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Volumn 51, Issue 10, 2011, Pages 2760-2767

Discovery of novel promising targets for anti-AIDS drug developments by computer modeling: Application to the HIV-1 gp120 V3 loop

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ANTIVIRAL AGENTS;

EID: 80054912888     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci200255t     Document Type: Article
Times cited : (12)

References (61)
  • 2
    • 26844437646 scopus 로고    scopus 로고
    • HIV-1 gp120 V3 loop for structure-based drug design
    • DOI 10.2174/138920305774329359
    • Sirois, S.; Sing, T.; Chou, K. C. HIV-1 gp120 V3 loop for structure-based drug design Curr. Protein Pept. Sci. 2005, 6 (5) 413-22 (Pubitemid 41448343)
    • (2005) Current Protein and Peptide Science , vol.6 , Issue.5 , pp. 413-422
    • Sirois, S.1    Sing, T.2    Chou, K.-C.3
  • 4
    • 52649116262 scopus 로고    scopus 로고
    • Determining the invariant structure elements of the HIV-1 variable V3 loops: Insight into the HIV-MN and HIV-Haiti isolates
    • Andrianov, A. M. Determining the invariant structure elements of the HIV-1 variable V3 loops: insight into the HIV-MN and HIV-Haiti isolates J. Biomol. Struct. Dyn. 2008, 26 (2) 247-54
    • (2008) J. Biomol. Struct. Dyn. , vol.26 , Issue.2 , pp. 247-254
    • Andrianov, A.M.1
  • 5
    • 33747682832 scopus 로고    scopus 로고
    • Determination of structurally conservative amino acids of the HIV-1 protein gp120 V3 loop as promising targets for drug design by protein engineering approaches
    • DOI 10.1134/S000629790608013X
    • Andrianov, A. M.; Veresov, V. G. Determination of structurally conservative amino acids of the HIV-1 protein gp120 V3 loop as promising targets for drug design by protein engineering approaches Biochemistry (Moscow) 2006, 71 (8) 906-14 (Pubitemid 44273669)
    • (2006) Biochemistry (Moscow) , vol.71 , Issue.8 , pp. 906-914
    • Andrianov, A.M.1    Veresov, V.G.2
  • 6
    • 34250740369 scopus 로고    scopus 로고
    • Structural analysis of the HIV-1 gp120 V3 loop: Application to the HIV-Haiti isolates
    • Andrianov, A. M.; Veresov, V. G. Structural analysis of the HIV-1 gp120 V3 loop: application to the HIV-Haiti isolates J. Biomol. Struct. Dyn. 2007, 24 (6) 597-608 (Pubitemid 46954294)
    • (2007) Journal of Biomolecular Structure and Dynamics , vol.24 , Issue.6 , pp. 597-608
    • Andrianov, A.M.1    Veresov, V.G.2
  • 7
    • 52649179214 scopus 로고    scopus 로고
    • Study on conformational homology of the HIV-1 gp120 protein V3 loop. Structural analysis of the HIV-RF and HIV-Thailand viral strains
    • Andrianov, A. M. Study on conformational homology of the HIV-1 gp120 protein V3 loop. Structural analysis of the HIV-RF and HIV-Thailand viral strains Biochemistry (Moscow) Suppl. Ser. B: Biomed. Chem. 2007, 1, 125-30
    • (2007) Biochemistry (Moscow) Suppl. Ser. B: Biomed. Chem. , vol.1 , pp. 125-130
    • Andrianov, A.M.1
  • 10
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali, A.; Blundell, T. L. Comparative Protein Modelling by Satisfaction of Spatial Restraints J. Mol. Biol. 1993, 234 (3) 779-815 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 11
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard, C. K.; Spellman, M. W.; Riddle, L.; Harris, R. J.; Thomas, J. N.; Gregory, T. J. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells J. Biol. Chem. 1990, 265 (18) 10373-82
    • (1990) J. Biol. Chem. , vol.265 , Issue.18 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 12
    • 0025739156 scopus 로고
    • Simulated annealing approach to the study of protein structures
    • Chou, K. C.; Carlacci, L. Simulated annealing approach to the study of protein structures Protein Eng. 1991, 4 (6) 661-7
    • (1991) Protein Eng. , vol.4 , Issue.6 , pp. 661-667
    • Chou, K.C.1    Carlacci, L.2
  • 13
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink, C.; Villa, A.; Mark, A. E.; van Gunsteren, W. F. A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6 J. Comput. Chem. 2004, 25 (13) 1656-76
    • (2004) J. Comput. Chem. , vol.25 , Issue.13 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 14
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen, H. J. C.; van der Spoel, D.; van Drunen, R. GROMACS: A message-passing parallel molecular dynamics implementation Comput. Phys. Commun. 1995, 91 (1-3) 43-56
    • (1995) Comput. Phys. Commun. , vol.91 , Issue.1-3 , pp. 43-56
    • Berendsen, H.J.C.1    Van Der Spoel, D.2    Van Drunen, R.3
  • 15
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A.; MacArthur, M. W.; Moss, D. S.; Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 1993, 26 (2) 283-91
    • (1993) J. Appl. Crystallogr. , vol.26 , Issue.2 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 16
    • 0029978353 scopus 로고    scopus 로고
    • Analysis of main chain torsion angles in proteins: Prediction of NMR coupling constants for native and random coil conformations
    • DOI 10.1006/jmbi.1996.0041
    • Smith, L. J.; Bolin, K. A.; Schwalbe, H.; MacArthur, M. W.; Thornton, J. M.; Dobson, C. M. Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations J. Mol. Biol. 1996, 255 (3) 494-506 (Pubitemid 26105572)
    • (1996) Journal of Molecular Biology , vol.255 , Issue.3 , pp. 494-506
    • Smith, L.J.1    Bolin, K.A.2    Schwalbe, H.3    MacArthur, M.W.4    Thornton, J.M.5    Dobson, C.M.6
  • 17
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson, E. G.; Thornton, J. M. PROMOTIF-a program to identify and analyze structural motifs in proteins Protein Sci. 1996, 5 (2) 212-20 (Pubitemid 26054277)
    • (1996) Protein Science , vol.5 , Issue.2 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 18
    • 0027349406 scopus 로고
    • Derivation of locally accurate spatial protein structure from NMR data
    • Sherman, S. A.; Johnson, M. E. Derivation of locally accurate spatial protein structure from NMR data Prog. Biophys. Mol. Biol. 1993, 59 (3) 285-339
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , Issue.3 , pp. 285-339
    • Sherman, S.A.1    Johnson, M.E.2
  • 19
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • In; Pullman, B. Reidel: Dordrecht, Vol.
    • Berendsen, H. J. C.; Postma, J. P. M.; van Gunsteren, W. F.; Hermans, J., Interaction models for water in relation to protein hydration. In Intermolecular Forces; Pullman, B., Ed.; Reidel: Dordrecht, 1981; Vol. 11, pp 331-42.
    • (1981) Intermolecular Forces , vol.11 , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 22
    • 0027160197 scopus 로고
    • Backbone-dependent rotamer library for proteins. Application to side-chain prediction
    • DOI 10.1006/jmbi.1993.1170
    • Dunbrack, R. L., Jr.; Karplus, M. Backbone-dependent rotamer library for proteins. Application to side-chain prediction J. Mol. Biol. 1993, 230 (2) 543-74 (Pubitemid 23161363)
    • (1993) Journal of Molecular Biology , vol.230 , Issue.2 , pp. 543-574
    • Dunbrack Jr., R.L.1    Karplus, M.2
  • 25
    • 0034974149 scopus 로고    scopus 로고
    • N-linked glycosylation sites adjacent to and within the V1/V2 and the V3 loops of dualtropic human immunodeficiency virus type 1 isolate DH12 gp120 affect coreceptor usage and cellular tropism
    • DOI 10.1128/JVI.75.13.5998-6006.2001
    • Ogert, R. A.; Lee, M. K.; Ross, W.; Buckler-White, A.; Martin, M. A.; Cho, M. W. N-linked glycosylation sites adjacent to and within the V1/V2 and the V3 loops of dualtropic human immunodeficiency virus type 1 isolate DH12 gp120 affect coreceptor usage and cellular tropism J. Virol. 2001, 75 (13) 5998-6006 (Pubitemid 32553130)
    • (2001) Journal of Virology , vol.75 , Issue.13 , pp. 5998-6006
    • Ogert, R.A.1    Lee, M.K.2    Ross, W.3    Buckler-White, A.4    Martin, M.A.5    Cho, M.W.6
  • 26
    • 1842562419 scopus 로고    scopus 로고
    • N-Linked Glycosylation of the V3 Loop and the Immunologically Silent Face of gp120 Protects Human Immunodeficiency Virus Type 1 SF162 from Neutralization by Anti-gp120 and Anti-gp41 Antibodies
    • DOI 10.1128/JVI.78.7.3279-3295.2004
    • McCaffrey, R. A.; Saunders, C.; Hensel, M.; Stamatatos, L. N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies J. Virol. 2004, 78 (7) 3279-95 (Pubitemid 38568268)
    • (2004) Journal of Virology , vol.78 , Issue.7 , pp. 3279-3295
    • McCaffrey, R.A.1    Saunders, C.2    Hensel, M.3    Stamatatos, L.4
  • 27
    • 23344435219 scopus 로고    scopus 로고
    • N-linked glycosylation in C2 region of HIV-1 envelope reduces sensitivity to neutralizing antibodies
    • DOI 10.1089/vim.2005.18.343
    • Teeraputon, S.; Louisirirojchanakul, S.; Auewarakul, P. N-linked glycosylation in C2 region of HIV-1 envelope reduces sensitivity to neutralizing antibodies Viral Immunol. 2005, 18 (2) 343-53 (Pubitemid 41106013)
    • (2005) Viral Immunology , vol.18 , Issue.2 , pp. 343-353
    • Teeraputon, S.1    Louisirirojchanakul, S.2    Auewarakul, P.3
  • 28
    • 0035199412 scopus 로고    scopus 로고
    • N-linked glycosylation in the V3 region of HIV type 1 surface antigen modulates coreceptor usage in viral infection
    • DOI 10.1089/08892220152644179
    • Li, Y.; Rey-Cuille, M. A.; Hu, S. L. N-linked glycosylation in the V3 region of HIV type 1 surface antigen modulates coreceptor usage in viral infection AIDS Res. Hum. Retroviruses 2001, 17 (16) 1473-9 (Pubitemid 33116750)
    • (2001) AIDS Research and Human Retroviruses , vol.17 , Issue.16 , pp. 1473-1479
    • Li, Y.1    Rey-Cuille, M.-A.2    Hu, S.-L.3
  • 29
    • 0034469170 scopus 로고    scopus 로고
    • The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors
    • DOI 10.1128/JVI.74.23.11008-11016.2000
    • Malenbaum, S. E.; Yang, D.; Cavacini, L.; Posner, M.; Robinson, J.; Cheng-Mayer, C. The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors J. Virol. 2000, 74 (23) 11008-16 (Pubitemid 32223966)
    • (2000) Journal of Virology , vol.74 , Issue.23 , pp. 11008-11016
    • Malenbaum, S.E.1    Yang, D.2    Cavacini, L.3    Posner, M.4    Robinson, J.5    Cheng-Mayer, C.6
  • 30
    • 0035918220 scopus 로고    scopus 로고
    • N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization
    • Pollakis, G.; Kang, S.; Kliphuis, A.; Chalaby, M. I.; Goudsmit, J.; Paxton, W. A. N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization J. Biol. Chem. 2001, 276 (16) 13433-41
    • (2001) J. Biol. Chem. , vol.276 , Issue.16 , pp. 13433-13441
    • Pollakis, G.1    Kang, S.2    Kliphuis, A.3    Chalaby, M.I.4    Goudsmit, J.5    Paxton, W.A.6
  • 31
    • 0035098352 scopus 로고    scopus 로고
    • Loss of N-linked glycans in the V3-loop region of gp120 is correlated to an enhanced infectivity of HIV-1
    • Polzer, S.; Dittmar, M. T.; Schmitz, H.; Meyer, B.; Muller, H.; Krausslich, H. G.; Schreiber, M. Loss of N-linked glycans in the V3-loop region of gp120 is correlated to an enhanced infectivity of HIV-1 Glycobiology 2001, 11 (1) 11-9 (Pubitemid 32201333)
    • (2001) Glycobiology , vol.11 , Issue.1 , pp. 11-19
    • Polzer, S.1    Dittmar, M.T.2    Schmitz, H.3    Meyer, B.4    Muller, H.5    Krausslich, H.-G.6    Schreiber, M.7
  • 32
    • 37549057278 scopus 로고    scopus 로고
    • Glycosylation of HIV-1 gp120 V3 loop: Towards the rational design of a synthetic carbohydrate vaccine
    • Sirois, S.; Touaibia, M.; Chou, K. C.; Roy, R. Glycosylation of HIV-1 gp120 V3 loop: towards the rational design of a synthetic carbohydrate vaccine Curr. Med. Chem. 2007, 14 (30) 3232-42
    • (2007) Curr. Med. Chem. , vol.14 , Issue.30 , pp. 3232-3242
    • Sirois, S.1    Touaibia, M.2    Chou, K.C.3    Roy, R.4
  • 33
    • 0036333648 scopus 로고    scopus 로고
    • The crown and stem of the V3 loop play distinct roles in human immunodeficiency virus type 1 envelope glycoprotein interactions with the CCR5 coreceptor
    • DOI 10.1128/JVI.76.17.8953-8957.2002
    • Cormier, E. G.; Dragic, T. The crown and stem of the V3 loop play distinct roles in human immunodeficiency virus type 1 envelope glycoprotein interactions with the CCR5 coreceptor J. Virol. 2002, 76 (17) 8953-7 (Pubitemid 34864089)
    • (2002) Journal of Virology , vol.76 , Issue.17 , pp. 8953-8957
    • Cormier, E.G.1    Dragic, T.2
  • 34
    • 0028327101 scopus 로고
    • Crystal structure of the principal neutralization site of HIV-1
    • Ghiara, J. B.; Stura, E. A.; Stanfield, R. L.; Profy, A. T.; Wilson, I. A. Crystal structure of the principal neutralization site of HIV-1 Science 1994, 264 (5155) 82-5 (Pubitemid 24146010)
    • (1994) Science , vol.264 , Issue.5155 , pp. 82-85
    • Ghiara, J.B.1    Stura, E.A.2    Stanfield, R.L.3    Profy, A.T.4    Wilson, I.A.5
  • 35
    • 0036771699 scopus 로고    scopus 로고
    • Sequence variation and consensus sequence of V3 loop on HIV-1 gp120
    • DOI 10.1016/S0165-2478(02)00101-3, PII S0165247802001013
    • Tian, H.; Lan, C.; Chen, Y. H. Sequence variation and consensus sequence of V3 loop on HIV-1 gp120 Immunol. Lett. 2002, 83 (3) 231-3 (Pubitemid 34722356)
    • (2002) Immunology Letters , vol.83 , Issue.3 , pp. 231-233
    • Tian, H.1    Lan, C.2    Chen, Y.-H.3
  • 36
    • 4444345855 scopus 로고    scopus 로고
    • Dual spatial folds and different local structures of the HIV-1 immunogenic crown in various virus isolates
    • Andrianov, A. M. Dual spatial folds and different local structures of the HIV-1 immunogenic crown in various virus isolates J. Biomol. Struct. Dyn. 2004, 22 (2) 159-70 (Pubitemid 39187032)
    • (2004) Journal of Biomolecular Structure and Dynamics , vol.22 , Issue.2 , pp. 159-170
    • Andrianov, A.M.1
  • 37
    • 0037322432 scopus 로고    scopus 로고
    • Structure and polymorphism of the principal neutralization site of Thailand HIV-1 isolate
    • Andrianov, A. M.; Sokolov, Y. A. Structure and polymorphism of the principal neutralization site of Thailand HIV-1 isolate J. Biomol. Struct. Dyn. 2003, 20 (4) 603-13 (Pubitemid 36206104)
    • (2003) Journal of Biomolecular Structure and Dynamics , vol.20 , Issue.4 , pp. 603-613
    • Andrianov, A.M.1    Sokolov, Y.A.2
  • 38
    • 1642474410 scopus 로고    scopus 로고
    • 3D Structure Model of the Principal Neutralizing Epitope of Minnesota HIV-1 Isolate
    • Andrianov, A. M.; Sokolov, Y. A. 3D structure model of the principal neutralizing epitope of Minnesota HIV-1 isolate J. Biomol. Struct. Dyn. 2004, 21 (4) 577-90 (Pubitemid 38120958)
    • (2004) Journal of Biomolecular Structure and Dynamics , vol.21 , Issue.4 , pp. 577-590
    • Andrianov, A.M.1    Sokolov, Y.A.2
  • 41
    • 54949111659 scopus 로고    scopus 로고
    • Neutralizing activity of antibodies to the V3 loop region of HIV-1 gp120 relative to their epitope fine specificity
    • Pantophlet, R.; Wrin, T.; Cavacini, L. A.; Robinson, J. E.; Burton, D. R. Neutralizing activity of antibodies to the V3 loop region of HIV-1 gp120 relative to their epitope fine specificity Virology 2008, 381 (2) 251-60
    • (2008) Virology , vol.381 , Issue.2 , pp. 251-260
    • Pantophlet, R.1    Wrin, T.2    Cavacini, L.A.3    Robinson, J.E.4    Burton, D.R.5
  • 42
    • 20544458737 scopus 로고    scopus 로고
    • Restricted variable residues in the C-terminal segment of HIV-1 V3 loop regulate the molecular anatomy of CCR5 utilization
    • DOI 10.1016/j.jmb.2005.05.024, PII S0022283605005553
    • Hu, Q.; Napier, K. B.; Trent, J. O.; Wang, Z.; Taylor, S.; Griffin, G. E.; Peiper, S. C.; Shattock, R. J. Restricted variable residues in the C-terminal segment of HIV-1 V3 loop regulate the molecular anatomy of CCR5 utilization J. Mol. Biol. 2005, 350 (4) 699-712 (Pubitemid 40848668)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.4 , pp. 699-712
    • Hu, Q.1    Napier, K.B.2    Trent, J.O.3    Wang, Z.4    Taylor, S.5    Griffin, G.E.6    Peiper, S.C.7    Shattock, R.J.8
  • 43
    • 0032954629 scopus 로고    scopus 로고
    • Global and local structural properties of the principal neutralizing determinant of the HIV-1 envelope protein gp120
    • Andrianov, A. M. Global and local structural properties of the principal neutralizing determinant of the HIV-1 envelope protein gp120 J. Biomol. Struct. Dyn. 1999, 16 (4) 931-53 (Pubitemid 29157661)
    • (1999) Journal of Biomolecular Structure and Dynamics , vol.16 , Issue.4 , pp. 931-953
    • Andrianov, A.M.1
  • 45
    • 0242331318 scopus 로고    scopus 로고
    • Recurring conformation of the human immunodeficiency virus type 1 gp120 V3 loop
    • DOI 10.1016/S0042-6822(03)00525-7
    • Stanfield, R. L.; Ghiara, J. B.; Ollmann Saphire, E.; Profy, A. T.; Wilson, I. A. Recurring conformation of the human immunodeficiency virus type 1 gp120 V3 loop Virology 2003, 315 (1) 159-73 (Pubitemid 37340058)
    • (2003) Virology , vol.315 , Issue.1 , pp. 159-173
    • Stanfield, R.L.1    Ghiara, J.B.2    Saphire, E.O.3    Profy, A.T.4    Wilson, I.A.5
  • 46
    • 0028938818 scopus 로고
    • Local and global structural properties of the HIV-MN V3 loop
    • Catasti, P.; Fontenot, J. D.; Bradbury, E. M.; Gupta, G. Local and global structural properties of the HIV-MN V3 loop J. Biol. Chem. 1995, 270 (5) 2224-32
    • (1995) J. Biol. Chem. , vol.270 , Issue.5 , pp. 2224-2232
    • Catasti, P.1    Fontenot, J.D.2    Bradbury, E.M.3    Gupta, G.4
  • 48
    • 0026002948 scopus 로고
    • Solution conformational preferences of immunogenic peptides derived from the principal neutralizing determinant of the HIV-1 envelope glycoprotein gp120
    • Chandrasekhar, K.; Profy, A. T.; Dyson, H. J. Solution conformational preferences of immunogenic peptides derived from the principal neutralizing determinant of the HIV-1 envelope glycoprotein gp120 Biochemistry 1991, 30 (38) 9187-94
    • (1991) Biochemistry , vol.30 , Issue.38 , pp. 9187-9194
    • Chandrasekhar, K.1    Profy, A.T.2    Dyson, H.J.3
  • 49
    • 0030913036 scopus 로고    scopus 로고
    • NMR study of the peptide present in the principal neutralizing determinant (PND) of HIV-1 envelope glycoprotein gp120
    • DOI 10.1016/S0165-022X(97)01205-0, PII S0165022X97012050
    • Sarma, A. V.; Raju, T. V.; Kunwar, A. C. NMR study of the peptide present in the principal neutralizing determinant (PND) of HIV-1 envelope glycoprotein gp120 J. Biochem. Biophys. Methods 1997, 34 (2) 83-98 (Pubitemid 27204968)
    • (1997) Journal of Biochemical and Biophysical Methods , vol.34 , Issue.2 , pp. 83-98
    • Sarma, A.V.S.1    Raju, T.V.2    Kunwar, A.C.3
  • 50
    • 0029670024 scopus 로고    scopus 로고
    • Conformational features of a synthetic cyclic peptide corresponding to the complete V3 loop of the RF HIV-1 strain in water and water/trifluoroethanol solutions
    • Vranken, W. F.; Budesinsky, M.; Martins, J. C.; Fant, F.; Boulez, K.; Gras-Masse, H.; Borremans, F. A. Conformational features of a synthetic cyclic peptide corresponding to the complete V3 loop of the RF HIV-1 strain in water and water/trifluoroethanol solutions Eur. J. Biochem. 1996, 236 (1) 100-8
    • (1996) Eur. J. Biochem. , vol.236 , Issue.1 , pp. 100-108
    • Vranken, W.F.1    Budesinsky, M.2    Martins, J.C.3    Fant, F.4    Boulez, K.5    Gras-Masse, H.6    Borremans, F.A.7
  • 51
    • 0029877461 scopus 로고    scopus 로고
    • Conformational preferences of a chimeric peptide HIV-1 immunogen from the C4-V3 domains of gp120 envelope protein of HIV-1 CAN0A based on solution NMR: Comparison to a related immunogenic peptide from HIV-1 RF
    • Vu, H. M.; de Lorimier, R.; Moody, M. A.; Haynes, B. F.; Spicer, L. D. Conformational preferences of a chimeric peptide HIV-1 immunogen from the C4-V3 domains of gp120 envelope protein of HIV-1 CAN0A based on solution NMR: comparison to a related immunogenic peptide from HIV-1 RF Biochemistry 1996, 35 (16) 5158-65
    • (1996) Biochemistry , vol.35 , Issue.16 , pp. 5158-5165
    • Vu, H.M.1    De Lorimier, R.2    Moody, M.A.3    Haynes, B.F.4    Spicer, L.D.5
  • 53
    • 0031557396 scopus 로고    scopus 로고
    • NMR structure of the principal neutralizing determinant of HIV-1 displayed in filamentous bacteriophage coat protein
    • DOI 10.1006/jmbi.1996.0821
    • Jelinek, R.; Terry, T. D.; Gesell, J. J.; Malik, P.; Perham, R. N.; Opella, S. J. NMR structure of the principal neutralizing determinant of HIV-1 displayed in filamentous bacteriophage coat protein J. Mol. Biol. 1997, 266 (4) 649-55 (Pubitemid 27113205)
    • (1997) Journal of Molecular Biology , vol.266 , Issue.4 , pp. 649-655
    • Jelinek, R.1    Terry, T.D.2    Gesell, J.J.3    Malik, P.4    Perham, R.N.5    Opella, S.J.6
  • 54
    • 0033080945 scopus 로고    scopus 로고
    • Dual conformations for the HIV-1 gp120 V3 loop in complexes with different neutralizing Fabs
    • DOI 10.1016/S0969-2126(99)80020-3
    • Stanfield, R.; Cabezas, E.; Satterthwait, A.; Stura, E.; Profy, A.; Wilson, I. Dual conformations for the HIV-1 gp120 V3 loop in complexes with different neutralizing fabs Structure 1999, 7 (2) 131-42 (Pubitemid 29159699)
    • (1999) Structure , vol.7 , Issue.2 , pp. 131-142
    • Stanfield, R.L.1    Cabezas, E.2    Satterthwait, A.C.3    Stura, E.A.4    Profy, A.T.5    Wilson, I.A.6
  • 55
    • 0036283987 scopus 로고    scopus 로고
    • Local structural properties of the V3 loop of Thailand HIV-1 isolate
    • Andrianov, A. M. Local structural properties of the V3 loop of Thailand HIV-1 isolate J. Biomol. Struct. Dyn. 2002, 19 (6) 973-89 (Pubitemid 34701118)
    • (2002) Journal of Biomolecular Structure and Dynamics , vol.19 , Issue.6 , pp. 973-989
    • Andrianov, A.M.1
  • 56
    • 0034844325 scopus 로고    scopus 로고
    • Conformational model for the consensus v3 loop of the envelope protein gp120 of hiv-1 in a 20% trifluoroethanol/water solution
    • DOI 10.1046/j.1432-1327.2001.02146.x
    • Vranken, W. F.; Fant, F.; Budesinsky, M.; Borremans, F. A. Conformational model for the consensus V3 loop of the envelope protein gp120 of HIV-1 in a 20% trifluoroethanol/water solution Eur. J. Biochem. 2001, 268 (9) 2620-8 (Pubitemid 32853000)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.9 , pp. 2620-2628
    • Vranken, W.F.1    Fant, F.2    Budesinsky, M.3    Borremans, F.A.M.4
  • 57
    • 77954191991 scopus 로고    scopus 로고
    • Structural conservation predominates over sequence variability in the crown of HIV type 1's V3 loop
    • Almond, D.; Kimura, T.; Kong, X.; Swetnam, J.; Zolla-Pazner, S.; Cardozo, T. Structural conservation predominates over sequence variability in the crown of HIV type 1's V3 loop AIDS Res. Hum. Retroviruses 2010, 26 (6) 717-23
    • (2010) AIDS Res. Hum. Retroviruses , vol.26 , Issue.6 , pp. 717-723
    • Almond, D.1    Kimura, T.2    Kong, X.3    Swetnam, J.4    Zolla-Pazner, S.5    Cardozo, T.6
  • 61
    • 0023346161 scopus 로고
    • Free energy calculations by computer simulation
    • Bash, P. A.; Singh, U. C.; Langridge, R.; Kollman, P. A. Free energy calculations by computer simulation Science 1987, 236 (4801) 564-8 (Pubitemid 17069921)
    • (1987) Science , vol.236 , Issue.4801 , pp. 564-568
    • Bash, P.A.1    Singh, U.C.2    Langridge, R.3    Kollman, P.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.