메뉴 건너뛰기




Volumn 1808, Issue 11, 2011, Pages 2685-2693

Mechanistic insights into the translocation of full length HIV-1 Tat across lipid membranes

Author keywords

Arginine rich motif; Cell penetrating peptide; Fluorescence microscopy; Giant unilamellar vesicle; Protein membrane interaction; Transactivator of transcription

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; CYSTEINE; PROLINE; TRANSACTIVATOR PROTEIN; TRYPTOPHAN;

EID: 80052262557     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.07.030     Document Type: Article
Times cited : (6)

References (54)
  • 1
    • 1242269845 scopus 로고    scopus 로고
    • Multiple effects of HIV-1 trans-activator protein on the pathogenesis of HIV-1 infection
    • DOI 10.1111/j.1365-2362.2004.01282.x
    • M.C.D.G. Huigen, W. Kamp, and H.S.L.M. Nottet Multiple effects of HIV-1 trans-activator protein on the pathogenesis of HIV-1 infection Eur. J. Clin. Invest. 34 2004 57 66 (Pubitemid 38221740)
    • (2004) European Journal of Clinical Investigation , vol.34 , Issue.1 , pp. 57-66
    • Huigen, M.C.D.G.1    Kamp, W.2    Nottet, H.S.L.M.3
  • 2
    • 0028290825 scopus 로고
    • Control of RNA initiation and elongation at the HIV-1 promoter
    • K.A. Jones, and B.M. Peterlin Control of RNA initiation and elongation at the HIV-1 promotor Annu. Rev. Biochem. 63 1994 717 743 (Pubitemid 24218647)
    • (1994) Annual Review of Biochemistry , vol.63 , pp. 717-743
    • Jones, K.A.1    Matija Peterlin, B.2
  • 3
    • 2542490238 scopus 로고    scopus 로고
    • Virus-host interactions: Role of HIV proteins Vif, Tat and Rev
    • K. Strebel Virus-host interactions: role of HIV proteins Vif, Tat and Rev AIDS 17 2003 25 34
    • (2003) AIDS , vol.17 , pp. 25-34
    • Strebel, K.1
  • 4
    • 0025344596 scopus 로고
    • Tat protein of HIV-1 stimulates growth of cells derived from Kaposi's sarcoma lesions of AIDS patients
    • B. Ensoli, G. Barillari, S.Z. Salahuddin, R.C. Gallo, and F. Wong-Staal Tat protein of HIV-1 stimulates growth of cells derived from Kaposi's sarcoma lesions of AIDS patients Nature 345 1990 84 86
    • (1990) Nature , vol.345 , pp. 84-86
    • Ensoli, B.1    Barillari, G.2    Salahuddin, S.Z.3    Gallo, R.C.4    Wong-Staal, F.5
  • 7
    • 0141866666 scopus 로고    scopus 로고
    • Discovery of a small molecule Tat-trans-activation-responsive RNA antagonist that potently inhibits human immunodeficiency virus-1 replication
    • DOI 10.1074/jbc.M301749200
    • S. Hwang, N. Tamilarasu, K. Kibler, H. Cao, A. Ali, Y.H. Ping, K.T. Jeang, and T.M. Rana Discovery of a small molecule Tat-trans-activation- responsive RNA antagonist that potently inhibits human immunodeficiency virus-1 replication J. Biol. Chem. 278 2003 39092 39103 (Pubitemid 37221813)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 39092-39103
    • Hwang, S.1    Tamilarasu, N.2    Kibler, K.3    Cao, H.4    Ali, A.5    Ping, Y.-H.6    Jeang, K.-T.7    Rana, T.M.8
  • 8
    • 2342507144 scopus 로고    scopus 로고
    • HIV-1 Tat Enters T Cells Using Coated Pits before Translocating from Acidified Endosomes and Eliciting Biological Responses
    • DOI 10.1091/mbc.E03-12-0921
    • A. Vendeville, F. Rayne, A. Bonhoure, N. Bettache, P. Montcourrier, and B. Beaumelle HIV-1 Tat enters T cells using coated pits before translocating from acidified endosomes and eliciting biological responses Mol. Biol. Cell 15 2004 2347 2360 (Pubitemid 38580651)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.5 , pp. 2347-2360
    • Vendeville, A.1    Rayne, F.2    Bonhoure, A.3    Bettache, N.4    Montcourrier, P.5    Beaumelle, B.6
  • 9
    • 33748648777 scopus 로고    scopus 로고
    • Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells
    • DOI 10.1096/fj.05-5523com
    • G. Tunnemann, R.M. Martin, S. Haupt, C. Patsch, F. Edenhofer, and M.C. Cardoso Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells FASEB J. 20 2006 1775 1784 (Pubitemid 44933791)
    • (2006) FASEB Journal , vol.20 , Issue.11 , pp. 1775-1784
    • Tunnemann, G.1    Martin, R.M.2    Haupt, S.3    Patsch, C.4    Edenhofer, F.5    Cardoso, M.C.6
  • 10
    • 31544438701 scopus 로고    scopus 로고
    • Break on through to the other side-biophysics and cell biology shed light on cell-penetrating peptides
    • R. Fischer, M. Fotin-Mleczek, H. Hufnagel, and R. Brock Break on through to the other side-biophysics and cell biology shed light on cell-penetrating peptides ChemBioChem 6 2005 2126 2142
    • (2005) ChemBioChem , vol.6 , pp. 2126-2142
    • Fischer, R.1    Fotin-Mleczek, M.2    Hufnagel, H.3    Brock, R.4
  • 11
    • 42049095153 scopus 로고    scopus 로고
    • Cell-penetrating peptides: From molecular mechanisms to therapeutics
    • DOI 10.1042/BC20070116
    • M.C. Morris, S. Deshayes, F. Heitz, and G. Divita Cell-penetrating peptides: from molecular mechanisms to therapeutics Biol. Cell 100 2008 201 217 (Pubitemid 351517084)
    • (2008) Biology of the Cell , vol.100 , Issue.4 , pp. 201-217
    • Morris, M.C.1    Deshayes, S.2    Heitz, F.3    Divita, G.4
  • 12
    • 50849144942 scopus 로고    scopus 로고
    • Cell penetrating peptide-modified pharmaceutical nanocarriers for intracellular drug and gene delivery
    • V.P. Torchilin Cell penetrating peptide-modified pharmaceutical nanocarriers for intracellular drug and gene delivery Biopolymers 90 2008 604 610
    • (2008) Biopolymers , vol.90 , pp. 604-610
    • Torchilin, V.P.1
  • 13
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics
    • F. Heitz, M.C. Morris, and G. Divita Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics Br. J. Pharmacol. 157 2009 195 206
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 195-206
    • Heitz, F.1    Morris, M.C.2    Divita, G.3
  • 14
    • 0141942113 scopus 로고    scopus 로고
    • A brief introduction to cell-penetrating peptides
    • DOI 10.1002/jmr.630
    • P. Lundberg, and Ü. Langel A brief introduction to cell-penetrating peptides J. Mol. Recognit. 16 2003 227 233 (Pubitemid 37231690)
    • (2003) Journal of Molecular Recognition , vol.16 , Issue.5 , pp. 227-233
    • Lundberg, P.1    Langel, U.2
  • 15
    • 77952231544 scopus 로고    scopus 로고
    • Cell-penetrating peptides and their therapeutic applications
    • V. Sebbage Cell-penetrating peptides and their therapeutic applications Biosci. Horiz. 2 2009 64 72
    • (2009) Biosci. Horiz. , vol.2 , pp. 64-72
    • Sebbage, V.1
  • 16
    • 34548149532 scopus 로고    scopus 로고
    • The many futures for cell-penetrating peptides: How soon is now?
    • J. Howl, I.D. Nicholl, and S. Jones Cell-penetrating peptides. The many futures for cell-penetrating peptides: how soon is now? Biochem. Soc. Trans. 35 2007 767 769 (Pubitemid 47310364)
    • (2007) Biochemical Society Transactions , vol.35 , Issue.4 , pp. 767-769
    • Howl, J.1    Nicholl, I.D.2    Jones, S.3
  • 17
    • 0034613057 scopus 로고    scopus 로고
    • The Antennapedia peptide penetratin translocates across lipid bilayers - The first direct observation
    • P.E.G. Thoren, D. Persson, M. Karlsson, and B. Norden The Antennapedia peptide penetratin translocates across lipid bilayers - the first direct observation FEBS Lett. 482 2000 265 268
    • (2000) FEBS Lett. , vol.482 , pp. 265-268
    • Thoren, P.E.G.1    Persson, D.2    Karlsson, M.3    Norden, B.4
  • 18
    • 0041843710 scopus 로고    scopus 로고
    • Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes
    • H. Binder, and G. Lindblom Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes Biophys. J. 85 2003 982 995 (Pubitemid 36909662)
    • (2003) Biophysical Journal , vol.85 , Issue.2 , pp. 982-995
    • Binder, H.1    Lindblom, G.2
  • 20
    • 65249174105 scopus 로고    scopus 로고
    • Magainin 2 induced pore formation in the lipid membrane depends on its concentration in the membrane interface
    • Y. Tamba, and M. Yamazaki Magainin 2 induced pore formation in the lipid membrane depends on its concentration in the membrane interface J. Phys. Chem. 113 2009 4846 4852
    • (2009) J. Phys. Chem. , vol.113 , pp. 4846-4852
    • Tamba, Y.1    Yamazaki, M.2
  • 21
    • 28544437689 scopus 로고    scopus 로고
    • Single giant unilamellar vesicle method reveals effect of antimicrobial peptide magainin 2 on membrane permeability
    • DOI 10.1021/bi051684w
    • Y. Tamba, and M. Yamazaki Single giant unilamellar vesicle method reveals effect of antimicrobial peptide magainin 2 on membrane permeability Biochemistry 44 2005 15823 15833 (Pubitemid 41746913)
    • (2005) Biochemistry , vol.44 , Issue.48 , pp. 15823-15833
    • Tamba, Y.1    Yamazaki, M.2
  • 22
    • 65249093640 scopus 로고    scopus 로고
    • Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation
    • G. Klocek, T. Schulthess, Y. Shai, and J. Seelig Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation Biochemistry 48 2009 2586 2596
    • (2009) Biochemistry , vol.48 , pp. 2586-2596
    • Klocek, G.1    Schulthess, T.2    Shai, Y.3    Seelig, J.4
  • 24
    • 0029042292 scopus 로고
    • Study of vesicle leakage induced by melittin
    • T. Benachir, and M. Lafleur Study of vesicle leakage induced by melittin Biochim. Biophys. Acta 1235 1995 452 460
    • (1995) Biochim. Biophys. Acta , vol.1235 , pp. 452-460
    • Benachir, T.1    Lafleur, M.2
  • 25
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • C.E. Dempsey The actions of melittin on membranes Biochim. Biophys. Acta 1031 1990 143 161
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 26
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: Structure-function study
    • DOI 10.1021/bi962507l
    • Z. Oren, and Y. Shai Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study Biochemistry 36 1997 1826 1835 (Pubitemid 27086279)
    • (1997) Biochemistry , vol.36 , Issue.7 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 27
    • 38049156027 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes
    • H.D. Herce, and A.E. Garcia Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes Proc. Natl. Acad. Sci. USA 104 2007 20805 20810
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20805-20810
    • Herce, H.D.1    Garcia, A.E.2
  • 28
    • 70350023192 scopus 로고    scopus 로고
    • Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides
    • H.D. Herce, A.E. Garcia, J. Litt, R.S. Kane, P. Martin, N. Enrique, A. Rebolledo, and V. Milesi Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides Biophys. J. 97 2009 1917 1925
    • (2009) Biophys. J. , vol.97 , pp. 1917-1925
    • Herce, H.D.1    Garcia, A.E.2    Litt, J.3    Kane, R.S.4    Martin, P.5    Enrique, N.6    Rebolledo, A.7    Milesi, V.8
  • 29
    • 33947686656 scopus 로고    scopus 로고
    • A fluorescence spectroscopy study on the interactions of the TAT-PTD peptide with model lipid membranes
    • DOI 10.1021/bi602527t
    • V. Tiriveedhi, and P. Butko A fluorescence spectroscopy study on the interactions of the Tat-PTD peptide with model lipid membranes Biochemistry 46 2007 3888 3895 (Pubitemid 46493489)
    • (2007) Biochemistry , vol.46 , Issue.12 , pp. 3888-3895
    • Tiriveedhi, V.1    Butko, P.2
  • 30
    • 0043166977 scopus 로고    scopus 로고
    • Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles. Binding mechanism and thermodynamic analysis
    • DOI 10.1021/bi0346805
    • A. Ziegler, X.L. Blatter, A. Seelig, and J. Seelig Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles. Binding mechanism and thermodynamic analysis Biochemistry 42 2003 9185 9194 (Pubitemid 36935428)
    • (2003) Biochemistry , vol.42 , Issue.30 , pp. 9185-9194
    • Ziegler, A.1    Li Blatter, X.2    Seelig, A.3    Seelig, J.4
  • 33
    • 8444227370 scopus 로고    scopus 로고
    • HIV-1 Tat-mediated effects on focal adhesion assembly and permeability in brain microvascular endothelial cells
    • H.K. Avraham, S. Jiang, T.H. Lee, O. Prakash, and S. Avraham HIV-1 Tat-mediated effects on focal adhesion assembly and permeability in brain microvascular endothelial cells J. Immunol. 173 2004 6228 6233 (Pubitemid 39487780)
    • (2004) Journal of Immunology , vol.173 , Issue.10 , pp. 6228-6233
    • Avraham, H.K.1    Jiang, S.2    Lee, T.-H.3    Prakash, O.4    Avraham, S.5
  • 34
    • 0032533253 scopus 로고    scopus 로고
    • The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein
    • M.E. Garber, P. Wei, V.N. Kewal Ramani, T.P. Mayall, C.H. Herrmann, A.P. Rice, D.R. Littmann, and K.A. Jones The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine cyc T1 protein Genes Dev. 12 1998 3512 3527 (Pubitemid 28553243)
    • (1998) Genes and Development , vol.12 , Issue.22 , pp. 3512-3527
    • Garber, M.E.1    Wei, P.2    KewalRamani, V.N.3    Mayall, T.P.4    Herrmann, C.H.5    Rice, A.P.6    Littman, D.R.7    Jones, K.A.8
  • 35
    • 0037417772 scopus 로고    scopus 로고
    • Molecular recognition of the human coactivator CBP by the HIV-1 transcriptional activator tat
    • DOI 10.1021/bi0270034
    • A.C. Vendel, and K.J. Lumb Molecular recognition of the human coactivator CBP by the HIV-1 transcriptional activator Tat Biochemistry 42 2003 910 916 (Pubitemid 36159522)
    • (2003) Biochemistry , vol.42 , Issue.4 , pp. 910-916
    • Vendel, A.C.1    Lumb, K.J.2
  • 36
    • 33646835410 scopus 로고    scopus 로고
    • HIV-1 Tat is a natively unfolded protein
    • S. Shojania, and J.D. O'Neil HIV-1 Tat is a natively unfolded protein J. Biol. Chem. 281 2006 8347 8356
    • (2006) J. Biol. Chem. , vol.281 , pp. 8347-8356
    • Shojania, S.1    O'Neil, J.D.2
  • 37
    • 78651521006 scopus 로고    scopus 로고
    • Formation of Tat-TAR containing ribonucleoprotein complexes for biochemical and structural analyses
    • J.M. Bigalke, N. Czudnochowski, V. F., K. Vogel-Bachmayr, K. Anand, and M. Geyer Formation of Tat-TAR containing ribonucleoprotein complexes for biochemical and structural analyses Methods 53 2011 78 84
    • (2011) Methods , vol.53 , pp. 78-84
    • Bigalke, J.M.1    Czudnochowski, N.F.V.2    Vogel-Bachmayr, K.3    Anand, K.4    Geyer, M.5
  • 38
    • 44949104715 scopus 로고    scopus 로고
    • HIV Tat forms pores in membranes by inducing saddle-splay curvature: Potential role of bidentate hydrogen bonding
    • A. Mishra, V.D. Gordon, L. Yang, R. Coridan, and G.C.L. Wong HIV Tat forms pores in membranes by inducing saddle-splay curvature: potential role of bidentate hydrogen bonding Angew. Chem. Int. Ed. 47 2008 1 5
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 1-5
    • Mishra, A.1    Gordon, V.D.2    Yang, L.3    Coridan, R.4    Wong, G.C.L.5
  • 39
    • 77954374712 scopus 로고    scopus 로고
    • Cell-penetrating HIV1 Tat peptides can generate pores in model membranes
    • C. Ciobanasu, J.P. Siebrasse, and U. Kubitscheck Cell-penetrating HIV1 Tat peptides can generate pores in model membranes Biophys. J. 99 2010 153 162
    • (2010) Biophys. J. , vol.99 , pp. 153-162
    • Ciobanasu, C.1    Siebrasse, J.P.2    Kubitscheck, U.3
  • 40
    • 1642304434 scopus 로고    scopus 로고
    • Membrane Binding and Translocation of Cell-Penetrating Peptides
    • DOI 10.1021/bi0360049
    • P.E.G. Thoren, D. Persson, E.K. Esbjörner, M. Goksör, P. Lincoln, and B. Norden Membrane binding and translocation of cell-penetrating peptides Biochemistry 43 2004 3471 3489 (Pubitemid 38391703)
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3471-3489
    • Thoren, P.E.G.1    Persson, D.2    Esbjorner, E.K.3    Goksor, M.4    Lincoln, P.5    Norden, B.6
  • 41
    • 17144373997 scopus 로고    scopus 로고
    • Membrane destabilizing properties of cell-penetrating peptides
    • DOI 10.1016/j.bpc.2004.11.016
    • P.E.G. Thoren, D. Persson, P. Lincoln, and B. Norden Membrane destabilizing properties of cell-penetrating peptides Biophys. Chem. 114 2005 169 179 (Pubitemid 40521515)
    • (2005) Biophysical Chemistry , vol.114 , Issue.2-3 , pp. 169-179
    • Thoren, P.E.G.1    Persson, D.2    Lincoln, P.3    Norden, B.4
  • 42
    • 33745151952 scopus 로고    scopus 로고
    • Membrane interactions of cell-penetrating peptides probed by tryptophan fluorescence and dichroism techniques: Correlations of structure to cellular uptake
    • DOI 10.1021/bi052095t
    • C.E. Caesar, E.K. Esbjörner, P. Lincoln, and B. Norden Membrane interactions of cell-penetrating peptides probed by tryptophan fluorescence and dichroism techniques: correlations of structure to cellular uptake Biochemistry 45 2006 7682 7692 (Pubitemid 43894958)
    • (2006) Biochemistry , vol.45 , Issue.24 , pp. 7682-7692
    • Caesar, C.E.B.1    Esbjorner, E.K.2    Lincoln, P.3    Norden, B.4
  • 44
    • 0026737184 scopus 로고
    • Kinetics of melittin induced pore formation in the membrane of lipid vesicles
    • G. Schwarz, R. Zong, and T. Popescu Kinetics of melittin induced pore formation in the membrane of lipid vesicles Biochim. Biophys. Acta 1110 1992 97 104
    • (1992) Biochim. Biophys. Acta , vol.1110 , pp. 97-104
    • Schwarz, G.1    Zong, R.2    Popescu, T.3
  • 45
    • 0029099270 scopus 로고
    • Pore kinetics reflected in the dequenching of a lipid vesicle entrapped fluorescent dye
    • G. Schwarz, and A. Arbuzova Pore kinetics reflected in the dequenching of a lipid vesicle entrapped fluorescent dye Biochim. Biophys. Acta 1239 1995 51 57
    • (1995) Biochim. Biophys. Acta , vol.1239 , pp. 51-57
    • Schwarz, G.1    Arbuzova, A.2
  • 47
    • 15544366924 scopus 로고    scopus 로고
    • Translocation of the cell-penetrating Tat peptide across artificial bilayers and into living cells
    • P. Curnow, H. Mellor, D.J. Stephens, M. Lorch, and P.J. Booth Translocation of the cell-penetrating Tat peptide across artificial bilayers and into living cells Biochem. Soc. Symp. 72 2005 199 209 (Pubitemid 44804746)
    • (2005) Biochemical Society Symposium , vol.72 , pp. 199-209
    • Curnow, P.1    Mellor, H.2    Stephens, D.J.3    Lorch, M.4    Booth, P.J.5
  • 49
    • 0037474028 scopus 로고    scopus 로고
    • No entry for TAT(44-57) into liposomes and intact MDCK cells: Novel approach to study membrane permeation of cell-penetrating peptides
    • DOI 10.1016/S0005-2736(02)00683-1
    • S.D. Krämer, and H. Wunderli-Allenspach No entry for Tat (44-57) into liposomes and intact MDCK cells: novel approach to study membrane permeation of cell-penetrating peptides Biochim. Biophys. Acta 1609 2003 161 169 (Pubitemid 36120723)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1609 , Issue.2 , pp. 161-169
    • Kramer, S.D.1    Wunderli-Allenspach, H.2
  • 51
    • 57149121459 scopus 로고    scopus 로고
    • Structural insights into the cyclin T1-Tat-TAR RNA transcription activation complex from EIAV
    • K. Anand, A. Schulte, K. Vogel-Bachmayr, K. Scheffzek, and M. Geyer Structural insights into the cyclin T1-Tat-TAR RNA transcription activation complex from EIAV Nat. Struct. Mol. Biol. 15 2008 1287 1292
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1287-1292
    • Anand, K.1    Schulte, A.2    Vogel-Bachmayr, K.3    Scheffzek, K.4    Geyer, M.5
  • 52
    • 0028858599 scopus 로고
    • Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex
    • J.D. Puglisi, S. Chen, S. Blanchard, and R. Frank Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex Science 270 1995 1200 1203
    • (1995) Science , vol.270 , pp. 1200-1203
    • Puglisi, J.D.1    Chen, S.2    Blanchard, S.3    Frank, R.4
  • 53
    • 0029613238 scopus 로고
    • Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex
    • DOI 10.1016/1074-5521(95)90089-6
    • X. Ye, R.A. Kumar, and D.J. Patel Molecular recognition on the bovine immunodeficiency virus Tat peptide-TAR RNA complex Chem. Biol. 2 1995 827 840 (Pubitemid 3014706)
    • (1995) Chemistry and Biology , vol.2 , Issue.12 , pp. 827-840
    • Ye Xiaomei1    Kumar, R.A.2    Patel, D.J.3
  • 54
    • 17744407410 scopus 로고    scopus 로고
    • Highly stable oligomerization forms of HIV-1 Tat detected by monoclonal antibodies and requirement of monomeric forms for the transactivating function on the HIV-1 LTR
    • DOI 10.1002/(SICI)1521-4141(200004)30:4<1120::AID-IMMU1120>3.0. CO;2-4
    • G. Tosi, R. Meazza, A. de Lerma Barbaro, A. D'Agostino, S. Mazza, G. Corradin, A. Albini, D.M. Noonan, S. Ferrini, and R.S. Accolla Highly stable oligomerization forms of HIV-1 Tat detected by monoclonal antibodies and requirement of monomeric forms for the transactivating function on the HIV-1 LTR Eur. J. Immunol. 30 2000 1120 1126 (Pubitemid 30216229)
    • (2000) European Journal of Immunology , vol.30 , Issue.4 , pp. 1120-1126
    • Tosi, G.1    Meazza, R.2    De Lerma Barbaro, A.3    D'Agostino, A.4    Mazza, S.5    Corradin, G.6    Albini, A.7    Noonan, D.M.8    Ferrini, S.9    Accolla, R.S.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.