메뉴 건너뛰기




Volumn 410, Issue 5, 2011, Pages 778-797

The conformation and orientation of a 27-residue CCR5 peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide

Author keywords

chemokine; interactions; NMR; protein structure; sulfotyrosine

Indexed keywords

CD4 ANTIGEN; CHEMOKINE RECEPTOR CCR5; GLYCOPROTEIN GP 120;

EID: 79960343575     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.04.023     Document Type: Article
Times cited : (39)

References (72)
  • 1
    • 0028788472 scopus 로고
    • The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection
    • Freed E.O.; and Martin M.A. The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection J. Biol. Chem. 270 1995 23883 23886
    • (1995) J. Biol. Chem. , vol.270 , pp. 23883-23886
    • Freed, E.O.1    Martin, M.A.2
  • 4
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng Y.; Broder C.C.; Kennedy P.E.; and Berger E.A. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor Science 272 1996 872 877 (Pubitemid 26154590)
    • (1996) Science , vol.272 , Issue.5263 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 5
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • DOI 10.1016/S0092-8674(00)81430-0
    • Chan D.C.; and Kim P.S. HIV entry and its inhibition Cell 93 1998 681 684 (Pubitemid 28257575)
    • (1998) Cell , vol.93 , Issue.5 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 6
    • 0032546952 scopus 로고    scopus 로고
    • A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding
    • DOI 10.1126/science.280.5371.1949
    • Rizzuto C.D.; Wyatt R.; Hernandez-Ramos N.; Sun Y.; Kwong P.D.; Hendrickson W.A.; and Sodroski J. A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding Science 280 1998 1949 1953 (Pubitemid 28299405)
    • (1998) Science , vol.280 , Issue.5371 , pp. 1949-1953
    • Rizzuto, C.D.1    Wyatt, R.2    Hernandez-Ramos, N.3    Sun, Y.4    Kwong, P.D.5    Hendrickson, W.A.6    Sodroski, J.7
  • 8
    • 53249113124 scopus 로고    scopus 로고
    • Soluble CD4 broadens neutralization of V3-directed monoclonal antibodies and guinea pig vaccine sera against HIV-1 subtype B and C reference viruses
    • Wu X.; Sambor A.; Nason M.C.; Yang Z.Y.; Wu L.; and Zolla-Pazner S. Soluble CD4 broadens neutralization of V3-directed monoclonal antibodies and guinea pig vaccine sera against HIV-1 subtype B and C reference viruses Virology 380 2008 285 295
    • (2008) Virology , vol.380 , pp. 285-295
    • Wu, X.1    Sambor, A.2    Nason, M.C.3    Yang, Z.Y.4    Wu, L.5    Zolla-Pazner, S.6
  • 9
    • 0034656348 scopus 로고    scopus 로고
    • NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding
    • DOI 10.1016/S0969-2126(00)00119-2
    • Tugarinov V.; Zvi A.; Levy R.; Hayek Y.; Matsushita S.; and Anglister J. NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding Structure 8 2000 385 395 (Pubitemid 30202899)
    • (2000) Structure , vol.8 , Issue.4 , pp. 385-395
    • Tugarinov, V.1    Zvi, A.2    Levy, R.3    Hayek, Y.4    Matsushita, S.5    Anglister, J.6
  • 10
    • 0037317611 scopus 로고    scopus 로고
    • Alternative conformations of HIV-1 V3 loops mimic β hairpins in chemokines, suggesting a mechanism for coreceptor selectivity
    • DOI 10.1016/S0969-2126(03)00011-X, PII S096921260300011X
    • Sharon M.; Kessler N.; Levy R.; Zolla-Pazner S.; Gorlach M.; and Anglister J. Alternative conformations of HIV-1 V3 loops mimic beta hairpins in chemokines, suggesting a mechanism for coreceptor selectivity Structure (London) 11 2003 225 236 (Pubitemid 36183646)
    • (2003) Structure , vol.11 , Issue.2 , pp. 225-236
    • Sharon, M.1    Kessler, N.2    Levy, R.3    Zolla-Pazner, S.4    Gorlach, M.5    Anglister, J.6
  • 11
    • 18544364608 scopus 로고    scopus 로고
    • Induced fit in HIV-neutralizing antibody complexes: Evidence for alternative conformations of the gp120 V3 loop and the molecular basis for broad neutralization
    • DOI 10.1021/bi047387t
    • Rosen O.; Chill J.; Sharon M.; Kessler N.; Mester B.; Zolla-Pazner S.; and Anglister J. Induced fit in HIV-neutralizing antibody complexes: evidence for alternative conformations of the gp120 V3 loop and the molecular basis for broad neutralization Biochemistry 44 2005 7250 7258 (Pubitemid 40656668)
    • (2005) Biochemistry , vol.44 , Issue.19 , pp. 7250-7258
    • Rosen, O.1    Chill, J.2    Sharon, M.3    Kessler, N.4    Mester, B.5    Zolla-Pazner, S.6    Anglister, J.7
  • 12
    • 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.; and 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. 76 2002 8953 8957 (Pubitemid 34864089)
    • (2002) Journal of Virology , vol.76 , Issue.17 , pp. 8953-8957
    • Cormier, E.G.1    Dragic, T.2
  • 14
    • 0037029863 scopus 로고    scopus 로고
    • HIV and chemokines: Implications for therapy and vaccine
    • DOI 10.1016/S0264-410X(02)00079-8, PII S0264410X02000798
    • Lusso P. HIV and chemokines: implications for therapy and vaccine Vaccine 20 2002 1964 1967 (Pubitemid 34450795)
    • (2002) Vaccine , vol.20 , Issue.15 , pp. 1964-1967
    • Lusso, P.1
  • 15
    • 0035173908 scopus 로고    scopus 로고
    • HIV-1 receptors and cell tropism
    • DOI 10.1093/bmb/58.1.43
    • Clapham P.R.; and McKnight A. HIV-1 receptors and cell tropism Br. Med. Bull. 58 2001 43 59 (Pubitemid 33070763)
    • (2001) British Medical Bulletin , vol.58 , pp. 43-59
    • Clapham, P.R.1    McKnight, A.2
  • 16
    • 0001633495 scopus 로고    scopus 로고
    • Genetic restriction of HIV-1 infection and progression to AIDS by a deletion allele of the CKR5 structural gene. Hemophilia Growth and Development Study, Multicenter AIDS Cohort Study, Multicenter Hemophilia Cohort Study, San Francisco City Cohort, ALIVE Study
    • Dean M.; Carrington M.; Winkler C.; Huttley G.A.; Smith M.W.; and Allikmets R. Genetic restriction of HIV-1 infection and progression to AIDS by a deletion allele of the CKR5 structural gene. Hemophilia Growth and Development Study, Multicenter AIDS Cohort Study, Multicenter Hemophilia Cohort Study, San Francisco City Cohort, ALIVE Study Science 273 1996 1856 1862
    • (1996) Science , vol.273 , pp. 1856-1862
    • Dean, M.1    Carrington, M.2    Winkler, C.3    Huttley, G.A.4    Smith, M.W.5    Allikmets, R.6
  • 18
    • 16044373004 scopus 로고    scopus 로고
    • Resistance to HIV-1 infection in caucasian individuals bearing mutant alleles of the CCR-5 chemokine receptor gene
    • Samson M.; Libert F.; Doranz B.J.; Rucker J.; Liesnard C.; and Farber C.M. Resistance to HIV-1 infection in caucasian individuals bearing mutant alleles of the CCR-5 chemokine receptor gene Nature 382 1996 722 725
    • (1996) Nature , vol.382 , pp. 722-725
    • Samson, M.1    Libert, F.2    Doranz, B.J.3    Rucker, J.4    Liesnard, C.5    Farber, C.M.6
  • 19
    • 0020596551 scopus 로고
    • Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS)
    • Barre-Sinoussi F.; Chermann J.C.; Rey F.; Nugeyre M.T.; Chamaret S.; and Gruest J. Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS) Science 220 1983 868 871 (Pubitemid 13080157)
    • (1983) Science , vol.220 , Issue.4599 , pp. 868-871
    • Barre Sinoussi, F.1    Chermann, J.C.2    Rey, F.3
  • 23
    • 0033515588 scopus 로고    scopus 로고
    • Epitope mapping of CCR5 reveals multiple conformational states and distinct but overlapping structures involved in chemokine and coreceptor function
    • Lee B.; Sharron M.; Blanpain C.; Doranz B.J.; Vakili J.; and Setoh P. Epitope mapping of CCR5 reveals multiple conformational states and distinct but overlapping structures involved in chemokine and coreceptor function J. Biol. Chem. 274 1999 9617 9626
    • (1999) J. Biol. Chem. , vol.274 , pp. 9617-9626
    • Lee, B.1    Sharron, M.2    Blanpain, C.3    Doranz, B.J.4    Vakili, J.5    Setoh, P.6
  • 26
    • 0034721834 scopus 로고    scopus 로고
    • A tyrosine-sulfated peptide based on the N terminus of CCR5 interacts with a CD4-enhanced epitope of the HIV-1 gp120 envelope glycoprotein and inhibits HIV-1 entry
    • Farzan M.; Vasilieva N.; Schnitzler C.E.; Chung S.; Robinson J.; and Gerard N.P. A tyrosine-sulfated peptide based on the N terminus of CCR5 interacts with a CD4-enhanced epitope of the HIV-1 gp120 envelope glycoprotein and inhibits HIV-1 entry J. Biol. Chem. 275 2000 33516 33521
    • (2000) J. Biol. Chem. , vol.275 , pp. 33516-33521
    • Farzan, M.1    Vasilieva, N.2    Schnitzler, C.E.3    Chung, S.4    Robinson, J.5    Gerard, N.P.6
  • 29
    • 0032102657 scopus 로고    scopus 로고
    • Structural interactions between chemokine receptors, gp120 Env and CD4
    • DOI 10.1006/smim.1998.0127
    • Choe H.; Martin K.A.; Farzan M.; Sodroski J.; Gerard N.P.; and Gerard C. Structural interactions between chemokine receptors, gp120 Env and CD4 Semin. Immunol. 10 1998 249 257 (Pubitemid 28347041)
    • (1998) Seminars in Immunology , vol.10 , Issue.3 , pp. 249-257
    • Choe, H.1    Martin, K.A.2    Farzan, M.3    Sodroski, J.4    Gerard, N.P.5    Gerard, C.6
  • 30
    • 60749126572 scopus 로고    scopus 로고
    • Binding thermodynamics of the N-terminal peptide of the CCR5 coreceptor to HIV-1 envelope glycoprotein gp120
    • Brower E.T.; Schon A.; Klein J.C.; and Freire E. Binding thermodynamics of the N-terminal peptide of the CCR5 coreceptor to HIV-1 envelope glycoprotein gp120 Biochemistry 48 2009 779 785
    • (2009) Biochemistry , vol.48 , pp. 779-785
    • Brower, E.T.1    Schon, A.2    Klein, J.C.3    Freire, E.4
  • 31
    • 85027927015 scopus 로고    scopus 로고
    • Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists
    • Wu B.; Chien E.Y.; Mol C.D.; Fenalti G.; Liu W.; and Katritch V. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists Science 330 2010 1066 1071
    • (2010) Science , vol.330 , pp. 1066-1071
    • Wu, B.1    Chien, E.Y.2    Mol, C.D.3    Fenalti, G.4    Liu, W.5    Katritch, V.6
  • 33
    • 0031900659 scopus 로고    scopus 로고
    • Alanine substitutions of polar and nonpolar residues in the amino- terminal domain of CCR5 differently impair entry of macrophage- and dualtropic isolates of human immunodeficiency virus type 1
    • Rabut G.E.; Konner J.A.; Kajumo F.; Moore J.P.; and Dragic T. Alanine substitutions of polar and nonpolar residues in the amino-terminal domain of CCR5 differently impair entry of macrophage- and dualtropic isolates of human immunodeficiency virus type 1 J. Virol. 72 1998 3464 3468 (Pubitemid 28175601)
    • (1998) Journal of Virology , vol.72 , Issue.4 , pp. 3464-3468
    • Rabut, G.E.E.1    Konner, J.A.2    Kajumo, F.3    Moore, J.P.4    Dragic, T.5
  • 36
    • 33748565349 scopus 로고    scopus 로고
    • Analytical ultracentrifugation for the study of protein association and assembly
    • DOI 10.1016/j.cbpa.2006.08.017, PII S1367593106001244, Analytical Techniques/Mechanisms
    • Howlett G.J.; Minton A.P.; and Rivas G. Analytical ultracentrifugation for the study of protein association and assembly Curr. Opin. Chem. Biol. 10 2006 430 436 (Pubitemid 44375070)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 430-436
    • Howlett, G.J.1    Minton, A.P.2    Rivas, G.3
  • 38
    • 23744510705 scopus 로고    scopus 로고
    • Highly conserved β16/β17 β-hairpin structure in human immunodeficiency virus type 1 YU2 gp120 is critical for CCR5 binding
    • DOI 10.1007/s00109-005-0673-1
    • Mechulam A.; Cerutti M.; Pugniere M.; Misse D.; Gajardo J.; and Roquet F. Highly conserved beta16/beta17 beta-hairpin structure in human immunodeficiency virus type 1 YU2 gp120 is critical for CCR5 binding J. Mol. Med. 83 2005 542 552 (Pubitemid 41126070)
    • (2005) Journal of Molecular Medicine , vol.83 , Issue.7 , pp. 542-552
    • Mechulam, A.1    Cerutti, M.2    Pugniere, M.3    Misse, D.4    Gajardo, J.5    Roquet, F.6    Robinson, J.7    Veas, F.8
  • 39
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi, R.; Billeter, M. & Wuthrich, K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics, 14, 51-55, 29-32. (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 40
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • Kabsch W.; and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 41
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • DOI 10.1002/(SICI)1521-3773(19990614)38:12<1784::AID-ANIE1784>3.0. CO;2-Q
    • Mayer M.; and Meyer B. Characterization of ligand binding by saturation transfer difference NMR spectroscopy Angew. Chem.; Int. Ed. 38 1999 1784 1788 (Pubitemid 29290947)
    • (1999) Angewandte Chemie - International Edition , vol.38 , Issue.12 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 42
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • DOI 10.1021/ja0100120
    • Mayer M.; and Meyer B. Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor J. Am. Chem. Soc. 123 2001 6108 6117 (Pubitemid 32888480)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.25 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 43
    • 23844472634 scopus 로고    scopus 로고
    • 1ρ relaxation in unlabeled proteins: Mobility changes in α-bungarotoxin upon binding of an acetylcholine receptor peptide
    • DOI 10.1021/bi050645h
    • Samson A.O.; Chill J.H.; and Anglister J. Two-dimensional measurement of proton T1rho relaxation in unlabeled proteins: mobility changes in alpha-bungarotoxin upon binding of an acetylcholine receptor peptide Biochemistry 44 2005 10926 10934 (Pubitemid 41153653)
    • (2005) Biochemistry , vol.44 , Issue.32 , pp. 10926-10934
    • Samson, A.O.1    Chill, J.H.2    Anglister, J.3
  • 45
    • 0028912992 scopus 로고
    • NMR mapping of the antigenic determinant recognized by an anti-gp120, human immunodeficiency virus neutralizing antibody
    • Zvi A.; Kustanovich I.; Feigelson D.; Levy R.; Eisenstein M.; and Matsushita S. NMR mapping of the antigenic determinant recognized by an anti-gp120, human immunodeficiency virus neutralizing antibody Eur. J. Biochem. 229 1995 178 187
    • (1995) Eur. J. Biochem. , vol.229 , pp. 178-187
    • Zvi, A.1    Kustanovich, I.2    Feigelson, D.3    Levy, R.4    Eisenstein, M.5    Matsushita, S.6
  • 46
    • 77955391393 scopus 로고    scopus 로고
    • The HADDOCK web server for data-driven biomolecular docking
    • de Vries S.J.; van Dijk M.; and Bonvin A.M. The HADDOCK web server for data-driven biomolecular docking Nat. Protoc. 5 2010 883 897
    • (2010) Nat. Protoc. , vol.5 , pp. 883-897
    • De Vries, S.J.1    Van Dijk, M.2    Bonvin, A.M.3
  • 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
    • DOI 10.1128/JVI.75.12.5541-5549.2001
    • Cormier E.G.; Tran D.N.; Yukhayeva L.; Olson W.C.; and Dragic T. 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 (Pubitemid 32488147)
    • (2001) Journal of Virology , vol.75 , Issue.12 , pp. 5541-5549
    • Cormier, E.G.1    Tran, D.N.H.2    Yukhayeva, L.3    Olson, W.C.4    Dragic, T.5
  • 49
    • 55749098114 scopus 로고    scopus 로고
    • Tyrosine-sulfate isosteres of CCR5 N-terminus as tools for studying HIV-1 entry
    • Lam S.N.; Acharya P.; Wyatt R.; Kwong P.D.; and Bewley C.A. Tyrosine-sulfate isosteres of CCR5 N-terminus as tools for studying HIV-1 entry Bioorg. Med. Chem. 16 2008 10113 10120
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 10113-10120
    • Lam, S.N.1    Acharya, P.2    Wyatt, R.3    Kwong, P.D.4    Bewley, C.A.5
  • 50
    • 33845767989 scopus 로고    scopus 로고
    • Recognition of RANTES by Extracellular Parts of the CCR5 Receptor
    • DOI 10.1016/j.jmb.2006.10.040, PII S0022283606014215
    • Duma L.; Haussinger D.; Rogowski M.; Lusso P.; and Grzesiek S. Recognition of RANTES by extracellular parts of the CCR5 receptor J. Mol. Biol. 365 2007 1063 1075 (Pubitemid 46014180)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.4 , pp. 1063-1075
    • Duma, L.1    Haussinger, D.2    Rogowski, M.3    Lusso, P.4    Grzesiek, S.5
  • 51
    • 0037119426 scopus 로고    scopus 로고
    • The role of post-translational modifications of the CXCR4 amino terminus in stromal-derived factor 1α association and HIV-1 entry
    • DOI 10.1074/jbc.M203361200
    • Farzan M.; Babcock G.J.; Vasilieva N.; Wright P.L.; Kiprilov E.; Mirzabekov T.; and Choe H. The role of post-translational modifications of the CXCR4 amino terminus in stromal-derived factor 1 alpha association and HIV-1 entry J. Biol. Chem. 277 2002 29484 29489 (Pubitemid 41079234)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.33 , pp. 29484-29489
    • Farzan, M.1    Babcock, G.J.2    Vasilieva, N.3    Wright, P.L.4    Kiprilov, E.5    Mirzabekov, T.6    Choe, H.7
  • 52
    • 33745173829 scopus 로고    scopus 로고
    • Recognition of a CXCR4 Sulfotyrosine by the Chemokine Stromal Cell-derived Factor-1α (SDF-1α/CXCL12)
    • DOI 10.1016/j.jmb.2006.04.052, PII S0022283606005316
    • Veldkamp C.T.; Seibert C.; Peterson F.C.; Sakmar T.P.; and Volkman B.F. Recognition of a CXCR4 sulfotyrosine by the chemokine stromal cell-derived factor-1alpha (SDF-1alpha/CXCL12) J. Mol. Biol. 359 2006 1400 1409 (Pubitemid 43903502)
    • (2006) Journal of Molecular Biology , vol.359 , Issue.5 , pp. 1400-1409
    • Veldkamp, C.T.1    Seibert, C.2    Peterson, F.C.3    Sakmar, T.P.4    Volkman, B.F.5
  • 53
    • 0026702003 scopus 로고
    • Minimal requirements for the human immunodeficiency virus type 1 V3 domain to support the syncytium-inducing phenotype: Analysis by single amino acid substitution
    • De Jong J.J.; De Ronde A.; Keulen W.; Tersmette M.; and Goudsmit J. Minimal requirements for the human immunodeficiency virus type 1 V3 domain to support the syncytium-inducing phenotype: analysis by single amino acid substitution J. Virol. 66 1992 6777 6780
    • (1992) J. Virol. , vol.66 , pp. 6777-6780
    • De Jong, J.J.1    De Ronde, A.2    Keulen, W.3    Tersmette, M.4    Goudsmit, J.5
  • 54
    • 42449125124 scopus 로고    scopus 로고
    • Correlated mutations at gp120 positions 322 and 440: Implications for gp120 structure
    • DOI 10.1002/prot.21982
    • Rosen O.; Samson A.O.; and Anglister J. Correlated mutations at gp120 positions 322 and 440: implications for gp120 structure Proteins 71 2008 1066 1070 (Pubitemid 351564034)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.3 , pp. 1066-1070
    • Rosen, O.1    Samson, A.O.2    Anglister, J.3
  • 55
    • 0027322968 scopus 로고
    • 3H)-containing peptides with 9-fluorenylmethyloxycarbonyl (Fmoc)-strategy and its application to the synthesis of cholecystokinin (CCK)-12
    • Yagami T.; Shiwa S.; Futaki S.; and Kitagawa K. Evaluation of the final deprotection system for the solid-phase synthesis of Tyr(SO3H)-containing peptides with 9-fluorenylmethyloxycarbonyl (Fmoc)-strategy and its application to the synthesis of cholecystokinin (CCK)-12 Chem. Pharm. Bull. (Tokyo) 41 1993 376 380 (Pubitemid 23128206)
    • (1993) Chemical and Pharmaceutical Bulletin , vol.41 , Issue.2 , pp. 376-380
    • Yagami, T.1    Shiwa, S.2    Futaki, S.3    Kitagawa, K.4
  • 56
    • 0041920924 scopus 로고    scopus 로고
    • Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition
    • DOI 10.1016/S0042-6822(03)00294-0
    • Koch M.; Pancera M.; Kwong P.D.; Kolchinsky P.; Grundner C.; and Wang L. Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition Virology 313 2003 387 400 (Pubitemid 37045357)
    • (2003) Virology , vol.313 , Issue.2 , pp. 387-400
    • Koch, M.1    Pancera, M.2    Kwong, P.D.3    Kolchinsky, P.4    Grundner, C.5    Wang, L.6    Hendrickson, W.A.7    Sodroski, J.8    Wyatt, R.9
  • 57
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • DOI 10.1073/pnas.212519299
    • Reeves P.J.; Callewaert N.; Contreras R.; and Khorana H.G. Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N- acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line Proc. Natl Acad. Sci. USA 99 2002 13419 13424 (Pubitemid 35215396)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.21 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 58
    • 33750002310 scopus 로고    scopus 로고
    • Exploring "one-shot" kinetics and small molecule analysis using the ProteOn XPR36 array biosensor
    • DOI 10.1016/j.ab.2006.08.005, PII S0003269706005707
    • Bravman T.; Bronner V.; Lavie K.; Notcovich A.; Papalia G.A.; and Myszka D.G. Exploring "one-shot" kinetics and small molecule analysis using the ProteOn XPR36 array biosensor Anal. Biochem. 358 2006 281 288 (Pubitemid 44573078)
    • (2006) Analytical Biochemistry , vol.358 , Issue.2 , pp. 281-288
    • Bravman, T.1    Bronner, V.2    Lavie, K.3    Notcovich, A.4    Papalia, G.A.5    Myszka, D.G.6
  • 59
    • 26644434120 scopus 로고    scopus 로고
    • The 2F5 epitope is helical in the HIV-1 entry inhibitor T-20
    • DOI 10.1021/bi0509245
    • Biron Z.; Khare S.; Quadt S.R.; Hayek Y.; Naider F.; and Anglister J. The 2F5 epitope is helical in the HIV-1 entry inhibitor T-20 Biochemistry 44 2005 13602 13611 (Pubitemid 41443688)
    • (2005) Biochemistry , vol.44 , Issue.41 , pp. 13602-13611
    • Biron, Z.1    Khare, S.2    Quadt, S.R.3    Hayek, Y.4    Naider, F.5    Anglister, J.6
  • 60
    • 0014965854 scopus 로고
    • Determination of equilibrium constants of associating protein systems. Graphical analysis for discrete and indefinite association
    • Chun P.W.; and Kim S.J. Determination of equilibrium constants of associating protein systems. Graphical analysis for discrete and indefinite association Biochemistry 9 1970 1957 1961
    • (1970) Biochemistry , vol.9 , pp. 1957-1961
    • Chun, P.W.1    Kim, S.J.2
  • 61
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M.; Saudek V.; and Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions J. Biomol. NMR 2 1992 661 665
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 63
    • 79960698472 scopus 로고
    • Water suppresion that works. Excitation sculpting using arbitrary waveforms and pulsed field gradients
    • Hwang T.L.; and Shaka A.J. Water suppresion that works. Excitation sculpting using arbitrary waveforms and pulsed field gradients J. Magn. Reson.; Ser. A 112 1995 275 279
    • (1995) J. Magn. Reson.; Ser. A , vol.112 , pp. 275-279
    • Hwang, T.L.1    Shaka, A.J.2
  • 64
    • 0027336415 scopus 로고
    • A T(1p)-filtered two-dimensional transferred NOE spectrum for studying antibody interactions with peptide antigens
    • Scherf T.; and Anglister J. A T1 rho-filtered two-dimensional transferred NOE spectrum for studying antibody interactions with peptide antigens Biophys. J. 64 1993 754 761 (Pubitemid 23130342)
    • (1993) Biophysical Journal , vol.64 , Issue.3 , pp. 754-761
    • Scherf, T.1    Anglister, J.2
  • 67
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson B.A.; and Blevins R.A. NMRView: a computer program for the visualization and analysis of NMR data J. Biomol. NMR 4 1994 603 614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 68
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson B.A. Using NMRView to visualize and analyze the NMR spectra of macromolecules Methods Mol. Biol. 278 2004 313 352
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 71
    • 0003620490 scopus 로고
    • NMR of macromolecules: A practical approach
    • D. Rickwood, B.D. Hames, Oxford University Press New York, NY
    • Roberts G.C.K. NMR of macromolecules: A practical approach D. Rickwood, B.D. Hames, The Practical Approach Series 1993 Oxford University Press New York, NY
    • (1993) The Practical Approach Series
    • Roberts, G.C.K.1
  • 72
    • 0001073978 scopus 로고
    • A resolution-sensitive procedure for comparing protein surfaces and its application to the comparison of antigen-combining sites
    • Gerstein M. A resolution-sensitive procedure for comparing protein surfaces and its application to the comparison of antigen-combining sites Acta Crystallogr.; Sect. A: Found. Crystallogr. 48 1992 271 276
    • (1992) Acta Crystallogr.; Sect. A: Found. Crystallogr. , vol.48 , pp. 271-276
    • Gerstein, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.