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Volumn 11, Issue 3, 2003, Pages 124-133

Spying on HIV with SPR

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; NUCLEIC ACID; PROTEIN;

EID: 0037342411     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0966-842X(03)00025-8     Document Type: Review
Times cited : (44)

References (107)
  • 1
    • 0034282271 scopus 로고    scopus 로고
    • Implementing surface plasmon resonance biosensors in drug discovery
    • Myszka D.G., Rich R.L. Implementing surface plasmon resonance biosensors in drug discovery. Pharm. Sci. Technol. Today. 3:2000;310-317.
    • (2000) Pharm. Sci. Technol. Today , vol.3 , pp. 310-317
    • Myszka, D.G.1    Rich, R.L.2
  • 2
    • 0345144163 scopus 로고    scopus 로고
    • Surface plasmon resonance biosensors
    • F.S. Ligler, & C.A. et al. Rowe Taitt. Elsevier Science
    • Homola J., et al. Surface plasmon resonance biosensors. Ligler F.S., Rowe Taitt C.A., et al. Optical Biosensors: Present and Future. 2002;207-251 Elsevier Science.
    • (2002) Optical Biosensors: Present and Future , pp. 207-251
    • Homola, J.1
  • 3
    • 0025502197 scopus 로고
    • Detection of antigen-antibody interactions by surface plasmon resonance. Application to epitope mapping
    • Fägerstam L.G., et al. Detection of antigen-antibody interactions by surface plasmon resonance. Application to epitope mapping. J. Mol. Recog. 3:1990;208-214.
    • (1990) J. Mol. Recog. , vol.3 , pp. 208-214
    • Fägerstam, L.G.1
  • 4
    • 0027916175 scopus 로고
    • Biospecific interaction analysis using biosensor technology
    • Malmqvist M. Biospecific interaction analysis using biosensor technology. Nature. 361:1993;186-187.
    • (1993) Nature , vol.361 , pp. 186-187
    • Malmqvist, M.1
  • 5
    • 0030174343 scopus 로고    scopus 로고
    • Epitope mapping by label-free biomolecular interaction analysis
    • Malmqvist M. Epitope mapping by label-free biomolecular interaction analysis. Methods. 9:1996;525-532.
    • (1996) Methods , vol.9 , pp. 525-532
    • Malmqvist, M.1
  • 6
    • 0033520038 scopus 로고    scopus 로고
    • Antibodies against human IFN-alpha and -beta recognized the immunosuppressive domain of HIV-1 gp41 and inhibit gp41-binding to the putative cellular receptor protein p45
    • Chen Y.H., et al. Antibodies against human IFN-alpha and -beta recognized the immunosuppressive domain of HIV-1 gp41 and inhibit gp41-binding to the putative cellular receptor protein p45. Immunol. Lett. 69:1999;253-257.
    • (1999) Immunol. Lett. , vol.69 , pp. 253-257
    • Chen, Y.H.1
  • 7
    • 0034703835 scopus 로고    scopus 로고
    • Antigenicity and immunogenicity of the HIV-1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein
    • Coëffier E., et al. Antigenicity and immunogenicity of the HIV-1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein. Vaccine. 19:2000;684-693.
    • (2000) Vaccine , vol.19 , pp. 684-693
    • Coëffier, E.1
  • 8
    • 0032840985 scopus 로고    scopus 로고
    • Structural and functional characterization of an epitope in the conserved C-terminal region of HIV-1 gp120
    • Ferrer M., et al. Structural and functional characterization of an epitope in the conserved C-terminal region of HIV-1 gp120. J. Pept. Res. 54:1999;32-42.
    • (1999) J. Pept. Res. , vol.54 , pp. 32-42
    • Ferrer, M.1
  • 9
    • 0032145892 scopus 로고    scopus 로고
    • Inhibition of HIV-1 gp120 binding to CD4 + T cells by monoclonal antibodies directed against the gp120 C1 or C4 region
    • Kröpelin M., et al. Inhibition of HIV-1 gp120 binding to CD4 + T cells by monoclonal antibodies directed against the gp120 C1 or C4 region. Immunol. Lett. 63:1998;19-25.
    • (1998) Immunol. Lett. , vol.63 , pp. 19-25
    • Kröpelin, M.1
  • 10
    • 0033557072 scopus 로고    scopus 로고
    • Characterization of conformation-dependent anti-gp120 murine monoclonal antibodies produced by immunization with monomeric and oligomeric human immunodeficiency virus type 1 envelope proteins
    • Sugiura W., et al. Characterization of conformation-dependent anti-gp120 murine monoclonal antibodies produced by immunization with monomeric and oligomeric human immunodeficiency virus type 1 envelope proteins. Virology. 254:1999;257-267.
    • (1999) Virology , vol.254 , pp. 257-267
    • Sugiura, W.1
  • 11
    • 0034284505 scopus 로고    scopus 로고
    • Generation of monoclonal antibodies specifically directed against the proximal zinc finger of HIV type 1 NCp7
    • De Rocquigny H., et al. Generation of monoclonal antibodies specifically directed against the proximal zinc finger of HIV type 1 NCp7. AIDS Res. Hum. Retroviruses. 16:2000;1259-1267.
    • (2000) AIDS Res. Hum. Retroviruses , vol.16 , pp. 1259-1267
    • De Rocquigny, H.1
  • 12
    • 0028874990 scopus 로고
    • Conformational changes between human immunodeficiency virus type 1 nucleocapsid protein NCp7 and its precursor NCp15 as detected by anti-NCp7 monoclonal antibodies
    • Tanchou V., et al. Conformational changes between human immunodeficiency virus type 1 nucleocapsid protein NCp7 and its precursor NCp15 as detected by anti-NCp7 monoclonal antibodies. J. Gen. Virol. 76:1995;2457-2466.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2457-2466
    • Tanchou, V.1
  • 13
    • 0028170064 scopus 로고
    • Monoclonal antibody-mediated inhibition of RNA binding and annealing activities of HIV type 1 nucleocapsid protein
    • Tanchou V., et al. Monoclonal antibody-mediated inhibition of RNA binding and annealing activities of HIV type 1 nucleocapsid protein. AIDS Res. Hum. Retroviruses. 10:1994;983-993.
    • (1994) AIDS Res. Hum. Retroviruses , vol.10 , pp. 983-993
    • Tanchou, V.1
  • 14
    • 0035061824 scopus 로고    scopus 로고
    • An immunodominant neutralization epitope on the 'thumb' subdomain of human immunodeficiency virus type 1 reverse transcriptase revealed by phage display antibodies
    • Ohba H., et al. An immunodominant neutralization epitope on the 'thumb' subdomain of human immunodeficiency virus type 1 reverse transcriptase revealed by phage display antibodies. J. Gen. Virol. 82:2001;813-820.
    • (2001) J. Gen. Virol. , vol.82 , pp. 813-820
    • Ohba, H.1
  • 15
    • 0037023718 scopus 로고    scopus 로고
    • Mapping the epitope of an inhibitory monoclonal antibody to the C-terminal DNA-binding domain of HIV-1 integrase
    • Yi J., et al. Mapping the epitope of an inhibitory monoclonal antibody to the C-terminal DNA-binding domain of HIV-1 integrase. J. Biol. Chem. 277:2002;12164-12174.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12164-12174
    • Yi, J.1
  • 16
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • Karlsson R., et al. Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J. Immunol. Methods. 145:1991;229-240.
    • (1991) J. Immunol. Methods , vol.145 , pp. 229-240
    • Karlsson, R.1
  • 17
    • 0027978869 scopus 로고
    • Real-time competitive kinetic analysis of interactions between low-molecular-weight ligands in solution and surface-immobilized receptors
    • Karlsson R. Real-time competitive kinetic analysis of interactions between low-molecular-weight ligands in solution and surface-immobilized receptors. Anal. Biochem. 221:1994;142-151.
    • (1994) Anal. Biochem. , vol.221 , pp. 142-151
    • Karlsson, R.1
  • 18
    • 0030053263 scopus 로고    scopus 로고
    • Binding kinetics of an antibody against HIV p24 core protein measured with real-time biomolecular interaction analysis suggest a slow conformational change in antigen p24
    • Glaser R.W., Hausdorf G. Binding kinetics of an antibody against HIV p24 core protein measured with real-time biomolecular interaction analysis suggest a slow conformational change in antigen p24. J. Immunol. Methods. 189:1996;1-14.
    • (1996) J. Immunol. Methods , vol.189 , pp. 1-14
    • Glaser, R.W.1    Hausdorf, G.2
  • 19
    • 0032456780 scopus 로고    scopus 로고
    • Thermodynamic analysis of protein interactions with biosensor technology
    • Roos H., et al. Thermodynamic analysis of protein interactions with biosensor technology. J. Mol. Recog. 11:1998;204-210.
    • (1998) J. Mol. Recog. , vol.11 , pp. 204-210
    • Roos, H.1
  • 20
    • 0032422168 scopus 로고    scopus 로고
    • Selection of human anti-human immunodeficiency virus type 1 envelope single-chain antibodies from a peripheral blood cell-based phage repertoire
    • de Haard J.J., et al. Selection of human anti-human immunodeficiency virus type 1 envelope single-chain antibodies from a peripheral blood cell-based phage repertoire. J. Gen. Virol. 79:1998;2883-2894.
    • (1998) J. Gen. Virol. , vol.79 , pp. 2883-2894
    • De Haard, J.J.1
  • 21
    • 0034826583 scopus 로고    scopus 로고
    • Differential recognition of epitopes present on monomeric and oligomeric forms of gp160 glycoprotein of human immunodeficiency virus type 1 by human monoclonal antibodies
    • Zeder-Lutz G., et al. Differential recognition of epitopes present on monomeric and oligomeric forms of gp160 glycoprotein of human immunodeficiency virus type 1 by human monoclonal antibodies. Eur. J. Biochem. 268:2001;2856-2866.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2856-2866
    • Zeder-Lutz, G.1
  • 22
    • 0028831142 scopus 로고
    • Neutralizing recombinant human antibodies to a conformational V2- and CD4-binding site-sensitive epitope of HIV-1 gp120 isolated by using an epitope-masking procedure
    • Ditzel H.J., et al. Neutralizing recombinant human antibodies to a conformational V2- and CD4-binding site-sensitive epitope of HIV-1 gp120 isolated by using an epitope-masking procedure. J. Immunol. 154:1995;893-906.
    • (1995) J. Immunol. , vol.154 , pp. 893-906
    • Ditzel, H.J.1
  • 23
    • 0031969423 scopus 로고    scopus 로고
    • Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity
    • Parren P.W., et al. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol. 72:1998;3512-3519.
    • (1998) J. Virol. , vol.72 , pp. 3512-3519
    • Parren, P.W.1
  • 24
    • 0033587488 scopus 로고    scopus 로고
    • Conformational changes of gp120 in epitopes near the CCR5 binding site are induced by CD4 and a CD4 miniprotein mimetic
    • Zhang W., et al. Conformational changes of gp120 in epitopes near the CCR5 binding site are induced by CD4 and a CD4 miniprotein mimetic. Biochemistry. 38:1999;9405-9416.
    • (1999) Biochemistry , vol.38 , pp. 9405-9416
    • Zhang, W.1
  • 25
    • 0035852822 scopus 로고    scopus 로고
    • Antibody 17b binding at the coreceptor site weakens the kinetics of the interaction of envelope glycoprotein gp120 with CD4
    • Zhang W., et al. Antibody 17b binding at the coreceptor site weakens the kinetics of the interaction of envelope glycoprotein gp120 with CD4. Biochemistry. 40:2001;1662-1670.
    • (2001) Biochemistry , vol.40 , pp. 1662-1670
    • Zhang, W.1
  • 26
    • 0034062062 scopus 로고    scopus 로고
    • Properties of a neutralizing antibody that recognizes a conformational form of epitope ERDRD in the gp41 C-terminal tail of human immunodeficiency virus type 1
    • Cleveland S.M., et al. Properties of a neutralizing antibody that recognizes a conformational form of epitope ERDRD in the gp41 C-terminal tail of human immunodeficiency virus type 1. J. Gen. Virol. 81:2000;1251-1260.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1251-1260
    • Cleveland, S.M.1
  • 27
    • 0028360038 scopus 로고
    • Effect of HIV-1 peptide presentation on the affinity constants of two monoclonal antibodies determined by BIAcore technology
    • Mani J.C., et al. Effect of HIV-1 peptide presentation on the affinity constants of two monoclonal antibodies determined by BIAcore technology. Mol. Immunol. 31:1994;439-444.
    • (1994) Mol. Immunol. , vol.31 , pp. 439-444
    • Mani, J.C.1
  • 28
    • 0032555564 scopus 로고    scopus 로고
    • Identification of V3 loop-binding proteins as potential receptors implicated in the binding of HIV particles to CD4(+) cells
    • Callebaut C., et al. Identification of V3 loop-binding proteins as potential receptors implicated in the binding of HIV particles to CD4(+) cells. J. Biol. Chem. 273:1998;21988-21997.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21988-21997
    • Callebaut, C.1
  • 29
    • 0031573212 scopus 로고    scopus 로고
    • Human monoclonal antibodies to the V3 loop of HIV-1 with intra- and interclade cross-reactivity
    • Gorny M.K., et al. Human monoclonal antibodies to the V3 loop of HIV-1 with intra- and interclade cross-reactivity. J. Immunol. 159:1997;5114-5122.
    • (1997) J. Immunol. , vol.159 , pp. 5114-5122
    • Gorny, M.K.1
  • 30
    • 0032994081 scopus 로고    scopus 로고
    • Cross-reactivity of anti-HIV-1-p17-derivative peptide (P30-52) antibody to Env V3 peptide
    • Ota A., et al. Cross-reactivity of anti-HIV-1-p17-derivative peptide (P30-52) antibody to Env V3 peptide. Hybridoma. 18:1999;149-157.
    • (1999) Hybridoma , vol.18 , pp. 149-157
    • Ota, A.1
  • 31
    • 0034711287 scopus 로고    scopus 로고
    • The binding of a glycoprotein 120 V3 loop peptide to HIV-1 neutralizing antibodies. Structural implications
    • Wu G., et al. The binding of a glycoprotein 120 V3 loop peptide to HIV-1 neutralizing antibodies. Structural implications. J. Biol. Chem. 275:2000;36645-36652.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36645-36652
    • Wu, G.1
  • 32
    • 0029927859 scopus 로고    scopus 로고
    • Affinity maturation of a high-affinity human monoclonal antibody against the third hypervariable loop of human immunodeficiency virus: Use of phage display to improve affinity and broaden strain reactivity
    • Thompson J., et al. Affinity maturation of a high-affinity human monoclonal antibody against the third hypervariable loop of human immunodeficiency virus: use of phage display to improve affinity and broaden strain reactivity. J. Mol. Biol. 256:1996;77-88.
    • (1996) J. Mol. Biol. , vol.256 , pp. 77-88
    • Thompson, J.1
  • 33
    • 0031674897 scopus 로고    scopus 로고
    • Evaluation of the affinity measurement of anti-HIV-1 p17 monoclonal antibody by BIAcore
    • Ota A., Ueda S. Evaluation of the affinity measurement of anti-HIV-1 p17 monoclonal antibody by BIAcore. Hybridoma. 17:1998;471-477.
    • (1998) Hybridoma , vol.17 , pp. 471-477
    • Ota, A.1    Ueda, S.2
  • 34
    • 0034596258 scopus 로고    scopus 로고
    • Accessibility of the high-mannose glycans of glycoprotein gp120 from human immunodeficiency virus type 1 probed by in vitro interaction with mannose-binding lectins
    • Astoul C.H., et al. Accessibility of the high-mannose glycans of glycoprotein gp120 from human immunodeficiency virus type 1 probed by in vitro interaction with mannose-binding lectins. Biochem. Biophys. Res. Commun. 274:2000;455-460.
    • (2000) Biochem. Biophys. Res. Commun. , vol.274 , pp. 455-460
    • Astoul, C.H.1
  • 35
    • 0030822348 scopus 로고    scopus 로고
    • Molecular mimicry between the rabies virus glycoprotein and human immunodeficiency virus-1 GP120: Cross-reacting antibodies induced by rabies vaccination
    • Bracci L., et al. Molecular mimicry between the rabies virus glycoprotein and human immunodeficiency virus-1 GP120: cross-reacting antibodies induced by rabies vaccination. Blood. 90:1997;3623-3628.
    • (1997) Blood , vol.90 , pp. 3623-3628
    • Bracci, L.1
  • 36
    • 0026768221 scopus 로고
    • Detection of receptor-ligand interactions using surface plasmon resonance: Model studies employing the HIV-1 gp120/CD4 interaction
    • Brigham-Burke M., et al. Detection of receptor-ligand interactions using surface plasmon resonance: model studies employing the HIV-1 gp120/CD4 interaction. Anal. Biochem. 205:1992;125-131.
    • (1992) Anal. Biochem. , vol.205 , pp. 125-131
    • Brigham-Burke, M.1
  • 37
    • 0032778348 scopus 로고    scopus 로고
    • The C domain of HIV-1 gp41 binds the putative cellular receptor protein P62
    • Chen Y.H., et al. The C domain of HIV-1 gp41 binds the putative cellular receptor protein P62. AIDS. 13:1999;1021-1024.
    • (1999) AIDS , vol.13 , pp. 1021-1024
    • Chen, Y.H.1
  • 38
    • 0033920212 scopus 로고    scopus 로고
    • Selective interactions of polyanions with basic surfaces on human immunodeficiency virus type 1 gp120
    • Moulard M., et al. Selective interactions of polyanions with basic surfaces on human immunodeficiency virus type 1 gp120. J. Virol. 74:2000;1948-1960.
    • (2000) J. Virol. , vol.74 , pp. 1948-1960
    • Moulard, M.1
  • 39
    • 0034255034 scopus 로고    scopus 로고
    • Energetics of the HIV gp120-CD4 binding reaction
    • Myszka D.G., et al. Energetics of the HIV gp120-CD4 binding reaction. Proc. Natl. Acad. Sci. U. S. A. 97:2000;9026-9031.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9026-9031
    • Myszka, D.G.1
  • 40
    • 0030446301 scopus 로고    scopus 로고
    • Kinetic and structural analysis of mutant CD4 receptors that are defective in HIV gp120 binding
    • Wu H., et al. Kinetic and structural analysis of mutant CD4 receptors that are defective in HIV gp120 binding. Proc. Natl. Acad. Sci. U. S. A. 93:1996;15030-15035.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 15030-15035
    • Wu, H.1
  • 41
    • 0034015712 scopus 로고    scopus 로고
    • HIV-1 gp41 by N-domain binds the potential receptor protein P45
    • Xiao Y., et al. HIV-1 gp41 by N-domain binds the potential receptor protein P45. Int. Arch. Allergy Immunol. 121:2000;253-257.
    • (2000) Int. Arch. Allergy Immunol. , vol.121 , pp. 253-257
    • Xiao, Y.1
  • 42
    • 0035955695 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant HIV gp140
    • Zhang C.W.-H., et al. Expression, purification, and characterization of recombinant HIV gp140. J. Biol. Chem. 276:2001;39577-39585.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39577-39585
    • Zhang, C.W.-H.1
  • 43
    • 0033975085 scopus 로고    scopus 로고
    • HIV-2 transmembrane protein gp36 binds to the putative cellular receptor proteins P45 and P62
    • Chen Y.H., et al. HIV-2 transmembrane protein gp36 binds to the putative cellular receptor proteins P45 and P62. Immunobiology. 201:2000;317-322.
    • (2000) Immunobiology , vol.201 , pp. 317-322
    • Chen, Y.H.1
  • 44
    • 0034860103 scopus 로고    scopus 로고
    • Characterization of interaction between C-domain on HIV-1 gp41 and the putative receptor protein p62
    • Yang H., et al. Characterization of interaction between C-domain on HIV-1 gp41 and the putative receptor protein p62. Immunobiology. 203:2001;778-785.
    • (2001) Immunobiology , vol.203 , pp. 778-785
    • Yang, H.1
  • 45
    • 0035123458 scopus 로고    scopus 로고
    • The highly conserved C-terminal dileucine motif in the cytosolic domain of the human immunodeficiency virus type 1 envelope glycoprotein is critical for its association with the AP-1 clathrin adaptor
    • Wyss S., et al. The highly conserved C-terminal dileucine motif in the cytosolic domain of the human immunodeficiency virus type 1 envelope glycoprotein is critical for its association with the AP-1 clathrin adaptor. J. Virol. 75:2001;2982-2992.
    • (2001) J. Virol. , vol.75 , pp. 2982-2992
    • Wyss, S.1
  • 46
    • 0034705106 scopus 로고    scopus 로고
    • Specific interaction of CCR5 amino-terminal domain peptides containing sulfotyrosines with HIV-1 envelope glycoprotein gp120
    • Cormier E.G., et al. Specific interaction of CCR5 amino-terminal domain peptides containing sulfotyrosines with HIV-1 envelope glycoprotein gp120. Proc. Natl. Acad. Sci. U. S. A. 97:2000;5762-5767.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5762-5767
    • Cormier, E.G.1
  • 47
    • 0035000023 scopus 로고    scopus 로고
    • Mapping the determinants of the CCR5 amino-terminal sulfopeptide interaction with soluble human immunodeficiency virus type 1 gp120-CD4 complexes
    • Cormier E.G., et al. Mapping the determinants of the CCR5 amino-terminal sulfopeptide interaction with soluble human immunodeficiency virus type 1 gp120-CD4 complexes. J. Virol. 75:2001;5541-5549.
    • (2001) J. Virol. , vol.75 , pp. 5541-5549
    • Cormier, E.G.1
  • 48
    • 0034633660 scopus 로고    scopus 로고
    • A biosensor assay for studying ligand-membrane receptor interactions: Binding of antibodies and HIV-1 Env to chemokine receptors
    • Hoffman T.L., et al. A biosensor assay for studying ligand-membrane receptor interactions: binding of antibodies and HIV-1 Env to chemokine receptors. Proc. Natl. Acad. Sci. U. S. A. 97:2000;11215-11220.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 11215-11220
    • Hoffman, T.L.1
  • 49
    • 0035168319 scopus 로고    scopus 로고
    • A cyclic dodecapeptide-multiple-antigen peptide conjugate from the undecapeptidyl arch (from Arg(168) to Cys(178)) of extracellular loop 2 in CCR5 as a novel human immunodeficiency virus type 1 vaccine
    • Misumi S., et al. A cyclic dodecapeptide-multiple-antigen peptide conjugate from the undecapeptidyl arch (from Arg(168) to Cys(178)) of extracellular loop 2 in CCR5 as a novel human immunodeficiency virus type 1 vaccine. J. Virol. 75:2001;11614-11620.
    • (2001) J. Virol. , vol.75 , pp. 11614-11620
    • Misumi, S.1
  • 50
    • 85031207766 scopus 로고    scopus 로고
    • Capture and reconstitution of G protein-coupled receptors on a biosensor surface
    • in press
    • Stenlund, P. et al. Capture and reconstitution of G protein-coupled receptors on a biosensor surface. Anal. Biochem. (in press).
    • Anal. Biochem.
    • Stenlund, P.1
  • 51
    • 0034214208 scopus 로고    scopus 로고
    • Characterization of the 'helix clamp' motif of HIV-1 reverse transcriptase using MALDI-TOF MS and surface plasmon resonance
    • Lin S., et al. Characterization of the 'helix clamp' motif of HIV-1 reverse transcriptase using MALDI-TOF MS and surface plasmon resonance. Anal. Chem. 72:2000;2635-2640.
    • (2000) Anal. Chem. , vol.72 , pp. 2635-2640
    • Lin, S.1
  • 52
    • 0035871105 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase interaction with model RNA-DNA duplexes
    • Gorshkova I.I., et al. HIV-1 reverse transcriptase interaction with model RNA-DNA duplexes. Anal. Biochem. 291:2001;198-206.
    • (2001) Anal. Biochem. , vol.291 , pp. 198-206
    • Gorshkova, I.I.1
  • 53
    • 0033574629 scopus 로고    scopus 로고
    • Evidence of interactions between the nucleocapsid protein NCp7 and the reverse transcriptase of HIV-1
    • Druillennec S., et al. Evidence of interactions between the nucleocapsid protein NCp7 and the reverse transcriptase of HIV-1. J. Biol. Chem. 274:1999;11283-11288.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11283-11288
    • Druillennec, S.1
  • 54
    • 0036296520 scopus 로고    scopus 로고
    • Selection and stabilization of the RNA aptamers against the human immunodeficiency virus type-1 nucleocapsid protein
    • Kim S.J., et al. Selection and stabilization of the RNA aptamers against the human immunodeficiency virus type-1 nucleocapsid protein. Biochem. Biophys. Res. Commun. 291:2002;925-931.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 925-931
    • Kim, S.J.1
  • 56
    • 0033614815 scopus 로고    scopus 로고
    • Divalent cations stimulate preferential recognition of a viral DNA end by HIV-1 integrase
    • Yi J., et al. Divalent cations stimulate preferential recognition of a viral DNA end by HIV-1 integrase. Biochemistry. 38:1999;8458-8468.
    • (1999) Biochemistry , vol.38 , pp. 8458-8468
    • Yi, J.1
  • 58
    • 0035933826 scopus 로고    scopus 로고
    • Pentosan polysulfate as an inhibitor of extracellular HIV-1 Tat
    • Rusnati M., et al. Pentosan polysulfate as an inhibitor of extracellular HIV-1 Tat. J. Biol. Chem. 276:2001;22420-22425.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22420-22425
    • Rusnati, M.1
  • 59
    • 0036227966 scopus 로고    scopus 로고
    • Small molecule modulators of HIV Rev/Rev response element interaction identified by random screening
    • Chapman R.L., et al. Small molecule modulators of HIV Rev/Rev response element interaction identified by random screening. Antiviral Res. 54:2002;149-162.
    • (2002) Antiviral Res. , vol.54 , pp. 149-162
    • Chapman, R.L.1
  • 60
    • 0030985913 scopus 로고    scopus 로고
    • Direct observation of aminoglycoside-RNA interactions by surface plasmon resonance
    • Hendrix M., et al. Direct observation of aminoglycoside-RNA interactions by surface plasmon resonance. J. Am. Chem. Soc. 119:1997;3641-3648.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3641-3648
    • Hendrix, M.1
  • 61
    • 0033580814 scopus 로고    scopus 로고
    • Real-time kinetics of HIV-1 Rev-Rev response element interactions
    • Van Ryk D.I., Venkatesan S. Real-time kinetics of HIV-1 Rev-Rev response element interactions. J. Biol. Chem. 274:1999;17452-17463.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17452-17463
    • Van Ryk, D.I.1    Venkatesan, S.2
  • 62
    • 0030310583 scopus 로고    scopus 로고
    • Binding kinetics and bioassay of RRE mRNA fragments to a peptide containing the recognition domain of HIV-1 Rev
    • West M.L., Ramsdale T.E. Binding kinetics and bioassay of RRE mRNA fragments to a peptide containing the recognition domain of HIV-1 Rev. Biomed. Pept. Proteins Nucleic Acids. 2:1996;85-88.
    • (1996) Biomed. Pept. Proteins Nucleic Acids , vol.2 , pp. 85-88
    • West, M.L.1    Ramsdale, T.E.2
  • 63
    • 0031281516 scopus 로고    scopus 로고
    • Analysis of interactions between huGATA-3 transcription factor and three GATA regulatory elements of HIV-1 long terminal repeat, by surface plasmon resonance
    • Galio L., et al. Analysis of interactions between huGATA-3 transcription factor and three GATA regulatory elements of HIV-1 long terminal repeat, by surface plasmon resonance. Anal. Biochem. 253:1997;70-77.
    • (1997) Anal. Biochem. , vol.253 , pp. 70-77
    • Galio, L.1
  • 64
    • 0032729972 scopus 로고    scopus 로고
    • Interaction of the human NF-κB p52 transcription factor with DNA-PNA hybrids mimicking the NF-κB binding sites of the human immunodeficiency virus type 1 promoter
    • Mischiati C., et al. Interaction of the human NF-κB p52 transcription factor with DNA-PNA hybrids mimicking the NF-κB binding sites of the human immunodeficiency virus type 1 promoter. J. Biol. Chem. 274:1999;33114-33122.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33114-33122
    • Mischiati, C.1
  • 65
    • 0033554559 scopus 로고    scopus 로고
    • Real-time study of interactions between a composite DNA regulatory region (HIV-1 LTR NRE) and several transcription factors of nuclear extracts
    • Galio L., et al. Real-time study of interactions between a composite DNA regulatory region (HIV-1 LTR NRE) and several transcription factors of nuclear extracts. Biochem. Biophys. Res. Commun. 264:1999;6-13.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 6-13
    • Galio, L.1
  • 66
    • 0037044192 scopus 로고    scopus 로고
    • 2′-O-methyl-RNA hairpins generate loop-loop complexes and selectively inhibit HIV-1 Tat-mediated transcription
    • Darfeuille F., et al. 2′-O-methyl-RNA hairpins generate loop-loop complexes and selectively inhibit HIV-1 Tat-mediated transcription. Biochemistry. 41:2002;12186-12192.
    • (2002) Biochemistry , vol.41 , pp. 12186-12192
    • Darfeuille, F.1
  • 67
    • 0037162493 scopus 로고    scopus 로고
    • Loop-loop interaction of HIV-1 TAR RNA with N3′→P5′ deoxyphosphoramidate aptamers inhibits in vitro Tat-mediated transcription
    • Darfeuille F., et al. Loop-loop interaction of HIV-1 TAR RNA with N3′→P5′ deoxyphosphoramidate aptamers inhibits in vitro Tat-mediated transcription. Proc. Natl. Acad. Sci. U. S. A. 99:2002;9709-9714.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9709-9714
    • Darfeuille, F.1
  • 68
    • 0034647516 scopus 로고    scopus 로고
    • Is a closing 'GA pair' a rule for stable loop-loop RNA complexes?
    • Duconge F., et al. Is a closing 'GA pair' a rule for stable loop-loop RNA complexes? J. Biol. Chem. 275:2000;21287-21294.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21287-21294
    • Duconge, F.1
  • 69
    • 0034192170 scopus 로고    scopus 로고
    • Surface plasmon resonance kinetic studies of the HIV TAR RNA kissing hairpin complex and its stabilization by 2-thiouridine modification
    • Nair T.M., et al. Surface plasmon resonance kinetic studies of the HIV TAR RNA kissing hairpin complex and its stabilization by 2-thiouridine modification. Nucleic Acids Res. 28:2000;1935-1940.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1935-1940
    • Nair, T.M.1
  • 70
    • 0035830704 scopus 로고    scopus 로고
    • Pyrimidine tract binding protein and La autoantigen interact differently with the 5′ untranslated regions of lentiviruses and oncoretrovirus mRNAs
    • Waysbort A., et al. Pyrimidine tract binding protein and La autoantigen interact differently with the 5′ untranslated regions of lentiviruses and oncoretrovirus mRNAs. FEBS Lett. 490:2001;54-58.
    • (2001) FEBS Lett. , vol.490 , pp. 54-58
    • Waysbort, A.1
  • 71
    • 0031282246 scopus 로고    scopus 로고
    • Biosensor technology and surface plasmon resonance for real-time detection of HIV-1 genomic sequences amplified by polymerase chain reaction
    • Bianchi N., et al. Biosensor technology and surface plasmon resonance for real-time detection of HIV-1 genomic sequences amplified by polymerase chain reaction. Clin. Diagn. Virol. 8:1997;199-208.
    • (1997) Clin. Diagn. Virol. , vol.8 , pp. 199-208
    • Bianchi, N.1
  • 72
    • 17944363138 scopus 로고    scopus 로고
    • Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
    • Garrus J.E., et al. Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell. 107:2001;55-65.
    • (2001) Cell , vol.107 , pp. 55-65
    • Garrus, J.E.1
  • 73
    • 0037093316 scopus 로고    scopus 로고
    • Structure and functional interactions of the Tsg101 UEV domain
    • Pornillos O., et al. Structure and functional interactions of the Tsg101 UEV domain. EMBO J. 21:2002;2397-2406.
    • (2002) EMBO J. , vol.21 , pp. 2397-2406
    • Pornillos, O.1
  • 74
    • 0031935140 scopus 로고    scopus 로고
    • Sequence-specific binding of human immunodeficiency virus type 1 nucleocapsid protein to short oligonucleotides
    • Fisher R.J., et al. Sequence-specific binding of human immunodeficiency virus type 1 nucleocapsid protein to short oligonucleotides. J. Virol. 72:1998;1902-1909.
    • (1998) J. Virol. , vol.72 , pp. 1902-1909
    • Fisher, R.J.1
  • 75
    • 0029620850 scopus 로고
    • Aspects of molecular interaction between HIV p17 and human γ interferon
    • Flamminio G., et al. Aspects of molecular interaction between HIV p17 and human γ interferon. AIDS Res. Hum. Retroviruses. 11:1995;1441-1447.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 1441-1447
    • Flamminio, G.1
  • 76
    • 19244375366 scopus 로고    scopus 로고
    • The inhibition of human immunodeficiency virus proteases by 'interface peptides'
    • Schramm H.J., et al. The inhibition of human immunodeficiency virus proteases by 'interface peptides'. Antiviral Res. 30:1996;155-170.
    • (1996) Antiviral Res. , vol.30 , pp. 155-170
    • Schramm, H.J.1
  • 77
    • 0031588011 scopus 로고    scopus 로고
    • Molecular recognition in the HIV-1 capsid/cyclophilin A complex
    • Yoo S., et al. Molecular recognition in the HIV-1 capsid/cyclophilin A complex. J. Mol. Biol. 269:1997;780-795.
    • (1997) J. Mol. Biol. , vol.269 , pp. 780-795
    • Yoo, S.1
  • 78
    • 0028805516 scopus 로고
    • A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein
    • Lee C.H., et al. A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein. EMBO J. 14:1995;5006-5015.
    • (1995) EMBO J. , vol.14 , pp. 5006-5015
    • Lee, C.H.1
  • 79
    • 0032566903 scopus 로고    scopus 로고
    • SH3-domain binding function of HIV-1 Nef is required for association with a PAK-related kinase
    • Manninen A., et al. SH3-domain binding function of HIV-1 Nef is required for association with a PAK-related kinase. Virology. 250:1998;273-282.
    • (1998) Virology , vol.250 , pp. 273-282
    • Manninen, A.1
  • 80
    • 0031017838 scopus 로고    scopus 로고
    • Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement
    • Moarefi I., et al. Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature. 385:1997;650-653.
    • (1997) Nature , vol.385 , pp. 650-653
    • Moarefi, I.1
  • 81
    • 0033934494 scopus 로고    scopus 로고
    • Interactions of the C-terminus of viral protein R with nucleic acids are modulated by its N-terminus
    • De Rocquigny H., et al. Interactions of the C-terminus of viral protein R with nucleic acids are modulated by its N-terminus. Eur. J. Biochem. 267:2000;3654-3660.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3654-3660
    • De Rocquigny, H.1
  • 82
    • 0034598337 scopus 로고    scopus 로고
    • The HIV-1 viral protein R induces apoptosis via a direct effect on the mitochondrial permeability transition pore
    • Jacotot E., et al. The HIV-1 viral protein R induces apoptosis via a direct effect on the mitochondrial permeability transition pore. J. Exp. Med. 191:2000;33-45.
    • (2000) J. Exp. Med. , vol.191 , pp. 33-45
    • Jacotot, E.1
  • 83
    • 0035910754 scopus 로고    scopus 로고
    • Control of mitochondrial membrane permeabilization by adenine nucleotide translocator interacting with HIV-1 viral protein rR and Bcl-2
    • Jacotot E., et al. Control of mitochondrial membrane permeabilization by adenine nucleotide translocator interacting with HIV-1 viral protein rR and Bcl-2. J. Exp. Med. 193:2001;509-519.
    • (2001) J. Exp. Med. , vol.193 , pp. 509-519
    • Jacotot, E.1
  • 84
    • 0034785763 scopus 로고    scopus 로고
    • Biochemical analyses of the interactions between human immunodeficiency virus type 1 Vpr and p6(Gag)
    • Jenkins Y., et al. Biochemical analyses of the interactions between human immunodeficiency virus type 1 Vpr and p6(Gag). J. Virol. 75:2001;10537-10542.
    • (2001) J. Virol. , vol.75 , pp. 10537-10542
    • Jenkins, Y.1
  • 85
    • 0029017743 scopus 로고
    • Characterization of a soluble, oligomeric HIV-1 gp160 protein as a potential immunogen
    • VanCott T.C., et al. Characterization of a soluble, oligomeric HIV-1 gp160 protein as a potential immunogen. J. Immunol. Methods. 183:1995;103-117.
    • (1995) J. Immunol. Methods , vol.183 , pp. 103-117
    • VanCott, T.C.1
  • 86
    • 0028135460 scopus 로고
    • Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technology and ELISA
    • Richalet-Sécordel P.M., et al. Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technology and ELISA. J. Immunol. Methods. 176:1994;221-234.
    • (1994) J. Immunol. Methods , vol.176 , pp. 221-234
    • Richalet-Sécordel, P.M.1
  • 87
    • 0032440408 scopus 로고    scopus 로고
    • Selection of recombinant, library-derived antibody fragments against p24 for human immunodeficiency virus type 1 diagnostics
    • de Haard J.J., et al. Selection of recombinant, library-derived antibody fragments against p24 for human immunodeficiency virus type 1 diagnostics. Clin. Diagn. Virol. 5:1998;636-644.
    • (1998) Clin. Diagn. Virol. , vol.5 , pp. 636-644
    • De Haard, J.J.1
  • 88
    • 0031112509 scopus 로고    scopus 로고
    • Vaccine-specific antibody responses induced by HIV-1 envelope subunit vaccines
    • Pincus S., et al. Vaccine-specific antibody responses induced by HIV-1 envelope subunit vaccines. J. Immunol. 158:1997;3511-3520.
    • (1997) J. Immunol. , vol.158 , pp. 3511-3520
    • Pincus, S.1
  • 89
    • 0028805926 scopus 로고
    • Differential role of V3-specific antibodies in neutralization assays involving primary and laboratory-adapted isolates of HIV type 1
    • Vancott T.C., et al. Differential role of V3-specific antibodies in neutralization assays involving primary and laboratory-adapted isolates of HIV type 1. AIDS Res. Hum. Retroviruses. 11:1995;1379-1391.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 1379-1391
    • Vancott, T.C.1
  • 90
    • 0030975067 scopus 로고    scopus 로고
    • Antibodies with specificity to native gp120 and neutralization activity against primary human immunodeficiency virus type 1 isolates elicited by immunization with oligomeric gp160
    • VanCott T.C., et al. Antibodies with specificity to native gp120 and neutralization activity against primary human immunodeficiency virus type 1 isolates elicited by immunization with oligomeric gp160. J. Virol. 71:1997;4319-4330.
    • (1997) J. Virol. , vol.71 , pp. 4319-4330
    • VanCott, T.C.1
  • 91
    • 0029112274 scopus 로고
    • The alpha-glucosidase inhibitor N-butyldeoxynojirimycin inhibits human immunodeficiency virus entry at the level of post-CD4 binding
    • Fischer P.B., et al. The alpha-glucosidase inhibitor N-butyldeoxynojirimycin inhibits human immunodeficiency virus entry at the level of post-CD4 binding. J. Virol. 69:1995;5791-5797.
    • (1995) J. Virol. , vol.69 , pp. 5791-5797
    • Fischer, P.B.1
  • 92
    • 0034693932 scopus 로고    scopus 로고
    • Design of a peptide inhibitor that blocks the cell fusion mediated by glycoprotein 41 of human immunodeficiency virus type 1
    • Jin B.S., et al. Design of a peptide inhibitor that blocks the cell fusion mediated by glycoprotein 41 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses. 16:2000;1797-1804.
    • (2000) AIDS Res. Hum. Retroviruses , vol.16 , pp. 1797-1804
    • Jin, B.S.1
  • 93
    • 0036162614 scopus 로고    scopus 로고
    • Revealing and utilizing receptor recognition mechanisms in a high-throughput world
    • Chaiken I. Revealing and utilizing receptor recognition mechanisms in a high-throughput world. J. Cell. Biochem. (Suppl. 37):2001;126-135.
    • (2001) J. Cell. Biochem. , Issue.SUPPL. 37 , pp. 126-135
    • Chaiken, I.1
  • 94
    • 0035605455 scopus 로고    scopus 로고
    • Capture and analysis of low molecular weight ligands by surface plasmon resonance combined with mass spectrometry
    • Sönksen C., et al. Capture and analysis of low molecular weight ligands by surface plasmon resonance combined with mass spectrometry. J. Mass Spectrom. 7:2001;385-391.
    • (2001) J. Mass Spectrom. , vol.7 , pp. 385-391
    • Sönksen, C.1
  • 95
    • 0030832691 scopus 로고    scopus 로고
    • Mode of interaction of G-quartets with the integrase of human immunodeficiency virus type 1
    • Cherepanov P., et al. Mode of interaction of G-quartets with the integrase of human immunodeficiency virus type 1. Mol. Pharmacol. 52:1997;771-780.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 771-780
    • Cherepanov, P.1
  • 96
    • 0034744992 scopus 로고    scopus 로고
    • P1/P1( modified HIV protease inhibitors as tools in two new sensitive surface plasmon resonance biosensor screening assays
    • Alterman M., et al. P1/P1( modified HIV protease inhibitors as tools in two new sensitive surface plasmon resonance biosensor screening assays. Eur. J. Pharm. Sci. 13:2001;203-212.
    • (2001) Eur. J. Pharm. Sci. , vol.13 , pp. 203-212
    • Alterman, M.1
  • 97
    • 0033778280 scopus 로고    scopus 로고
    • Characterization of a set of HIV-1 protease inhibitors using binding kinetics data from a biosensor-based screen
    • Hämäläinen M.D., et al. Characterization of a set of HIV-1 protease inhibitors using binding kinetics data from a biosensor-based screen. J. Biomol. Screen. 5:2000;353-360.
    • (2000) J. Biomol. Screen. , vol.5 , pp. 353-360
    • Hämäläinen, M.D.1
  • 98
    • 0345196632 scopus 로고    scopus 로고
    • Screening of compounds interacting with HIV-1 proteinase using optical biosensor technology
    • Markgren P.-O., et al. Screening of compounds interacting with HIV-1 proteinase using optical biosensor technology. Anal. Biochem. 265:1998;340-350.
    • (1998) Anal. Biochem. , vol.265 , pp. 340-350
    • Markgren, P.-O.1
  • 99
    • 0343484958 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction between HIV-1 protease and inhibitors using optical biosensor technology
    • Markgren P.-O., et al. Kinetic analysis of the interaction between HIV-1 protease and inhibitors using optical biosensor technology. Anal. Biochem. 279:2000;71-78.
    • (2000) Anal. Biochem. , vol.279 , pp. 71-78
    • Markgren, P.-O.1
  • 100
    • 0035871240 scopus 로고    scopus 로고
    • Determination of interaction kinetic constants for HIV-1 protease inhibitors using optical biosensor technology
    • Markgren P.-O., et al. Determination of interaction kinetic constants for HIV-1 protease inhibitors using optical biosensor technology. Anal. Biochem. 291:2001;207-218.
    • (2001) Anal. Biochem. , vol.291 , pp. 207-218
    • Markgren, P.-O.1
  • 101
    • 0037028049 scopus 로고    scopus 로고
    • Relationships between structure and interaction kinetics for HIV-1 proteinase inhibitors
    • Markgren P.-O., et al. Relationships between structure and interaction kinetics for HIV-1 proteinase inhibitors. J. Med. Chem. 45:2002;5430-5439.
    • (2002) J. Med. Chem. , vol.45 , pp. 5430-5439
    • Markgren, P.-O.1
  • 102
    • 0035814798 scopus 로고    scopus 로고
    • A heterocyclic inhibitor of the REV-RRE complex binds to RRE as a dimer
    • Li K., et al. A heterocyclic inhibitor of the REV-RRE complex binds to RRE as a dimer. Biochemistry. 40:2001;1150-1158.
    • (2001) Biochemistry , vol.40 , pp. 1150-1158
    • Li, K.1
  • 103
    • 0033932507 scopus 로고    scopus 로고
    • Biospecific interaction analysis (BIA) of low-molecular weight DNA-binding drugs
    • Gambari R., et al. Biospecific interaction analysis (BIA) of low-molecular weight DNA-binding drugs. J. Pharmacol. Exp. Ther. 294:2000;370-377.
    • (2000) J. Pharmacol. Exp. Ther. , vol.294 , pp. 370-377
    • Gambari, R.1
  • 104
    • 0031886388 scopus 로고    scopus 로고
    • Human immunodeficiency virus glycoprotein gp120 as the primary target for the antiviral action of AR177 (Zintevir)
    • Esté J.A., et al. Human immunodeficiency virus glycoprotein gp120 as the primary target for the antiviral action of AR177 (Zintevir). Mol. Pharmacol. 53:1998;340-345.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 340-345
    • Esté, J.A.1
  • 105
    • 0029091404 scopus 로고
    • Lack of induction of antibodies specific for conserved, discontinuous epitopes of H0IV-1 envelope glycoprotein by candidate AIDS vaccines
    • VanCott T.C., et al. Lack of induction of antibodies specific for conserved, discontinuous epitopes of H0IV-1 envelope glycoprotein by candidate AIDS vaccines. J. Immunol. 155:1995;4100-4110.
    • (1995) J. Immunol. , vol.155 , pp. 4100-4110
    • VanCott, T.C.1
  • 106
    • 0036670299 scopus 로고    scopus 로고
    • Elimination of ingredients effect to improve the detection of anti HIV-1 p24 antibody in human serum using SPR apparatus
    • Hifumi E., et al. Elimination of ingredients effect to improve the detection of anti HIV-1 p24 antibody in human serum using SPR apparatus. Anal. Sci. 18:2002;863-867.
    • (2002) Anal. Sci. , vol.18 , pp. 863-867
    • Hifumi, E.1
  • 107
    • 0029921155 scopus 로고    scopus 로고
    • Preliminary crystallographic studies of an anti-HIV-1 protease antibody that inhibits enzyme activity
    • Lescar J., et al. Preliminary crystallographic studies of an anti-HIV-1 protease antibody that inhibits enzyme activity. Protein Sci. 5:1996;966-968.
    • (1996) Protein Sci. , vol.5 , pp. 966-968
    • Lescar, J.1


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