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Volumn 20, Issue 7, 2015, Pages 12623-12651

Integrase inhibitor prodrugs: Approaches to enhancing the Anti-HIV activity of β-Diketo acids

Author keywords

Antiviral activity; Hiv 1 integrase inhibitors; Prodrugs

Indexed keywords

INTEGRASE; INTEGRASE INHIBITOR; OXOACID; PRODRUG; PYRIDONE DERIVATIVE;

EID: 84938395278     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules200712623     Document Type: Review
Times cited : (24)

References (73)
  • 2
    • 77954633050 scopus 로고    scopus 로고
    • HIV persistence and the prospect of long-term drug-free remissions for HIV-infected individuals
    • Trono, D.; Van Lint, C.; Rouzioux, C.; Verdin, E.; Barre-Sinoussi, F.; Chun, T.W.; Chomont, N. HIV persistence and the prospect of long-term drug-free remissions for HIV-infected individuals. Science 2010, 329, 174-180.
    • (2010) Science , vol.329 , pp. 174-180
    • Trono, D.1    Van Lint, C.2    Rouzioux, C.3    Verdin, E.4    Barre-Sinoussi, F.5    Chun, T.W.6    Chomont, N.7
  • 3
    • 34447548922 scopus 로고    scopus 로고
    • HIV integrase inhibitors as therapeutic agents in AIDS
    • Nair, V.; Chi, G. HIV integrase inhibitors as therapeutic agents in AIDS. Rev. Med. Virol. 2007, 17, 277-295.
    • (2007) Rev. Med. Virol. , vol.17 , pp. 277-295
    • Nair, V.1    Chi, G.2
  • 4
    • 31544474642 scopus 로고    scopus 로고
    • HIV integrase inhibitors with nucleobase scaffolds: Discovery of a highly potent anti-HIV agent
    • Nair, V.; Chi, G.; Ptak, R.; Neamati, N. HIV integrase inhibitors with nucleobase scaffolds: Discovery of a highly potent anti-HIV agent. J. Med. Chem. 2006, 49, 445-447.
    • (2006) J. Med. Chem. , vol.49 , pp. 445-447
    • Nair, V.1    Chi, G.2    Ptak, R.3    Neamati, N.4
  • 6
    • 31544453250 scopus 로고    scopus 로고
    • Novel inhibitors of HIV integrase: The discovery of potential anti-HIV therapeutic agents
    • Nair, V. Novel inhibitors of HIV integrase: The discovery of potential anti-HIV therapeutic agents. Front. Med. Chem. Online 2005, 2, 3-20.
    • (2005) Front. Med. Chem. Online , vol.2 , pp. 3-20
    • Nair, V.1
  • 8
    • 63849102924 scopus 로고    scopus 로고
    • Quantitative prediction of human clearance guiding the development of raltegravir (MK-0518, Isentress) and related HIV integrase inhibitors
    • Laufer, R.; Paz, O.G.; di Marco, A.; Bonelli, F.; Monteagudo, E.; Summa, V.; Rowley, M. Quantitative prediction of human clearance guiding the development of raltegravir (MK-0518, Isentress) and related HIV integrase inhibitors. Drug Metab. Dispos. 2009, 37, 873-883.
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 873-883
    • Laufer, R.1    Paz, O.G.2    Di Marco, A.3    Bonelli, F.4    Monteagudo, E.5    Summa, V.6    Rowley, M.7
  • 10
    • 73849124557 scopus 로고    scopus 로고
    • Pharmacokinetics and safety of S/GSK1349572, a next-generation HIV integrase inhibitor, in healthy volunteers
    • Min, S.; Song, I.; Borland, J.; Chen, S.G.; Lou, Y.; Fujiwara, T.; Piscitelli, S.C. Pharmacokinetics and safety of S/GSK1349572, a next-generation HIV integrase inhibitor, in healthy volunteers. Antimicrob. Agents Chemother. 2010, 54, 254-258.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 254-258
    • Min, S.1    Song, I.2    Borland, J.3    Chen, S.G.4    Lou, Y.5    Fujiwara, T.6    Piscitelli, S.C.7
  • 11
    • 62249163679 scopus 로고    scopus 로고
    • Elvitegravir, an oral HIV integrase inhibitor, for the potential treatment of HIV infection
    • Klibanov, O.M. Elvitegravir, an oral HIV integrase inhibitor, for the potential treatment of HIV infection. Curr. Opin. Investig. Drugs 2009, 10, 190-200.
    • (2009) Curr. Opin. Investig. Drugs , vol.10 , pp. 190-200
    • Klibanov, O.M.1
  • 12
    • 0032601403 scopus 로고    scopus 로고
    • HIV-1 integrase: Structural organization, conformational changes, and catalysis
    • Asante-Appiah, E.; Skalka, A.M. HIV-1 integrase: Structural organization, conformational changes, and catalysis. Adv. Virus Res. 1999, 52, 351-369.
    • (1999) Adv. Virus Res. , vol.52 , pp. 351-369
    • Asante-Appiah, E.1    Skalka, A.M.2
  • 13
    • 0032601402 scopus 로고    scopus 로고
    • HIV integrase structure and function
    • Esposito, D.; Craigie, R. HIV integrase structure and function. Adv. Virus Res. 1999, 52, 319-333.
    • (1999) Adv. Virus Res. , vol.52 , pp. 319-333
    • Esposito, D.1    Craigie, R.2
  • 15
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • Hare, S.; Gupta, S.S.; Valkov, E.; Engelman, A.; Cherepanov, P. Retroviral intasome assembly and inhibition of DNA strand transfer. Nature 2010, 464, 232-236.
    • (2010) Nature , vol.464 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Valkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 16
    • 0036095978 scopus 로고    scopus 로고
    • HIV integrase as a target for antiviral chemotherapy
    • Nair, V. HIV integrase as a target for antiviral chemotherapy. Rev. Med. Virol. 2002, 12, 179-193.
    • (2002) Rev. Med. Virol. , vol.12 , pp. 179-193
    • Nair, V.1
  • 17
    • 84910629450 scopus 로고    scopus 로고
    • The role of drug transporters in the kidney: Lessons from tenofovir
    • Moss, D.M.; Neary, M.; Owen, A. The role of drug transporters in the kidney: Lessons from tenofovir. Front. Pharmacol. 2014, 5, 248, doi:10.3389/fphar.2014.00248.
    • (2014) Front. Pharmacol. , vol.5 , pp. 248
    • Moss, D.M.1    Neary, M.2    Owen, A.3
  • 18
    • 84884974017 scopus 로고    scopus 로고
    • Cutting-edge view on the current state of antiviral drug development
    • De Clercq, E. A Cutting-edge view on the current state of antiviral drug development. Med. Res. Rev. 2013, 33, 1249-1277.
    • (2013) Med. Res. Rev. , vol.33 , pp. 1249-1277
    • De Clercq, E.A.1
  • 19
    • 84886096395 scopus 로고    scopus 로고
    • Prodrug strategies for improved efficacy of nucleoside antiviral inhibitors
    • Hurwitz, S.J.; Schinazi, R.F. Prodrug strategies for improved efficacy of nucleoside antiviral inhibitors. Curr. Opin. HIV AIDS 2013, 8, 556-564.
    • (2013) Curr. Opin. HIV AIDS , vol.8 , pp. 556-564
    • Hurwitz, S.J.1    Schinazi, R.F.2
  • 20
    • 84930902992 scopus 로고    scopus 로고
    • HIV treatment 2020: What will it look like?
    • Gulick, R. HIV treatment 2020: What will it look like? J. Int. AIDS Soc. 2014, 17, doi:10.7448/IAS.17.4.19528.
    • (2014) J. Int. AIDS Soc. , vol.17
    • Gulick, R.1
  • 22
    • 84938402428 scopus 로고    scopus 로고
    • Prodrugs in the treatment of viral diseases
    • Sofia, M.J. Prodrugs in the treatment of viral diseases. RSC Drug Discov. Ser. 2013, 32, 421-450.
    • (2013) RSC Drug Discov. Ser. , vol.32 , pp. 421-450
    • Sofia, M.J.1
  • 23
    • 14944344464 scopus 로고    scopus 로고
    • New approaches toward anti-HIV chemotherapy
    • De Clercq, E. New approaches toward anti-HIV chemotherapy. J. Med. Chem. 2005, 48, 1297-1313.
    • (2005) J. Med. Chem. , vol.48 , pp. 1297-1313
    • De Clercq, E.1
  • 25
    • 0034697650 scopus 로고    scopus 로고
    • Recognition and inhibition of HIV integrase by novel dinucleotides
    • Taktakishvili, M.; Neamati, N.; Pommier, Y.; Pal, S.; Nair, V. Recognition and inhibition of HIV integrase by novel dinucleotides. J. Am. Chem. Soc. 2000, 122, 5671-5677.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5671-5677
    • Taktakishvili, M.1    Neamati, N.2    Pommier, Y.3    Pal, S.4    Nair, V.5
  • 32
    • 0037303182 scopus 로고    scopus 로고
    • S-1360 Shionogi-GlaxoSmithKline
    • Billich, A. S-1360 Shionogi-GlaxoSmithKline. Curr. Opin. Investig. Drugs 2003, 4, 206-209.
    • (2003) Curr. Opin. Investig. Drugs , vol.4 , pp. 206-209
    • Billich, A.1
  • 38
    • 0008293521 scopus 로고    scopus 로고
    • Retroviral integrase: A novel target in antiviral drug development and basic in vitro assays with purified enzyme in
    • Kinchington, D., Schinazi, R., Eds.; Humana: Totowa, NJ, USA
    • Mazumder, A.; Neamati, N.; Sundar, S.; Owen, J.; Pommier, Y. Retroviral integrase: A novel target in antiviral drug development and basic in vitro assays with purified enzyme in. In Antiviral Methods and Protocols; Kinchington, D., Schinazi, R., Eds.; Humana: Totowa, NJ, USA, 1999; Volume 24, pp. 327-338.
    • (1999) Antiviral Methods and Protocols , vol.24 , pp. 327-338
    • Mazumder, A.1    Neamati, N.2    Sundar, S.3    Owen, J.4    Pommier, Y.5
  • 40
    • 84858256291 scopus 로고    scopus 로고
    • Diketoacid inhibitors of HIV-1 integrase: From L-708,906 to raltegravir and beyond
    • Beare, K.D.; Coster, M.J.; Rutledge, P.J. Diketoacid inhibitors of HIV-1 integrase: From L-708,906 to raltegravir and beyond. Curr. Med. Chem. 2012, 19, 1177-1192.
    • (2012) Curr. Med. Chem. , vol.19 , pp. 1177-1192
    • Beare, K.D.1    Coster, M.J.2    Rutledge, P.J.3
  • 41
    • 79955870873 scopus 로고    scopus 로고
    • Binding modes of diketo-acid inhibitors of HIV-1 integrase: A comparative molecular dynamics simulation study
    • Huang, M.; Grant, G.H.; Richards, W.G. Binding modes of diketo-acid inhibitors of HIV-1 integrase: A comparative molecular dynamics simulation study. J. Mol. Graph. Model. 2011, 29, 956-964.
    • (2011) J. Mol. Graph. Model. , vol.29 , pp. 956-964
    • Huang, M.1    Grant, G.H.2    Richards, W.G.3
  • 42
    • 0034871310 scopus 로고    scopus 로고
    • Specific inhibition of human immunodeficiency virus type 1 (HIV-1) integration in cell culture: Putative inhibitors of HIV-1 integrase
    • Vandegraaff, N.; Kumar, R.; Hocking, H.; Burke, T.R.; Mills, J.; Rhodes, D.; Burrell, C.J.; Li, P. Specific inhibition of human immunodeficiency virus type 1 (HIV-1) integration in cell culture: Putative inhibitors of HIV-1 integrase. Antimicrob. Agents Chemother. 2001, 45, 2510-2516.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 2510-2516
    • Vandegraaff, N.1    Kumar, R.2    Hocking, H.3    Burke, T.R.4    Mills, J.5    Rhodes, D.6    Burrell, C.J.7    Li, P.8
  • 43
    • 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.C.; 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.C.1    St John-Williams, L.2    Yamaguchi, T.3    Fujishita, T.4    Walsh, J.S.5
  • 46
    • 33645405333 scopus 로고    scopus 로고
    • Novel bifunctional quinolonyl diketo acid derivatives as HIV-1 integrase inhibitors: Design, synthesis, biological activities, and mechanism of action
    • Di Santo, R.; Costi, R.; Roux, A.; Artico, M.; Lavecchia, A.; Marinelli, L.; Novellino, E.; Palmisano, L.; Andreotti, M.; Amici, R.; et al. Novel bifunctional quinolonyl diketo acid derivatives as HIV-1 integrase inhibitors: Design, synthesis, biological activities, and mechanism of action. J. Med. Chem. 2006, 49, 1939-1945.
    • (2006) J. Med. Chem. , vol.49 , pp. 1939-1945
    • Di Santo, R.1    Costi, R.2    Roux, A.3    Artico, M.4    Lavecchia, A.5    Marinelli, L.6    Novellino, E.7    Palmisano, L.8    Andreotti, M.9    Amici, R.10
  • 47
    • 2342561153 scopus 로고    scopus 로고
    • Rational design and synthesis of novel dimeric diketoacid-containing inhibitors of HIV-1 integrase: Implication for binding to two metal ions on the active site of integrase
    • Long, Y.Q.; Jiang, X.H.; Dayam, R.; Sanchez, T.; Shoemaker, R.; Sei, S.; Neamati, N. Rational design and synthesis of novel dimeric diketoacid-containing inhibitors of HIV-1 integrase: Implication for binding to two metal ions on the active site of integrase. J. Med. Chem. 2004, 47, 2561-2573.
    • (2004) J. Med. Chem. , vol.47 , pp. 2561-2573
    • Long, Y.Q.1    Jiang, X.H.2    Dayam, R.3    Sanchez, T.4    Shoemaker, R.5    Sei, S.6    Neamati, N.7
  • 48
    • 49149122931 scopus 로고    scopus 로고
    • Novel dimeric aryldiketo containing inhibitors of HIV-1 integrase: Effects of the phenyl substituent and the linker orientation
    • Zeng, L.F.; Jiang, X.H.; Sanchez, T.; Zhang, H.S.; Dayam, R.; Neamati, N.; Long, Y.Q. Novel dimeric aryldiketo containing inhibitors of HIV-1 integrase: Effects of the phenyl substituent and the linker orientation. Bioorg. Med. Chem. 2008, 16, 7777-7787.
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 7777-7787
    • Zeng, L.F.1    Jiang, X.H.2    Sanchez, T.3    Zhang, H.S.4    Dayam, R.5    Neamati, N.6    Long, Y.Q.7
  • 49
    • 33845944851 scopus 로고    scopus 로고
    • Novel HIV integrase inhibitors with anti-HIV activity: Insights into integrase inhibition from docking studies
    • Cox, A.G.; Nair, V. Novel HIV integrase inhibitors with anti-HIV activity: Insights into integrase inhibition from docking studies. Antivir. Chem. Chemother. 2006, 17, 343-353.
    • (2006) Antivir. Chem. Chemother. , vol.17 , pp. 343-353
    • Cox, A.G.1    Nair, V.2
  • 50
    • 33846913023 scopus 로고    scopus 로고
    • A novel diketo phosphonic acid that exhibits specific, strand-transfer inhibition of HIV integrase and anti-HIV activity
    • Chi, G.C.; Nair, V.; Semenova, E.; Pommier, Y. A novel diketo phosphonic acid that exhibits specific, strand-transfer inhibition of HIV integrase and anti-HIV activity. Bioorg. Med. Chem. Lett. 2007, 17, 1266-1269.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 1266-1269
    • Chi, G.C.1    Nair, V.2    Semenova, E.3    Pommier, Y.4
  • 51
    • 33144458429 scopus 로고    scopus 로고
    • beta-Diketo acids with purine nucleobase scaffolds: Novel, selective inhibitors of the strand transfer step of HIV integrase
    • Nair, V.; Uchil, V.; Neamati, N. beta-Diketo acids with purine nucleobase scaffolds: Novel, selective inhibitors of the strand transfer step of HIV integrase. Bioorg. Med. Chem. Lett. 2006, 16, 1920-1923.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 1920-1923
    • Nair, V.1    Uchil, V.2    Neamati, N.3
  • 53
    • 0002356855 scopus 로고
    • A new method for acylation of enolates by means of dialkyl acylphosphonates as acylating agents
    • Sekine, M.; Kume, A.; Nakajima, M.; Hata, T. A new method for acylation of enolates by means of dialkyl acylphosphonates as acylating agents. Chem. Lett. 1981, 10, 1087-1090.
    • (1981) Chem. Lett. , vol.10 , pp. 1087-1090
    • Sekine, M.1    Kume, A.2    Nakajima, M.3    Hata, T.4
  • 54
    • 0001743806 scopus 로고
    • A selective method for the direct conversion of aldehydes into beta-keto-esters with ethyl diazoacetate catalyzed by Tin(II)
    • Holmquist, C.R.; Roskamp, E.J. A selective method for the direct conversion of aldehydes into beta-keto-esters with ethyl diazoacetate catalyzed by Tin(II) Chloride. J. Org. Chem. 1989, 54, 3258-3260.
    • (1989) Chloride. J. Org. Chem. , vol.54 , pp. 3258-3260
    • Holmquist, C.R.1    Roskamp, E.J.2
  • 55
    • 37049072636 scopus 로고
    • Acylphosphonic acids and methyl hydrogen acylphosphonates-physical and chemical-properties and theoretical calculations
    • Karaman, R.; Goldblum, A.; Breuer, E.; Leader, H. Acylphosphonic acids and methyl hydrogen acylphosphonates-physical and chemical-properties and theoretical calculations. J. Chem. Soc. Perkin Trans. 1 1989, 4, 765-774.
    • (1989) J. Chem. Soc. Perkin Trans. 1 , vol.4 , pp. 765-774
    • Karaman, R.1    Goldblum, A.2    Breuer, E.3    Leader, H.4
  • 57
    • 0011956364 scopus 로고
    • Effect of fluorine substitution on phenol acidities in the gas-phase and in aqueous-solution - A computational study using continuum solvation models
    • Urban, J.J.; Vontersch, R.L.; Famini, G.R. Effect of fluorine substitution on phenol acidities in the gas-phase and in aqueous-solution - A computational study using continuum solvation models. J. Org. Chem. 1994, 59, 5239-5245.
    • (1994) J. Org. Chem. , vol.59 , pp. 5239-5245
    • Urban, J.J.1    Vontersch, R.L.2    Famini, G.R.3
  • 58
    • 0027432004 scopus 로고
    • Synthesis of chiral and bioactive fluoroorganic compounds
    • Resnati, G. Synthesis of chiral and bioactive fluoroorganic compounds. Tetrahedron 1993, 49, 9385-9445.
    • (1993) Tetrahedron , vol.49 , pp. 9385-9445
    • Resnati, G.1
  • 59
    • 33746610484 scopus 로고    scopus 로고
    • The strength of weak interactions: Aromatic fluorine in drug design
    • DiMagno, S.G.; Sun, H.R. The strength of weak interactions: Aromatic fluorine in drug design. Curr. Top. Med. Chem. 2006, 6, 1473-1482.
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 1473-1482
    • DiMagno, S.G.1    Sun, H.R.2
  • 60
    • 84863823336 scopus 로고    scopus 로고
    • 3′-Processing and strand transfer catalysed by retroviral integrase in crystallo
    • Hare, S.; Maertens, G.N.; Cherepanov, P. 3′-Processing and strand transfer catalysed by retroviral integrase in crystallo. EMBO J. 2012, 31, 3020-3028.
    • (2012) EMBO J. , vol.31 , pp. 3020-3028
    • Hare, S.1    Maertens, G.N.2    Cherepanov, P.3
  • 63
    • 83455170860 scopus 로고
    • Reactions of 2-aminopyridine with benzyl-chloride - Benzylation of pyridine ring
    • Kowalski, P. Reactions of 2-aminopyridine with benzyl-chloride - benzylation of pyridine ring. Pol. J. Chem. 1984, 58, 959-960.
    • (1984) Pol. J. Chem. , vol.58 , pp. 959-960
    • Kowalski, P.1
  • 64
    • 0023233102 scopus 로고
    • Novel approaches to functionalized nucleosides via palladium-catalyzed cross coupling with organostannanes
    • Nair, V.; Turner, G.A.; Chamberlain, S.D. Novel approaches to functionalized nucleosides via palladium-catalyzed cross coupling with organostannanes. J. Am. Chem. Soc. 1987, 109, 7223-7224.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 7223-7224
    • Nair, V.1    Turner, G.A.2    Chamberlain, S.D.3
  • 65
    • 0023753835 scopus 로고
    • New methodologies for the synthesis of C-2 functionalized hypoxanthine nucleosides
    • Nair, V.; Turner, G.A.; Buenger, G.S.; Chamberlain, S.D. new methodologies for the synthesis of C-2 functionalized hypoxanthine nucleosides. J. Org. Chem. 1988, 53, 3051-3057.
    • (1988) J. Org. Chem. , vol.53 , pp. 3051-3057
    • Nair, V.1    Turner, G.A.2    Buenger, G.S.3    Chamberlain, S.D.4
  • 66
    • 0141789700 scopus 로고    scopus 로고
    • Highly efficient preparation of aryl beta-diketo acids with tert-butyl methyl oxalate
    • Jiang, X.H.; Song, L.D.; Long, Y.Q. Highly efficient preparation of aryl beta-diketo acids with tert-butyl methyl oxalate. J. Org. Chem. 2003, 68, 7555-7558.
    • (2003) J. Org. Chem. , vol.68 , pp. 7555-7558
    • Jiang, X.H.1    Song, L.D.2    Long, Y.Q.3
  • 67
    • 35548969410 scopus 로고    scopus 로고
    • A novel strategy to assemble the beta-diketo acid pharmacophore of HIV integrase inhibitors on purine nucleobase scaffolds
    • Uchil, V.; Seo, B.; Nair, V. A novel strategy to assemble the beta-diketo acid pharmacophore of HIV integrase inhibitors on purine nucleobase scaffolds. J. Org. Chem. 2007, 72, 8577-8579.
    • (2007) J. Org. Chem. , vol.72 , pp. 8577-8579
    • Uchil, V.1    Seo, B.2    Nair, V.3
  • 70
    • 33748636018 scopus 로고    scopus 로고
    • Introduction to in vitro estimation of metabolic stability and drug interactions of new chemical entities in drug discovery and development
    • Baranczewski, P.; Stanczak, A.; Sundberg, K.; Svensson, R.; Wallin, A.; Jansson, J.; Garberg, P.; Postlind, H. Introduction to in vitro estimation of metabolic stability and drug interactions of new chemical entities in drug discovery and development. Pharmacol. Rep. 2006, 58, 453-472.
    • (2006) Pharmacol. Rep. , vol.58 , pp. 453-472
    • Baranczewski, P.1    Stanczak, A.2    Sundberg, K.3    Svensson, R.4    Wallin, A.5    Jansson, J.6    Garberg, P.7    Postlind, H.8
  • 71
    • 0030812882 scopus 로고    scopus 로고
    • In vitro comparison of cytochrome P450-mediated metabolic activities in human, dog, cat, and horse
    • Chauret, N.; Gauthier, A.; Martin, J.; NicollGriffith, D.A. In vitro comparison of cytochrome P450-mediated metabolic activities in human, dog, cat, and horse. Drug Metab. Dispos. 1997, 25, 1130-1136.
    • (1997) Drug Metab. Dispos. , vol.25 , pp. 1130-1136
    • Chauret, N.1    Gauthier, A.2    Martin, J.3    NicollGriffith, D.A.4
  • 72
    • 6944221357 scopus 로고    scopus 로고
    • Drug-drug interactions for UDP-glucuronosyltransferase substrates: A pharmacokinetic explanation for typically observed low exposure (AUC(i)/AUC) ratios
    • Williams, J.A.; Hyland, R.; Jones, B.C.; Smith, D.A.; Hurst, S.; Goosen, T.C.; Peterkin, V.; Koup, J.R.; Ball, S.E. Drug-drug interactions for UDP-glucuronosyltransferase substrates: A pharmacokinetic explanation for typically observed low exposure (AUC(i)/AUC) ratios. Drug Metab. Dispos. 2004, 32, 1201-1208.
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 1201-1208
    • Williams, J.A.1    Hyland, R.2    Jones, B.C.3    Smith, D.A.4    Hurst, S.5    Goosen, T.C.6    Peterkin, V.7    Koup, J.R.8    Ball, S.E.9
  • 73
    • 84877244757 scopus 로고    scopus 로고
    • A novel anti-HIV active integrase inhibitor with a favorable in vitro cytochrome P-450 and uridine 5′-diphospho-glucuronosyltransferase metabolism profile
    • Okello, M.O.; Mishra, S.; Nishonov, M.; Mankowski, M.K.; Russell, J.D.; Wei, J.; Hogan, P.A.; Ptak, R.G.; Nair, V. A novel anti-HIV active integrase inhibitor with a favorable in vitro cytochrome P-450 and uridine 5′-diphospho-glucuronosyltransferase metabolism profile. Antivir. Res. 2013, 98, 365-372.
    • (2013) Antivir. Res. , vol.98 , pp. 365-372
    • Okello, M.O.1    Mishra, S.2    Nishonov, M.3    Mankowski, M.K.4    Russell, J.D.5    Wei, J.6    Hogan, P.A.7    Ptak, R.G.8    Nair, V.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.