메뉴 건너뛰기




Volumn 18, Issue 22, 2011, Pages 3335-3342

Diketo acids derivatives as dual inhibitors of human immunodeficiency virus type 1 integrase and the reverse transcriptase RNase H Domain

Author keywords

Diketo acids; Dual inhibitors; HIV 1; IN inhibitor; Integrase; Pyrrole derivatives; Quinolinone drivatives; Reverse transcriptase; Ribonuclease H; RNase H; RNase H inhibitor

Indexed keywords

DIKETO ACID DERIVATIVE; DNA DIRECTED DNA POLYMERASE; DOUBLE STRANDED DNA; ELVITEGRAVIR; INTEGRASE INHIBITOR; OXOACID; RALTEGRAVIR; RIBONUCLEASE H; RIBONUCLEASE H INHIBITOR; RNA DIRECTED DNA POLYMERASE; RNA DIRECTED DNA POLYMERASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 79961078738     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/092986711796504619     Document Type: Conference Paper
Times cited : (32)

References (63)
  • 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
    • DOI 10.1006/jmbi.1998.2002
    • 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. (Pubitemid 28418789)
    • (1998) Journal of Molecular Biology , vol.282 , Issue.2 , pp. 359-368
    • Maignan, S.1    Guilloteau, J.-P.2    Zhou-Liu, Q.3    Clement-Mella, C.4    Mikol, V.5
  • 3
    • 0030746054 scopus 로고    scopus 로고
    • Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity
    • DOI 10.1074/jbc.272.29.18161
    • Bujacz, G.; Alexandratos, J.; Wlodawer, A.; Merkel, G.; Andrake, M.; Katz, R.A.; Skalka, A.M. Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity. J. Biol. Chem., 1997, 272, 18161-18168. (Pubitemid 27306402)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.29 , pp. 18161-18168
    • Bujacz, G.1    Alexandratos, J.2    Wlodawer, A.3    Merkel, G.4    Andrake, M.5    Katz, R.A.6    Skalka, A.M.7
  • 4
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, RuvC and RNase H
    • 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
  • 5
    • 0026019625 scopus 로고
    • Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism
    • Beese, L.S.; Steitz, T.A. Structural basis for the 3'-5'exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. EMBO J., 1991, 10, 25-33. (Pubitemid 21905263)
    • (1991) EMBO Journal , vol.10 , Issue.1 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 9
    • 3042843657 scopus 로고    scopus 로고
    • HIV-1 integrase inhibitors: A decade of research and two drugs in clinical trial
    • DOI 10.2174/1568026043388394
    • 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. (Pubitemid 38854857)
    • (2004) Current Topics in Medicinal Chemistry , vol.4 , Issue.10 , pp. 1059-1077
    • Johnson, A.A.1    Marchand, C.2    Pommier, Y.3
  • 10
    • 33644867960 scopus 로고    scopus 로고
    • HIV-1 integrase inhibitors: 2003-2004
    • Dayam, R.; Deng, J.; Neamati, N. HIV-1 integrase inhibitors: 2003-2004 update. Med. Res. Rev., 2006, 26, 271-309.
    • Med. Res. Rev. , vol.2006 , Issue.26 , pp. 271-309
    • Dayam, R.1    Deng, J.2    Neamati, N.3
  • 11
    • 33746888209 scopus 로고    scopus 로고
    • Designing HIV integrase inhibitors-shooting the last arrow
    • DOI 10.2174/092986706777935096
    • Makhija, M.T. Designing HIV integrase inhibitors: Shooting the last arrow. Curr. Med. Chem., 2006, 13, 2429-2441. (Pubitemid 44184645)
    • (2006) Current Medicinal Chemistry , vol.13 , Issue.20 , pp. 2429-2441
    • Makhija, M.T.1
  • 12
    • 33746046396 scopus 로고    scopus 로고
    • The hunt for HIV-1 integrase inhibitors
    • DOI 10.1089/apc.2006.20.489
    • Lataillade, M.; Kozal, M.J. The hunt for HIV-1 integrase inhibitors. AIDS Patient Care STDS, 2006, 20, 489-501. (Pubitemid 44078768)
    • (2006) AIDS Patient Care and STDs , vol.20 , Issue.7 , pp. 489-501
    • Lataillade, M.1    Kozal, M.J.2
  • 13
    • 0042423356 scopus 로고    scopus 로고
    • Structure-activity relationships of HIV-1 integrase inhibitors - Enzyme-ligand interactions
    • DOI 10.2174/0929867033456981
    • Maurin, C.; Bailly, F.; Cotelle, P. Structure-activity relationships of HIV-1 integrase inhibitors: enzyme-ligand interactions. Curr. Med. Chem., 2003, 10, 1795-1810. (Pubitemid 37038601)
    • (2003) Current Medicinal Chemistry , vol.10 , Issue.18 , pp. 1795-1810
    • Maurin, C.1    Bailly, F.2    Cotelle, P.3
  • 15
    • 0041488800 scopus 로고    scopus 로고
    • Small-molecule HIV-1 integrase inhibitors: The 2001-2002
    • Dayam, R.; Neamati, N. Small-molecule HIV-1 integrase inhibitors: the 2001-2002 update. Curr. Pharm. Des., 2003, 9, 1789-1802.
    • Curr. Pharm. Des. , vol.2003 , Issue.9 , pp. 1789-1802
    • Dayam, R.1    Neamati, N.2
  • 16
    • 0036107683 scopus 로고    scopus 로고
    • Patented small molecule inhibitors of HIV-1 integrase: A 10-year saga
    • DOI 10.1517/13543776.12.5.709
    • Neamati, N. Patented small molecules inhibitors of HIV-1 integrase: a 10- year saga. Expert Opin. Ther. Patents, 2002, 12, 709-724. (Pubitemid 34537680)
    • (2002) Expert Opinion on Therapeutic Patents , vol.12 , Issue.5 , pp. 709-724
    • Neamati, N.1
  • 18
    • 0034911386 scopus 로고    scopus 로고
    • Inhibition of HIV-1 integrase by small molecules: The potential for a new class of AIDS chemotherapeutics
    • Young, S.D. Inhibition of HIV-1 integrase by small molecules: the potential for a new class of AIDS chemotherapeutics. Curr. Opin. Drug Discov. Devel., 2001, 4, 402-410. (Pubitemid 32678529)
    • (2001) Current Opinion in Drug Discovery and Development , vol.4 , Issue.4 , pp. 402-410
    • Young, S.D.1
  • 20
    • 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
    • DOI 10.1016/S0140-6736(07)60597-2, PII S0140673607605972
    • 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 treatmentexperienced patients with multidrug-resistant virus: A phase II randomized controlled trial. Lancet, 2007, 369, 1261-1269. (Pubitemid 46553846)
    • (2007) Lancet , vol.369 , Issue.9569 , 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
  • 24
    • 0002296754 scopus 로고    scopus 로고
    • Coffin, J.M.; Hughes, H; Varmus, H.E. Eds., Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY
    • Telesnitsky, A.; Goff, S.P. in Retroviruses, Coffin, J.M.; Hughes, H; Varmus, H.E. Eds., Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, 1997, pp. 121-160.
    • (1997) Retroviruses , pp. 121-160
    • Telesnitsky, A.1    Goff, S.P.2
  • 25
    • 0002615512 scopus 로고    scopus 로고
    • Crouch, R.J; Toulmé, J.J. Eds. Les Editions Inserm: Paris
    • Hughes, S.H.; Arnold, E.; Hostomsky, Z. In Ribonucleases H, Crouch, R.J; Toulmé, J.J. Eds. Les Editions Inserm: Paris, 1998; pp.195-224.
    • (1998) Ribonucleases H , pp. 195-224
    • Hughes, S.H.1    Arnold, E.2    Hostomsky, Z.3
  • 27
    • 0032723359 scopus 로고    scopus 로고
    • Integrating DNA: Transposases and retroviral integrases
    • DOI 10.1146/annurev.micro.53.1.245
    • Haren, L.; Ton-Hoang, B.; Chandler, M. Integrating DNA: Transposases and retroviral integrases. Annu. Rev. Microbiol., 1999, 53, 245-281. (Pubitemid 29503732)
    • (1999) Annual Review of Microbiology , vol.53 , pp. 245-281
    • Haren, L.1    Ton-Hoang, B.2    Chandler, M.3
  • 29
    • 33646497669 scopus 로고    scopus 로고
    • Recent progress in the design of small molecule inhibitors of HIV RNase H
    • Klumpp, K.; Mirzadegan, T. Recent progress in the design of small molecule inhibitors of HIV RNase H. Curr. Pharm. Drug, 2006, 12, 1909-1922.
    • (2006) Curr. Pharm. Drug , vol.12 , pp. 1909-1922
    • Klumpp, K.1    Mirzadegan, T.2
  • 30
    • 0032545251 scopus 로고    scopus 로고
    • Activation/attenuation model for RNase H. A one-metal mechanism with second-metal inhibition
    • Keck, J.L.; Goedken, E.R.; Marqusee, S. Activation/attenuation model for RNase H. A one-metal mechanism with second-metal inhibition. J. Biol. Chem., 1998, 273, 34128-34133.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34128-34133
    • Keck, J.L.1    Goedken, E.R.2    Marqusee, S.3
  • 31
    • 0027377121 scopus 로고
    • Crystal structure of Escherichia coli RNase HI in complex with Mg2+ at 2.8 A resolution: Proof for a single Mg(2+)-binding site
    • Katayanagi, K.; Okumura, M.; Morikawa, K. Crystal structure of Escherichia coli RNase HI in complex with Mg2+ at 2.8 A resolution: proof for a single Mg(2+)-binding site. Proteins, 1993, 17, 337-347.
    • (1993) Proteins , vol.17 , pp. 337-347
    • Katayanagi, K.1    Okumura, M.2    Morikawa, K.3
  • 32
    • 0025093302 scopus 로고
    • Site-directed mutagenesis of the conserved Asp-443 and Asp-498 carboxy-terminal residues of HIV-1 reverse transcriptase
    • Mizrahi, V.; Usdin, M.; Harington, A.; Dudding, L. Site-directed mutagenesis of the conserved Asp-443 and Asp-498 carboxy-terminal residues of HIV-1 reverse transcriptase. Nucleic Acids Res., 1990, 18, 5359-5363.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5359-5363
    • Mizrahi, V.1    Usdin, M.2    Harington, A.3    Dudding, L.4
  • 33
    • 0028016271 scopus 로고
    • Mutagenesis of the conserved aspartic acid 443, glutamic acid 478, asparagine 494, and aspartic acid 498 residues in the ribonuclease H domain of p66/p51 human immunodeficiency virus type i reverse transcriptase. Expression and biochemical analysis
    • Mizrahi, V.; Brooksbank, R.; Nkabinde, N. Mutagenesis of the conserved aspartic acid 443, glutamic acid 478, asparagine 494, and aspartic acid 498 residues in the ribonuclease H domain of p66/p51 human immunodeficiency virus type I reverse transcriptase. Expression and biochemical analysis. J. Biol. Chem., 1994, 269, 19245-19249.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19245-19249
    • Mizrahi, V.1    Brooksbank, R.2    Nkabinde, N.3
  • 34
    • 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
  • 35
    • 0025129937 scopus 로고
    • Structure of ribonuclease H phased at 2 A 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 A 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
  • 36
    • 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. (Pubitemid 21916941)
    • (1991) Science , vol.252 , Issue.5002 , pp. 88-95
    • Davies III, J.F.1    Hostomska, Z.2    Hostomsky, Z.3    Jordan, S.R.4    Matthews, D.A.5
  • 37
    • 43049106403 scopus 로고    scopus 로고
    • Novel HIV-1 reverse transcriptase inhibitors
    • Jochmans, D. Novel HIV-1 reverse transcriptase inhibitors. Virus Res., 2008, 134, 171-185.
    • (2008) Virus Res. , vol.134 , pp. 171-185
    • Jochmans, D.1
  • 38
    • 61449189645 scopus 로고    scopus 로고
    • Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV
    • De Clercq, E. Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV. Int. J. Antimicrob. Agents, 2009, 33, 307-320.
    • (2009) Int. J. Antimicrob. Agents , vol.33 , pp. 307-320
    • De Clercq, E.1
  • 39
    • 77955648999 scopus 로고    scopus 로고
    • HIV-1 RT-associated RNase H function inhibitors: Recent advances in drug development
    • Tramontano, E.; Di Santo, R. HIV-1 RT-associated RNase H function inhibitors: recent advances in drug development. Curr. Med. Chem., 2010, 17, 2837-2853.
    • (2010) Curr. Med. Chem. , vol.17 , pp. 2837-2853
    • Tramontano, E.1    Di Santo, R.2
  • 41
    • 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
    • DOI 10.1016/j.antiviral.2004.11.002
    • 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. (Pubitemid 40222288)
    • (2005) Antiviral Research , 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
  • 45
    • 33645104685 scopus 로고    scopus 로고
    • Preferential inhibition of the magnesiumdependent strand transfer reaction of HIV-1 integrase byα-hydroxytropolones
    • Semenova, E.A.; Johnson, A.A.; Marchand, C.; Davis, D.A.; Yarchoan, R.; Pommier, Y. Preferential inhibition of the magnesiumdependent strand transfer reaction of HIV-1 integrase byα-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
  • 47
    • 33745107517 scopus 로고    scopus 로고
    • HIV-1 RNase H: Recent progress in an exciting, yet little explored, drug target
    • DOI 10.2174/138955706777435733
    • Tramontano, E. HIV-1 RNase H: recent progress in an exciting, yet little explored, drug target Mini-Rev. Med. Chem., 2006, 6, 727-737. (Pubitemid 43881124)
    • (2006) Mini-Reviews in Medicinal Chemistry , vol.6 , Issue.6 , pp. 727-737
    • Tramontano, E.1
  • 48
    • 15144355755 scopus 로고    scopus 로고
    • Geometrically and conformationally restrained cinnamoyl compounds as inhibitors of HIV-1 integrase: Synthesis, biological evaluation, and molecular modeling
    • DOI 10.1021/jm9707232
    • Artico, M.; Di Santo, R.; Costi, R.; Novellino, E.; Greco, G.; Massa, S.; Tramontano, E.; Marongiu, M.E.; De Montis, A.; La Colla, P. Geometrically and conformationally restrained cinnamoyl-compounds as inhibitors of HIV- 1 integrase: synthesis, biological evaluation and molecular modeling. J. Med. Chem., 1998, 41, 3948-3960. (Pubitemid 28483472)
    • (1998) Journal of Medicinal Chemistry , vol.41 , Issue.21 , pp. 3948-3960
    • Artico, M.1    Santo, R.D.2    Costi, R.3    Novellino, E.4    Greco, G.5    Massa, S.6    Tramontane, E.7    Marongiu, M.E.8    De Montis, A.9    Colla, P.L.10
  • 49
    • 0347301799 scopus 로고    scopus 로고
    • 2,6-Bis(3,4,5-trihydroxybenzylydene) derivatives of cyclohexanone: Novel potent HIV-1 integrase inhibitors that prevent HIV-1 multiplication in cell-based assays
    • DOI 10.1016/j.bmc.2003.10.005
    • Costi, R.; Di Santo R.; Artico, M.; Massa, S.; Ragno, R.; Loddo, R.; La Colla, M.; Tramomtano, E.; La Colla, P.; Pani, A. 2,6-Bis(3,4,5- trihydroxybenzylidene) derivatives of cyclohexanone: novel potent HIV-1 integrase inhibitors that prevent HIV-1 multiplication in cell-based assays. Bioorg. Med. Chem., 2004, 12, 199-215. (Pubitemid 38096232)
    • (2004) Bioorganic and Medicinal Chemistry , vol.12 , Issue.1 , pp. 199-215
    • Costi, R.1    Di Santo, R.2    Artico, M.3    Massa, S.4    Ragno, R.5    Loddo, R.6    La Colla, M.7    Tramontano, E.8    La Colla, P.9    Pani, A.10
  • 53
    • 0037317788 scopus 로고    scopus 로고
    • HIV-1 integrase inhibitors that block HIV-1 replication in infected cells. Planning synthetic derivatives from natural products
    • Di Santo, R.; Costi, R.; Artico, M.; Tramontano, E.; La Colla, P.; Pani, A. HIV-1 integrase inhibitors that block HIV-1 replication in infected cells. Planning synthetic derivatives from natural products. Pure Appl. Chem., 2003, 75, 195-206.
    • (2003) Pure Appl. Chem. , vol.75 , pp. 195-206
    • Di Santo, R.1    Costi, R.2    Artico, M.3    Tramontano, E.4    La Colla, P.5    Pani, A.6
  • 54
    • 19544380093 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of heteroaryl diketohexenoic and diketobutanoic acids as HIV-1 integrase inhibitors endowed with antiretroviral activity
    • DOI 10.1016/j.farmac.2005.03.008, PII S0014827X05000613
    • Di Santo, R.; Costi, R.; Artico, M.; Ragno, R.; Greco, G.; Novellino, E.; Marchand, C.; Pommier, Y. Design, synthesis and biological evaluation of heteroaryl diketohexenoic and diketobutanoic acids as HIV-1 integrase inhibitors endowed with antiretroviral activity. Il Farmaco, 2005, 60, 409-417. (Pubitemid 40731526)
    • (2005) Farmaco , vol.60 , Issue.5 , pp. 409-417
    • Di Santo, R.1    Costi, R.2    Artico, M.3    Ragno, R.4    Greco, G.5    Novellino, E.6    Marchand, C.7    Pommier, Y.8
  • 60
    • 46249087616 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 (HIV-1) integration: A potential target for microbicides to prevent cell-free or cell-associated HIV-1 infection
    • DOI 10.1128/AAC.01627-07
    • Terrazas-Aranda, K.; Van Herrewege, Y.; Hazuda, D.; Lewi, P.; Costi, R.; Di Santo, R.; Cara, A.; Vanham, G. Human immunodeficiency virus type 1 (HIV-1) integration: a potential target for microbicides to prevent cell-free or cell-associated HIV-1 infection. Antimicrob. Agents Chemother., 2008, 52, 2544-2554. (Pubitemid 351915687)
    • (2008) Antimicrobial Agents and Chemotherapy , vol.52 , Issue.7 , pp. 2544-2554
    • Terrazas-Aranda, K.1    Van Herrewege, Y.2    Hazuda, D.3    Lewi, P.4    Costi, R.5    Di Santo, R.6    Cara, A.7    Vanham, G.8
  • 63
    • 33847098825 scopus 로고    scopus 로고
    • Probing HIV-1 integrase inhibitor binding sites with position-specific integrase-DNA cross-linking assays
    • DOI 10.1124/mol.106.030817
    • Johnson, A.A.; Marchand, C.; Patil, S.S.; Costi, R.; Di Santo, R.; Burke, T.R., Jr.; Pommier, Y. Probing HIV-1 integrase inhibitor binding sites with position-specific integrase-DNA cross-linking assays. Mol. Pharmacol., 2007, 71(3), 893-901. (Pubitemid 46294101)
    • (2007) Molecular Pharmacology , vol.71 , Issue.3 , pp. 893-901
    • Johnson, A.A.1    Marchand, C.2    Patil, S.S.3    Costi, R.4    Di Santo, R.5    Burke Jr., T.R.6    Pommier, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.