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Volumn 58, Issue 8, 2014, Pages 4915-4919

SAMHD1 has differential impact on the efficacies of HIV nucleoside reverse transcriptase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; DIDEOXYNUCLEOTIDE; LAMIVUDINE; LUCIFERASE; MONOMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; PHOSPHONIC ACID DERIVATIVE; RNA DIRECTED DNA POLYMERASE; RNA DIRECTED DNA POLYMERASE INHIBITOR; SAMHD1 PROTEIN, HUMAN; SMALL INTERFERING RNA; STAVUDINE; TENOFOVIR; ZIDOVUDINE;

EID: 84905380670     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.02745-14     Document Type: Article
Times cited : (25)

References (63)
  • 2
    • 78649858731 scopus 로고    scopus 로고
    • Ribonucleoside triphosphates as substrate of human immunodeficiency virus type 1 reverse transcriptase in human macrophages
    • Kennedy EM, Gavegnano C, Nguyen L, Slater R, Lucas A, Fromentin E, Schinazi RF, Kim B. 2010. Ribonucleoside triphosphates as substrate of human immunodeficiency virus type 1 reverse transcriptase in human macrophages. J. Biol. Chem. 285:39380-39391. http://dx.doi.org/10.1074/jbc.M110.178582.
    • (2010) J. Biol. Chem. , vol.285 , pp. 39380-39391
    • Kennedy, E.M.1    Gavegnano, C.2    Nguyen, L.3    Slater, R.4    Lucas, A.5    Fromentin, E.6    Schinazi, R.F.7    Kim, B.8
  • 7
    • 0028874048 scopus 로고
    • Rapid turnover of plasma virions and CD4 lymphocytes in HIV-1 infection
    • Ho DD, Neumann AU, Perelson AS, Chen W, Leonard JM, Markowitz M. 1995. Rapid turnover of plasma virions and CD4 lymphocytes in HIV-1 infection. Natur. 373:123-126. http://dx.doi.org/10.1038/373123a0.
    • (1995) Natur. , vol.373 , pp. 123-126
    • Ho, D.D.1    Neumann, A.U.2    Perelson, A.S.3    Chen, W.4    Leonard, J.M.5    Markowitz, M.6
  • 8
    • 67649253072 scopus 로고    scopus 로고
    • HIV interactions with monocytes and dendritic cells: Viral latency and reservoirs
    • Coleman CM, Wu L. 2009. HIV interactions with monocytes and dendritic cells: viral latency and reservoirs. Retrovirolog. 6:51. http://dx.doi.org/10. 1186/1742-4690-6-51.
    • (2009) Retrovirolog. , vol.6 , pp. 51
    • Coleman, C.M.1    Wu, L.2
  • 9
    • 77956497003 scopus 로고    scopus 로고
    • A cryptic sensor for HIV-1 activates antiviral innate immunity in dendritic cells
    • Manel N, Hogstad B, Wang Y, Levy DE, Unutmaz D, Littman DR. 2010. A cryptic sensor for HIV-1 activates antiviral innate immunity in dendritic cells. Natur. 467:214-217. http://dx.doi.org/10.1038/nature09337.
    • (2010) Natur. , vol.467 , pp. 214-217
    • Manel, N.1    Hogstad, B.2    Wang, Y.3    Levy, D.E.4    Unutmaz, D.5    Littman, D.R.6
  • 10
    • 77950632109 scopus 로고    scopus 로고
    • Host hindrance to HIV-1 replication in monocytes and macrophages
    • Bergamaschi A, Pancino G. 2010. Host hindrance to HIV-1 replication in monocytes and macrophages. Retrovirolog. 7:31. http://dx.doi.org/10.1186/1742- 4690-7-31.
    • (2010) Retrovirolog. , vol.7 , pp. 31
    • Bergamaschi, A.1    Pancino, G.2
  • 15
    • 83755162644 scopus 로고    scopus 로고
    • Aicardi-Goutieres syndrome gene and HIV-1 restriction factor SAMHD1 is a dGTPregulated deoxynucleotide triphosphohydrolase
    • Powell RD, Holland PJ, Hollis T, Perrino FW. 2011. Aicardi-Goutieres syndrome gene and HIV-1 restriction factor SAMHD1 is a dGTPregulated deoxynucleotide triphosphohydrolase. J. Biol. Chem. 286:43596-43600. http://dx.doi.org/10.1074/jbc.C111.317628.
    • (2011) J. Biol. Chem. , vol.286 , pp. 43596-43600
    • Powell, R.D.1    Holland, P.J.2    Hollis, T.3    Perrino, F.W.4
  • 17
    • 84862654149 scopus 로고    scopus 로고
    • Tight interplay among SAMHD1 protein level, cellular dNTP levels, and HIV-1 proviral DNA synthesis kinetics in human primary monocyte-derived macrophages
    • Kim B, Nguyen LA, Daddacha W, Hollenbaugh JA. 2012. Tight interplay among SAMHD1 protein level, cellular dNTP levels, and HIV-1 proviral DNA synthesis kinetics in human primary monocyte-derived macrophages. J. Biol. Chem. 287:21570-21574. http://dx.doi.org/10.1074/jbc.C112.374843.
    • (2012) J. Biol. Chem. , vol.287 , pp. 21570-21574
    • Kim, B.1    Nguyen, L.A.2    Daddacha, W.3    Hollenbaugh, J.A.4
  • 18
    • 84874959500 scopus 로고    scopus 로고
    • Nuclease activity of the human SAMHD1 protein implicated in the Aicardi-Goutieres syndrome and HIV-1 restriction
    • Beloglazova N, Flick R, Tchigvintsev A, Brown G, Popovic A, Nocek B, Yakunin AF. 2013. Nuclease activity of the human SAMHD1 protein implicated in the Aicardi-Goutieres syndrome and HIV-1 restriction. J. Biol. Chem. 288:8101-8110. http://dx.doi.org/10.1074/jbc.M112.431148.
    • (2013) J. Biol. Chem. , vol.288 , pp. 8101-8110
    • Beloglazova, N.1    Flick, R.2    Tchigvintsev, A.3    Brown, G.4    Popovic, A.5    Nocek, B.6    Yakunin, A.F.7
  • 19
    • 84880050735 scopus 로고    scopus 로고
    • Anti-HIV host factor SAMHD1 regulates viral sensitivity to nucleoside reverse transcriptase inhibitors via modulation of cellular deoxyribonucleoside triphosphate (dNTP) levels
    • Amie SM, Daly MB, Noble E, Schinazi RF, Bambara RA, Kim B. 2013. Anti-HIV host factor SAMHD1 regulates viral sensitivity to nucleoside reverse transcriptase inhibitors via modulation of cellular deoxyribonucleoside triphosphate (dNTP) levels. J. Biol. Chem. 288:20683-20691. http://dx.doi.org/ 10.1074/jbc.M113.472159.
    • (2013) J. Biol. Chem. , vol.288 , pp. 20683-20691
    • Amie, S.M.1    Daly, M.B.2    Noble, E.3    Schinazi, R.F.4    Bambara, R.A.5    Kim, B.6
  • 21
    • 33747100570 scopus 로고    scopus 로고
    • Pharmacology of current and promising nucleosides for the treatment of human immunodeficiency viruses
    • Schinazi RF, Hernandez-Santiago BI, Hurwitz SJ. 2006. Pharmacology of current and promising nucleosides for the treatment of human immunodeficiency viruses. Antiviral Res. 71:322-334. http://dx.doi.org/10.1016/j.antiviral.2006. 03.012.
    • (2006) Antiviral Res. , vol.71 , pp. 322-334
    • Schinazi, R.F.1    Hernandez-Santiago, B.I.2    Hurwitz, S.J.3
  • 22
    • 0034566114 scopus 로고    scopus 로고
    • Inhibitors of HIV-1 reverse transcriptase
    • Parniak MA, Sluis-Cremer N. 2000. Inhibitors of HIV-1 reverse transcriptase. Adv. Pharmacol. 49:67-109. http://dx.doi.org/10.1016/S1054- 3589(00)49024-1.
    • (2000) Adv. Pharmacol. , vol.49 , pp. 67-109
    • Parniak, M.A.1    Sluis-Cremer, N.2
  • 23
    • 34250811436 scopus 로고    scopus 로고
    • Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV
    • De Clercq E. 2007. Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV. Verh. K. Acad. Geneeskd. Belg. 69:81-104. http://dx.doi.org/10.1016/j.ijantimicag.2008.10.010.
    • (2007) Verh. K. Acad. Geneeskd. Belg. , vol.69 , pp. 81-104
    • De Clercq, E.1
  • 24
    • 60549106419 scopus 로고    scopus 로고
    • Antimicrobial strategies: Inhibition of viral polymerases by 3=-hydroxyl nucleosides
    • Deval J. 2009. Antimicrobial strategies: inhibition of viral polymerases by 3=-hydroxyl nucleosides. Drug. 69:151-166. http://dx.doi.org/10.2165/ 00003495-200969020-00002.
    • (2009) Drug. , vol.69 , pp. 151-166
    • Deval, J.1
  • 25
    • 37249019061 scopus 로고    scopus 로고
    • Inhibitors of HIV-1 reverse transcriptase
    • Ilina T, Parniak MA. 2008. Inhibitors of HIV-1 reverse transcriptase. Adv. Pharmacol. 56:121-167. http://dx.doi.org/10.1016/S1054-3589(07)56005-9.
    • (2008) Adv. Pharmacol. , vol.56 , pp. 121-167
    • Ilina, T.1    Parniak, M.A.2
  • 26
    • 77955594846 scopus 로고    scopus 로고
    • Structural aspects of drug resistance and inhibition of HIV-1 reverse transcriptase
    • Singh K, Marchand B, Kirby KA, Michailidis E, Sarafianos SG. 2010. Structural aspects of drug resistance and inhibition of HIV-1 reverse transcriptase. Viruse. 2:606-638. http://dx.doi.org/10.3390/v2020606.
    • (2010) Viruse. , vol.2 , pp. 606-638
    • Singh, K.1    Marchand, B.2    Kirby, K.A.3    Michailidis, E.4    Sarafianos, S.G.5
  • 27
    • 58149133507 scopus 로고    scopus 로고
    • Structure and function of HIV-1 reverse transcriptase: Molecular mechanisms of polymerization and inhibition
    • Sarafianos SG, Marchand B, Das K, Himmel DM, Parniak MA, Hughes SH, Arnold E. 2009. Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition. J. Mol. Biol. 385:693-713. http://dx.doi.org/10.1016/j.jmb.2008.10.071.
    • (2009) J. Mol. Biol. , vol.385 , pp. 693-713
    • Sarafianos, S.G.1    Marchand, B.2    Das, K.3    Himmel, D.M.4    Parniak, M.A.5    Hughes, S.H.6    Arnold, E.7
  • 28
    • 0036696712 scopus 로고    scopus 로고
    • Targeting HIV: Antiretroviral therapy and development of drug resistance
    • Menendez-Arias L. 2002. Targeting HIV: antiretroviral therapy and development of drug resistance. Trends Pharmacol. Sci. 23:381-388. http://dx.doi.org/10.1016/S0165-6147(02)02054-0.
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 381-388
    • Menendez-Arias, L.1
  • 29
    • 43049105858 scopus 로고    scopus 로고
    • Mechanisms of resistance to nucleoside analogue inhibitors of HIV-1 reverse transcriptase
    • Menendez-Arias L. 2008. Mechanisms of resistance to nucleoside analogue inhibitors of HIV-1 reverse transcriptase. Virus Res. 134:124-146. http://dx.doi.org/10.1016/j.virusres.2007.12.015.
    • (2008) Virus Res. , vol.134 , pp. 124-146
    • Menendez-Arias, L.1
  • 35
    • 79959501411 scopus 로고    scopus 로고
    • The sugar ring conformation of 4=-ethynyl-2-fluoro-2=-deoxyadenosine and its recognition by the polymerase active site of HIV reverse transcriptase
    • Noisy-le-grand
    • Kirby KA, Singh K, Michailidis E, Marchand B, Kodama EN, Ashida N, Mitsuya H, Parniak MA, Sarafianos SG. 2011. The sugar ring conformation of 4=-ethynyl-2-fluoro-2=-deoxyadenosine and its recognition by the polymerase active site of HIV reverse transcriptase. Cell. Mol. Biol. (Noisy-le-grand. 57:40-46.
    • (2011) Cell. Mol. Biol. , vol.57 , pp. 40-46
    • Kirby, K.A.1    Singh, K.2    Michailidis, E.3    Marchand, B.4    Kodama, E.N.5    Ashida, N.6    Mitsuya, H.7    Parniak, M.A.8    Sarafianos, S.G.9
  • 36
  • 38
    • 0023785829 scopus 로고
    • Inhibition of human immunodeficiency virus (HIV-1/HTLV-IIIBa-L) replication in fresh and cultured human peripheral blood monocytes/macrophages by azidothymidine and related 2=, 3=-dideoxynucleosides
    • Perno CF, Yarchoan R, Cooney DA, Hartman NR, Gartner S, Popovic M, Hao Z, Gerrard TL, Wilson YA, Johns DG, Broder S. 1988. Inhibition of human immunodeficiency virus (HIV-1/HTLV-IIIBa-L) replication in fresh and cultured human peripheral blood monocytes/macrophages by azidothymidine and related 2=, 3=-dideoxynucleosides. J. Exp. Med. 168:1111-1125. http://dx.doi.org/10.1084/ jem.168.3.1111.
    • (1988) J. Exp. Med. , vol.168 , pp. 1111-1125
    • Perno, C.F.1    Yarchoan, R.2    Cooney, D.A.3    Hartman, N.R.4    Gartner, S.5    Popovic, M.6    Hao, Z.7    Gerrard, T.L.8    Wilson, Y.A.9    Johns, D.G.10    Broder, S.11
  • 39
    • 0035174783 scopus 로고    scopus 로고
    • Phosphorylation of nucleoside analog antiretrovirals: A review for clinicians
    • Stein DS, Moore KH. 2001. Phosphorylation of nucleoside analog antiretrovirals: a review for clinicians. Pharmacotherap. 21:11-34. http://dx.doi.org/10.1592/phco.21.1.11.34439.
    • (2001) Pharmacotherap. , vol.21 , pp. 11-34
    • Stein, D.S.1    Moore, K.H.2
  • 40
    • 23144439258 scopus 로고    scopus 로고
    • Intracellular interactions between nucleos (t) ide inhibitors of HIV reverse transcriptase
    • Ray AS. 2005. Intracellular interactions between nucleos (t) ide inhibitors of HIV reverse transcriptase. AIDS Rev. 7:113-125.
    • (2005) AIDS Rev. , vol.7 , pp. 113-125
    • Ray, A.S.1
  • 41
    • 84867685145 scopus 로고    scopus 로고
    • Identification and characterization of naturally occurring splice variants of SAMHD1
    • Welbourn S, Miyagi E, White TE, Diaz-Griffero F, Strebel K. 2012. Identification and characterization of naturally occurring splice variants of SAMHD1. Retrovirolog. 9:86. http://dx.doi.org/10.1186/1742-4690-9-86.
    • (2012) Retrovirolog. , vol.9 , pp. 86
    • Welbourn, S.1    Miyagi, E.2    White, T.E.3    Diaz-Griffero, F.4    Strebel, K.5
  • 43
    • 0034679569 scopus 로고    scopus 로고
    • Structural basis for activation of alpha-boranophosphate nucleotide analogues targeting drug-resistant reverse transcriptase
    • Meyer P, Schneider B, Sarfati S, Deville-Bonne D, Guerreiro C, Boretto J, Janin J, Veron M, Canard B. 2000. Structural basis for activation of alpha-boranophosphate nucleotide analogues targeting drug-resistant reverse transcriptase. EMBO J. 19:3520-3529. http://dx.doi.org/10.1093/emboj/19.14.3520.
    • (2000) EMBO J. , vol.19 , pp. 3520-3529
    • Meyer, P.1    Schneider, B.2    Sarfati, S.3    Deville-Bonne, D.4    Guerreiro, C.5    Boretto, J.6    Janin, J.7    Veron, M.8    Canard, B.9
  • 44
    • 1442351728 scopus 로고    scopus 로고
    • The cellular pharmacology of nucleoside- and nucleotide-analogue reverse-transcriptase inhibitors and its relationship to clinical toxicities
    • Anderson PL, Kakuda TN, Lichtenstein KA. 2004. The cellular pharmacology of nucleoside- and nucleotide-analogue reverse-transcriptase inhibitors and its relationship to clinical toxicities. Clin. Infect. Dis. 38:743-753. http://dx.doi.org/10.1086/381678.
    • (2004) Clin. Infect. Dis. , vol.38 , pp. 743-753
    • Anderson, P.L.1    Kakuda, T.N.2    Lichtenstein, K.A.3
  • 45
    • 33745698359 scopus 로고    scopus 로고
    • Mitochondrial AZT metabolism
    • Samuels DC. 2006. Mitochondrial AZT metabolism. IUBMB Lif. 58:403-408. http://dx.doi.org/10.1080/15216540600791571.
    • (2006) IUBMB Lif. , vol.58 , pp. 403-408
    • Samuels, D.C.1
  • 46
    • 0024435381 scopus 로고
    • Phosphorylation of 2=, 3=-dideoxyinosine by cytosolic 5=-nucleotidase of human lymphoid cells
    • Johnson MA, Fridland A. 1989. Phosphorylation of 2=, 3=-dideoxyinosine by cytosolic 5=-nucleotidase of human lymphoid cells. Mol. Pharmacol. 36:291-295.
    • (1989) Mol. Pharmacol. , vol.36 , pp. 291-295
    • Johnson, M.A.1    Fridland, A.2
  • 47
    • 17644420382 scopus 로고    scopus 로고
    • A computational model of mitochondrial deoxynucleotide metabolism and DNA replication
    • Bradshaw PC, Samuels DC. 2005. A computational model of mitochondrial deoxynucleotide metabolism and DNA replication. Am. J. Physiol. Cell Physiol. 288:C989-C1002. http://dx.doi.org/10.1152/ajpcell.00530.2004.
    • (2005) Am. J. Physiol. Cell Physiol. , vol.288
    • Bradshaw, P.C.1    Samuels, D.C.2
  • 48
    • 0036693511 scopus 로고    scopus 로고
    • Structure and function of cellular deoxyribonucleoside kinases
    • Eriksson S, Munch-Petersen B, Johansson K, Eklund H. 2002. Structure and function of cellular deoxyribonucleoside kinases. Cell. Mol. Life Sci. 59:1327-1346. http://dx.doi.org/10.1007/s00018-002-8511-x.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1327-1346
    • Eriksson, S.1    Munch-Petersen, B.2    Johansson, K.3    Eklund, H.4
  • 49
    • 0028920558 scopus 로고
    • Cytotoxicity of 3=-azido-3=-deoxythymidine correlates with 3=-azidothymidine-5=-monophosphate (AZTMP) levels, whereas antihuman immunodeficiency virus (HIV) activity correlates with 3=-azidothymidine-5=- triphosphate (AZTTP) levels in cultured CEM Tlymphoblastoid cells
    • Tornevik Y, Ullman B, Balzarini J, Wahren B, Eriksson S. 1995. Cytotoxicity of 3=-azido-3=-deoxythymidine correlates with 3=-azidothymidine-5=- monophosphate (AZTMP) levels, whereas antihuman immunodeficiency virus (HIV) activity correlates with 3=-azidothymidine-5=-triphosphate (AZTTP) levels in cultured CEM Tlymphoblastoid cells. Biochem. Pharmacol. 49:829-837. http://dx.doi.org/10.1016/0006-2952(94)00453-S.
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 829-837
    • Tornevik, Y.1    Ullman, B.2    Balzarini, J.3    Wahren, B.4    Eriksson, S.5
  • 50
    • 0028144849 scopus 로고
    • Metabolism of 3=-azido-3=-deoxythymidine (AZT) in human placental trophoblasts and Hofbauer cells
    • http://dx.doi.org/10.1016/0006-29529490111-2.
    • Qian M, Bui T, Ho RJ, Unadkat JD. 1994. Metabolism of 3=-azido-3=-deoxythymidine (AZT) in human placental trophoblasts and Hofbauer cells. Biochem. Pharmacol. 48:383-389. http://dx.doi.org/10.1016/0091-3057(94) 90542-8, http://dx.doi.org/10.1016/0006-2952 (94)90111-2.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 383-389
    • Qian, M.1    Bui, T.2    Ho, R.J.3    Unadkat, J.D.4
  • 52
    • 0028300765 scopus 로고
    • Divergent antihuman immunodeficiency virus activity and anabolic phosphorylation of 2=, 3=-dideoxynucleoside analogs in resting and activated human cells
    • Gao WY, Agbaria R, Driscoll JS, Mitsuya H. 1994. Divergent antihuman immunodeficiency virus activity and anabolic phosphorylation of 2=, 3=-dideoxynucleoside analogs in resting and activated human cells. J. Biol. Chem. 269:12633-12638.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12633-12638
    • Gao, W.Y.1    Agbaria, R.2    Driscoll, J.S.3    Mitsuya, H.4
  • 54
    • 0024592935 scopus 로고
    • Differential patterns of intracellular metabolism of 2=, 3=-didehydro-2=, 3=-dideoxythymidine and 3=-azido-2=, 3=-dideoxythymidine, two potent anti-human immunodeficiency virus compounds
    • Balzarini J, Herdewijn P, De Clercq E. 1989. Differential patterns of intracellular metabolism of 2=, 3=-didehydro-2=, 3=-dideoxythymidine and 3=-azido-2=, 3=-dideoxythymidine, two potent anti-human immunodeficiency virus compounds. J. Biol. Chem. 264:6127-6133.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6127-6133
    • Balzarini, J.1    Herdewijn, P.2    De Clercq, E.3
  • 56
    • 2642620186 scopus 로고    scopus 로고
    • Pre-steady state of reaction of nucleoside diphosphate kinase with anti-HIV nucleotides
    • Schneider B, Xu YW, Sellam O, Sarfati R, Janin J, Veron M, Deville-Bonne D. 1998. Pre-steady state of reaction of nucleoside diphosphate kinase with anti-HIV nucleotides. J. Biol. Chem. 273:11491-11497. http://dx.doi.org/10.1074/ jbc.273.19.11491.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11491-11497
    • Schneider, B.1    Xu, Y.W.2    Sellam, O.3    Sarfati, R.4    Janin, J.5    Veron, M.6    Deville-Bonne, D.7
  • 59
    • 77950646448 scopus 로고    scopus 로고
    • Limelight on two HIV/SIV accessory proteins in macrophage infection: Is Vpx overshadowing Vpr?
    • Ayinde D, Maudet C, Transy C, Margottin-Goguet F. 2010. Limelight on two HIV/SIV accessory proteins in macrophage infection: is Vpx overshadowing Vpr? Retrovirolog. 7:35. http://dx.doi.org/10.1186/1742-4690-7-35.
    • (2010) Retrovirolog. , vol.7 , pp. 35
    • Ayinde, D.1    Maudet, C.2    Transy, C.3    Margottin-Goguet, F.4
  • 60
    • 79958172300 scopus 로고    scopus 로고
    • A simple, versatile and efficient method to genetically modify human monocyte-derived dendritic cells with HIV-1-derived lentiviral vectors
    • Berger G, Durand S, Goujon C, Nguyen XN, Cordeil S, Darlix JL, Cimarelli A. 2011. A simple, versatile and efficient method to genetically modify human monocyte-derived dendritic cells with HIV-1-derived lentiviral vectors. Nat. Protoc. 6:806-816. http://dx.doi.org/10.1038/nprot.2011.327.
    • (2011) Nat. Protoc. , vol.6 , pp. 806-816
    • Berger, G.1    Durand, S.2    Goujon, C.3    Nguyen, X.N.4    Cordeil, S.5    Darlix, J.L.6    Cimarelli, A.7
  • 61
    • 33744832621 scopus 로고    scopus 로고
    • With a little help from a friend: Increasing HIV transduction of monocyte-derived dendritic cells with virion-like particles of SIVMAC
    • Goujon C, Jarrosson-Wuilleme L, Bernaud J, Rigal D, Darlix JL, Cimarelli A. 2006. With a little help from a friend: increasing HIV transduction of monocyte-derived dendritic cells with virion-like particles of SIVMAC. Gene Ther. 13:991-994. http://dx.doi.org/10.1038/sj.gt.3302753.
    • (2006) Gene Ther. , vol.13 , pp. 991-994
    • Goujon, C.1    Jarrosson-Wuilleme, L.2    Bernaud, J.3    Rigal, D.4    Darlix, J.L.5    Cimarelli, A.6
  • 62
    • 33846701783 scopus 로고    scopus 로고
    • SIVSM/HIV-2 Vpx proteins promote retroviral escape from a proteasome-dependent restriction pathway present in human dendritic cells
    • Goujon C, Riviere L, Jarrosson-Wuilleme L, Bernaud J, Rigal D, Darlix JL, Cimarelli A. 2007. SIVSM/HIV-2 Vpx proteins promote retroviral escape from a proteasome-dependent restriction pathway present in human dendritic cells. Retrovirolog. 4:2. http://dx.doi.org/10.1186/1742-4690-4-2.
    • (2007) Retrovirolog. , vol.4 , pp. 2
    • Goujon, C.1    Riviere, L.2    Jarrosson-Wuilleme, L.3    Bernaud, J.4    Rigal, D.5    Darlix, J.L.6    Cimarelli, A.7


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