메뉴 건너뛰기




Volumn 392, Issue 2, 2009, Pages 243-250

Epistasis among Deleterious Mutations in the HIV-1 Protease

Author keywords

epistasis; fitness; HIV 1; mutation; protease

Indexed keywords

NUCLEOTIDE; PROTEINASE;

EID: 68949209095     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.07.015     Document Type: Article
Times cited : (23)

References (66)
  • 1
    • 33646182934 scopus 로고    scopus 로고
    • An integrated view of protein evolution
    • Pal C., Papp B., and Lercher M.J. An integrated view of protein evolution. Nat. Rev., Genet. 7 (2006) 337-348
    • (2006) Nat. Rev., Genet. , vol.7 , pp. 337-348
    • Pal, C.1    Papp, B.2    Lercher, M.J.3
  • 2
    • 23944490117 scopus 로고    scopus 로고
    • Missense meanderings in sequence space: a biophysical view of protein evolution
    • DePristo M.A., Weinreich D.M., and Hartl D.L. Missense meanderings in sequence space: a biophysical view of protein evolution. Nat. Rev., Genet. 6 (2005) 678-687
    • (2005) Nat. Rev., Genet. , vol.6 , pp. 678-687
    • DePristo, M.A.1    Weinreich, D.M.2    Hartl, D.L.3
  • 3
    • 34248364854 scopus 로고    scopus 로고
    • Epistasis between deleterious mutations and the evolution of recombination
    • Kouyos R.D., Silander O.K., and Bonhoeffer S. Epistasis between deleterious mutations and the evolution of recombination. Trends Ecol. Evol. 22 (2007) 308-315
    • (2007) Trends Ecol. Evol. , vol.22 , pp. 308-315
    • Kouyos, R.D.1    Silander, O.K.2    Bonhoeffer, S.3
  • 4
    • 33845864966 scopus 로고    scopus 로고
    • Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein
    • Bershtein S., Segal M., Bekerman R., Tokuriki N., and Tawfik D.S. Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein. Nature 444 (2006) 929-932
    • (2006) Nature , vol.444 , pp. 929-932
    • Bershtein, S.1    Segal, M.2    Bekerman, R.3    Tokuriki, N.4    Tawfik, D.S.5
  • 5
    • 33645691679 scopus 로고    scopus 로고
    • Evolution of hormone-receptor complexity by molecular exploitation
    • Bridgham J.T., Carroll S.M., and Thornton J.W. Evolution of hormone-receptor complexity by molecular exploitation. Science 312 (2006) 97-101
    • (2006) Science , vol.312 , pp. 97-101
    • Bridgham, J.T.1    Carroll, S.M.2    Thornton, J.W.3
  • 6
    • 34548040966 scopus 로고    scopus 로고
    • Crystal structure of an ancient protein: evolution by conformational epistasis
    • Ortlund E.A., Bridgham J.T., Redinbo M.R., and Thornton J.W. Crystal structure of an ancient protein: evolution by conformational epistasis. Science 317 (2007) 1544-1548
    • (2007) Science , vol.317 , pp. 1544-1548
    • Ortlund, E.A.1    Bridgham, J.T.2    Redinbo, M.R.3    Thornton, J.W.4
  • 10
    • 33645666942 scopus 로고    scopus 로고
    • Darwinian evolution scan follow only very few mutational paths to fitter proteins
    • Weinreich D.M., Delaney N.F., DePristo M.A., and Hartl D.L. Darwinian evolution scan follow only very few mutational paths to fitter proteins. Science 312 (2006) 111-114
    • (2006) Science , vol.312 , pp. 111-114
    • Weinreich, D.M.1    Delaney, N.F.2    DePristo, M.A.3    Hartl, D.L.4
  • 11
    • 34548018528 scopus 로고    scopus 로고
    • Mechanistic approaches to the study of evolution: the functional synthesis
    • Dean A.M., and Thornton J.W. Mechanistic approaches to the study of evolution: the functional synthesis. Nat. Rev., Genet. 8 (2007) 675-688
    • (2007) Nat. Rev., Genet. , vol.8 , pp. 675-688
    • Dean, A.M.1    Thornton, J.W.2
  • 12
    • 0030869269 scopus 로고    scopus 로고
    • Treatment with indinavir, zidovudine, and lamivudine in adults with human immunodeficiency virus infection and prior antiretroviral therapy
    • Gulick R.M., Mellors J.W., Havlir D., Eron J.J., Gonzalez C., McMahon D., et al. Treatment with indinavir, zidovudine, and lamivudine in adults with human immunodeficiency virus infection and prior antiretroviral therapy. N. Engl. J. Med. 337 (1997) 734-739
    • (1997) N. Engl. J. Med. , vol.337 , pp. 734-739
    • Gulick, R.M.1    Mellors, J.W.2    Havlir, D.3    Eron, J.J.4    Gonzalez, C.5    McMahon, D.6
  • 13
    • 0442268112 scopus 로고    scopus 로고
    • A controlled trial of two nucleoside analogues plus indinavir in persons with human immunodeficiency virus infection and CD4 cell counts of 200 per cubic millimeter or less. AIDS Clinical Trials Group 320 Study Team
    • Hammer S.M., Squires K.E., Hughes M.D., Grimes J.M., Demeter L.M., Currier J.S., et al. A controlled trial of two nucleoside analogues plus indinavir in persons with human immunodeficiency virus infection and CD4 cell counts of 200 per cubic millimeter or less. AIDS Clinical Trials Group 320 Study Team. N. Engl. J. Med. 337 (1997) 725-733
    • (1997) N. Engl. J. Med. , vol.337 , pp. 725-733
    • Hammer, S.M.1    Squires, K.E.2    Hughes, M.D.3    Grimes, J.M.4    Demeter, L.M.5    Currier, J.S.6
  • 14
    • 33846829804 scopus 로고    scopus 로고
    • HIV-1 protease catalytic efficiency effects caused by random single amino acid substitutions
    • Parera M., Fernandez G., Clotet B., and Martinez M.A. HIV-1 protease catalytic efficiency effects caused by random single amino acid substitutions. Mol. Biol. Evol. 24 (2007) 382-387
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 382-387
    • Parera, M.1    Fernandez, G.2    Clotet, B.3    Martinez, M.A.4
  • 15
    • 0032539934 scopus 로고    scopus 로고
    • A genetic screen for the isolation and characterization of site-specific proteases
    • Sices H.J., and Kristie T.M. A genetic screen for the isolation and characterization of site-specific proteases. Proc. Natl. Acad. Sci. USA 95 (1998) 2828-2833
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2828-2833
    • Sices, H.J.1    Kristie, T.M.2
  • 16
    • 0034007774 scopus 로고    scopus 로고
    • A bacteriophage lambda-based genetic screen for characterization of the activity and phenotype of the human immunodeficiency virus type 1 protease
    • Martinez M.A., Cabana M., Parera M., Gutierrez A., Este J.A., and Clotet B. A bacteriophage lambda-based genetic screen for characterization of the activity and phenotype of the human immunodeficiency virus type 1 protease. Antimicrob. Agents Chemother. 44 (2000) 1132-1139
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 1132-1139
    • Martinez, M.A.1    Cabana, M.2    Parera, M.3    Gutierrez, A.4    Este, J.A.5    Clotet, B.6
  • 17
    • 0036384360 scopus 로고    scopus 로고
    • Catalytic efficiency and phenotype of HIV-1 proteases encoding single critical resistance substitutions
    • Cabana M., Fernandez G., Parera M., Clotet B., and Martinez M.A. Catalytic efficiency and phenotype of HIV-1 proteases encoding single critical resistance substitutions. Virology 300 (2002) 71-78
    • (2002) Virology , vol.300 , pp. 71-78
    • Cabana, M.1    Fernandez, G.2    Parera, M.3    Clotet, B.4    Martinez, M.A.5
  • 18
    • 33847210305 scopus 로고    scopus 로고
    • Fitness landscape of human immunodeficiency virus type 1 protease quasispecies
    • Fernandez G., Clotet B., and Martinez M.A. Fitness landscape of human immunodeficiency virus type 1 protease quasispecies. J. Virol. 81 (2007) 2485-2496
    • (2007) J. Virol. , vol.81 , pp. 2485-2496
    • Fernandez, G.1    Clotet, B.2    Martinez, M.A.3
  • 19
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • Tokuriki N., and Tawfik D.S. Protein dynamism and evolvability. Science 324 (2009) 203-207
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2
  • 21
    • 3042681604 scopus 로고    scopus 로고
    • Protein tolerance to random amino acid change
    • Guo H.H., Choe J., and Loeb L.A. Protein tolerance to random amino acid change. Proc. Natl Acad. Sci. USA 101 (2004) 9205-9210
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9205-9210
    • Guo, H.H.1    Choe, J.2    Loeb, L.A.3
  • 22
    • 34249660610 scopus 로고    scopus 로고
    • Highly tolerated amino acid substitutions increase the fidelity of Escherichia coli DNA polymerase I
    • Loh E., Choe J., and Loeb L.A. Highly tolerated amino acid substitutions increase the fidelity of Escherichia coli DNA polymerase I. J. Biol. Chem. 282 (2007) 12201-12209
    • (2007) J. Biol. Chem. , vol.282 , pp. 12201-12209
    • Loh, E.1    Choe, J.2    Loeb, L.A.3
  • 23
    • 0028076771 scopus 로고
    • Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as "spacers" which do not require a specific sequence
    • Markiewicz P., Kleina L.G., Cruz C., Ehret S., and Miller J.H. Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as "spacers" which do not require a specific sequence. J. Mol. Biol. 240 (1994) 421-433
    • (1994) J. Mol. Biol. , vol.240 , pp. 421-433
    • Markiewicz, P.1    Kleina, L.G.2    Cruz, C.3    Ehret, S.4    Miller, J.H.5
  • 24
    • 0032546542 scopus 로고    scopus 로고
    • A search for single substitutions that eliminate enzymatic function in a bacterial ribonuclease
    • Axe D.D., Foster N.W., and Fersht A.R. A search for single substitutions that eliminate enzymatic function in a bacterial ribonuclease. Biochemistry 37 (1998) 7157-7166
    • (1998) Biochemistry , vol.37 , pp. 7157-7166
    • Axe, D.D.1    Foster, N.W.2    Fersht, A.R.3
  • 26
    • 0032928065 scopus 로고    scopus 로고
    • Replicative fitness of protease inhibitor-resistant mutants of human immunodeficiency virus type 1
    • Martinez-Picado J., Savara A.V., Sutton L., and D'Aquila R.T. Replicative fitness of protease inhibitor-resistant mutants of human immunodeficiency virus type 1. J. Virol. 73 (1999) 3744-3752
    • (1999) J. Virol. , vol.73 , pp. 3744-3752
    • Martinez-Picado, J.1    Savara, A.V.2    Sutton, L.3    D'Aquila, R.T.4
  • 27
    • 0032804864 scopus 로고    scopus 로고
    • Increased fitness of drug resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy
    • Nijhuis M., Schuurman R., de Jong D., Erickson J., Gustchina E., Albert J., et al. Increased fitness of drug resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy. AIDS 13 (1999) 2349-2359
    • (1999) AIDS , vol.13 , pp. 2349-2359
    • Nijhuis, M.1    Schuurman, R.2    de Jong, D.3    Erickson, J.4    Gustchina, E.5    Albert, J.6
  • 28
    • 0037469371 scopus 로고    scopus 로고
    • Evolution of mutational robustness
    • Wilke C.O., and Adami C. Evolution of mutational robustness. Mutat. Res. 522 (2003) 3-11
    • (2003) Mutat. Res. , vol.522 , pp. 3-11
    • Wilke, C.O.1    Adami, C.2
  • 29
    • 33645800999 scopus 로고    scopus 로고
    • Mechanisms of genetic robustness in RNA viruses
    • Elena S.F., Carrasco P., Daros J.A., and Sanjuan R. Mechanisms of genetic robustness in RNA viruses. EMBO Rep. 7 (2006) 168-173
    • (2006) EMBO Rep. , vol.7 , pp. 168-173
    • Elena, S.F.1    Carrasco, P.2    Daros, J.A.3    Sanjuan, R.4
  • 32
    • 0036306115 scopus 로고    scopus 로고
    • Why are proteins so robust to site mutations?
    • Taverna D.M., and Goldstein R.A. Why are proteins so robust to site mutations?. J. Mol. Biol. 315 (2002) 479-484
    • (2002) J. Mol. Biol. , vol.315 , pp. 479-484
    • Taverna, D.M.1    Goldstein, R.A.2
  • 33
    • 14844325784 scopus 로고    scopus 로고
    • Robustness, evolvability, and neutrality
    • Wagner A. Robustness, evolvability, and neutrality. FEBS Lett. 579 (2005) 1772-1778
    • (2005) FEBS Lett. , vol.579 , pp. 1772-1778
    • Wagner, A.1
  • 36
    • 0029075130 scopus 로고
    • Lower in vivo mutation rate of human immunodeficiency virus type 1 than that predicted from the fidelity of purified reverse transcriptase
    • Mansky L.M., and Temin H.M. Lower in vivo mutation rate of human immunodeficiency virus type 1 than that predicted from the fidelity of purified reverse transcriptase. J. Virol. 69 (1995) 5087-5094
    • (1995) J. Virol. , vol.69 , pp. 5087-5094
    • Mansky, L.M.1    Temin, H.M.2
  • 38
    • 0141676563 scopus 로고    scopus 로고
    • High rates of human immunodeficiency virus type 1 recombination: near-random segregation of markers one kilobase apart in one round of viral replication
    • Rhodes T., Wargo H., and Hu W.S. High rates of human immunodeficiency virus type 1 recombination: near-random segregation of markers one kilobase apart in one round of viral replication. J. Virol. 77 (2003) 11193-11200
    • (2003) J. Virol. , vol.77 , pp. 11193-11200
    • Rhodes, T.1    Wargo, H.2    Hu, W.S.3
  • 40
    • 0028952146 scopus 로고
    • HIV population dynamics in vivo: implications for genetic variation, pathogenesis, and therapy
    • Coffin J.M. HIV population dynamics in vivo: implications for genetic variation, pathogenesis, and therapy. Science 267 (1995) 483-489
    • (1995) Science , vol.267 , pp. 483-489
    • Coffin, J.M.1
  • 41
    • 33846277942 scopus 로고    scopus 로고
    • The evolution of sex: empirical insights into the roles of epistasis and drift
    • de Visser J.A., and Elena S.F. The evolution of sex: empirical insights into the roles of epistasis and drift. Nat. Rev., Genet. 8 (2007) 139-149
    • (2007) Nat. Rev., Genet. , vol.8 , pp. 139-149
    • de Visser, J.A.1    Elena, S.F.2
  • 43
    • 3142755598 scopus 로고    scopus 로고
    • Epistasis and its relationship to canalization in the RNA virus phi 6
    • Burch C.L., and Chao L. Epistasis and its relationship to canalization in the RNA virus phi 6. Genetics 167 (2004) 559-567
    • (2004) Genetics , vol.167 , pp. 559-567
    • Burch, C.L.1    Chao, L.2
  • 44
    • 7444221704 scopus 로고    scopus 로고
    • The contribution of epistasis to the architecture of fitness in an RNA virus
    • Sanjuan R., Moya A., and Elena S.F. The contribution of epistasis to the architecture of fitness in an RNA virus. Proc. Natl Acad. Sci. USA 101 (2004) 15376-15379
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 15376-15379
    • Sanjuan, R.1    Moya, A.2    Elena, S.F.3
  • 45
    • 33745267732 scopus 로고    scopus 로고
    • Effects of random mutations in the human immunodeficiency virus type 1 transcriptional promoter on viral fitness in different host cell environments
    • van Opijnen T., Boerlijst M.C., and Berkhout B. Effects of random mutations in the human immunodeficiency virus type 1 transcriptional promoter on viral fitness in different host cell environments. J. Virol. 80 (2006) 6678-6685
    • (2006) J. Virol. , vol.80 , pp. 6678-6685
    • van Opijnen, T.1    Boerlijst, M.C.2    Berkhout, B.3
  • 46
    • 34347332282 scopus 로고    scopus 로고
    • Variable epistatic effects between mutations at host recognition sites in phiX174 bacteriophage
    • Pepin K.M., and Wichman H.A. Variable epistatic effects between mutations at host recognition sites in phiX174 bacteriophage. Evolution 61 (2007) 1710-1724
    • (2007) Evolution , vol.61 , pp. 1710-1724
    • Pepin, K.M.1    Wichman, H.A.2
  • 47
    • 0031458777 scopus 로고    scopus 로고
    • Test of synergistic interactions among deleterious mutations in bacteria
    • Elena S.F., and Lenski R.E. Test of synergistic interactions among deleterious mutations in bacteria. Nature 390 (1997) 395-398
    • (1997) Nature , vol.390 , pp. 395-398
    • Elena, S.F.1    Lenski, R.E.2
  • 48
    • 0031020691 scopus 로고    scopus 로고
    • An experimental test for synergistic epistasis and its application in Chlamydomonas
    • de Visser J.A., Hoekstra R.F., and van den Ende H. An experimental test for synergistic epistasis and its application in Chlamydomonas. Genetics 145 (1997) 815-819
    • (1997) Genetics , vol.145 , pp. 815-819
    • de Visser, J.A.1    Hoekstra, R.F.2    van den Ende, H.3
  • 49
    • 0033709990 scopus 로고    scopus 로고
    • Factors affecting the genetic load in Drosophila: synergistic epistasis and correlations among fitness components
    • Whitlock M.C., and Bourguet D. Factors affecting the genetic load in Drosophila: synergistic epistasis and correlations among fitness components. Evolution 54 (2000) 1654-1660
    • (2000) Evolution , vol.54 , pp. 1654-1660
    • Whitlock, M.C.1    Bourguet, D.2
  • 50
    • 0034765995 scopus 로고    scopus 로고
    • Direct estimate of the mutation rate and the distribution of fitness effects in the yeast Saccharomyces cerevisiae
    • Wloch D.M., Szafraniec K., Borts R.H., and Korona R. Direct estimate of the mutation rate and the distribution of fitness effects in the yeast Saccharomyces cerevisiae. Genetics 159 (2001) 441-452
    • (2001) Genetics , vol.159 , pp. 441-452
    • Wloch, D.M.1    Szafraniec, K.2    Borts, R.H.3    Korona, R.4
  • 51
    • 0036218367 scopus 로고    scopus 로고
    • A comprehensive model of mutations affecting fitness and inferences for Arabidopsis thaliana
    • Shaw F.H., Geyer C.J., and Shaw R.G. A comprehensive model of mutations affecting fitness and inferences for Arabidopsis thaliana. Evolution 56 (2002) 453-463
    • (2002) Evolution , vol.56 , pp. 453-463
    • Shaw, F.H.1    Geyer, C.J.2    Shaw, R.G.3
  • 52
    • 0036239186 scopus 로고    scopus 로고
    • Dependence of epistasis on environment and mutation severity as revealed by in silico mutagenesis of phage t7
    • You L., and Yin J. Dependence of epistasis on environment and mutation severity as revealed by in silico mutagenesis of phage t7. Genetics 160 (2002) 1273-1281
    • (2002) Genetics , vol.160 , pp. 1273-1281
    • You, L.1    Yin, J.2
  • 53
    • 0038668776 scopus 로고    scopus 로고
    • The evolutionary origin of complex features
    • Lenski R.E., Ofria C., Pennock R.T., and Adami C. The evolutionary origin of complex features. Nature 423 (2003) 139-144
    • (2003) Nature , vol.423 , pp. 139-144
    • Lenski, R.E.1    Ofria, C.2    Pennock, R.T.3    Adami, C.4
  • 54
    • 1842507188 scopus 로고    scopus 로고
    • Compensatory mutations cause excess of antagonistic epistasis in RNA secondary structure folding
    • Wilke C.O., Lenski R.E., and Adami C. Compensatory mutations cause excess of antagonistic epistasis in RNA secondary structure folding. BMC Evol. Biol. 3 (2003) 3
    • (2003) BMC Evol. Biol. , vol.3 , pp. 3
    • Wilke, C.O.1    Lenski, R.E.2    Adami, C.3
  • 56
    • 21044438202 scopus 로고    scopus 로고
    • The rate of compensatory mutation in the DNA bacteriophage phiX174
    • Poon A., and Chao L. The rate of compensatory mutation in the DNA bacteriophage phiX174. Genetics 170 (2005) 989-999
    • (2005) Genetics , vol.170 , pp. 989-999
    • Poon, A.1    Chao, L.2
  • 57
    • 33749242962 scopus 로고    scopus 로고
    • Epistasis correlates to genomic complexity
    • Sanjuan R., and Elena S.F. Epistasis correlates to genomic complexity. Proc. Natl Acad. Sci. USA 103 (2006) 14402-14405
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 14402-14405
    • Sanjuan, R.1    Elena, S.F.2
  • 58
    • 33745614283 scopus 로고    scopus 로고
    • In silico predicted robustness of viroids RNA secondary structures. I. The effect of single mutations
    • Sanjuan R., Forment J., and Elena S.F. In silico predicted robustness of viroids RNA secondary structures. I. The effect of single mutations. Mol. Biol. Evol. 23 (2006) 1427-1436
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 1427-1436
    • Sanjuan, R.1    Forment, J.2    Elena, S.F.3
  • 59
    • 33644745138 scopus 로고    scopus 로고
    • Sexual reproduction selects for robustness and negative epistasis in artificial gene networks
    • Azevedo R.B., Lohaus R., Srinivasan S., Dang K.K., and Burch C.L. Sexual reproduction selects for robustness and negative epistasis in artificial gene networks. Nature 440 (2006) 87-90
    • (2006) Nature , vol.440 , pp. 87-90
    • Azevedo, R.B.1    Lohaus, R.2    Srinivasan, S.3    Dang, K.K.4    Burch, C.L.5
  • 60
    • 34047143174 scopus 로고    scopus 로고
    • Epistatic buffering of fitness loss in yeast double deletion strains
    • Jasnos L., and Korona R. Epistatic buffering of fitness loss in yeast double deletion strains. Nat. Genet. 39 (2007) 550-554
    • (2007) Nat. Genet. , vol.39 , pp. 550-554
    • Jasnos, L.1    Korona, R.2
  • 61
    • 34247881991 scopus 로고    scopus 로고
    • Analysis of epistatic interactions and fitness landscapes using a new geometric approach
    • Beerenwinkel N., Pachter L., Sturmfels B., Elena S.F., and Lenski R.E. Analysis of epistatic interactions and fitness landscapes using a new geometric approach. BMC Evol. Biol. 7 (2007) 60
    • (2007) BMC Evol. Biol. , vol.7 , pp. 60
    • Beerenwinkel, N.1    Pachter, L.2    Sturmfels, B.3    Elena, S.F.4    Lenski, R.E.5
  • 62
    • 34547890683 scopus 로고    scopus 로고
    • Coevolution of robustness, epistasis, and recombination favors asexual reproduction
    • MacCarthy T., and Bergman A. Coevolution of robustness, epistasis, and recombination favors asexual reproduction. Proc. Natl Acad. Sci. USA 104 (2007) 12801-12806
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 12801-12806
    • MacCarthy, T.1    Bergman, A.2
  • 64
    • 0038673317 scopus 로고    scopus 로고
    • Genetic screen for monitoring hepatitis C virus NS3 serine protease activity
    • Martinez M.A., and Clotet B. Genetic screen for monitoring hepatitis C virus NS3 serine protease activity. Antimicrob. Agents Chemother. 47 (2003) 1760-1765
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 1760-1765
    • Martinez, M.A.1    Clotet, B.2
  • 65
    • 10044247531 scopus 로고    scopus 로고
    • Genetic screen for monitoring severe acute respiratory syndrome coronavirus 3C-like protease
    • Parera M., Clotet B., and Martinez M.A. Genetic screen for monitoring severe acute respiratory syndrome coronavirus 3C-like protease. J. Virol. 78 (2004) 14057-14061
    • (2004) J. Virol. , vol.78 , pp. 14057-14061
    • Parera, M.1    Clotet, B.2    Martinez, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.