메뉴 건너뛰기




Volumn 42, Issue 9, 2010, Pages 1482-1488

Rev-derived peptides inhibit HIV-1 replication by antagonism of Rev and a co-receptor, CXCR4

Author keywords

Alpha helix; CXCR4; HIV 1; Inhibitor; Rev

Indexed keywords

ARGININE; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR4; N [4 [[[6,7 DIHYDRO 2 (4 METHYLPHENYL) 5H BENZOCYCLOHEPTEN 8 YL]CARBONYL]AMINO]BENZYL] N,N DIMETHYL 2H TETRAHYDROPYRAN 4 AMINIUM CHLORIDE; PLERIXAFOR; REV PROTEIN; REV PROTEIN 1-21; REV PROTEIN 34-50; RNA BINDING PROTEIN; UNCLASSIFIED DRUG; ZIDOVUDINE; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; PEPTIDE;

EID: 77955096962     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2010.05.005     Document Type: Article
Times cited : (7)

References (48)
  • 1
    • 0025296036 scopus 로고
    • Structure-function analyses of the HTLV-I Rex and HIV-1 Rev RNA response elements: insights into the mechanism of Rex and Rev action
    • Ahmed Y.F., Hanly S.M., Malim M.H., Cullen B.R., Greene W.C. Structure-function analyses of the HTLV-I Rex and HIV-1 Rev RNA response elements: insights into the mechanism of Rex and Rev action. Genes Dev 1990, 4:1014-1022.
    • (1990) Genes Dev , vol.4 , pp. 1014-1022
    • Ahmed, Y.F.1    Hanly, S.M.2    Malim, M.H.3    Cullen, B.R.4    Greene, W.C.5
  • 2
    • 0032954383 scopus 로고    scopus 로고
    • T134, a small-molecule CXCR4 inhibitor, has no cross-drug resistance with AMD3100, a CXCR4 antagonist with a different structure
    • Arakaki R., Tamamura H., Premanathan M., Kanbara K., Ramanan S., Katsura Mochizuki K., et al. T134, a small-molecule CXCR4 inhibitor, has no cross-drug resistance with AMD3100, a CXCR4 antagonist with a different structure. J Virol 1999, 73:1719-1723.
    • (1999) J Virol , vol.73 , pp. 1719-1723
    • Arakaki, R.1    Tamamura, H.2    Premanathan, M.3    Kanbara, K.4    Ramanan, S.5    Katsura Mochizuki, K.6
  • 3
    • 13044256383 scopus 로고    scopus 로고
    • A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-HIV-1 activity
    • Baba M., Nishimura O., Kanzaki N., Okamoto M., Sawada H., Iizawa Y., et al. A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-HIV-1 activity. Proc Natl Acad Sci U S A 1999, 96:5698-5703.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 5698-5703
    • Baba, M.1    Nishimura, O.2    Kanzaki, N.3    Okamoto, M.4    Sawada, H.5    Iizawa, Y.6
  • 4
    • 0029784592 scopus 로고    scopus 로고
    • Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex
    • Battiste J.L., Mao H., Rao N.S., Tan R., Muhandiram D.R., Kay L.E., et al. Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex. Science 1996, 273:1547-1551.
    • (1996) Science , vol.273 , pp. 1547-1551
    • Battiste, J.L.1    Mao, H.2    Rao, N.S.3    Tan, R.4    Muhandiram, D.R.5    Kay, L.E.6
  • 5
    • 0025954618 scopus 로고
    • The type I human T-cell leukemia virus (HTLV-I) Rex trans-activator binds directly to the HTLV-I Rex and the type 1 human immunodeficiency virus Rev RNA response elements
    • Bogerd H.P., Huckaby G.L., Ahmed Y.F., Hanly S.M., Greene W.C. The type I human T-cell leukemia virus (HTLV-I) Rex trans-activator binds directly to the HTLV-I Rex and the type 1 human immunodeficiency virus Rev RNA response elements. Proc Natl Acad Sci U S A 1991, 88:5704-5708.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 5704-5708
    • Bogerd, H.P.1    Huckaby, G.L.2    Ahmed, Y.F.3    Hanly, S.M.4    Greene, W.C.5
  • 6
    • 0031567148 scopus 로고    scopus 로고
    • A dynamic in vivo view of the HIV-I Rev-RRE interaction
    • Charpentier B., Stutz F., Rosbash M. A dynamic in vivo view of the HIV-I Rev-RRE interaction. J Mol Biol 1997, 266:950-962.
    • (1997) J Mol Biol , vol.266 , pp. 950-962
    • Charpentier, B.1    Stutz, F.2    Rosbash, M.3
  • 7
    • 52049106911 scopus 로고    scopus 로고
    • A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA
    • Daugherty M.D., D'Orso I., Frankel A.D. A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. Mol Cell 2008, 31:824-834.
    • (2008) Mol Cell , vol.31 , pp. 824-834
    • Daugherty, M.D.1    D'Orso, I.2    Frankel, A.D.3
  • 8
    • 0024846372 scopus 로고
    • Functional analysis of CAR, the target sequence for the Rev protein of HIV-1
    • Dayton E.T., Powell D.M., Dayton A.I. Functional analysis of CAR, the target sequence for the Rev protein of HIV-1. Science 1989, 246:1625-1629.
    • (1989) Science , vol.246 , pp. 1625-1629
    • Dayton, E.T.1    Powell, D.M.2    Dayton, A.I.3
  • 10
    • 0030773515 scopus 로고    scopus 로고
    • A small-molecule inhibitor directed against the chemokine receptor CXCR4 prevents its use as an HIV-1 coreceptor
    • Doranz B.J., Grovit-Ferbas K., Sharron M.P., Mao S.H., Goetz M.B., Daar E.S., et al. A small-molecule inhibitor directed against the chemokine receptor CXCR4 prevents its use as an HIV-1 coreceptor. J Exp Med 1997, 186:1395-1400.
    • (1997) J Exp Med , vol.186 , pp. 1395-1400
    • Doranz, B.J.1    Grovit-Ferbas, K.2    Sharron, M.P.3    Mao, S.H.4    Goetz, M.B.5    Daar, E.S.6
  • 11
    • 0029160316 scopus 로고
    • The roles of nucleolar structure and function in the subcellular location of the HIV-1 Rev protein
    • Dundr M., Leno G.H., Hammarskjold M.L., Rekosh D., Helga-Maria C., Olson M.O. The roles of nucleolar structure and function in the subcellular location of the HIV-1 Rev protein. J Cell Sci 1995, 108(Pt 8):2811-2823.
    • (1995) J Cell Sci , vol.108 , Issue.PART 8 , pp. 2811-2823
    • Dundr, M.1    Leno, G.H.2    Hammarskjold, M.L.3    Rekosh, D.4    Helga-Maria, C.5    Olson, M.O.6
  • 12
    • 34347378496 scopus 로고    scopus 로고
    • HIV entry inhibitors
    • Este J.A., Telenti A. HIV entry inhibitors. Lancet 2007, 370:81-88.
    • (2007) Lancet , vol.370 , pp. 81-88
    • Este, J.A.1    Telenti, A.2
  • 13
    • 0025289880 scopus 로고
    • Feedback regulation of human immunodeficiency virus type 1 expression by the Rev protein
    • Felber B.K., Drysdale C.M., Pavlakis G.N. Feedback regulation of human immunodeficiency virus type 1 expression by the Rev protein. J Virol 1990, 64:3734-3741.
    • (1990) J Virol , vol.64 , pp. 3734-3741
    • Felber, B.K.1    Drysdale, C.M.2    Pavlakis, G.N.3
  • 15
    • 0029130169 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fischer U., Huber J., Boelens W.C., Mattaj I.W., Luhrmann R. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 1995, 82:475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Luhrmann, R.5
  • 16
    • 0030794881 scopus 로고    scopus 로고
    • Embodying a stable alpha-helical protein structure through efficient chemical ligation via thioether formation
    • Futaki S., Ishikawa T., Niwa M., Kitagawa K., Yagami T. Embodying a stable alpha-helical protein structure through efficient chemical ligation via thioether formation. Bioorg Med Chem 1997, 5:1883-1891.
    • (1997) Bioorg Med Chem , vol.5 , pp. 1883-1891
    • Futaki, S.1    Ishikawa, T.2    Niwa, M.3    Kitagawa, K.4    Yagami, T.5
  • 17
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • Futaki S., Suzuki T., Ohashi W., Yagami T., Tanaka S., Ueda K., et al. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J Biol Chem 2001, 276:5836-5840.
    • (2001) J Biol Chem , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6
  • 18
    • 0027216157 scopus 로고
    • Multiple arginine residues within the basic domain of HTLV-I Rex are required for specific RNA binding and function
    • Hammes S.R., Greene W.C. Multiple arginine residues within the basic domain of HTLV-I Rex are required for specific RNA binding and function. Virology 1993, 193:41-49.
    • (1993) Virology , vol.193 , pp. 41-49
    • Hammes, S.R.1    Greene, W.C.2
  • 19
    • 0029868515 scopus 로고    scopus 로고
    • Selection of RNA-binding peptides in vivo
    • Harada K., Martin S.S., Frankel A.D. Selection of RNA-binding peptides in vivo. Nature 1996, 380:175-179.
    • (1996) Nature , vol.380 , pp. 175-179
    • Harada, K.1    Martin, S.S.2    Frankel, A.D.3
  • 20
    • 0030726778 scopus 로고    scopus 로고
    • Molding a peptide into an RNA site by in vivo peptide evolution
    • Harada K., Martin S.S., Tan R., Frankel A.D. Molding a peptide into an RNA site by in vivo peptide evolution. Proc Natl Acad Sci U S A 1997, 94:11887-11892.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11887-11892
    • Harada, K.1    Martin, S.S.2    Tan, R.3    Frankel, A.D.4
  • 21
    • 0035265946 scopus 로고    scopus 로고
    • Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants
    • Jain C., Belasco J.G. Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants. Mol Cell 2001, 7:603-614.
    • (2001) Mol Cell , vol.7 , pp. 603-614
    • Jain, C.1    Belasco, J.G.2
  • 22
    • 0033572743 scopus 로고    scopus 로고
    • Anchoring an extended HTLV-1 Rex peptide within an RNA major groove containing junctional base triples
    • Jiang F., Gorin A., Hu W., Majumdar A., Baskerville S., Xu W., et al. Anchoring an extended HTLV-1 Rex peptide within an RNA major groove containing junctional base triples. Structure 1999, 7:1461-1472.
    • (1999) Structure , vol.7 , pp. 1461-1472
    • Jiang, F.1    Gorin, A.2    Hu, W.3    Majumdar, A.4    Baskerville, S.5    Xu, W.6
  • 23
    • 0028047576 scopus 로고
    • Subcellular distribution of human immunodeficiency virus type 1 Rev and colocalization of Rev with RNA splicing factors in a speckled pattern in the nucleoplasm
    • Kalland K.H., Szilvay A.M., Langhoff E., Haukenes G. Subcellular distribution of human immunodeficiency virus type 1 Rev and colocalization of Rev with RNA splicing factors in a speckled pattern in the nucleoplasm. J Virol 1994, 68:1475-1485.
    • (1994) J Virol , vol.68 , pp. 1475-1485
    • Kalland, K.H.1    Szilvay, A.M.2    Langhoff, E.3    Haukenes, G.4
  • 24
    • 0026540537 scopus 로고
    • Specific binding of a basic peptide from HIV-1 Rev
    • Kjems J., Calnan B.J., Frankel A.D., Sharp P.A. Specific binding of a basic peptide from HIV-1 Rev. EMBO J 1992, 11:1119-1129.
    • (1992) EMBO J , vol.11 , pp. 1119-1129
    • Kjems, J.1    Calnan, B.J.2    Frankel, A.D.3    Sharp, P.A.4
  • 25
    • 0034744423 scopus 로고    scopus 로고
    • 4'-Ethynyl nucleoside analogs: potent inhibitors of multidrug-resistant human immunodeficiency virus variants in vitro
    • Kodama E.I., Kohgo S., Kitano K., Machida H., Gatanaga H., Shigeta S., et al. 4'-Ethynyl nucleoside analogs: potent inhibitors of multidrug-resistant human immunodeficiency virus variants in vitro. Antimicrob Agents Chemother 2001, 45:1539-1546.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1539-1546
    • Kodama, E.I.1    Kohgo, S.2    Kitano, K.3    Machida, H.4    Gatanaga, H.5    Shigeta, S.6
  • 26
    • 0038576281 scopus 로고    scopus 로고
    • Enfuvirtide, an HIV-1 fusion inhibitor, for drug-resistant HIV infection in North and South America
    • Lalezari J.P., Henry K., O'Hearn M., Montaner J.S., Piliero P.J., Trottier B., et al. Enfuvirtide, an HIV-1 fusion inhibitor, for drug-resistant HIV infection in North and South America. N Engl J Med 2003, 348:2175-2185.
    • (2003) N Engl J Med , vol.348 , pp. 2175-2185
    • Lalezari, J.P.1    Henry, K.2    O'Hearn, M.3    Montaner, J.S.4    Piliero, P.J.5    Trottier, B.6
  • 27
    • 0037849954 scopus 로고    scopus 로고
    • Efficacy of enfuvirtide in patients infected with drug-resistant HIV-1 in Europe and Australia
    • Lazzarin A., Clotet B., Cooper D., Reynes J., Arasteh K., Nelson M., et al. Efficacy of enfuvirtide in patients infected with drug-resistant HIV-1 in Europe and Australia. N Engl J Med 2003, 348:2186-2195.
    • (2003) N Engl J Med , vol.348 , pp. 2186-2195
    • Lazzarin, A.1    Clotet, B.2    Cooper, D.3    Reynes, J.4    Arasteh, K.5    Nelson, M.6
  • 28
    • 6444234180 scopus 로고    scopus 로고
    • The helical alanine controversy: an (Ala)6 insertion dramatically increases helicity
    • Lin J.C., Barua B., Andersen N.H. The helical alanine controversy: an (Ala)6 insertion dramatically increases helicity. J Am Chem Soc 2004, 126:13679-13684.
    • (2004) J Am Chem Soc , vol.126 , pp. 13679-13684
    • Lin, J.C.1    Barua, B.2    Andersen, N.H.3
  • 29
    • 3543144738 scopus 로고    scopus 로고
    • Spirodiketopiperazine-based CCR5 inhibitor which preserves CC-chemokine/CCR5 interactions and exerts potent activity against R5 human immunodeficiency virus type 1 in vitro
    • Maeda K., Nakata H., Koh Y., Miyakawa T., Ogata H., Takaoka Y., et al. Spirodiketopiperazine-based CCR5 inhibitor which preserves CC-chemokine/CCR5 interactions and exerts potent activity against R5 human immunodeficiency virus type 1 in vitro. J Virol 2004, 78:8654-8662.
    • (2004) J Virol , vol.78 , pp. 8654-8662
    • Maeda, K.1    Nakata, H.2    Koh, Y.3    Miyakawa, T.4    Ogata, H.5    Takaoka, Y.6
  • 30
    • 0024382709 scopus 로고
    • Functional dissection of the HIV-1 Rev trans-activator-derivation of a trans-dominant repressor of Rev function
    • Malim M.H., Bohnlein S., Hauber J., Cullen B.R. Functional dissection of the HIV-1 Rev trans-activator-derivation of a trans-dominant repressor of Rev function. Cell 1989, 58:205-214.
    • (1989) Cell , vol.58 , pp. 205-214
    • Malim, M.H.1    Bohnlein, S.2    Hauber, J.3    Cullen, B.R.4
  • 31
    • 0025818452 scopus 로고
    • HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: implications for HIV-1 latency
    • Malim M.H., Cullen B.R. HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: implications for HIV-1 latency. Cell 1991, 65:241-248.
    • (1991) Cell , vol.65 , pp. 241-248
    • Malim, M.H.1    Cullen, B.R.2
  • 32
    • 0024518918 scopus 로고
    • The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA
    • Malim M.H., Hauber J., Le S.Y., Maizel J.V., Cullen B.R. The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA. Nature 1989, 338:254-257.
    • (1989) Nature , vol.338 , pp. 254-257
    • Malim, M.H.1    Hauber, J.2    Le, S.Y.3    Maizel, J.V.4    Cullen, B.R.5
  • 33
    • 0028108364 scopus 로고
    • A molecular rheostat. Co-operative rev binding to stem I of the rev-response element modulates human immunodeficiency virus type-1 late gene expression
    • Mann D.A., Mikaelian I., Zemmel R.W., Green S.M., Lowe A.D., Kimura T., et al. A molecular rheostat. Co-operative rev binding to stem I of the rev-response element modulates human immunodeficiency virus type-1 late gene expression. J Mol Biol 1994, 241:193-207.
    • (1994) J Mol Biol , vol.241 , pp. 193-207
    • Mann, D.A.1    Mikaelian, I.2    Zemmel, R.W.3    Green, S.M.4    Lowe, A.D.5    Kimura, T.6
  • 34
    • 0024707204 scopus 로고
    • Unusually stable helix formation in short alanine-based peptides
    • Marqusee S., Robbins V.H., Baldwin R.L. Unusually stable helix formation in short alanine-based peptides. Proc Natl Acad Sci U S A 1989, 86:5286-5290.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 5286-5290
    • Marqusee, S.1    Robbins, V.H.2    Baldwin, R.L.3
  • 35
    • 0032815929 scopus 로고    scopus 로고
    • Inhibitory mechanism of the CXCR4 antagonist T22 against human immunodeficiency virus type 1 infection
    • Murakami T., Zhang T.Y., Koyanagi Y., Tanaka Y., Kim J., Suzuki Y., et al. Inhibitory mechanism of the CXCR4 antagonist T22 against human immunodeficiency virus type 1 infection. J Virol 1999, 73:7489-7496.
    • (1999) J Virol , vol.73 , pp. 7489-7496
    • Murakami, T.1    Zhang, T.Y.2    Koyanagi, Y.3    Tanaka, Y.4    Kim, J.5    Suzuki, Y.6
  • 36
    • 0031759170 scopus 로고    scopus 로고
    • Transduction of full-length TAT fusion proteins into mammalian cells: TAT-p27Kip1 induces cell migration
    • Nagahara H., Vocero-Akbani A.M., Snyder E.L., Ho A., Latham D.G., Lissy N.A., et al. Transduction of full-length TAT fusion proteins into mammalian cells: TAT-p27Kip1 induces cell migration. Nat Med 1998, 4:1449-1452.
    • (1998) Nat Med , vol.4 , pp. 1449-1452
    • Nagahara, H.1    Vocero-Akbani, A.M.2    Snyder, E.L.3    Ho, A.4    Latham, D.G.5    Lissy, N.A.6
  • 37
    • 11144236493 scopus 로고    scopus 로고
    • Mutations conferring resistance to human immunodeficiency virus type 1 fusion inhibitors are restricted by gp41 and Rev-responsive element functions
    • Nameki D., Kodama E., Ikeuchi M., Mabuchi N., Otaka A., Tamamura H., et al. Mutations conferring resistance to human immunodeficiency virus type 1 fusion inhibitors are restricted by gp41 and Rev-responsive element functions. J Virol 2005, 79:764-770.
    • (2005) J Virol , vol.79 , pp. 764-770
    • Nameki, D.1    Kodama, E.2    Ikeuchi, M.3    Mabuchi, N.4    Otaka, A.5    Tamamura, H.6
  • 38
    • 0025184516 scopus 로고
    • Interaction of the human immunodeficiency virus type 1 Rev protein with a structured region in env mRNA is dependent on multimer formation mediated through a basic stretch of amino acids
    • Olsen H.S., Cochrane A.W., Dillon P.J., Nalin C.M., Rosen C.A. Interaction of the human immunodeficiency virus type 1 Rev protein with a structured region in env mRNA is dependent on multimer formation mediated through a basic stretch of amino acids. Genes Dev 1990, 4:1357-1364.
    • (1990) Genes Dev , vol.4 , pp. 1357-1364
    • Olsen, H.S.1    Cochrane, A.W.2    Dillon, P.J.3    Nalin, C.M.4    Rosen, C.A.5
  • 39
    • 0023705436 scopus 로고
    • Functional replacement of the HIV-1 rev protein by the HTLV-1 rex protein
    • Rimsky L., Hauber J., Dukovich M., Malim M.H., Langlois A., Cullen B.R., et al. Functional replacement of the HIV-1 rev protein by the HTLV-1 rex protein. Nature 1988, 335:738-740.
    • (1988) Nature , vol.335 , pp. 738-740
    • Rimsky, L.1    Hauber, J.2    Dukovich, M.3    Malim, M.H.4    Langlois, A.5    Cullen, B.R.6
  • 41
    • 0023812595 scopus 로고
    • Sequence requirements for nucleolar localization of human T cell leukemia virus type I pX protein, which regulates viral RNA processing
    • Siomi H., Shida H., Nam S.H., Nosaka T., Maki M., Hatanaka M. Sequence requirements for nucleolar localization of human T cell leukemia virus type I pX protein, which regulates viral RNA processing. Cell 1988, 55:197-209.
    • (1988) Cell , vol.55 , pp. 197-209
    • Siomi, H.1    Shida, H.2    Nam, S.H.3    Nosaka, T.4    Maki, M.5    Hatanaka, M.6
  • 42
    • 0028786017 scopus 로고
    • Analysis of trafficking of Rev and transdominant Rev proteins in living cells using green fluorescent protein fusions: transdominant Rev blocks the export of Rev from the nucleus to the cytoplasm
    • Stauber R., Gaitanaris G.A., Pavlakis G.N. Analysis of trafficking of Rev and transdominant Rev proteins in living cells using green fluorescent protein fusions: transdominant Rev blocks the export of Rev from the nucleus to the cytoplasm. Virology 1995, 213:439-449.
    • (1995) Virology , vol.213 , pp. 439-449
    • Stauber, R.1    Gaitanaris, G.A.2    Pavlakis, G.N.3
  • 43
    • 0029066104 scopus 로고
    • Nuclear export of the human immunodeficiency virus type 1 nucleocytoplasmic shuttle protein Rev is mediated by its activation domain and is blocked by transdominant negative mutants
    • Szilvay A.M., Brokstad K.A., Kopperud R., Haukenes G., Kalland K.H. Nuclear export of the human immunodeficiency virus type 1 nucleocytoplasmic shuttle protein Rev is mediated by its activation domain and is blocked by transdominant negative mutants. J Virol 1995, 69:3315-3323.
    • (1995) J Virol , vol.69 , pp. 3315-3323
    • Szilvay, A.M.1    Brokstad, K.A.2    Kopperud, R.3    Haukenes, G.4    Kalland, K.H.5
  • 45
    • 0030815316 scopus 로고    scopus 로고
    • HIV-1 protease does not play a critical role in the early stages of HIV-1 infection
    • Uchida H., Maeda Y., Mitsuya H. HIV-1 protease does not play a critical role in the early stages of HIV-1 infection. Antiviral Res 1997, 36:107-113.
    • (1997) Antiviral Res , vol.36 , pp. 107-113
    • Uchida, H.1    Maeda, Y.2    Mitsuya, H.3
  • 46
    • 62049085108 scopus 로고    scopus 로고
    • Synonymous mutations in stem-loop III of Rev responsive elements enhance HIV-1 replication impaired by primary mutations for resistance to enfuvirtide
    • Ueno M., Kodama E.N., Shimura K., Sakurai Y., Kajiwara K., Sakagami S., Oishi S., Fujii N., Matsuoka M. Synonymous mutations in stem-loop III of Rev responsive elements enhance HIV-1 replication impaired by primary mutations for resistance to enfuvirtide. Antiviral Res 2009, 82:67-72.
    • (2009) Antiviral Res , vol.82 , pp. 67-72
    • Ueno, M.1    Kodama, E.N.2    Shimura, K.3    Sakurai, Y.4    Kajiwara, K.5    Sakagami, S.6    Oishi, S.7    Fujii, N.8    Matsuoka, M.9
  • 48
    • 0025917131 scopus 로고
    • Oligomerization and RNA binding domains of the type 1 human immunodeficiency virus Rev protein: a dual function for an arginine-rich binding motif
    • Zapp M.L., Hope T.J., Parslow T.G., Green M.R. Oligomerization and RNA binding domains of the type 1 human immunodeficiency virus Rev protein: a dual function for an arginine-rich binding motif. Proc Natl Acad Sci U S A 1991, 88:7734-7738.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 7734-7738
    • Zapp, M.L.1    Hope, T.J.2    Parslow, T.G.3    Green, M.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.