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Volumn 89, Issue 1, 2015, Pages 552-567

Uneven genetic robustness of HIV-1 integrase

Author keywords

[No Author keywords available]

Indexed keywords

HIV 1 INTEGRASE; INTEGRASE; UNCLASSIFIED DRUG; GAG PROTEIN; MUTANT PROTEIN; P31 INTEGRASE PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 84919430559     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02451-14     Document Type: Article
Times cited : (20)

References (92)
  • 3
    • 84867403182 scopus 로고    scopus 로고
    • RNA virus genetic robustness: possible causes and some consequences
    • Elena SF. 2012. RNA virus genetic robustness: possible causes and some consequences. Curr Opin Virol 2:525-530. http://dx.doi.org/10.1016/j.coviro.2012.06.008.
    • (2012) Curr Opin Virol , vol.2 , pp. 525-530
    • Elena, S.F.1
  • 5
    • 84876406925 scopus 로고    scopus 로고
    • The role of mutational robustness in RNA virus evolution
    • Lauring AS, Frydman J, Andino R. 2013. The role of mutational robustness in RNA virus evolution. Nat Rev Microbiol 11:327-336. http://dx.doi.org/10.1038/nrmicro3003.
    • (2013) Nat Rev Microbiol , vol.11 , pp. 327-336
    • Lauring, A.S.1    Frydman, J.2    Andino, R.3
  • 6
    • 34347327212 scopus 로고    scopus 로고
    • Selection for robustness in mutagenized RNA viruses
    • Sanjuan R, Cuevas JM, Furio V, Holmes EC, Moya A. 2007. Selection for robustness in mutagenized RNA viruses. PLoS Genet 3:e93. http://dx.doi.org/10.1371/journal.pgen.0030093.
    • (2007) PLoS Genet , vol.3
    • Sanjuan, R.1    Cuevas, J.M.2    Furio, V.3    Holmes, E.C.4    Moya, A.5
  • 7
    • 33846018059 scopus 로고    scopus 로고
    • The fittest versus the flattest: experimental confirmation of the quasispecies effect with subviral pathogens
    • Codoner FM, Daros JA, Sole RV, Elena SF. 2006. The fittest versus the flattest: experimental confirmation of the quasispecies effect with subviral pathogens. PLoS Pathog 2:e136. http://dx.doi.org/10.1371/journal.ppat.0020136.
    • (2006) PLoS Pathog , vol.2
    • Codoner, F.M.1    Daros, J.A.2    Sole, R.V.3    Elena, S.F.4
  • 9
    • 2942565781 scopus 로고    scopus 로고
    • The distribution of fitness effects caused by single-nucleotide substitutions in anRNAvirus
    • Sanjuan R, Moya A, Elena SF. 2004. The distribution of fitness effects caused by single-nucleotide substitutions in anRNAvirus. Proc Natl Acad Sci USA 101:8396-8401. http://dx.doi.org/10.1073/pnas.0400146101.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8396-8401
    • Sanjuan, R.1    Moya, A.2    Elena, S.F.3
  • 10
    • 36348963100 scopus 로고    scopus 로고
    • Distribution of fitness and virulence effects caused by single-nucleotide substitutions in tobacco etch virus
    • Carrasco P, de la Iglesia F, Elena SF. 2007. Distribution of fitness and virulence effects caused by single-nucleotide substitutions in tobacco etch virus. J Virol 81:12979-12984. http://dx.doi.org/10.1128/JVI.00524-07.
    • (2007) J Virol , vol.81 , pp. 12979-12984
    • Carrasco, P.1    de la Iglesia, F.2    Elena, S.F.3
  • 12
    • 0030972160 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition
    • Miller MD, Farnet CM, Bushman FD. 1997. Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition. J Virol 71:5382-5390.
    • (1997) J Virol , vol.71 , pp. 5382-5390
    • Miller, M.D.1    Farnet, C.M.2    Bushman, F.D.3
  • 13
    • 0034812967 scopus 로고    scopus 로고
    • Asymmetric processing of human immunodeficiency virus type 1 cDNA in vivo: implications for functional end coupling during the chemical steps of DNA transposition
    • Chen H, Engelman A. 2001. Asymmetric processing of human immunodeficiency virus type 1 cDNA in vivo: implications for functional end coupling during the chemical steps of DNA transposition. Mol Cell Biol 21: 6758-6767. http://dx.doi.org/10.1128/MCB.21.20.6758-6767.2001.
    • (2001) Mol Cell Biol , vol.21 , pp. 6758-6767
    • Chen, H.1    Engelman, A.2
  • 14
    • 0031449687 scopus 로고    scopus 로고
    • A large nucleoprotein assembly at the ends of the viral DNA mediates retroviral DNA integration
    • Wei SQ, Mizuuchi K, Craigie R. 1997. A large nucleoprotein assembly at the ends of the viral DNA mediates retroviral DNA integration. EMBO J 16:7511-7520. http://dx.doi.org/10.1093/emboj/16.24.7511.
    • (1997) EMBO J , vol.16 , pp. 7511-7520
    • Wei, S.Q.1    Mizuuchi, K.2    Craigie, R.3
  • 15
    • 0025366844 scopus 로고
    • Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity
    • Sherman PA, Fyfe JA. 1990. Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity. Proc Natl Acad Sci USA 87:5119-5123. http://dx.doi.org/10.1073/pnas.87.13.5119.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5119-5123
    • Sherman, P.A.1    Fyfe, J.A.2
  • 16
    • 0026330796 scopus 로고
    • HIV-1 DNA integration: mechanism of viralDNAcleavage andDNAstrand transfer
    • Engelman A, Mizuuchi K, Craigie R. 1991. HIV-1 DNA integration: mechanism of viralDNAcleavage andDNAstrand transfer. Cell 67:1211-1221. http://dx.doi.org/10.1016/0092-8674(91)90297-C.
    • (1991) Cell , vol.67 , pp. 1211-1221
    • Engelman, A.1    Mizuuchi, K.2    Craigie, R.3
  • 17
    • 0025133394 scopus 로고
    • Retroviral DNA integration directed by HIV integration protein in vitro
    • Bushman FD, Fujiwara T, Craigie R. 1990. Retroviral DNA integration directed by HIV integration protein in vitro. Science 249:1555-1558. http://dx.doi.org/10.1126/science.2171144.
    • (1990) Science , vol.249 , pp. 1555-1558
    • Bushman, F.D.1    Fujiwara, T.2    Craigie, R.3
  • 18
    • 0026034790 scopus 로고
    • Activities of human immunodeficiency virus (HIV) integration protein in vitro: specific cleavage and integration of HIV DNA
    • Bushman FD, Craigie R. 1991. Activities of human immunodeficiency virus (HIV) integration protein in vitro: specific cleavage and integration of HIV DNA. Proc Natl Acad Sci USA 88:1339-1343. http://dx.doi.org/10.1073/pnas.88.4.1339.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 1339-1343
    • Bushman, F.D.1    Craigie, R.2
  • 19
    • 0030478950 scopus 로고    scopus 로고
    • Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
    • Zheng R, Jenkins TM, Craigie R. 1996. Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. Proc Natl Acad Sci USA 93:13659-13664. http://dx.doi.org/10.1073/pnas.93.24.13659.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13659-13664
    • Zheng, R.1    Jenkins, T.M.2    Craigie, R.3
  • 20
    • 0026719238 scopus 로고
    • Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases
    • Kulkosky J, Jones KS, Katz RA, Mack JP, Skalka AM. 1992. Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases. Mol Cell Biol 12:2331-2338.
    • (1992) Mol Cell Biol , vol.12 , pp. 2331-2338
    • Kulkosky, J.1    Jones, K.S.2    Katz, R.A.3    Mack, J.P.4    Skalka, A.M.5
  • 21
    • 79952070221 scopus 로고    scopus 로고
    • Structural biology of retroviral DNA integration
    • Li X, Krishnan L, Cherepanov P, Engelman A. 2011. Structural biology of retroviral DNA integration. Virology 411:194-205. http://dx.doi.org/10.1016/j.virol.2010.12.008.
    • (2011) Virology , vol.411 , pp. 194-205
    • Li, X.1    Krishnan, L.2    Cherepanov, P.3    Engelman, A.4
  • 22
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases
    • Dyda F, Hickman AB, Jenkins TM, Engelman A, Craigie R, Davies DR. 1994. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science 266:1981-1986. http://dx.doi.org/10.1126/science.7801124.
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1    Hickman, A.B.2    Jenkins, T.M.3    Engelman, A.4    Craigie, R.5    Davies, D.R.6
  • 23
    • 0026539155 scopus 로고
    • Localization of DNA binding activity of HIV-1 integrase to the C-terminal half of the protein
    • Woerner AM, Klutch M, Levin JG, Marcus-Sekura CJ. 1992. Localization of DNA binding activity of HIV-1 integrase to the C-terminal half of the protein. AIDS Res Hum Retroviruses 8:297-304. http://dx.doi.org/10.1089/aid.1992.8.297.
    • (1992) AIDS Res Hum Retroviruses , vol.8 , pp. 297-304
    • Woerner, A.M.1    Klutch, M.2    Levin, J.G.3    Marcus-Sekura, C.J.4
  • 26
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • Hare S, Gupta SS, Valkov E, Engelman A, Cherepanov P. 2010. Retroviral intasome assembly and inhibition of DNA strand transfer. Nature 464:232-236. http://dx.doi.org/10.1038/nature08784.
    • (2010) Nature , vol.464 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Valkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 27
    • 78149434355 scopus 로고    scopus 로고
    • The mechanism of retroviral integration from X-ray structures of its key intermediates
    • Maertens GN, Hare S, Cherepanov P. 2010. The mechanism of retroviral integration from X-ray structures of its key intermediates. Nature 468: 326-329. http://dx.doi.org/10.1038/nature09517.
    • (2010) Nature , vol.468 , pp. 326-329
    • Maertens, G.N.1    Hare, S.2    Cherepanov, P.3
  • 28
    • 84878252974 scopus 로고    scopus 로고
    • A homology model of HIV-1 integrase and analysis of mutations designed to test the model
    • Johnson BC, Metifiot M, Ferris A, Pommier Y, Hughes SH. 2013. A homology model of HIV-1 integrase and analysis of mutations designed to test the model. J Mol Biol 425:2133-2146. http://dx.doi.org/10.1016/j.jmb.2013.03.027.
    • (2013) J Mol Biol , vol.425 , pp. 2133-2146
    • Johnson, B.C.1    Metifiot, M.2    Ferris, A.3    Pommier, Y.4    Hughes, S.H.5
  • 30
    • 0032617446 scopus 로고    scopus 로고
    • In vivo analysis of retroviral integrase structure and function
    • Engelman A. 1999. In vivo analysis of retroviral integrase structure and function. Adv Virus Res 52:411-426. http://dx.doi.org/10.1016/S0065-3527(08)60309-7.
    • (1999) Adv Virus Res , vol.52 , pp. 411-426
    • Engelman, A.1
  • 31
    • 0027456715 scopus 로고
    • Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding
    • Bushman FD, Engelman A, Palmer I, Wingfield P, Craigie R. 1993. Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding. Proc Natl Acad Sci USA 90:3428-3432. http://dx.doi.org/10.1073/pnas.90.8.3428.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3428-3432
    • Bushman, F.D.1    Engelman, A.2    Palmer, I.3    Wingfield, P.4    Craigie, R.5
  • 32
    • 0026740842 scopus 로고
    • Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 IN protein in vitro
    • Drelich M, Wilhelm R, Mous J. 1992. Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 IN protein in vitro. Virology 188:459-468. http://dx.doi.org/10.1016/0042-6822(92)90499-F.
    • (1992) Virology , vol.188 , pp. 459-468
    • Drelich, M.1    Wilhelm, R.2    Mous, J.3
  • 33
    • 0027210608 scopus 로고
    • Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein
    • Vink C, Oude Groeneger AM, Plasterk RH. 1993. Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein. Nucleic Acids Res 21:1419-1425. http://dx.doi.org/10.1093/nar/21.6.1419.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1419-1425
    • Vink, C.1    Oude Groeneger, A.M.2    Plasterk, R.H.3
  • 34
    • 77951746962 scopus 로고    scopus 로고
    • Characterization of the HIV-1 integrase chromatin-and LEDGF/p75-binding abilities by mutagenic analysis within the catalytic core domain of integrase
    • Zheng Y, Ao Z, Jayappa KD, Yao X. 2010. Characterization of the HIV-1 integrase chromatin-and LEDGF/p75-binding abilities by mutagenic analysis within the catalytic core domain of integrase. Virol J 7:68. http://dx.doi.org/10.1186/1743-422X-7-68.
    • (2010) Virol J , vol.7 , pp. 68
    • Zheng, Y.1    Ao, Z.2    Jayappa, K.D.3    Yao, X.4
  • 35
    • 84867249710 scopus 로고    scopus 로고
    • Identification of residues in the C-terminal domain of HIV-1 integrase that mediate binding to the transportin-SR2 protein
    • De Houwer S, Demeulemeester J, Thys W, Taltynov O, Zmajkovicova K, Christ F, Debyser Z. 2012. Identification of residues in the C-terminal domain of HIV-1 integrase that mediate binding to the transportin-SR2 protein. J Biol Chem 287:34059-34068. http://dx.doi.org/10.1074/jbc.M112.387944.
    • (2012) J Biol Chem , vol.287 , pp. 34059-34068
    • De Houwer, S.1    Demeulemeester, J.2    Thys, W.3    Taltynov, O.4    Zmajkovicova, K.5    Christ, F.6    Debyser, Z.7
  • 36
    • 1242297002 scopus 로고    scopus 로고
    • Specificity of interaction of INI1/hSNF5 with retroviral integrases and its functional significance
    • Yung E, Sorin M, Wang EJ, Perumal S, Ott D, Kalpana GV. 2004. Specificity of interaction of INI1/hSNF5 with retroviral integrases and its functional significance. J Virol 78:2222-2231. http://dx.doi.org/10.1128/JVI.78.5.2222-2231.2004.
    • (2004) J Virol , vol.78 , pp. 2222-2231
    • Yung, E.1    Sorin, M.2    Wang, E.J.3    Perumal, S.4    Ott, D.5    Kalpana, G.V.6
  • 37
    • 0028936208 scopus 로고
    • Identification and characterization of a temperature-sensitive mutant of human immunodeficiency virus type 1 by alanine scanning mutagenesis of the integrase gene
    • Wiskerchen M, Muesing MA. 1995. Identification and characterization of a temperature-sensitive mutant of human immunodeficiency virus type 1 by alanine scanning mutagenesis of the integrase gene. J Virol 69:597-601.
    • (1995) J Virol , vol.69 , pp. 597-601
    • Wiskerchen, M.1    Muesing, M.A.2
  • 38
    • 0026649557 scopus 로고
    • Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro
    • Engelman A, Craigie R. 1992. Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro. J Virol 66:6361-6369.
    • (1992) J Virol , vol.66 , pp. 6361-6369
    • Engelman, A.1    Craigie, R.2
  • 39
    • 0028915128 scopus 로고
    • Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replication
    • Engelman A, Englund G, Orenstein JM, Martin MA, Craigie R. 1995. Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replication. J Virol 69:2729-2736.
    • (1995) J Virol , vol.69 , pp. 2729-2736
    • Engelman, A.1    Englund, G.2    Orenstein, J.M.3    Martin, M.A.4    Craigie, R.5
  • 40
    • 0030988998 scopus 로고    scopus 로고
    • Structure-based mutagenesis of the catalytic domain of human immunodeficiency virus type 1 integrase
    • Engelman A, Liu Y, Chen H, Farzan M, Dyda F. 1997. Structure-based mutagenesis of the catalytic domain of human immunodeficiency virus type 1 integrase. J Virol 71:3507-3514.
    • (1997) J Virol , vol.71 , pp. 3507-3514
    • Engelman, A.1    Liu, Y.2    Chen, H.3    Farzan, M.4    Dyda, F.5
  • 41
    • 0030828521 scopus 로고    scopus 로고
    • Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking
    • Jenkins TM, Esposito D, Engelman A, Craigie R. 1997. Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking. EMBO J 16:6849-6859. http://dx.doi.org/10.1093/emboj/16.22.6849.
    • (1997) EMBO J , vol.16 , pp. 6849-6859
    • Jenkins, T.M.1    Esposito, D.2    Engelman, A.3    Craigie, R.4
  • 42
  • 43
    • 0030986376 scopus 로고    scopus 로고
    • Solution structure of the N-terminal zinc binding domain of HIV-1 integrase
    • Cai M, Zheng R, Caffrey M, Craigie R, Clore GM, Gronenborn AM. 1997. Solution structure of the N-terminal zinc binding domain of HIV-1 integrase. Nat Struct Biol 4:567-577. http://dx.doi.org/10.1038/nsb0797-567.
    • (1997) Nat Struct Biol , vol.4 , pp. 567-577
    • Cai, M.1    Zheng, R.2    Caffrey, M.3    Craigie, R.4    Clore, G.M.5    Gronenborn, A.M.6
  • 44
    • 33644861936 scopus 로고    scopus 로고
    • Integration requires a specific interaction of the donor DNA terminal 5'-cytosine with glutamine 148 of the HIV-1 integrase flexible loop
    • Johnson AA, Santos W, Pais GC, Marchand C, Amin R, Burke TR, Jr, Verdine G, Pommier Y. 2006. Integration requires a specific interaction of the donor DNA terminal 5'-cytosine with glutamine 148 of the HIV-1 integrase flexible loop. J Biol Chem 281:461-467. http://dx.doi.org/10.1074/jbc.M511348200.
    • (2006) J Biol Chem , vol.281 , pp. 461-467
    • Johnson, A.A.1    Santos, W.2    Pais, G.C.3    Marchand, C.4    Amin, R.5    Burke Jr., T.R.6    Verdine, G.7    Pommier, Y.8
  • 47
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797. http://dx.doi.org/10.1093/nar/gkh340.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 48
    • 73649127602 scopus 로고    scopus 로고
    • The fitness effects of random mutations in single-stranded DNA and RNA bacteriophages
    • Domingo-Calap P, Cuevas JM, Sanjuan R. 2009. The fitness effects of random mutations in single-stranded DNA and RNA bacteriophages. PLoS Genet 5:e1000742. http://dx.doi.org/10.1371/journal.pgen.1000742.
    • (2009) PLoS Genet , vol.5
    • Domingo-Calap, P.1    Cuevas, J.M.2    Sanjuan, R.3
  • 49
    • 0028225959 scopus 로고
    • Human immunodeficiency virus type 1 integrase: effect on viral replication of mutations at highly conserved residues
    • Cannon PM, Wilson W, Byles E, Kingsman SM, Kingsman AJ. 1994. Human immunodeficiency virus type 1 integrase: effect on viral replication of mutations at highly conserved residues. J Virol 68:4768-4775.
    • (1994) J Virol , vol.68 , pp. 4768-4775
    • Cannon, P.M.1    Wilson, W.2    Byles, E.3    Kingsman, S.M.4    Kingsman, A.J.5
  • 50
    • 79959822636 scopus 로고    scopus 로고
    • Clathrin facilitates the morphogenesis of retrovirus particles
    • Zhang F, Zang T, Wilson SJ, Johnson MC, Bieniasz PD. 2011. Clathrin facilitates the morphogenesis of retrovirus particles. PLoS Pathog 7:e1002119. http://dx.doi.org/10.1371/journal.ppat.1002119.
    • (2011) PLoS Pathog , vol.7
    • Zhang, F.1    Zang, T.2    Wilson, S.J.3    Johnson, M.C.4    Bieniasz, P.D.5
  • 54
    • 0028197601 scopus 로고
    • In vivo characterization of mutants of the bacteriophage f1 gene V protein isolated by saturation mutagenesis
    • Terwilliger TC, Zabin HB, Horvath MP, Sandberg WS, Schlunk PM. 1994. In vivo characterization of mutants of the bacteriophage f1 gene V protein isolated by saturation mutagenesis. J Mol Biol 236:556-571. http://dx.doi.org/10.1006/jmbi.1994.1165.
    • (1994) J Mol Biol , vol.236 , pp. 556-571
    • Terwilliger, T.C.1    Zabin, H.B.2    Horvath, M.P.3    Sandberg, W.S.4    Schlunk, P.M.5
  • 55
    • 0026583835 scopus 로고
    • Random mutagenesis of the thymidine kinase gene of varicella-zoster virus
    • Suzutani T, Lacey SF, Powell KL, Purifoy DJ, Honess RW. 1992. Random mutagenesis of the thymidine kinase gene of varicella-zoster virus. J Virol 66:2118-2124.
    • (1992) J Virol , vol.66 , pp. 2118-2124
    • Suzutani, T.1    Lacey, S.F.2    Powell, K.L.3    Purifoy, D.J.4    Honess, R.W.5
  • 56
    • 3042681604 scopus 로고    scopus 로고
    • Protein tolerance to random amino acid change
    • Guo HH, Choe J, Loeb LA. 2004. Protein tolerance to random amino acid change. Proc Natl Acad Sci USA 101:9205-9210. http://dx.doi.org/10.1073/pnas.0403255101.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9205-9210
    • Guo, H.H.1    Choe, J.2    Loeb, L.A.3
  • 57
    • 84866514981 scopus 로고    scopus 로고
    • Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB
    • Ihssen J, Kowarik M, Wiesli L, Reiss R, Wacker M, Thony-Meyer L. 2012. Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB. BMC Biotechnol 12:67. http://dx.doi.org/10.1186/1472-6750-12-67.
    • (2012) BMC Biotechnol , vol.12 , pp. 67
    • Ihssen, J.1    Kowarik, M.2    Wiesli, L.3    Reiss, R.4    Wacker, M.5    Thony-Meyer, L.6
  • 60
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey BM, von Schwedler U, Sundquist WI, Aiken C. 2002. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J Virol 76:5667-5677. http://dx.doi.org/10.1128/JVI.76.11.5667-5677.2002.
    • (2002) J Virol , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 61
    • 47049130164 scopus 로고    scopus 로고
    • Imaging the biogenesis of individual HIV-1 virions in live cells
    • Jouvenet N, Bieniasz PD, Simon SM. 2008. Imaging the biogenesis of individual HIV-1 virions in live cells. Nature 454:236-240. http://dx.doi.org/10.1038/nature06998.
    • (2008) Nature , vol.454 , pp. 236-240
    • Jouvenet, N.1    Bieniasz, P.D.2    Simon, S.M.3
  • 63
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B
    • Luban J, Bossolt KL, Franke EK, Kalpana GV, Goff SP. 1993. Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell 73:1067-1078.
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 66
    • 0041856142 scopus 로고    scopus 로고
    • LEDGF/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells
    • Maertens G, Cherepanov P, Pluymers W, Busschots K, De Clercq E, Debyser Z, Engelborghs Y. 2003. LEDGF/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells. J Biol Chem 278:33528-33539. http://dx.doi.org/10.1074/jbc.M303594200.
    • (2003) J Biol Chem , vol.278 , pp. 33528-33539
    • Maertens, G.1    Cherepanov, P.2    Pluymers, W.3    Busschots, K.4    De Clercq, E.5    Debyser, Z.6    Engelborghs, Y.7
  • 68
    • 0032477738 scopus 로고    scopus 로고
    • Structure-function analysis of integrase interactor 1/hSNF5L1 reveals differential properties of two repeat motifs present in the highly conserved region
    • Morozov A, Yung E, Kalpana GV. 1998. Structure-function analysis of integrase interactor 1/hSNF5L1 reveals differential properties of two repeat motifs present in the highly conserved region. Proc Natl Acad Sci U S A 95:1120-1125. http://dx.doi.org/10.1073/pnas.95.3.1120.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 1120-1125
    • Morozov, A.1    Yung, E.2    Kalpana, G.V.3
  • 69
    • 0027525261 scopus 로고
    • Genetic analysis of homomeric interactions of human immunodeficiency virus type 1 integrase using the yeast twohybrid system
    • Kalpana GV, Goff SP. 1993. Genetic analysis of homomeric interactions of human immunodeficiency virus type 1 integrase using the yeast twohybrid system. Proc Natl Acad Sci USA 90:10593-10597. http://dx.doi.org/10.1073/pnas.90.22.10593.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10593-10597
    • Kalpana, G.V.1    Goff, S.P.2
  • 70
    • 0029980485 scopus 로고    scopus 로고
    • A soluble active mutant of HIV-1 integrase: involvement of both the core and carboxylterminal domains in multimerization
    • Jenkins TM, Engelman A, Ghirlando R, Craigie R. 1996. A soluble active mutant of HIV-1 integrase: involvement of both the core and carboxylterminal domains in multimerization. J Biol Chem 271:7712-7718. http://dx.doi.org/10.1074/jbc.271.13.7712.
    • (1996) J Biol Chem , vol.271 , pp. 7712-7718
    • Jenkins, T.M.1    Engelman, A.2    Ghirlando, R.3    Craigie, R.4
  • 71
    • 70049117341 scopus 로고    scopus 로고
    • Structural basis for functional tetramerization of lentiviral integrase
    • Hare S, Di Nunzio F, Labeja A, Wang J, Engelman A, Cherepanov P. 2009. Structural basis for functional tetramerization of lentiviral integrase. PLoS Pathog 5:e1000515. http://dx.doi.org/10.1371/journal.ppat.1000515.
    • (2009) PLoS Pathog , vol.5
    • Hare, S.1    Di Nunzio, F.2    Labeja, A.3    Wang, J.4    Engelman, A.5    Cherepanov, P.6
  • 72
    • 79952856172 scopus 로고    scopus 로고
    • Interplay between RNA structure and protein evolution in HIV-1
    • Sanjuan R, Borderia AV. 2011. Interplay between RNA structure and protein evolution in HIV-1. Mol Biol Evol 28:1333-1338. http://dx.doi.org/10.1093/molbev/msq329.
    • (2011) Mol Biol Evol , vol.28 , pp. 1333-1338
    • Sanjuan, R.1    Borderia, A.V.2
  • 73
    • 84886937649 scopus 로고    scopus 로고
    • Quantifying selection against synonymous mutations in HIV-1 env evolution
    • Zanini F, Neher RA. 2013. Quantifying selection against synonymous mutations in HIV-1 env evolution. J Virol 87:11843-11850. http://dx.doi.org/10.1128/JVI.01529-13.
    • (2013) J Virol , vol.87 , pp. 11843-11850
    • Zanini, F.1    Neher, R.A.2
  • 74
    • 65949090611 scopus 로고    scopus 로고
    • Probing the sequence space available for HIV-1 evolution
    • ter Brake O, von Eije KJ, Berkhout B. 2008. Probing the sequence space available for HIV-1 evolution. AIDS 22:1875-1877. http://dx.doi.org/10.1097/QAD.0b013e328309efe3.
    • (2008) AIDS , vol.22 , pp. 1875-1877
    • ter Brake, O.1    von Eije, K.J.2    Berkhout, B.3
  • 75
    • 84879018021 scopus 로고    scopus 로고
    • On the role of four small hairpins in the HIV-1 RNA genome
    • Knoepfel SA, Berkhout B. 2013. On the role of four small hairpins in the HIV-1 RNA genome. RNA Biol 10:540-552. http://dx.doi.org/10.4161/rna.24133.
    • (2013) RNA Biol , vol.10 , pp. 540-552
    • Knoepfel, S.A.1    Berkhout, B.2
  • 77
    • 78649411452 scopus 로고    scopus 로고
    • Constraints on HIV-1 diversity from protein structure
    • Woo J, Robertson DL, Lovell SC. 2010. Constraints on HIV-1 diversity from protein structure. J Virol 84:12995-13003. http://dx.doi.org/10.1128/JVI.00702-10.
    • (2010) J Virol , vol.84 , pp. 12995-13003
    • Woo, J.1    Robertson, D.L.2    Lovell, S.C.3
  • 78
    • 0036838711 scopus 로고    scopus 로고
    • Nuclear localization of human immunodeficiency virus type 1 preintegration complexes (PICs): V165A and R166A are pleiotropic integrase mutants primarily defective for integration, not PIC nuclear import
    • Limon A, Devroe E, Lu R, Ghory HZ, Silver PA, Engelman A. 2002. Nuclear localization of human immunodeficiency virus type 1 preintegration complexes (PICs): V165A and R166A are pleiotropic integrase mutants primarily defective for integration, not PIC nuclear import. J Virol 76:10598-10607. http://dx.doi.org/10.1128/JVI.76.21.10598-10607.2002.
    • (2002) J Virol , vol.76 , pp. 10598-10607
    • Limon, A.1    Devroe, E.2    Lu, R.3    Ghory, H.Z.4    Silver, P.A.5    Engelman, A.6
  • 79
    • 34249726735 scopus 로고    scopus 로고
    • The role of lysine 186 in HIV-1 integrase multimerization
    • Berthoux L, Sebastian S, Muesing MA, Luban J. 2007. The role of lysine 186 in HIV-1 integrase multimerization. Virology 364:227-236. http://dx.doi.org/10.1016/j.virol.2007.02.029.
    • (2007) Virology , vol.364 , pp. 227-236
    • Berthoux, L.1    Sebastian, S.2    Muesing, M.A.3    Luban, J.4
  • 80
    • 45249094281 scopus 로고    scopus 로고
    • Four-tiered pi interaction at the dimeric interface of HIV-1 integrase critical for DNA integration and viral infectivity
    • Al-Mawsawi LQ, Hombrouck A, Dayam R, Debyser Z, Neamati N. 2008. Four-tiered pi interaction at the dimeric interface of HIV-1 integrase critical for DNA integration and viral infectivity. Virology 377:355-363. http://dx.doi.org/10.1016/j.virol.2008.04.030.
    • (2008) Virology , vol.377 , pp. 355-363
    • Al-Mawsawi, L.Q.1    Hombrouck, A.2    Dayam, R.3    Debyser, Z.4    Neamati, N.5
  • 81
    • 84866485829 scopus 로고    scopus 로고
    • A symmetric region of the HIV-1 integrase dimerization interface is essential for viral replication
    • Serrao E, Thys W, Demeulemeester J, Al-Mawsawi LQ, Christ F, Debyser Z, Neamati N. 2012. A symmetric region of the HIV-1 integrase dimerization interface is essential for viral replication. PLoS One 7:e45177. http://dx.doi.org/10.1371/journal.pone.0045177.
    • (2012) PLoS One , vol.7
    • Serrao, E.1    Thys, W.2    Demeulemeester, J.3    Al-Mawsawi, L.Q.4    Christ, F.5    Debyser, Z.6    Neamati, N.7
  • 82
    • 28444445583 scopus 로고    scopus 로고
    • Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75
    • Cherepanov P, Ambrosio AL, Rahman S, Ellenberger T, Engelman A. 2005. Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75. Proc Natl Acad Sci USA 102:17308-17313. http://dx.doi.org/10.1073/pnas.0506924102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17308-17313
    • Cherepanov, P.1    Ambrosio, A.L.2    Rahman, S.3    Ellenberger, T.4    Engelman, A.5
  • 83
    • 84878869428 scopus 로고    scopus 로고
    • Allosteric inhibition of HIV-1 integrase activity
    • Engelman A, Kessl JJ, Kvaratskhelia M. 2013. Allosteric inhibition of HIV-1 integrase activity. Curr Opin Chem Biol 17:339-345. http://dx.doi.org/10.1016/j.cbpa.2013.04.010.
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 339-345
    • Engelman, A.1    Kessl, J.J.2    Kvaratskhelia, M.3
  • 85
    • 0014436758 scopus 로고
    • Molecular pathology of human haemoglobin
    • Perutz MF, Lehmann H. 1968. Molecular pathology of human haemoglobin. Nature 219:902-909. http://dx.doi.org/10.1038/219902a0.
    • (1968) Nature , vol.219 , pp. 902-909
    • Perutz, M.F.1    Lehmann, H.2
  • 92
    • 50049135016 scopus 로고    scopus 로고
    • Robustness promotes evolvability of thermotolerance in an RNA virus
    • McBride RC, Ogbunugafor CB, Turner PE. 2008. Robustness promotes evolvability of thermotolerance in an RNA virus. BMC Evol Biol 8:231. http://dx.doi.org/10.1186/1471-2148-8-231.
    • (2008) BMC Evol Biol , vol.8 , pp. 231
    • McBride, R.C.1    Ogbunugafor, C.B.2    Turner, P.E.3


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