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Volumn 16, Issue 1, 2011, Pages 774-789

The discovery of small-molecule mimicking peptides through phage display

Author keywords

Biotin mimics; Phage display peptides; Sugar mimics

Indexed keywords

PEPTIDE;

EID: 79251501357     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules16010774     Document Type: Review
Times cited : (13)

References (62)
  • 1
    • 0025288944 scopus 로고
    • Avidin and streptavidin
    • Green, N. M. Avidin and streptavidin. Method. Enzymol. 1990, 184, 51-67.
    • (1990) Method. Enzymol. , vol.184 , pp. 51-67
    • Green, N.M.1
  • 3
    • 0025004285 scopus 로고
    • Random peptide libraries: A source of specific protein binding molecules
    • Devlin, J. J.; Panganiban, L. C.; Devlin, P. E. Random peptide libraries: A source of specific protein binding molecules. Science 1990, 249, 404-406.
    • (1990) Science , vol.249 , pp. 404-406
    • Devlin, J.J.1    Panganiban, L.C.2    Devlin, P.E.3
  • 4
    • 0026419328 scopus 로고
    • A new type of synthetic peptide library for identifying ligand-binding activity
    • Lam, K. S.; Salmon, S. E.; Hersh, E. M.; Hruby, V. J.; Kazmierski, W. M.; Knapp, R. J. A new type of synthetic peptide library for identifying ligand-binding activity. Nature 1991, 354, 82-84.
    • (1991) Nature , vol.354 , pp. 82-84
    • Lam, K.S.1    Salmon, S.E.2    Hersh, E.M.3    Hruby, V.J.4    Kazmierski, W.M.5    Knapp, R.J.6
  • 5
    • 0026807019 scopus 로고
    • Crystal structure and ligand-binding studies of a screened peptide complexed with streptavidin
    • Weber, P. C.; Pantoliano, M. W.; Thompson, L. D. Crystal structure and ligand-binding studies of a screened peptide complexed with streptavidin. Biochemistry 1992, 31, 9350-9354.
    • (1992) Biochemistry , vol.31 , pp. 9350-9354
    • Weber, P.C.1    Pantoliano, M.W.2    Thompson, L.D.3
  • 6
    • 0027287466 scopus 로고
    • An M13 phage library displaying random 38-amino-acid peptides as a source of novel sequences with affinity to selected targets
    • Kay, B. K.; Adey, N. B.; He, Y. S.; Manfredi, J. P.; Mataragnon, A. H.; Fowlkes, D. M. An M13 phage library displaying random 38-amino-acid peptides as a source of novel sequences with affinity to selected targets. Gene 1993, 128, 59-65.
    • (1993) Gene , vol.128 , pp. 59-65
    • Kay, B.K.1    Adey, N.B.2    He, Y.S.3    Manfredi, J.P.4    Mataragnon, A.H.5    Fowlkes, D.M.6
  • 7
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • Mammen, M.; Choi, S. K.; Whitesides, G. M. Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors. Angew. Chem. Int. Ed. 1998, 37, 2754-2794.
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 2754-2794
    • Mammen, M.1    Choi, S.K.2    Whitesides, G.M.3
  • 8
    • 0346981999 scopus 로고    scopus 로고
    • Influencing receptorligand binding mechanisms with multivalent ligand architecture
    • Gestwicki, J. E.; Cairo, C. W.; Strong, L. E.; Oetjen, K. A.; Kiessling, L. L. Influencing receptorligand binding mechanisms with multivalent ligand architecture. J. Am. Chem. Soc. 2002, 124, 14922-14933.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14922-14933
    • Gestwicki, J.E.1    Cairo, C.W.2    Strong, L.E.3    Oetjen, K.A.4    Kiessling, L.L.5
  • 9
    • 0027253452 scopus 로고
    • M13 bacteriophage displaying disulfide-constrained microproteins
    • McLafferty, M. A.; Kent, R. B.; Ladner, R. C.; Markland, W. M13 bacteriophage displaying disulfide-constrained microproteins. Gene 1993, 128, 29-36.
    • (1993) Gene , vol.128 , pp. 29-36
    • McLafferty, M.A.1    Kent, R.B.2    Ladner, R.C.3    Markland, W.4
  • 10
    • 0000548761 scopus 로고
    • Crystallographic and thermodynamic comparison of structurally diverse molecules binding to streptavidin
    • Weber, P. C.; Pantoliano, M. W.; Salemme, F. R. Crystallographic and thermodynamic comparison of structurally diverse molecules binding to streptavidin. Acta Crystallogr. D 1995, 51, 590-596.
    • (1995) Acta Crystallogr. D , vol.51 , pp. 590-596
    • Weber, P.C.1    Pantoliano, M.W.2    Salemme, F.R.3
  • 11
    • 0028808005 scopus 로고
    • Screening of cyclic peptide phage libraries identifies ligands that bind streptavidin with high affinities
    • Giebel, L. B.; Cass, R. T.; Milligan, D. L.; Young, D. C.; Arze, R.; Johnson, C. R. Screening of cyclic peptide phage libraries identifies ligands that bind streptavidin with high affinities. Biochemistry-US 1995, 34, 15430-15435.
    • (1995) Biochemistry-US , vol.34 , pp. 15430-15435
    • Giebel, L.B.1    Cass, R.T.2    Milligan, D.L.3    Young, D.C.4    Arze, R.5    Johnson, C.R.6
  • 12
    • 0028841829 scopus 로고
    • Binding to protein targets of peptidic leads discovered by phage display: Crystal structures of streptavidin-bound linear and cyclic peptide ligands containing the HPQ sequence
    • Katz, B. A. Binding to protein targets of peptidic leads discovered by phage display: Crystal structures of streptavidin-bound linear and cyclic peptide ligands containing the HPQ sequence. Biochemistry-US 1995, 34, 15421-15429.
    • (1995) Biochemistry-US , vol.34 , pp. 15421-15429
    • Katz, B.A.1
  • 13
    • 0029152204 scopus 로고
    • Structure-based design of high-affinity streptavidin binding cyclic peptide ligands containing thioether cross-links
    • Katz, B. A.; Johnson, C. R.; Cass, R. T. Structure-based design of high-affinity streptavidin binding cyclic peptide ligands containing thioether cross-links. J. Am. Chem. Soc. 1995, 117, 8541-8547.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8541-8547
    • Katz, B.A.1    Johnson, C.R.2    Cass, R.T.3
  • 14
    • 67650305952 scopus 로고    scopus 로고
    • Phage-encoded combinatorial chemical libraries based on bicyclic peptides
    • Heinis, C.; Rutherford, T.; Freund, S.; Winter, G. Phage-encoded combinatorial chemical libraries based on bicyclic peptides. Nat. Chem. Biol. 2009, 5, 502-507.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 502-507
    • Heinis, C.1    Rutherford, T.2    Freund, S.3    Winter, G.4
  • 15
    • 34248155381 scopus 로고    scopus 로고
    • The Trp cage motif as a scaffold for the display of a randomized peptide library on bacteriophage T7
    • Herman, R. E.; Badders, D.; Fuller, M.; Makienko, E. G.; Houston, M. E.; Quay, S. C.; Johnson, P. H. The Trp cage motif as a scaffold for the display of a randomized peptide library on bacteriophage T7. J. Biol. Chem. 2007, 282, 9813-9824.
    • (2007) J. Biol. Chem. , vol.282 , pp. 9813-9824
    • Herman, R.E.1    Badders, D.2    Fuller, M.3    Makienko, E.G.4    Houston, M.E.5    Quay, S.C.6    Johnson, P.H.7
  • 16
    • 0027280631 scopus 로고
    • Antibody as a surrogate receptor in the screening of a phage display library
    • Roberts, D.; Guegler, K.; Winter, J. Antibody as a surrogate receptor in the screening of a phage display library. Gene 1993, 128, 67-69.
    • (1993) Gene , vol.128 , pp. 67-69
    • Roberts, D.1    Guegler, K.2    Winter, J.3
  • 17
    • 0033829057 scopus 로고    scopus 로고
    • Phages from landscape libraries as substitute antibodies
    • Petrenko, V. A.; Smith, G. P. Phages from landscape libraries as substitute antibodies. Protein Eng. 2000, 13, 589-592.
    • (2000) Protein Eng. , vol.13 , pp. 589-592
    • Petrenko, V.A.1    Smith, G.P.2
  • 18
    • 33747655831 scopus 로고    scopus 로고
    • Highly selective cyclic peptide ligands for NeutrAvidin and avidin identified by phage display
    • Meyer, S. C.; Gaj, T.; Ghosh, I. Highly selective cyclic peptide ligands for NeutrAvidin and avidin identified by phage display. Chem. Biol. Drug Des. 2006, 68, 3-10.
    • (2006) Chem. Biol. Drug Des. , vol.68 , pp. 3-10
    • Meyer, S.C.1    Gaj, T.2    Ghosh, I.3
  • 19
  • 20
    • 0027499708 scopus 로고
    • The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment
    • Schmidt, T. G. M.; Skerra, A. The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment. Protein Eng. 1993, 6, 109-122.
    • (1993) Protein Eng. , vol.6 , pp. 109-122
    • Schmidt, T.G.M.1    Skerra, A.2
  • 21
    • 0035197422 scopus 로고    scopus 로고
    • A recombinant scFv/streptavidin-binding peptide fusion protein for the quantitative determination of the scorpion venom neurotoxin Aahl
    • Aubrey, N.; Devaux, C.; di Luccio, E.; Goyffon, M.; Rochat, H.; Billiald, P. A recombinant scFv/streptavidin-binding peptide fusion protein for the quantitative determination of the scorpion venom neurotoxin Aahl. Biol. Chem. 2001, 382, 1621-1628.
    • (2001) Biol. Chem. , vol.382 , pp. 1621-1628
    • Aubrey, N.1    Devaux, C.2    Di Luccio, E.3    Goyffon, M.4    Rochat, H.5    Billiald, P.6
  • 22
    • 0035543198 scopus 로고    scopus 로고
    • One-step purification of recombinant proteins using a nanomolar-affinity streptavidinbinding peptide, the SBP-Tag
    • Keefe, A. D.; Wilson, D. S.; Seelig, B.; Szostak, J. W. One-step purification of recombinant proteins using a nanomolar-affinity streptavidinbinding peptide, the SBP-Tag. Protein Express. Purif. 2001, 23, 440-446.
    • (2001) Protein Express. Purif. , vol.23 , pp. 440-446
    • Keefe, A.D.1    Wilson, D.S.2    Seelig, B.3    Szostak, J.W.4
  • 23
    • 0033621512 scopus 로고    scopus 로고
    • Applications of a peptide ligand for streptavidin: The strep-tag
    • Skerra, A.; Schmidt, T. G. M. Applications of a peptide ligand for streptavidin: The strep-tag. Biomol. Eng. 1999, 16, 79-86.
    • (1999) Biomol. Eng. , vol.16 , pp. 79-86
    • Skerra, A.1    Schmidt, T.G.M.2
  • 24
    • 0347597739 scopus 로고    scopus 로고
    • The nano-tag, a streptavidin-binding peptide for the purification and detection of recombinant proteins
    • Lamla, T.; Erdmann, V. A. The nano-tag, a streptavidin-binding peptide for the purification and detection of recombinant proteins. Protein Express. Purif. 2004, 33, 39-47.
    • (2004) Protein Express. Purif. , vol.33 , pp. 39-47
    • Lamla, T.1    Erdmann, V.A.2
  • 25
    • 0028922586 scopus 로고
    • Ligplot-A program to generate schematic diagrams of protein ligand interactions
    • Wallace, A. C.; Laskowski, R. A.; Thornton, J. M. Ligplot-A program to generate schematic diagrams of protein ligand interactions. Protein Eng. 1995, 8, 127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 26
    • 0024588901 scopus 로고
    • Structural origins of high-affinity biotin binding to streptavidin
    • Weber, P. C.; Ohlendorf, D. H.; Wendoloski, J. J.; Salemme, F. R. Structural origins of high-affinity biotin binding to streptavidin. Science 1989, 243, 85-88.
    • (1989) Science , vol.243 , pp. 85-88
    • Weber, P.C.1    Ohlendorf, D.H.2    Wendoloski, J.J.3    Salemme, F.R.4
  • 27
    • 0035937499 scopus 로고    scopus 로고
    • Chemical glycobiology
    • Bertozzi, C. R.; Kiessling, L. L. Chemical glycobiology. Science 2001, 291, 2357-2364.
    • (2001) Science , vol.291 , pp. 2357-2364
    • Bertozzi, C.R.1    Kiessling, L.L.2
  • 29
  • 30
    • 0040657616 scopus 로고
    • Advances in selective chemical syntheses of complex oligosaccharides
    • Paulsen, H. Advances in selective chemical syntheses of complex oligosaccharides. Angew. Chem. Int. Ed. 1982, 21, 155-173.
    • (1982) Angew. Chem. Int. Ed. , vol.21 , pp. 155-173
    • Paulsen, H.1
  • 31
    • 0035805264 scopus 로고    scopus 로고
    • Adventures in carbohydrate chemistry: New synthetic technologies, chemical synthesis, molecular design, and chemical biology
    • Nicolaou, K. C.; Mitchell, H. J. Adventures in carbohydrate chemistry: New synthetic technologies, chemical synthesis, molecular design, and chemical biology. Angew. Chem. Int. Ed. 2001, 40, 1577-1624.
    • (2001) Angew. Chem. Int. Ed. , vol.40 , pp. 1577-1624
    • Nicolaou, K.C.1    Mitchell, H.J.2
  • 32
    • 45349108661 scopus 로고    scopus 로고
    • Glycosylation methods in oligosaccharide synthesis. Part 1
    • Carmona, A. T.; Moreno-Vargas, A. J.; Robina, I. Glycosylation methods in oligosaccharide synthesis. Part 1. Curr. Org. Synth. 2008, 5, 33-60.
    • (2008) Curr. Org. Synth. , vol.5 , pp. 33-60
    • Carmona, A.T.1    Moreno-Vargas, A.J.2    Robina, I.3
  • 33
    • 0034498920 scopus 로고    scopus 로고
    • Solid-phase oligosaccharide synthesis and combinatorial carbohydrate libraries
    • Seeberger, P. H.; Haase, W.-C. Solid-phase oligosaccharide synthesis and combinatorial carbohydrate libraries. Chem. Rev. 2000, 100, 4349-4393.
    • (2000) Chem. Rev. , vol.100 , pp. 4349-4393
    • Seeberger, P.H.1    Haase, W.-C.2
  • 34
    • 26044440288 scopus 로고    scopus 로고
    • Automated synthesis of oligosaccharides as a basis for drug discovery
    • Seeberger, P. H.; Werz, D. B. Automated synthesis of oligosaccharides as a basis for drug discovery. Nat. Rev. Drug Discov. 2005, 4, 751-763.
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 751-763
    • Seeberger, P.H.1    Werz, D.B.2
  • 35
    • 0033549740 scopus 로고    scopus 로고
    • Carbohydrate mimetics: A new strategy for tackling the problem of carbohydrate-mediated biological recognition
    • Sears, P.; Wong, C.-H. Carbohydrate mimetics: A new strategy for tackling the problem of carbohydrate-mediated biological recognition. Angew. Chem. Int. Ed. 1999, 38, 2300-2324.
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 2300-2324
    • Sears, P.1    Wong, C.-H.2
  • 36
    • 12144277460 scopus 로고    scopus 로고
    • Septanose carbohydrates: Synthesis and conformational studies of methyl α-D-glycero-D-idoseptanoside and methyl β-D-glycero-D-guloseptanoside
    • DeMatteo, M. P.; Snyder, N. L.; Morton, M.; Baldisseri, D. M.; Hadad, C. M.; Peczuh, M. W. Septanose carbohydrates: Synthesis and conformational studies of methyl α-D-glycero-D-idoseptanoside and methyl β-D-glycero-D- guloseptanoside. J. Org. Chem. 2005, 70, 24-38.
    • (2005) J. Org. Chem. , vol.70 , pp. 24-38
    • DeMatteo, M.P.1    Snyder, N.L.2    Morton, M.3    Baldisseri, D.M.4    Hadad, C.M.5    Peczuh, M.W.6
  • 39
    • 0034717303 scopus 로고    scopus 로고
    • Structural and functional consequences of peptide-carbohydrate mimicry - Crystal structure of a carbohydrate-mimicking peptide bound to concanavalin A
    • Jain, D.; Kaur, K.; Sundaravadivel, B.; Salunke, D. M. Structural and functional consequences of peptide-carbohydrate mimicry - Crystal structure of a carbohydrate-mimicking peptide bound to concanavalin A. J. Biol. Chem. 2000, 275, 16098-16102.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16098-16102
    • Jain, D.1    Kaur, K.2    Sundaravadivel, B.3    Salunke, D.M.4
  • 40
    • 0031058735 scopus 로고    scopus 로고
    • Topological analysis of the functional mimicry between a peptide and a carbohydrate moiety
    • Kaur, K. J.; Khurana, S.; Salunke, D. M. Topological analysis of the functional mimicry between a peptide and a carbohydrate moiety. J. Biol. Chem. 1997, 272, 5539-5543.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5539-5543
    • Kaur, K.J.1    Khurana, S.2    Salunke, D.M.3
  • 41
    • 0035014622 scopus 로고    scopus 로고
    • Plasticity in protein-peptide recognition: Crystal structures of two different peptides bound to concanavalin A
    • Jain, D.; Kaur, K. J.; Salunke, D. M. Plasticity in protein-peptide recognition: Crystal structures of two different peptides bound to concanavalin A. Biophys. J. 2001, 80, 2912-2921.
    • (2001) Biophys. J. , vol.80 , pp. 2912-2921
    • Jain, D.1    Kaur, K.J.2    Salunke, D.M.3
  • 42
    • 10344248176 scopus 로고    scopus 로고
    • Plasticity within the antigencombining site may manifest as molecular mimicry in the humoral immune response
    • Goel, M.; Krishnan, L.; Kaur, S.; Kaur, K. J.; Salunke, D. M. Plasticity within the antigencombining site may manifest as molecular mimicry in the humoral immune response. J. Immunol. 2004, 173, 7358-7367.
    • (2004) J. Immunol. , vol.173 , pp. 7358-7367
    • Goel, M.1    Krishnan, L.2    Kaur, S.3    Kaur, K.J.4    Salunke, D.M.5
  • 44
    • 0026546880 scopus 로고
    • Screening for receptor ligands using large libraries of peptides linked to the C terminus of the lac repressor
    • Cull, M. G.; Miller, J. F.; Schatz, P. J. Screening for receptor ligands using large libraries of peptides linked to the C terminus of the lac repressor. Proc. Natl. Acad. Sci. USA 1992, 89, 1865-1869.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1865-1869
    • Cull, M.G.1    Miller, J.F.2    Schatz, P.J.3
  • 45
    • 0027215581 scopus 로고
    • Identification of a peptide which binds to the carbohydrate-specific monoclonal antibody B3
    • Hoess, R.; Brinkmann, U.; Handel, T.; Pastan, I. Identification of a peptide which binds to the carbohydrate-specific monoclonal antibody B3. Gene 1993, 128, 43-49.
    • (1993) Gene , vol.128 , pp. 43-49
    • Hoess, R.1    Brinkmann, U.2    Handel, T.3    Pastan, I.4
  • 46
    • 0032899929 scopus 로고    scopus 로고
    • y immune responses in rabbits and mice
    • y immune responses in rabbits and mice. J. Peptide Res. 1999, 53, 252-260.
    • (1999) J. Peptide Res. , vol.53 , pp. 252-260
    • Lou, Q.1    Pastan, I.2
  • 47
    • 0030576498 scopus 로고    scopus 로고
    • Peptide libraries define the fine specificity of anti-polysaccharide antibodies to Cryptococcus neoformans
    • Valadon, P.; Nussbaum, G.; Boyd, L. F.; Margulies, D. H.; Scharff, M. D. Peptide libraries define the fine specificity of anti-polysaccharide antibodies to Cryptococcus neoformans. J. Mol. Biol. 1996, 261, 11-22.
    • (1996) J. Mol. Biol. , vol.261 , pp. 11-22
    • Valadon, P.1    Nussbaum, G.2    Boyd, L.F.3    Margulies, D.H.4    Scharff, M.D.5
  • 48
    • 17744417978 scopus 로고    scopus 로고
    • The threedimensional structures of a polysaccharide binding antibody to Cryptococcus neoformans and its complex with a peptide from a phage display library: Implications for the identification of peptide mimotopes
    • Young, A. C. M.; Valadon, P.; Arturo Casadevall, A.; Scharff, M. D.; Sacchettini, J. C. The threedimensional structures of a polysaccharide binding antibody to Cryptococcus neoformans and its complex with a peptide from a phage display library: Implications for the identification of peptide mimotopes. J. Mol. Biol. 1997, 274, 622-634.
    • (1997) J. Mol. Biol. , vol.274 , pp. 622-634
    • Young, A.C.M.1    Valadon, P.2    Arturo Casadevall, A.3    Scharff, M.D.4    Sacchettini, J.C.5
  • 50
    • 0029920670 scopus 로고    scopus 로고
    • Probing the basis of antibody reactivity with a panel of constrained peptide libraries displayed by filamentous phage
    • Bonnycastle, L. L. C.; Mehroke, J. S.; Rashed, M.; Gong, X.; Scott, J. K. Probing the basis of antibody reactivity with a panel of constrained peptide libraries displayed by filamentous phage. J. Mol. Biol. 1996, 258, 747-762.
    • (1996) J. Mol. Biol. , vol.258 , pp. 747-762
    • Bonnycastle, L.L.C.1    Mehroke, J.S.2    Rashed, M.3    Gong, X.4    Scott, J.K.5
  • 51
    • 0031882455 scopus 로고    scopus 로고
    • Peptides that mimic the group B Streptococcal type III capsular polysaccharide antigen
    • Pincus, S. H.; Smith, M. J.; Jennings, H. J.; Burritt, J. B.; Glee, P. M. Peptides that mimic the group B Streptococcal type III capsular polysaccharide antigen. J. Immunol. 1998, 160, 293-298.
    • (1998) J. Immunol. , vol.160 , pp. 293-298
    • Pincus, S.H.1    Smith, M.J.2    Jennings, H.J.3    Burritt, J.B.4    Glee, P.M.5
  • 52
    • 0033986926 scopus 로고    scopus 로고
    • Selection of an immunogenic peptide mimic of the capsular polysaccharide of Neisseria meningitidis serogroup A using a peptide display library
    • Grothaus, M. C.; Srivastava, N.; Smithson, S. L.; Kieber-Emmons, T.; Williams, D. B.; Carlone, G. M.; Westerink, M. A. J. Selection of an immunogenic peptide mimic of the capsular polysaccharide of Neisseria meningitidis serogroup A using a peptide display library. Vaccine 2000, 18, 1253-1263.
    • (2000) Vaccine , vol.18 , pp. 1253-1263
    • Grothaus, M.C.1    Srivastava, N.2    Smithson, S.L.3    Kieber-Emmons, T.4    Williams, D.B.5    Carlone, G.M.6    Westerink, M.A.J.7
  • 55
    • 0032217063 scopus 로고    scopus 로고
    • GD1K-replica peptides functionally mimic GD1K, an adhesion molecule of metastatic tumor cells, and suppress the tumor metastasis
    • Ishikawa, D.; Kikkawa, H.; Ogino, K.; Hirabayashi, Y.; Oku, N.; Taki, T. GD1K-replica peptides functionally mimic GD1K, an adhesion molecule of metastatic tumor cells, and suppress the tumor metastasis. FEBS Lett. 1998, 441, 20-24.
    • (1998) FEBS Lett. , vol.441 , pp. 20-24
    • Ishikawa, D.1    Kikkawa, H.2    Ogino, K.3    Hirabayashi, Y.4    Oku, N.5    Taki, T.6
  • 56
    • 33646025829 scopus 로고    scopus 로고
    • Identification of peptide mimetics of xenoreactive α-Gal antigenic epitope by phage display
    • Lang, J.; Zhan, J.; Xu, L.; Yan, Z. Identification of peptide mimetics of xenoreactive α-Gal antigenic epitope by phage display. Biochem. Biophys. Res. Commun. 2006, 344, 214-220.
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 214-220
    • Lang, J.1    Zhan, J.2    Xu, L.3    Yan, Z.4
  • 57
    • 34249781722 scopus 로고    scopus 로고
    • Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-boundstructures
    • Borrok, M. J.; Kiessling, L. L.; Forest, K. T. Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-boundstructures. Protein Sci. 2007, 16, 1032-1041.
    • (2007) Protein Sci. , vol.16 , pp. 1032-1041
    • Borrok, M.J.1    Kiessling, L.L.2    Forest, K.T.3
  • 58
    • 66449102696 scopus 로고    scopus 로고
    • Phage display screening against a set of targets to establish peptide-based sugar mimetics and molecular docking to predict binding site
    • Yu, L.; Yu, P. S.; Mui, E. Y. Y.; McKelvie, J. C.; Pham, T. P. T.; Yap, Y. W.; Wong, W. Q.; Wu, J.; Deng, W.; Orner, B. P. Phage display screening against a set of targets to establish peptide-based sugar mimetics and molecular docking to predict binding site. Bioorg. Med. Chem. 2009, 17, 4825-4832.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 4825-4832
    • Yu, L.1    Yu, P.S.2    Mui, E.Y.Y.3    McKelvie, J.C.4    Pham, T.P.T.5    Yap, Y.W.6    Wong, W.Q.7    Wu, J.8    Deng, W.9    Orner, B.P.10
  • 60
    • 0028038824 scopus 로고
    • Refined structure of concanavalin A complexed with methyl α-D-mannopyranoside at 2.0 A resolution and comparison with the saccharide-free structure
    • Naismith, J. H.; Emmerich, C.; Habash, J.; Harrop, S. J.; Helliwell, J. R.; Hunter, W. N.; Raftery, J.; Kalb, A. J.; Yariv, J. Refined structure of concanavalin A complexed with methyl α-D-mannopyranoside at 2.0 A resolution and comparison with the saccharide-free structure. Acta Crystallogr. D 1994, 50, 847-858.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 847-858
    • Naismith, J.H.1    Emmerich, C.2    Habash, J.3    Harrop, S.J.4    Helliwell, J.R.5    Hunter, W.N.6    Raftery, J.7    Kalb, A.J.8    Yariv, J.9


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