriptase complex with DNA and nevirapine reveals non-nucleoside inhibition mechanism. Nat Struct Mol Biol 19(2):253-259. doi: 10.1038/nsmb.2223
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.2 , pp. 253-259
    • Das, K.1    Martinez, S.E.2    Bauman, J.D.3    Arnold, E.4
  • 17
    • 0025908083 scopus 로고
    • Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
    • Davies JF 2nd, Hostomska Z, Hostomsky Z, Jordan SR, Matthews DA (1991) Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase. Science 252(5002):88-95
    • (1991) Science , vol.252 , Issue.5002 , pp. 88-95
    • Davies, J.F.1    Hostomska, Z.2    Hostomsky, Z.3    Jordan, S.R.4    Matthews, D.A.5
  • 18
    • 80052957480 scopus 로고    scopus 로고
    • The effects of RNase H inhibitors and nevirapine on the susceptibility of HIV-1 to AZT and 3TC
    • Davis CA, Parniak MA, Hughes SH (2011) The effects of RNase H inhibitors and nevirapine on the susceptibility of HIV-1 to AZT and 3TC. Virology 419(2):64-71. doi: 10.1016/j.virol.2011.08.010
    • (2011) Virology , vol.419 , Issue.2 , pp. 64-71
    • Davis, C.A.1    Parniak, M.A.2    Hughes, S.H.3
  • 19
    • 61449189645 scopus 로고    scopus 로고
    • Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV
    • De Clercq E (2009) Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV. Int J Antimicrob Agents 33(4):307-320. doi: 10.1016/j.ijantimicag.2008.10.010
    • (2009) Int J Antimicrob Agents , vol.33 , Issue.4 , pp. 307-320
    • De Clercq, E.1
  • 20
    • 34250811908 scopus 로고    scopus 로고
    • Mutations in human immunodeficiency virus type 1 RNase H primer grip enhance 3′-azido-3′-deoxythymidine resistance
    • Delviks-Frankenberry KA, Nikolenko GN, Barr R, Pathak VK (2007) Mutations in human immunodeficiency virus type 1 RNase H primer grip enhance 3′-azido-3′-deoxythymidine resistance. J Virol 81(13):6837-6845
    • (2007) J Virol , vol.81 , Issue.13 , pp. 6837-6845
    • Delviks-Frankenberry, K.A.1    Nikolenko, G.N.2    Barr, R.3    Pathak, V.K.4
  • 22
    • 79952178100 scopus 로고    scopus 로고
    • The "connection" between HIV drug resistance and RNase H
    • Delviks-Frankenberry KA, Nikolenko GN, Pathak VK (2010) The "connection" between HIV drug resistance and RNase H. Viruses 2(7):1476-1503. doi: 10.3390/v2071476
    • (2010) Viruses , vol.2 , Issue.7 , pp. 1476-1503
    • Delviks-Frankenberry, K.A.1    Nikolenko, G.N.2    Pathak, V.K.3
  • 23
    • 0027328663 scopus 로고
    • Parameters that influence the binding of human immunodeficiency virus reverse transcriptase to nucleic acid structures
    • DeStefano JJ, Bambara RA, Fay PJ (1993) Parameters that influence the binding of human immunodeficiency virus reverse transcriptase to nucleic acid structures. Biochemistry 32(27): 6908-6915
    • (1993) Biochemistry , vol.32 , Issue.27 , pp. 6908-6915
    • Destefano, J.J.1    Bambara, R.A.2    Fay, P.J.3
  • 25
    • 0022498061 scopus 로고
    • Characterization of highly immunogenic p66/p51 as the reverse transcriptase of HTLV-III/LAV
    • (Washington, DC 1883)
    • Di Marzo Veronese F, Copeland TD, DeVico AL, Rahman R, Oroszlan S, Gallo RC, Sarngadharan MG (1986) Characterization of highly immunogenic p66/p51 as the reverse transcriptase of HTLV-III/LAV. Science (Washington, DC 1883-) 231(4743):1289-1291
    • (1986) Science , vol.231 , Issue.4743 , pp. 1289-1291
    • Di Marzo-Veronese, F.1    Copeland, T.D.2    Devico, A.L.3    Rahman, R.4    Oroszlan, S.5    Gallo, R.C.6    Sarngadharan, M.G.7
  • 26
    • 52049107430 scopus 로고    scopus 로고
    • Connection domain mutations N348I and A360V in HIV-1 reverse transcriptase enhance resistance to 3′-azido-3′-deoxythymidine through both RNase H-dependent and -independent mechanisms
    • Ehteshami M, Beilhartz GL, Scarth BJ, Tchesnokov EP, McCormick S, Wynhoven B et al (2008) Connection domain mutations N348I and A360V in HIV-1 reverse transcriptase enhance resistance to 3′-azido-3′-deoxythymidine through both RNase H-dependent and -independent mechanisms. J Biol Chem 283(32):22222-22232
    • (2008) J Biol Chem , vol.283 , Issue.32 , pp. 22222-22232
    • Ehteshami, M.1    Beilhartz, G.L.2    Scarth, B.J.3    Tchesnokov, E.P.4    McCormick, S.5    Wynhoven, B.6
  • 27
    • 0025924750 scopus 로고
    • Reverse transcriptase. RNase H from the human immunodeficiency virus. Relationship of the DNA polymerase and RNA hydrolysis activities
    • Furfine ES, Reardon JE (1991) Reverse transcriptase. RNase H from the human immunodeficiency virus. Relationship of the DNA polymerase and RNA hydrolysis activities. J Biol Chem 266(1):406-412
    • (1991) J Biol Chem , vol.266 , Issue.1 , pp. 406-412
    • Furfine, E.S.1    Reardon, J.E.2
  • 28
    • 0032847978 scopus 로고    scopus 로고
    • Inhibitors of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase
    • Gabbara S, Davis WR, Hupe L, Hupe D, Peliska JA (1999) Inhibitors of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase. Biochemistry 38(40):13070-13076
    • (1999) Biochemistry , vol.38 , Issue.40 , pp. 13070-13076
    • Gabbara, S.1    Davis, W.R.2    Hupe, L.3    Hupe, D.4    Peliska, J.A.5
  • 29
    • 0028945841 scopus 로고
    • HIV-1 reverse transcriptase-associated RNase H cleaves RNA/RNA in arrested complexes: Implications for the mechanism by which RNase H discriminates between RNA/RNA and RNA/DNA
    • Gotte M, Fackler S, Hermann T, Perola E, Cellai L, Gross HJ et al (1995) HIV-1 reverse transcriptase-associated RNase H cleaves RNA/RNA in arrested complexes: implications for the mechanism by which RNase H discriminates between RNA/RNA and RNA/DNA. EMBO J 14(4):833-841
    • (1995) EMBO J , vol.14 , Issue.4 , pp. 833-841
    • Gotte, M.1    Fackler, S.2    Hermann, T.3    Perola, E.4    Cellai, L.5    Gross, H.J.6
  • 30
    • 0039634849 scopus 로고    scopus 로고
    • Localization of the active site of HIV-1 reverse transcriptase-associated RNase H domain on a DNA template using site-specific generated hydroxyl radicals
    • Gotte M, Maier G, Gross HJ, Heumann H (1998) Localization of the active site of HIV-1 reverse transcriptase-associated RNase H domain on a DNA template using site-specific generated hydroxyl radicals. J Biol Chem 273(17):10139-10146
    • (1998) J Biol Chem , vol.273 , Issue.17 , pp. 10139-10146
    • Gotte, M.1    Maier, G.2    Gross, H.J.3    Heumann, H.4
  • 31
    • 77949567911 scopus 로고    scopus 로고
    • Reverse transcriptase in motion: Conformational dynamics of enzyme-substrate interactions
    • Gotte M, Rausch JW, Marchand B, Sarafianos S, Le Grice SF (2010) Reverse transcriptase in motion: conformational dynamics of enzyme-substrate interactions. Biochim Biophys Acta 1804(5):1202-1212. doi: 10.1016/j.bbapap.2009.07.020
    • (2010) Biochim Biophys Acta , vol.1804 , Issue.5 , pp. 1202-1212
    • Gotte, M.1    Rausch, J.W.2    Marchand, B.3    Sarafianos, S.4    Le Grice, S.F.5
  • 32
    • 11144355815 scopus 로고    scopus 로고
    • Activity of the isolated HIV RNase H domain and specific inhibition by N-hydroxyimides
    • Hang JQ, Rajendran S, Yang Y, Li Y, In PW, Overton H et al (2004) Activity of the isolated HIV RNase H domain and specific inhibition by N-hydroxyimides. Biochem Biophys Res Commun 317(2):321-329
    • (2004) Biochem Biophys Res Commun , vol.317 , Issue.2 , pp. 321-329
    • Hang, J.Q.1    Rajendran, S.2    Yang, Y.3    Li, Y.4    In, P.W.5    Overton, H.6
  • 33
    • 33751538895 scopus 로고    scopus 로고
    • Substrate-dependent inhibition or stimulation of HIV RNase H activity by non-nucleoside reverse transcriptase inhibitors (NNRTIs)
    • Hang JQ, Li Y, Yang Y, Cammack N, Mirzadegan T, Klumpp K (2007) Substrate-dependent inhibition or stimulation of HIV RNase H activity by non-nucleoside reverse transcriptase inhibitors (NNRTIs). Biochem Biophys Res Commun 352(2):341-350
    • (2007) Biochem Biophys Res Commun , vol.352 , Issue.2 , pp. 341-350
    • Hang, J.Q.1    Li, Y.2    Yang, Y.3    Cammack, N.4    Mirzadegan, T.5    Klumpp, K.6
  • 34
    • 0023673620 scopus 로고
    • Identification and characterization of HIVspecific RNase H by monoclonal antibody
    • Hansen J, Schulze T, Mellert W, Moelling K (1988) Identification and characterization of HIVspecific RNase H by monoclonal antibody. EMBO J 7(1):239-243
    • (1988) EMBO J , vol.7 , Issue.1 , pp. 239-243
    • Hansen, J.1    Schulze, T.2    Mellert, W.3    Moelling, K.4
  • 35
    • 78650533230 scopus 로고    scopus 로고
    • Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance. [Research support, Non-U.S. Gov't]
    • Hare S, Vos AM, Clayton RF, Thuring JW, Cummings MD, Cherepanov P (2010) Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance. [Research support, Non-U.S. Gov't]. Proc Natl Acad Sci USA 107(46):20057-20062. doi: 10.1073/pnas.1010246107
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.46 , pp. 20057-20062
    • Hare, S.1    Vos, A.M.2    Clayton, R.F.3    Thuring, J.W.4    Cummings, M.D.5    Cherepanov, P.6
  • 36
    • 0034723439 scopus 로고    scopus 로고
    • Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells
    • Hazuda DJ, Felock P, Witmer M, Wolfe A, Stillmock K, Grobler JA et al (2000) Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells. Science 287(5453):646-650
    • (2000) Science , vol.287 , Issue.5453 , pp. 646-650
    • Hazuda, D.J.1    Felock, P.2    Witmer, M.3    Wolfe, A.4    Stillmock, K.5    Grobler, J.A.6
  • 37
    • 37249062449 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase structure with RNase H inhibitor dihydroxy benzoyl naphthyl hydrazone bound at a novel site
    • Himmel DM, Sarafianos SG, Dharmasena S, Hossain MM, McCoy-Simandle K, Ilina T et al (2006) HIV-1 reverse transcriptase structure with RNase H inhibitor dihydroxy benzoyl naphthyl hydrazone bound at a novel site. ACS Chem Biol 1(11):702-712
    • (2006) ACS Chem Biol , vol.1 , Issue.11 , pp. 702-712
    • Himmel, D.M.1    Sarafianos, S.G.2    Dharmasena, S.3    Hossain, M.M.4    McCoy-Simandle, K.5    Ilina, T.6
  • 38
    • 71049185147 scopus 로고    scopus 로고
    • Structure of HIV-1 reverse transcriptase with the inhibitor beta-Thujaplicinol bound at the RNase H active site
    • Himmel DM, Maegley KA, Pauly TA, Bauman JD, Das K, Dharia C et al (2009) Structure of HIV-1 reverse transcriptase with the inhibitor beta-Thujaplicinol bound at the RNase H active site. Structure 17(12):1625-1635
    • (2009) Structure , vol.17 , Issue.12 , pp. 1625-1635
    • Himmel, D.M.1    Maegley, K.A.2    Pauly, T.A.3    Bauman, J.D.4    Das, K.5    Dharia, C.6
  • 39
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug resistance
    • Huang H, Chopra R, Verdine GL, Harrison SC (1998) Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 282(5394): 1669-1675
    • (1998) Science , vol.282 , Issue.5394 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 40
    • 0027318776 scopus 로고
    • Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA
    • Jacobo-Molina A, Ding J, Nanni RG, Clark AD Jr, Lu X, Tantillo C et al (1993) Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA. Proc Natl Acad Sci USA 90(13):6320-6324
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.13 , pp. 6320-6324
    • Jacobo-Molina, A.1    Ding, J.2    Nanni, R.G.3    Clark, A.D.4    Lu, X.5    Tantillo, C.6
  • 42
    • 0028904435 scopus 로고
    • Substitution of a highly basic helix/loop sequence into the RNase H domain of human immunodeficiency virus reverse transcriptase restores its Mn(2+)-dependent RNase H activity
    • Keck JL, Marqusee S (1995) Substitution of a highly basic helix/loop sequence into the RNase H domain of human immunodeficiency virus reverse transcriptase restores its Mn(2+)-dependent RNase H activity. Proc Natl Acad Sci USA 92(7):2740-2744
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.7 , pp. 2740-2744
    • Keck, J.L.1    Marqusee, S.2
  • 43
    • 0032545251 scopus 로고    scopus 로고
    • Activation/attenuation model for RNase H. A onemetal mechanism with second-metal inhibition
    • Keck JL, Goedken ER, Marqusee S (1998) Activation/attenuation model for RNase H. A onemetal mechanism with second-metal inhibition. J Biol Chem 273(51):34128-34133
    • (1998) J Biol Chem , vol.273 , Issue.51 , pp. 34128-34133
    • Keck, J.L.1    Goedken, E.R.2    Marqusee, S.3
  • 44
    • 70349638920 scopus 로고    scopus 로고
    • RNase H active site inhibitors of human immunodeficiency virus type 1 reverse transcriptase: Design, biochemical activity, and structural information
    • Kirschberg TA, Balakrishnan M, Squires NH, Barnes T, Brendza KM, Chen X et al (2009) RNase H active site inhibitors of human immunodeficiency virus type 1 reverse transcriptase: design, biochemical activity, and structural information. J Med Chem 52(19):5781-5784. doi: 10.1021/jm900597q
    • (2009) J Med Chem , vol.52 , Issue.19 , pp. 5781-5784
    • Kirschberg, T.A.1    Balakrishnan, M.2    Squires, N.H.3    Barnes, T.4    Brendza, K.M.5    Chen, X.6
  • 45
    • 33646497669 scopus 로고    scopus 로고
    • Recent progress in the design of small molecule inhibitors of HIV RNase H
    • Klumpp K, Mirzadegan T (2006) Recent progress in the design of small molecule inhibitors of HIV RNase H. Curr Pharm Des 12(15):1909-1922
    • (2006) Curr Pharm des , vol.12 , Issue.15 , pp. 1909-1922
    • Klumpp, K.1    Mirzadegan, T.2
  • 46
    • 10744226166 scopus 로고    scopus 로고
    • Two-metal ion mechanism of RNA cleavage by HIV RNase H and mechanism-based design of selective HIV RNase H inhibitors
    • Klumpp K, Hang JQ, Rajendran S, Yang Y, Derosier A, Wong Kai In P et al (2003) Two-metal ion mechanism of RNA cleavage by HIV RNase H and mechanism-based design of selective HIV RNase H inhibitors. Nucleic Acids Res 31(23):6852-6859
    • (2003) Nucleic Acids Res , vol.31 , Issue.23 , pp. 6852-6859
    • Klumpp, K.1    Hang, J.Q.2    Rajendran, S.3    Yang, Y.4    Derosier, A.5    Wong Kai-In, P.6
  • 47
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt LA, Wang J, Friedman JM, Rice PA, Steitz TA (1992) Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256(5065): 1783-1790
    • (1992) Science , vol.256 , Issue.5065 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 48
    • 79956334444 scopus 로고    scopus 로고
    • Structural and binding analysis of pyrimidinol carboxylic acid and N-hydroxy quinazolinedione HIV-1 RNase H inhibitors
    • Lansdon EB, Liu Q, Leavitt SA, Balakrishnan M, Perry JK, Lancaster-Moyer C et al (2011) Structural and binding analysis of pyrimidinol carboxylic acid and N-hydroxy quinazolinedione HIV-1 RNase H inhibitors. Antimicrob Agents Chemother 55(6):2905-2915. doi: 10.1128/AAC.01594-10
    • (2011) Antimicrob Agents Chemother , vol.55 , Issue.6 , pp. 2905-2915
    • Lansdon, E.B.1    Liu, Q.2    Leavitt, S.A.3    Balakrishnan, M.4    Perry, J.K.5    Lancaster-Moyer, C.6
  • 49
    • 0025041016 scopus 로고
    • The inhibition of human immunodeficiency virus type 1 reverse transcriptase by avarol and avarone derivatives
    • Loya S, Hizi A (1990) The inhibition of human immunodeficiency virus type 1 reverse transcriptase by avarol and avarone derivatives. FEBS Lett 269(1):131-134
    • (1990) FEBS Lett , vol.269 , Issue.1 , pp. 131-134
    • Loya, S.1    Hizi, A.2
  • 50
    • 0027322533 scopus 로고
    • The interaction of illimaquinone, a selective inhibitor of the RNase H activity, with the reverse transcriptases of human immunodeficiency and murine leukemia retroviruses
    • Loya S, Hizi A (1993) The interaction of illimaquinone, a selective inhibitor of the RNase H activity, with the reverse transcriptases of human immunodeficiency and murine leukemia retroviruses. J Biol Chem 268(13):9323-9328
    • (1993) J Biol Chem , vol.268 , Issue.13 , pp. 9323-9328
    • Loya, S.1    Hizi, A.2
  • 51
    • 0024999408 scopus 로고
    • Illimaquinone, a selective inhibitor of the RNase H activity of human immunodeficiency virus type 1 reverse transcriptase
    • Loya S, Tal R, Kashman Y, Hizi A (1990) Illimaquinone, a selective inhibitor of the RNase H activity of human immunodeficiency virus type 1 reverse transcriptase. Antimicrob Agents Chemother 34(10):2009-2012
    • (1990) Antimicrob Agents Chemother , vol.34 , Issue.10 , pp. 2009-2012
    • Loya, S.1    Tal, R.2    Kashman, Y.3    Hizi, A.4
  • 52
    • 15844371219 scopus 로고    scopus 로고
    • Structural basis for 5′-end-specific recognition of guide RNA by the A. fulgidus Piwi protein
    • Ma JB, Yuan YR, Meister G, Pei Y, Tuschl T, Patel DJ (2005) Structural basis for 5′-end-specific recognition of guide RNA by the A. fulgidus Piwi protein. Nature 434(7033):666-670
    • (2005) Nature , vol.434 , Issue.7033 , pp. 666-670
    • Ma, J.B.1    Yuan, Y.R.2    Meister, G.3    Pei, Y.4    Tuschl, T.5    Patel, D.J.6
  • 53
    • 0036221012 scopus 로고    scopus 로고
    • Inhibitory effects of quinones on RNase H activity associated with HIV-1 reverse transcriptase
    • Min BS, Miyashiro H, Hattori M (2002) Inhibitory effects of quinones on RNase H activity associated with HIV-1 reverse transcriptase. Phytother Res PTR 16(Suppl 1):S57-S62
    • (2002) Phytother Res PTR , vol.16 , pp. S57-S62
    • Min, B.S.1    Miyashiro, H.2    Hattori, M.3
  • 55
    • 59649101866 scopus 로고    scopus 로고
    • Retroviral integrase superfamily: The structural perspective
    • Nowotny M (2009) Retroviral integrase superfamily: the structural perspective. EMBO Rep 10(2):144-151. doi: 10.1038/embor.2008.256
    • (2009) EMBO Rep , vol.10 , Issue.2 , pp. 144-151
    • Nowotny, M.1
  • 56
    • 21244451435 scopus 로고    scopus 로고
    • Crystal structures of RNase H bound to an RNA/DNA hybrid: Substrate specificity and metal-dependent catalysis
    • Nowotny M, Gaidamakov SA, Crouch RJ, Yang W (2005) Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis. Cell 121(7):1005-1016
    • (2005) Cell , vol.121 , Issue.7 , pp. 1005-1016
    • Nowotny, M.1    Gaidamakov, S.A.2    Crouch, R.J.3    Yang, W.4
  • 57
    • 35348978302 scopus 로고    scopus 로고
    • Structure of human RNase H1 complexed with an RNA/DNA hybrid: Insight into HIV reverse transcription
    • Nowotny M, Gaidamakov SA, Ghirlando R, Cerritelli SM, Crouch RJ, Yang W (2007) Structure of human RNase H1 complexed with an RNA/DNA hybrid: insight into HIV reverse transcription. Mol Cell 28(2):264-276
    • (2007) Mol Cell , vol.28 , Issue.2 , pp. 264-276
    • Nowotny, M.1    Gaidamakov, S.A.2    Ghirlando, R.3    Cerritelli, S.M.4    Crouch, R.J.5    Yang, W.6
  • 58
    • 0030029792 scopus 로고    scopus 로고
    • Helix structure and ends of RNA/DNA hybrids direct the cleavage specificity of HIV-1 reverse transcriptase RNase H
    • Palaniappan C, Fuentes GM, Rodriguez-Rodriguez L, Fay PJ, Bambara RA (1996) Helix structure and ends of RNA/DNA hybrids direct the cleavage specificity of HIV-1 reverse transcriptase RNase H. J Biol Chem 271(4):2063-2070
    • (1996) J Biol Chem , vol.271 , Issue.4 , pp. 2063-2070
    • Palaniappan, C.1    Fuentes, G.M.2    Rodriguez-Rodriguez, L.3    Fay, P.J.4    Bambara, R.A.5
  • 59
    • 0344453794 scopus 로고    scopus 로고
    • Use of a pharmacophore model to discover a new class of influenza endonuclease inhibitors
    • Parkes KE, Ermert P, Fassler J, Ives J, Martin JA, Merrett JH et al (2003) Use of a pharmacophore model to discover a new class of influenza endonuclease inhibitors. J Med Chem 46(7): 1153-1164
    • (2003) J Med Chem , vol.46 , Issue.7 , pp. 1153-1164
    • Parkes, K.E.1    Ermert, P.2    Fassler, J.3    Ives, J.4    Martin, J.A.5    Merrett, J.H.6
  • 60
    • 0141758137 scopus 로고    scopus 로고
    • A fluorescence-based highthroughput screening assay for inhibitors of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H activity
    • Parniak MA, Min KL, Budihas SR, Le Grice SF, Beutler JA (2003) A fluorescence-based highthroughput screening assay for inhibitors of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H activity. Anal Biochem 322(1):33-39. doi: 10.1016/j.ab.2003.06.001
    • (2003) Anal Biochem , vol.322 , Issue.1 , pp. 33-39
    • Parniak, M.A.1    Min, K.L.2    Budihas, S.R.3    Le Grice, S.F.4    Beutler, J.A.5
  • 61
    • 0026486193 scopus 로고
    • Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase. [Research Support, U.S. Gov't, P.H.S.]
    • Peliska JA, Benkovic SJ (1992) Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase. [Research Support, U.S. Gov't, P.H.S.]. Science 258(5085):1112-1118
    • (1992) Science , vol.258 , Issue.5085 , pp. 1112-1118
    • Peliska, J.A.1    Benkovic, S.J.2
  • 62
    • 2942525660 scopus 로고    scopus 로고
    • 'Binding, bending and bonding': Polypurine tract-primed initiation of plus-strand DNA synthesis in human immunodeficiency virus
    • Rausch JW, Le Grice SF (2004) 'Binding, bending and bonding': polypurine tract-primed initiation of plus-strand DNA synthesis in human immunodeficiency virus. Int J Biochem Cell Biol 36(9):1752-1766. doi: 10.1016/j.biocel.2004.02.016
    • (2004) Int J Biochem Cell Biol , vol.36 , Issue.9 , pp. 1752-1766
    • Rausch, J.W.1    Le Grice, S.F.2
  • 63
    • 0035965124 scopus 로고    scopus 로고
    • Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors
    • Ren J, Nichols C, Bird L, Chamberlain P, Weaver K, Short S et al (2001) Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors. J Mol Biol 312(4):795-805. doi: 10.1006/jmbi.2001.4988
    • (2001) J Mol Biol , vol.312 , Issue.4 , pp. 795-805
    • Ren, J.1    Nichols, C.2    Bird, L.3    Chamberlain, P.4    Weaver, K.5    Short, S.6
  • 64
    • 0028842293 scopus 로고
    • The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1
    • Rodgers DW, Gamblin SJ, Harris BA, Ray S, Culp JS, Hellmig B et al (1995) The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1. Proc Natl Acad Sci USA 92(4):1222-1226
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.4 , pp. 1222-1226
    • Rodgers, D.W.1    Gamblin, S.J.2    Harris, B.A.3    Ray, S.4    Culp, J.S.5    Hellmig, B.6
  • 65
    • 26844566830 scopus 로고    scopus 로고
    • Structure and mechanism of DNA polymerases
    • Rothwell PJ, Waksman G (2005) Structure and mechanism of DNA polymerases. Adv Protein Chem 71:401-440. doi: 10.1016/S0065-3233(04)71011-6
    • (2005) Adv Protein Chem , vol.71 , pp. 401-440
    • Rothwell, P.J.1    Waksman, G.2
  • 66
    • 4444309793 scopus 로고    scopus 로고
    • New nucleoside/nucleotide backbone options: A review of recent studies
    • Ruane PJ, DeJesus E (2004) New nucleoside/nucleotide backbone options: a review of recent studies. J Acquir Immune Defic Syndr 37(Suppl 1):S21-S29
    • (2004) J Acquir Immune Defic Syndr , vol.37 , pp. S21-S29
    • Ruane, P.J.1    Dejesus, E.2
  • 67
    • 0035868713 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA
    • Sarafianos SG, Das K, Tantillo C, Clark AD Jr, Ding J, Whitcomb JM et al (2001) Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA. EMBO J 20(6):1449-1461
    • (2001) EMBO J , vol.20 , Issue.6 , pp. 1449-1461
    • Sarafianos, S.G.1    Das, K.2    Tantillo, C.3    Clark, A.D.4    Ding, J.5    Whitcomb, J.M.6
  • 68
    • 0024847468 scopus 로고
    • Point mutations in conserved amino acid residues within the C-terminal domain of HIV-1 reverse transcriptase specifically repress RNase H function
    • Schatz O, Cromme FV, Gruninger-Leitch F, Le Grice SF (1989) Point mutations in conserved amino acid residues within the C-terminal domain of HIV-1 reverse transcriptase specifically repress RNase H function. FEBS Lett 257(2):311-314
    • (1989) FEBS Lett , vol.257 , Issue.2 , pp. 311-314
    • Schatz, O.1    Cromme, F.V.2    Gruninger-Leitch, F.3    Le Grice, S.F.4
  • 69
    • 43049125772 scopus 로고    scopus 로고
    • RNase H activity: Structure, specificity, and function in reverse transcription
    • Schultz SJ, Champoux JJ (2008) RNase H activity: structure, specificity, and function in reverse transcription. Virus Res 134(1-2):86-103. doi: 10.1016/j.virusres.2007.12.007
    • (2008) Virus Res , vol.134 , Issue.1-2 , pp. 86-103
    • Schultz, S.J.1    Champoux, J.J.2
  • 70
    • 7944237580 scopus 로고    scopus 로고
    • Recognition of internal cleavage sites by retroviral RNases H
    • Schultz SJ, Zhang M, Champoux JJ (2004) Recognition of internal cleavage sites by retroviral RNases H. J Mol Biol 344(3):635-652. doi: 10.1016/j.jmb.2004.09.081
    • (2004) J Mol Biol , vol.344 , Issue.3 , pp. 635-652
    • Schultz, S.J.1    Zhang, M.2    Champoux, J.J.3
  • 71
    • 0037474193 scopus 로고    scopus 로고
    • Inhibition of HIV-1 ribonuclease H by a novel diketo acid, 4-[5-(benzoylamino)thien-2-yl]-2,4-dioxobutanoic acid
    • Shaw-Reid CA, Munshi V, Graham P, Wolfe A, Witmer M, Danzeisen R et al (2003) Inhibition of HIV-1 ribonuclease H by a novel diketo acid, 4-[5-(benzoylamino)thien-2-yl]-2,4-dioxobutanoic acid. J Biol Chem 278(5):2777-2780. doi: 10.1074/jbc.C200621200
    • (2003) J Biol Chem , vol.278 , Issue.5 , pp. 2777-2780
    • Shaw-Reid, C.A.1    Munshi, V.2    Graham, P.3    Wolfe, A.4    Witmer, M.5    Danzeisen, R.6
  • 72
    • 13444257639 scopus 로고    scopus 로고
    • Dissecting the effects of DNA polymerase and ribonuclease H inhibitor combinations on HIV-1 reversetranscriptase activities
    • Shaw-Reid CA, Feuston B, Munshi V, Getty K, Krueger J, Hazuda DJ et al (2005) Dissecting the effects of DNA polymerase and ribonuclease H inhibitor combinations on HIV-1 reversetranscriptase activities. Biochemistry 44(5):1595-1606. doi: 10.1021/bi0486740
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1595-1606
    • Shaw-Reid, C.A.1    Feuston, B.2    Munshi, V.3    Getty, K.4    Krueger, J.5    Hazuda, D.J.6
  • 73
    • 0026052102 scopus 로고
    • Chimeric human immunodeficiency virus type 1/type 2 reverse transcriptases display reversed sensitivity to nonnucleoside analog inhibitors
    • Shih CK, Rose JM, Hansen GL, Wu JC, Bacolla A, Griffin JA (1991) Chimeric human immunodeficiency virus type 1/type 2 reverse transcriptases display reversed sensitivity to nonnucleoside analog inhibitors. Proc Natl Acad Sci USA 88(21):9878-9882
    • (1991) Proc Natl Acad Sci USA , vol.88 , Issue.21 , pp. 9878-9882
    • Shih, C.K.1    Rose, J.M.2    Hansen, G.L.3    Wu, J.C.4    Bacolla, A.5    Griffin, J.A.6
  • 74
    • 0033770149 scopus 로고    scopus 로고
    • Molecular mechanisms of HIV-1 resistance to nucleoside reverse transcriptase inhibitors (NRTIs)
    • Sluis-Cremer N, Arion D, Parniak MA (2000) Molecular mechanisms of HIV-1 resistance to nucleoside reverse transcriptase inhibitors (NRTIs). Cell Mol Life Sci CMLS 57(10): 1408-1422
    • (2000) Cell Mol Life Sci CMLS , vol.57 , Issue.10 , pp. 1408-1422
    • Sluis-Cremer, N.1    Arion, D.2    Parniak, M.A.3
  • 75
    • 0036076157 scopus 로고    scopus 로고
    • Destabilization of the HIV-1 reverse transcriptase dimer upon interaction with N-acyl hydrazone inhibitors
    • Sluis-Cremer N, Arion D, Parniak MA (2002) Destabilization of the HIV-1 reverse transcriptase dimer upon interaction with N-acyl hydrazone inhibitors. Mol Pharmacol 62(2):398-405
    • (2002) Mol Pharmacol , vol.62 , Issue.2 , pp. 398-405
    • Sluis-Cremer, N.1    Arion, D.2    Parniak, M.A.3
  • 76
    • 4444302947 scopus 로고    scopus 로고
    • Crystal structure of argonaute and its implications for RISC slicer activity
    • Song JJ, Smith SK, Hannon GJ, Joshua-Tor L (2004) Crystal structure of argonaute and its implications for RISC slicer activity. Science 305(5689):1434-1437
    • (2004) Science , vol.305 , Issue.5689 , pp. 1434-1437
    • Song, J.J.1    Smith, S.K.2    Hannon, G.J.3    Joshua-Tor, L.4
  • 77
    • 0027931296 scopus 로고
    • Construction of an enzymatically active ribonuclease H domain of human immunodeficiency virus type 1 reverse transcriptase
    • Stahl SJ, Kaufman JD, Vikic-Topic S, Crouch RJ, Wingfield PT (1994) Construction of an enzymatically active ribonuclease H domain of human immunodeficiency virus type 1 reverse transcriptase. Protein Eng 7(9):1103-1108
    • (1994) Protein Eng , vol.7 , Issue.9 , pp. 1103-1108
    • Stahl, S.J.1    Kaufman, J.D.2    Vikic-Topic, S.3    Crouch, R.J.4    Wingfield, P.T.5
  • 78
    • 0347361643 scopus 로고    scopus 로고
    • Discovery of alpha, gamma-diketo acids as potent selective and reversible inhibitors of hepatitis C virus NS5b RNA-dependent RNA polymerase
    • Summa V, Petrocchi A, Pace P, Matassa VG, De Francesco R, Altamura S et al (2004) Discovery of alpha, gamma-diketo acids as potent selective and reversible inhibitors of hepatitis C virus NS5b RNA-dependent RNA polymerase. J Med Chem 47(1):14-17. doi: 10.1021/jm0342109
    • (2004) J Med Chem , vol.47 , Issue.1 , pp. 14-17
    • Summa, V.1    Petrocchi, A.2    Pace, P.3    Matassa, V.G.4    De Francesco, R.5    Altamura, S.6
  • 79
    • 0025812772 scopus 로고
    • Inhibition of the RNase H activity of HIV reverse transcriptase by azidothymidylate
    • Tan CK, Civil R, Mian AM, So AG, Downey KM (1991) Inhibition of the RNase H activity of HIV reverse transcriptase by azidothymidylate. Biochemistry 30(20):4831-4835
    • (1991) Biochemistry , vol.30 , Issue.20 , pp. 4831-4835
    • Tan, C.K.1    Civil, R.2    Mian, A.M.3    So, A.G.4    Downey, K.M.5
  • 80
    • 0002296754 scopus 로고    scopus 로고
    • Reverse transcriptase and the generation of retroviral DNA
    • Coffin JM, Hughes SH, Varmus HE (eds). Cold Spring Harbor Laboratory Press, Plainview
    • Telesnitsky A, Goff SP (1997) Reverse transcriptase and the generation of retroviral DNA. In: Coffin JM, Hughes SH, Varmus HE (eds) Retroviruses. Cold Spring Harbor Laboratory Press, Plainview, pp. 121-160
    • (1997) Retroviruses , pp. 121-160
    • Telesnitsky, A.1    Goff, S.P.2
  • 81
    • 0028171260 scopus 로고
    • Inhibition of cap (m7GpppXm)-dependent endonuclease of influenza virus by 4-substituted 2,4-dioxobutanoic acid compounds
    • Tomassini J, Selnick H, Davies ME, Armstrong ME, Baldwin J, Bourgeois M et al (1994) Inhibition of cap (m7GpppXm)-dependent endonuclease of influenza virus by 4-substituted 2,4-dioxobutanoic acid compounds. Antimicrob Agents Chemother 38(12):2827-2837
    • (1994) Antimicrob Agents Chemother , vol.38 , Issue.12 , pp. 2827-2837
    • Tomassini, J.1    Selnick, H.2    Davies, M.E.3    Armstrong, M.E.4    Baldwin, J.5    Bourgeois, M.6
  • 82
    • 13544276913 scopus 로고    scopus 로고
    • 6-[1-(4-Fluorophenyl) methyl-1H-pyrrol-2-yl)]-2,4-dioxo-5-hexenoic acid ethyl ester a novel diketo acid derivative which selectively inhibits the HIV-1 viral replication in cell culture and the ribonuclease H activity in vitro
    • Tramontano E, Esposito F, Badas R, Di Santo R, Costi R, La Colla P (2005) 6-[1-(4-Fluorophenyl) methyl-1H-pyrrol-2-yl)]-2,4-dioxo-5-hexenoic acid ethyl ester a novel diketo acid derivative which selectively inhibits the HIV-1 viral replication in cell culture and the ribonuclease H activity in vitro. Antiviral Res 65(2):117-124
    • (2005) Antiviral Res , vol.65 , Issue.2 , pp. 117-124
    • Tramontano, E.1    Esposito, F.2    Badas, R.3    Di Santo, R.4    Costi, R.5    La Colla, P.6
  • 83
    • 0037465825 scopus 로고    scopus 로고
    • Dispensability of glutamic acid 48 and aspartic acid 134 for Mn2+-dependent activity of E. coli ribonuclease HI
    • Tsunaka Y, Haruki M, Morikawa M, Oobatake M, Kanaya S (2003) Dispensability of glutamic acid 48 and aspartic acid 134 for Mn2+-dependent activity of E. coli ribonuclease HI. Biochemistry 42(11):3366-3374. doi: 10.1021/bi0205606
    • (2003) Biochemistry , vol.42 , Issue.11 , pp. 3366-3374
    • Tsunaka, Y.1    Haruki, M.2    Morikawa, M.3    Oobatake, M.4    Kanaya, S.5
  • 84
    • 11844284013 scopus 로고    scopus 로고
    • Identification of single Mn(2+) binding sites required for activation of the mutant proteins of E. coli RNase HI at Glu48 and/or Asp134 by X-ray crystallography
    • Tsunaka Y, Takano K, Matsumura H, Yamagata Y, Kanaya S (2005) Identification of single Mn(2+) binding sites required for activation of the mutant proteins of E. coli RNase HI at Glu48 and/or Asp134 by X-ray crystallography. J Mol Biol 345(5):1171-1183
    • (2005) J Mol Biol , vol.345 , Issue.5 , pp. 1171-1183
    • Tsunaka, Y.1    Takano, K.2    Matsumura, H.3    Yamagata, Y.4    Kanaya, S.5
  • 85
    • 58149160464 scopus 로고    scopus 로고
    • Vinylogous ureas as a novel class of inhibitors of reverse transcriptase-associated ribonuclease H activity
    • Wendeler M, Lee HF, Bermingham A, Miller JT, Chertov O, Bona MK et al (2008) Vinylogous ureas as a novel class of inhibitors of reverse transcriptase-associated ribonuclease H activity. ACS Chem Biol 3(10):635-644
    • (2008) ACS Chem Biol , vol.3 , Issue.10 , pp. 635-644
    • Wendeler, M.1    Lee, H.F.2    Bermingham, A.3    Miller, J.T.4    Chertov, O.5    Bona, M.K.6
  • 86
    • 0028344281 scopus 로고
    • Catalytically distinct conformations of the ribonuclease H of HIV-1 reverse transcriptase by substrate cleavage patterns and inhibition by azidothymidylate and N-ethylmaleimide
    • Zhan X, Tan CK, Scott WA, Mian AM, Downey KM, So AG (1994) Catalytically distinct conformations of the ribonuclease H of HIV-1 reverse transcriptase by substrate cleavage patterns and inhibition by azidothymidylate and N-ethylmaleimide. Biochemistry 33(6):1366-1372
    • (1994) Biochemistry , vol.33 , Issue.6 , pp. 1366-1372
    • Zhan, X.1    Tan, C.K.2    Scott, W.A.3    Mian, A.M.4    Downey, K.M.5    So, A.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.