메뉴 건너뛰기




Volumn 51, Issue 24, 2008, Pages 7717-7730

Design, synthesis, and biological evaluation of a series of 2-hydroxyisoquinoline-1,3(2H,4H)-diones as dual inhibitors of human immunodeficiency virus type 1 integrase and the reverse transcriptase RNase H domain

Author keywords

[No Author keywords available]

Indexed keywords

2 (4 FLUOROPHENYL) N (2 HYDROXY 1,3 DIOXO 1,2,3,4 TETRAHYDROISOQUINOLIN 7 YL)ACETAMIDE; 2 BENZYLOXY 7 (3,4 DIMETHOXYPHENYL)ISOQUINOLINE 1,3(2H,4H) DIONE; 2 HYDROXY 7 (4 HYDROXYPHENYL)ISOQUINOLINE 1,3(2H,4H) DIONE; 2 HYDROXY 7 IODOISOQUINOLINE 1,3(2H,4H) DIONE; 2 HYDROXY 7 NITROISOQUINOLINE 1,3(2H,4H) DIONE; 2 HYDROXY 7 PHENYLISOQUINOLINE 1,3(2H,4H) DIONE; 2 HYDROXY 7 [4 (TRIFLUOROMETHYL)PHENYL]ISOQUINOLINE 1,3(2H,4H) DIONE; 2 HYDROXYISOQUINOLINE 1,3(2H,4H) DIONE; 2 HYDROXYISOQUINOLINE 1,3(2H,4H) DIONE DERIVATIVE; 2,7 DIHYDROXYISOQUINOLINE 1,3(2H,4H) DIONE; 7 (3,4 DIHYDROXYPHENYL) 2 HYDROXYISOQUINOLINE 1,3(2H,4H) DIONE; 7 (4 FLUOROPHENYL) 2 HYDROXYISOQUINOLINE 1,3(2H,4H) DIONE; 7 AMINO 2 HYDROXYISOQUINOLINE 1,3(2H,4H) DIONE; 7 BROMO 2 HYDROXYISOQUINOLINE 1,3(2H,4H) DIONE; 7 CHLORO 2 HYDROXYISOQUINOLINE 1,3(2H,4H) DIONE; ELVITEGRAVIR; INTEGRASE INHIBITOR; N (2 HYDROXY 1,3 DIOXO 1,2,3,4 TETRAHYDROISOQUINOLIN 7 YL) 2 PHENYLACETAMIDE; N (2 HYDROXY 1,3 DIOXO 1,2,3,4 TETRAHYDROISOQUINOLIN 7 YL) 3 NITROBENZAMIDE; N (2 HYDROXY 1,3 DIOXO 1,2,3,4 TETRAHYDROISOQUINOLIN 7 YL) 4 FLUOROBENZAMIDE; N (2 HYDROXY 1,3 DIOXO 1,2,3,4 TETRAHYDROISOQUINOLIN 7 YL)ACETAMIDE; N (2 HYDROXY 1,3 DIOXO 1,2,3,4 TETRAHYDROISOQUINOLIN 7 YL)BENZAMIDE; N (2 HYDROXY 1,3 DIOXO 1,2,3,4 TETRAHYDROISOQUINOLIN 7 YL)PENTANAMIDE; N (4 FLUOROBENZYL) 8 HYDROXY 5 (TETRAHYDRO 2H 1,2 THIAZIN 2 YL) 1,6 NAPHTHYRIDINE 7 CARBOXAMIDE S,S DIOXIDE; RALTEGRAVIR; RIBONUCLEASE H; RNA DIRECTED DNA POLYMERASE; RNA DIRECTED DNA POLYMERASE INHIBITOR; UNCLASSIFIED DRUG; UNINDEXED DRUG; VIRUS ENZYME;

EID: 58149083480     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm8007085     Document Type: Article
Times cited : (119)

References (54)
  • 2
    • 0032544311 scopus 로고    scopus 로고
    • Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: High level of similarity of the active site with other viral integrases
    • Maignan, S.; Guilloteau, J. P.; Zhou-Liu, Q.; Clément-Mella, C.; Mikol, V. Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: High level of similarity of the active site with other viral integrases. J. Mol. Biol. 1998, 282, 359-368.
    • (1998) J. Mol. Biol , vol.282 , pp. 359-368
    • Maignan, S.1    Guilloteau, J.P.2    Zhou-Liu, Q.3    Clément-Mella, C.4    Mikol, V.5
  • 3
    • 33746888209 scopus 로고    scopus 로고
    • Designing HIV integrase inhibitors: Shooting the last arrow
    • Makhija, M. T. Designing HIV integrase inhibitors: Shooting the last arrow. Curr. Med. Chem. 2006, 13, 2429-2441.
    • (2006) Curr. Med. Chem , vol.13 , pp. 2429-2441
    • Makhija, M.T.1
  • 4
    • 33746046396 scopus 로고    scopus 로고
    • The hunt for HIV-1 integrase inhibitors
    • Lataillade, M.; Kozal, M. J. The hunt for HIV-1 integrase inhibitors. AIDS Patient Care STDS 2006, 20, 489-501.
    • (2006) AIDS Patient Care STDS , vol.20 , pp. 489-501
    • Lataillade, M.1    Kozal, M.J.2
  • 5
    • 33644867960 scopus 로고    scopus 로고
    • HIV-1 integrase inhibitors: 2003-2004 update
    • Dayam, R.; Deng, J.; Neamati, N. HIV-1 integrase inhibitors: 2003-2004 update. Med. Res. Rev. 2006, 26, 271-309.
    • (2006) Med. Res. Rev , vol.26 , pp. 271-309
    • Dayam, R.1    Deng, J.2    Neamati, N.3
  • 7
    • 3042843657 scopus 로고    scopus 로고
    • HIV-1 integrase inhibitors: A decade of research and two drugs in clinical trial
    • Johnson, A. A.; Marchand, C.; Pommier, Y. HIV-1 integrase inhibitors: A decade of research and two drugs in clinical trial. Curr. Top. Med. Chem. 2004, 4, 1059-1077.
    • (2004) Curr. Top. Med. Chem , vol.4 , pp. 1059-1077
    • Johnson, A.A.1    Marchand, C.2    Pommier, Y.3
  • 8
    • 0042423356 scopus 로고    scopus 로고
    • Structure-activity relationships of HIV-1 integrase inhibitors: Enzyme-ligand interactions
    • Maurin, C.; Bailly, F.; Cotelle, P. Structure-activity relationships of HIV-1 integrase inhibitors: Enzyme-ligand interactions. Curr. Med. Chem. 2003, 10, 1795-1810.
    • (2003) Curr. Med. Chem , vol.10 , pp. 1795-1810
    • Maurin, C.1    Bailly, F.2    Cotelle, P.3
  • 9
    • 33745666317 scopus 로고    scopus 로고
    • Patented HIV-1 integrase inhibitors (1998-2005). Recent Patents Anti-Infect
    • Cotelle, P. Patented HIV-1 integrase inhibitors (1998-2005). Recent Patents Anti-Infect. Drug Discovery 2006, 1, 1-15.
    • (2006) Drug Discovery , vol.1 , pp. 1-15
    • Cotelle, P.1
  • 11
    • 34147136222 scopus 로고    scopus 로고
    • Safety and efficacy of the HIV-1 integrase inhibitor raltegravir (MK-0518) in treatment-experienced patients with multidrug-resistant virus: A phase II randomised controlled trial
    • Grinsztejn, B.; Nguyen, B. Y.; Katlama, C.; Gatell, J. M.; Lazzarin, A.; Vittecoq, D.; Gonzalez, C. J.; Chen, J.; Harvey, C. M.; Isaacs, R. D. Safety and efficacy of the HIV-1 integrase inhibitor raltegravir (MK-0518) in treatment-experienced patients with multidrug-resistant virus: A phase II randomised controlled trial. Lancet 2007, 369, 1261-1269.
    • (2007) Lancet , vol.369 , pp. 1261-1269
    • Grinsztejn, B.1    Nguyen, B.Y.2    Katlama, C.3    Gatell, J.M.4    Lazzarin, A.5    Vittecoq, D.6    Gonzalez, C.J.7    Chen, J.8    Harvey, C.M.9    Isaacs, R.D.10
  • 13
    • 0000829669 scopus 로고    scopus 로고
    • HIVs and their replication
    • Knipe, D, Howley, P, Eds, Lippincott Williams & Wilkins: Philadelphia
    • Freed, E. O.; Martin, M. A. HIVs and their replication. In Fields Virology; Knipe, D., Howley, P., Eds.; Lippincott Williams & Wilkins: Philadelphia, 2001; pp 1971-2042.
    • (2001) Fields Virology , pp. 1971-2042
    • Freed, E.O.1    Martin, M.A.2
  • 14
    • 0002296754 scopus 로고    scopus 로고
    • Reverse transcriptase and the generation of viral DNA
    • Coffin, J. M, Hughes, S. H, Varmus, H. E, Eds, Cold Spring Harbor Laboratory Press: Plainview, NY
    • Telesnitsky, A.; Goff, S. P. Reverse transcriptase and the generation of viral DNA. In Retroviruses; Coffin, J. M., Hughes, S. H., Varmus, H. E., Eds.; Cold Spring Harbor Laboratory Press: Plainview, NY, 1997; pp 121-160.
    • (1997) Retroviruses , pp. 121-160
    • Telesnitsky, A.1    Goff, S.P.2
  • 16
    • 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, G. L.; Harrison, S. C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug resistance. Science 1998, 282, 1669-1675.
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 17
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, RuvC and RNase H
    • (a) Yang, W.; Steitz, T. A. Recombining the structures of HIV integrase, RuvC and RNase H. Structure 1995, 3, 131-134.
    • (1995) Structure , vol.3 , pp. 131-134
    • Yang, W.1    Steitz, T.A.2
  • 18
    • 0032723359 scopus 로고    scopus 로고
    • Integrating DNA: Transposases and retroviral integrases
    • (b) Haren, L.; Ton-Hoang, B.; Chandler, M. Integrating DNA: Transposases and retroviral integrases. Annu. Rev. Microbiol. 1999, 53, 245-281.
    • (1999) Annu. Rev. Microbiol , vol.53 , pp. 245-281
    • Haren, L.1    Ton-Hoang, B.2    Chandler, M.3
  • 19
    • 6944235757 scopus 로고    scopus 로고
    • Closely related antiretroviral agents as inhibitors of two HIV-1 enzymes, ribonuclease H and integrase: "Killing two birds with one stone
    • Andréola, M. L. Closely related antiretroviral agents as inhibitors of two HIV-1 enzymes, ribonuclease H and integrase: "Killing two birds with one stone". Curr. Pharm. Des. 2004, 10, 3713-3723.
    • (2004) Curr. Pharm. Des , vol.10 , pp. 3713-3723
    • Andréola, M.L.1
  • 20
    • 0025129937 scopus 로고
    • Structure of ribonuclease H phased at 2 Å resolution by MAD analysis of the selenomethionyl protein
    • Yang, W.; Hendrickson, W. A.; Crouch, R. J.; Satow, Y. Structure of ribonuclease H phased at 2 Å resolution by MAD analysis of the selenomethionyl protein. Science 1990, 249, 1398-1405.
    • (1990) Science , vol.249 , pp. 1398-1405
    • Yang, W.1    Hendrickson, W.A.2    Crouch, R.J.3    Satow, Y.4
  • 21
    • 0025908083 scopus 로고
    • Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
    • Davies, J. F., II; Hostomska, Z.; Hostomsky, Z.; Jordan, S. R.; Matthews, D. A. Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase. Science 1991, 252, 88-95.
    • (1991) Science , vol.252 , pp. 88-95
    • Davies II, J.F.1    Hostomska, Z.2    Hostomsky, Z.3    Jordan, S.R.4    Matthews, D.A.5
  • 22
    • 0029786278 scopus 로고    scopus 로고
    • Biochemical analysis of catalytically crucial aspartate mutants of human immunodeficiency virus type 1 reverse transcriptase
    • Kaushik, N.; Rege, N.; Yadav, P. N.; Sarafianos, S. G.; Modak, M. J.; Pandey, V. N. Biochemical analysis of catalytically crucial aspartate mutants of human immunodeficiency virus type 1 reverse transcriptase. Biochemistry 1996, 35, 11536-11546.
    • (1996) Biochemistry , vol.35 , pp. 11536-11546
    • Kaushik, N.1    Rege, N.2    Yadav, P.N.3    Sarafianos, S.G.4    Modak, M.J.5    Pandey, V.N.6
  • 25
    • 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. 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. 2005, 65, 117-124.
    • (2005) Antiviral Res , vol.65 , pp. 117-124
    • Tramontano, E.1    Esposito, F.2    Badas, R.3    Di Santo, R.4    Costi, R.5    La Colla, P.6
  • 29
    • 33645104685 scopus 로고    scopus 로고
    • Preferential inhibition of the magnesium-dependent strand transfer reaction of HIV-1 integrase by α-hydroxytropolones
    • Semenova, E. A.; Johnson, A. A.; Marchand, C.; Davis, D. A.; Yarchoan, R.; Pommier, Y. Preferential inhibition of the magnesium-dependent strand transfer reaction of HIV-1 integrase by α-hydroxytropolones. Mol. Pharmacol. 2006, 69, 1454-1460.
    • (2006) Mol. Pharmacol , vol.69 , pp. 1454-1460
    • Semenova, E.A.1    Johnson, A.A.2    Marchand, C.3    Davis, D.A.4    Yarchoan, R.5    Pommier, Y.6
  • 34
    • 0345314349 scopus 로고
    • N-Hydroxyimides. II
    • Ames, D. E.; Grey, T. F. N-Hydroxyimides. II. J. Chem. Soc. 1955, 351, 3518-3521.
    • (1955) J. Chem. Soc , vol.351 , pp. 3518-3521
    • Ames, D.E.1    Grey, T.F.2
  • 36
    • 0012740193 scopus 로고
    • The synthesis of 7-methoxyisoquinolone
    • Ungnade, H.; Nightingale, D.; French, H. The synthesis of 7-methoxyisoquinolone. J. Org. Chem. 1945, 10, 533-536.
    • (1945) J. Org. Chem , vol.10 , pp. 533-536
    • Ungnade, H.1    Nightingale, D.2    French, H.3
  • 37
    • 84981404701 scopus 로고
    • Zur cycliesierung von salicylsäureamiden und Salicylhydroxamsäuren von 1,1′-carbonyldiimidazol.
    • Geffken, D. Zur cycliesierung von salicylsäureamiden und Salicylhydroxamsäuren von 1,1′-carbonyldiimidazol. Liebigs Ann. Chem. 1981, 1513-1514.
    • (1981) Liebigs Ann. Chem , pp. 1513-1514
    • Geffken, D.1
  • 42
    • 1542286600 scopus 로고    scopus 로고
    • Enzymology of a carbonyl reduction clearance pathway for the HIV integrase inhibitor, S-1360: Role of human liver cytosolic aldo-keto reductases
    • Rosemond, M. J.; St John-Williams, L.; Yamaguchi, T.; Fujishita, T.; Walsh, J. S. Enzymology of a carbonyl reduction clearance pathway for the HIV integrase inhibitor, S-1360: Role of human liver cytosolic aldo-keto reductases. Chem.-Biol. Interact. 2004, 147, 129-139.
    • (2004) Chem.-Biol. Interact , vol.147 , pp. 129-139
    • Rosemond, M.J.1    St John-Williams, L.2    Yamaguchi, T.3    Fujishita, T.4    Walsh, J.S.5
  • 43
    • 33846164748 scopus 로고    scopus 로고
    • Design of second generation HIV-1 integrase inhibitors
    • Deng, J.; Dayam, R.; Al-Mawsawi, L. Q.; Neamati, N. Design of second generation HIV-1 integrase inhibitors. Curr. Pharm. Des. 2007, 13, 129-141.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 129-141
    • Deng, J.1    Dayam, R.2    Al-Mawsawi, L.Q.3    Neamati, N.4
  • 44
    • 0037303182 scopus 로고    scopus 로고
    • S-1360 Shionogi-GlaxoSmithKline
    • Billich, A. S-1360 Shionogi-GlaxoSmithKline. Curr. Opin. Invest. Drugs 2003, 4, 206-209.
    • (2003) Curr. Opin. Invest. Drugs , vol.4 , pp. 206-209
    • Billich, A.1
  • 46
    • 34547583281 scopus 로고    scopus 로고
    • Rationally designed dual inhibitors of HIV-1 reverse transcriptase and integrase
    • Wang, Z.; Bennett, E. M.; Wilson, D. J.; Salomon, C.; Vince, R. Rationally designed dual inhibitors of HIV-1 reverse transcriptase and integrase. J. Med. Chem. 2007, 50, 3416-3419.
    • (2007) J. Med. Chem , vol.50 , pp. 3416-3419
    • Wang, Z.1    Bennett, E.M.2    Wilson, D.J.3    Salomon, C.4    Vince, R.5
  • 50
    • 0034672040 scopus 로고    scopus 로고
    • Rapid microtiter assays for poxvirus topoisomerase, mammalian type IB topoisomerase and HIV-1 integrase: Application to inhibitor isolation
    • Hwang, Y.; Rhodes, D.; Bushman, F. Rapid microtiter assays for poxvirus topoisomerase, mammalian type IB topoisomerase and HIV-1 integrase: Application to inhibitor isolation. Nucleic Acids Res. 2000, 28, 4884-4892.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4884-4892
    • Hwang, Y.1    Rhodes, D.2    Bushman, F.3
  • 53
    • 0024416124 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 RNase H by polysulfated polyanions
    • Moelling, K.; Schulze, T.; Diringer, H. Inhibition of human immunodeficiency virus type 1 RNase H by polysulfated polyanions. J. Virol. 1989, 63, 5489-5491.
    • (1989) J. Virol , vol.63 , pp. 5489-5491
    • Moelling, K.1    Schulze, T.2    Diringer, H.3
  • 54
    • 0033614007 scopus 로고    scopus 로고
    • Cross-linking localization of a HIV-1 reverse transcriptase peptide involved in the binding of primer tRNALys3
    • Dufour, E.; Reinbolt, J.; Castroviejo, M.; Ehresmann, B.; Litvak, S.; Tarrago-Litvak, L.; Andreola, M. L. Cross-linking localization of a HIV-1 reverse transcriptase peptide involved in the binding of primer tRNALys3. J. Mol. Biol. 1999, 285, 1339-1346.
    • (1999) J. Mol. Biol , vol.285 , pp. 1339-1346
    • Dufour, E.1    Reinbolt, J.2    Castroviejo, M.3    Ehresmann, B.4    Litvak, S.5    Tarrago-Litvak, L.6    Andreola, M.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.