메뉴 건너뛰기




Volumn 28, Issue , 1999, Pages 269-293

Structure and conformation of complex carbohydrates of glycoproteins, glycolipids, and bacterial polysaccharides

Author keywords

Molecular modeling; NMR; Oligosaccharide; X ray crystallography

Indexed keywords

BACTERIAL POLYSACCHARIDE; GLYCOLIPID; GLYCOPROTEIN; LECTIN; OLIGOSACCHARIDE;

EID: 0032985340     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.28.1.269     Document Type: Article
Times cited : (143)

References (150)
  • 1
    • 0000814214 scopus 로고
    • Determination of the chemical structure of complex polysaccharides by heteronuclear NMR spectroscopy
    • 1. Abeygunawardana C, Bush CA. 1993. Determination of the chemical structure of complex polysaccharides by heteronuclear NMR spectroscopy. Adv. Biophys. Chem. 3:199-249
    • (1993) Adv. Biophys. Chem. , vol.3 , pp. 199-249
    • Abeygunawardana, C.1    Bush, C.A.2
  • 2
    • 0024821263 scopus 로고
    • Molecular mechanics. The MM3 force field for hydrocarbons
    • 2. Allinger NL, Rahman M, Lii J-H. 1989. Molecular mechanics. The MM3 force field for hydrocarbons. J. Am. Chem. Soc. 111:8551-67
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8551-8567
    • Allinger, N.L.1    Rahman, M.2    Lii, J.-H.3
  • 3
    • 0000526534 scopus 로고
    • A molecular mechanics force field (MM3) for alcohol and ethers
    • 3. Allinger NL, Rahman M, Lii J-H. 1990. A molecular mechanics force field (MM3) for alcohol and ethers. J. Am. Chem. Soc. 112:8293-307
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 8293-8307
    • Allinger, N.L.1    Rahman, M.2    Lii, J.-H.3
  • 4
    • 0029243119 scopus 로고
    • Identification of protein-mediated indirect NOE effects in a disaccharide-Fab complex by transferred ROESY
    • 4. Arepalli SR, Glaudemans CPJ, Daves GD, Kovac P, Bax A. 1995. Identification of protein-mediated indirect NOE effects in a disaccharide-Fab complex by transferred ROESY. J. Magn. Reson. 106:195-98
    • (1995) J. Magn. Reson. , vol.106 , pp. 195-198
    • Arepalli, S.R.1    Glaudemans, C.P.J.2    Daves, G.D.3    Kovac, P.4    Bax, A.5
  • 5
    • 0027174064 scopus 로고
    • Structure and dynamics of sialic acid at the surface of a magnetically oriented membrane system
    • 5. Aubin Y, Prestegard JH. 1993. Structure and dynamics of sialic acid at the surface of a magnetically oriented membrane system. Biochemistry 32:3422-28
    • (1993) Biochemistry , vol.32 , pp. 3422-3428
    • Aubin, Y.1    Prestegard, J.H.2
  • 7
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • 7. Bax A, Davis DG. 1985. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 63:207-13
    • (1985) J. Magn. Reson. , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 9
    • 0030947182 scopus 로고    scopus 로고
    • Simulation of protein-sugar interactions: A computational model of the complex between ganglioside GM1 and the heat-labile enterotoxin of Escherichia coli
    • 9. Bernardi A, Raimondi L, Zuccotto F. 1997. Simulation of protein-sugar interactions: a computational model of the complex between ganglioside GM1 and the heat-labile enterotoxin of Escherichia coli. J. Med. Chem. 40:1855-62
    • (1997) J. Med. Chem. , vol.40 , pp. 1855-1862
    • Bernardi, A.1    Raimondi, L.2    Zuccotto, F.3
  • 12
    • 0032483725 scopus 로고    scopus 로고
    • On the development of a Karplus relationship for three-bond C-O-C-C spin-coupling constants in carbohydrates
    • 12. Bose B, Zhao S, Stenulz R, Cloran F, Bondo F, et al. 1998. On the development of a Karplus relationship for three-bond C-O-C-C spin-coupling constants in carbohydrates. J. Am. Chem. Soc. 120: 11158-73
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11158-11173
    • Bose, B.1    Zhao, S.2    Stenulz, R.3    Cloran, F.4    Bondo, F.5
  • 13
    • 0028676128 scopus 로고
    • Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides
    • 13. Bourne Y, Bolgiano B, Liao DL, Strecker G, Cantau P, et al. 1994. Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides. Nat. Struct. Biol. 1:863-70
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 863-870
    • Bourne, Y.1    Bolgiano, B.2    Liao, D.L.3    Strecker, G.4    Cantau, P.5
  • 14
    • 0028773158 scopus 로고
    • Structure of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: Role of the fucose moeity
    • 14. Bourne Y, Mazurier J, Legrand D, Rougé P, Montreuil J, et al. 1994. Structure of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moeity. Structure 2:209-19
    • (1994) Structure , vol.2 , pp. 209-219
    • Bourne, Y.1    Mazurier, J.2    Legrand, D.3    Rougé, P.4    Montreuil, J.5
  • 15
    • 0026500777 scopus 로고
    • X-ray structure of a biantennary octasaccharide-lectin complex at 2.3 angstroms resolution
    • 15. Bourne Y, Rougé P, Cambillau C. 1992. X-ray structure of a biantennary octasaccharide-lectin complex at 2.3 angstroms resolution. J. Biol. Chem. 267:197-203
    • (1992) J. Biol. Chem. , vol.267 , pp. 197-203
    • Bourne, Y.1    Rougé, P.2    Cambillau, C.3
  • 16
    • 0000046092 scopus 로고
    • The role of hydrogen bonding in carbohydrates: Dynamics simulations of maltose in aqueous solution
    • 16. Brady JW, Schmidt RK. 1993. The role of hydrogen bonding in carbohydrates: dynamics simulations of maltose in aqueous solution. J. Phys. Chem. 97:958-66
    • (1993) J. Phys. Chem. , vol.97 , pp. 958-966
    • Brady, J.W.1    Schmidt, R.K.2
  • 17
    • 0028824476 scopus 로고
    • The dependence of glucan conformational dynamics on linkage position and stereo-chemistry
    • 17. Brant DA, Liu HS, Zhu ZS. 1995. The dependence of glucan conformational dynamics on linkage position and stereo-chemistry. Carbohydr. Res. 278:11-26
    • (1995) Carbohydr. Res. , vol.278 , pp. 11-26
    • Brant, D.A.1    Liu, H.S.2    Zhu, Z.S.3
  • 18
    • 0024490495 scopus 로고
    • Conformational analysis of the sialyl alpha(2 → 3/6)N-acelyllactosamine structural element occurring in glycoproteins, by two-dimensional NOE 1H-NMR spectroscopy in combination with energy calculations by hard-sphere
    • 18. Breg J, Kroon-Batenburg LM, Strecker G, Montreuil J, Vliegenthart JF. 1989. Conformational analysis of the sialyl alpha(2 → 3/6)N-acelyllactosamine structural element occurring in glycoproteins, by two-dimensional NOE 1H-NMR spectroscopy in combination with energy calculations by hard-sphere. Eur. J. Biochem. 178:727-39
    • (1989) Eur. J. Biochem. , vol.178 , pp. 727-739
    • Breg, J.1    Kroon-Batenburg, L.M.2    Strecker, G.3    Montreuil, J.4    Vliegenthart, J.F.5
  • 19
    • 0021103699 scopus 로고
    • Solution conformation of alpha D (1 → 3) and alpha D (1 → 6) linked oligomannosides using proton magnetic resonance
    • 19. Brisson JR, Carver JP. 1983. Solution conformation of alpha D (1 → 3) and alpha D (1 → 6) linked oligomannosides using proton magnetic resonance. Biochemistry 22:1362-68
    • (1983) Biochemistry , vol.22 , pp. 1362-1368
    • Brisson, J.R.1    Carver, J.P.2
  • 20
    • 0030953911 scopus 로고    scopus 로고
    • NMR and molecular dynamics studies of the conformational epitope of the type III group B Streptococcus capsular polysaccharides and derivatives
    • 20. Brisson JR, Uhrinova S, Woods RJ, van der Zwan M, Jarrell HC, el al. 1997. NMR and molecular dynamics studies of the conformational epitope of the type III group B Streptococcus capsular polysaccharides and derivatives. Biochemistry 36:3278-92
    • (1997) Biochemistry , vol.36 , pp. 3278-3292
    • Brisson, J.R.1    Uhrinova, S.2    Woods, R.J.3    Van Der Zwan, M.4    Jarrell, H.C.5
  • 21
    • 0028300617 scopus 로고
    • Solution structure of a trisaccharide-antibody complex: Comparison of NMR measurements with a crystal structure
    • 21. Bundle DR, Baumann H, Brisson JR, Gagné SM, Zdanov A, et al. 1994. Solution structure of a trisaccharide-antibody complex: comparison of NMR measurements with a crystal structure. Biochemistry 33:5183-92
    • (1994) Biochemistry , vol.33 , pp. 5183-5192
    • Bundle, D.R.1    Baumann, H.2    Brisson, J.R.3    Gagné, S.M.4    Zdanov, A.5
  • 22
    • 0001435954 scopus 로고
    • Experimental determination of the three dimensional structure of oligosaccharides
    • 22. Bush CA. 1992. Experimental determination of the three dimensional structure of oligosaccharides. Curr. Opin. Struct. Biol. 2:655-60
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 655-660
    • Bush, C.A.1
  • 23
    • 0028672731 scopus 로고
    • Computer simulations of NOESY spectra of complex oligosaccharides
    • 23. Bush CA. 1994. Computer simulations of NOESY spectra of complex oligosaccharides. Methods Enzymol. 240:446-59
    • (1994) Methods Enzymol. , vol.240 , pp. 446-459
    • Bush, C.A.1
  • 24
    • 0000511751 scopus 로고
    • Three-dimensional conformations of complex carbohydrates
    • 24. Bush CA, Cagas P. 1992. Three-dimensional conformations of complex carbohydrates. Adv. Biophys. Chem. 2:149-80
    • (1992) Adv. Biophys. Chem. , vol.2 , pp. 149-180
    • Bush, C.A.1    Cagas, P.2
  • 25
    • 0025610124 scopus 로고
    • Determination of the conformation of Lewis blood group oligosaccharides by simulation of two-dimensional nuclear Overhauser data
    • 25. Cagas P, Bush CA. 1990. Determination of the conformation of Lewis blood group oligosaccharides by simulation of two-dimensional nuclear Overhauser data. Biopolymers 30:1123-38
    • (1990) Biopolymers , vol.30 , pp. 1123-1138
    • Cagas, P.1    Bush, C.A.2
  • 26
    • 0001672511 scopus 로고
    • Experimental structure determination of oligosaccharides
    • 26. Carver JP. 1991. Experimental structure determination of oligosaccharides. Curr. Opin. Struct. Biol. 1:716-20
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 716-720
    • Carver, J.P.1
  • 27
    • 0029948364 scopus 로고    scopus 로고
    • Conformational analysis of blood group A trisaccharide in solution and in the binding site of Dolichos biflorus lectin using transient and transferred nuclear Overhauser enhancement (NOE) and rotating-frame NOE experiments
    • 27. Casset F, Peters T, Etzler M, Korchagina E, Nifant'ev N, et al. 1996. Conformational analysis of blood group A trisaccharide in solution and in the binding site of Dolichos biflorus lectin using transient and transferred nuclear Overhauser enhancement (NOE) and rotating-frame NOE experiments. Eur. J. Biochem. 239:710-19
    • (1996) Eur. J. Biochem. , vol.239 , pp. 710-719
    • Casset, F.1    Peters, T.2    Etzler, M.3    Korchagina, E.4    Nifant'ev, N.5
  • 28
    • 34547829658 scopus 로고    scopus 로고
    • Molecular architecture of polysaccharide helices in oriented fibers
    • 28. Chandrasekaran R. 1997. Molecular architecture of polysaccharide helices in oriented fibers. Adv. Carbohydr. Chem. Biochem. 52:311-439
    • (1997) Adv. Carbohydr. Chem. Biochem. , vol.52 , pp. 311-439
    • Chandrasekaran, R.1
  • 29
    • 0030058697 scopus 로고    scopus 로고
    • 13C spin coupling constants in carbohydrates: Effect of structure on coupling magnitude and sign
    • 13C spin coupling constants in carbohydrates: effect of structure on coupling magnitude and sign. Carbohydr. Res. 280:177-86
    • (1996) Carbohydr. Res. , vol.280 , pp. 177-186
    • Church, T.1    Carmichael, I.2    Serianni, A.S.3
  • 30
    • 0001342923 scopus 로고
    • Theory of the time dependent transferred nuclear Overhauser effect: Applications to structural analysis of ligand-protein complexes in solution
    • 30. Clore GM, Gronenborn A. 1983. Theory of the time dependent transferred nuclear Overhauser effect: applications to structural analysis of ligand-protein complexes in solution. J. Magn. Reson. 53:423-42
    • (1983) J. Magn. Reson. , vol.53 , pp. 423-442
    • Clore, G.M.1    Gronenborn, A.2
  • 31
    • 0025046144 scopus 로고
    • Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic resonance relaxation of proteins
    • 31. Clore GM, Szabo A, Bax A, Kay LE, Driscoll PC, Gronenborn AM. 1990. Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic resonance relaxation of proteins. J. Am. Chem. Soc. 112:4989-91
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Bax, A.3    Kay, L.E.4    Driscoll, P.C.5    Gronenborn, A.M.6
  • 32
    • 0028015857 scopus 로고
    • The conformation of the sialyl Lewis X ligand changes upon binding to E-selectin
    • 32. Cooke RM, Hale RS, Lister SG, Shah G, Weir MP. 1994. The conformation of the sialyl Lewis X ligand changes upon binding to E-selectin. Biochemistry 33:1059-96
    • (1994) Biochemistry , vol.33 , pp. 1059-1096
    • Cooke, R.M.1    Hale, R.S.2    Lister, S.G.3    Shah, G.4    Weir, M.P.5
  • 33
    • 0023661070 scopus 로고
    • Virtual and solution conformations of oligosaccharides
    • 33. Cumming DA, Carver JP. 1987. Virtual and solution conformations of oligosaccharides. Biochemistry 26:6664-76
    • (1987) Biochemistry , vol.26 , pp. 6664-6676
    • Cumming, D.A.1    Carver, J.P.2
  • 34
    • 0026319774 scopus 로고
    • Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment
    • 34. Cygler M, Rose DR, Bundle DR. 1991. Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment. Science 253:442-45
    • (1991) Science , vol.253 , pp. 442-445
    • Cygler, M.1    Rose, D.R.2    Bundle, D.R.3
  • 35
    • 0001221633 scopus 로고
    • Hydroxyl and amido groups as long-range sensors in conformational analysis by nuclear Overhauser enhancement: A source of experimental evidence for conformational flexibility of oligosaccharides
    • 35. Dabrowski J, Poppe L. 1989. Hydroxyl and amido groups as long-range sensors in conformational analysis by nuclear Overhauser enhancement: a source of experimental evidence for conformational flexibility of oligosaccharides. J. Am. Chem. Soc. 111:1510-11
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 1510-1511
    • Dabrowski, J.1    Poppe, L.2
  • 37
    • 0001582736 scopus 로고
    • A novel method for determining internuclear distances and correlation times from NMR cross-relaxation rates
    • 37. Davis DG. 1987. A novel method for determining internuclear distances and correlation times from NMR cross-relaxation rates. J. Am. Chem. Soc. 109:3472-74
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 3472-3474
    • Davis, D.G.1
  • 38
    • 0000529842 scopus 로고
    • A new NMR method for measuring the rotational correlation time of molecules in the liquid state
    • 38. Desvaux H, Goldman M. 1994. A new NMR method for measuring the rotational correlation time of molecules in the liquid state. Mol. Phvs. 81:955-74
    • (1994) Mol. Phys. , vol.81 , pp. 955-974
    • Desvaux, H.1    Goldman, M.2
  • 40
    • 0031569879 scopus 로고    scopus 로고
    • Making a fitting choice: Common aspects of sugar-binding sites in plant and animal lectins
    • 40. Drickamer K. 1997. Making a fitting choice: common aspects of sugar-binding sites in plant and animal lectins. Structure 5:465-68
    • (1997) Structure , vol.5 , pp. 465-468
    • Drickamer, K.1
  • 42
    • 0030917883 scopus 로고    scopus 로고
    • Binding of the influenza A virus to cell-surface receptors: Structures of five hemagglutinin-sialyloligosaccharide complexes determined by X-ray crystallography
    • 42. Eisen MB, Sabesan S, Skehel JJ, Wiley DC. 1997. Binding of the influenza A virus to cell-surface receptors: structures of five hemagglutinin-sialyloligosaccharide complexes determined by X-ray crystallography. Virology 232:19-31
    • (1997) Virology , vol.232 , pp. 19-31
    • Eisen, M.B.1    Sabesan, S.2    Skehel, J.J.3    Wiley, D.C.4
  • 43
    • 1842384715 scopus 로고
    • Molecular relaxation of sucrose in aqueous solution: How a nanosecond molecular dynamics simulation helps to reconcile NMR data
    • 43. Engelsen SB, du Penhoat CH, Perez S. 1995, Molecular relaxation of sucrose in aqueous solution: How a nanosecond molecular dynamics simulation helps to reconcile NMR data. J. Phys. Chem. 99:13334-51
    • (1995) J. Phys. Chem. , vol.99 , pp. 13334-13351
    • Engelsen, S.B.1    Du Penhoat, C.H.2    Perez, S.3
  • 45
    • 0029846624 scopus 로고    scopus 로고
    • Experimental evidence of conformational differences between C-glycosides and O-glycosides in solution and in the protein-bound state: The C-lactose/O-lactose case
    • 45. Espinosa JF, Canada J, Asensio JL, Martin-Pastor M, Dietrich H, et al. 1996. Experimental evidence of conformational differences between C-glycosides and O-glycosides in solution and in the protein-bound state: the C-lactose/O-lactose case. J. Am. Chem. Soc. 118:10862-71
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10862-10871
    • Espinosa, J.F.1    Canada, J.2    Asensio, J.L.3    Martin-Pastor, M.4    Dietrich, H.5
  • 46
    • 0001240739 scopus 로고
    • Cell-cell adhesion and membrane glycosylation
    • 46. Feizi T. 1991. Cell-cell adhesion and membrane glycosylation. Curr. Opin. Struct. Biol. 1:766-70
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 766-770
    • Feizi, T.1
  • 47
    • 0028165950 scopus 로고
    • 13C labeled polysaccharide from Streptococcus mitis J22
    • 13C labeled polysaccharide from Streptococcus mitis J22. Biopolymers 34:1327-38
    • (1994) Biopolymers , vol.34 , pp. 1327-1338
    • Gitti, R.1    Long, G.2    Bush, C.A.3
  • 48
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important molecules
    • 48. Goodford PJA. 1985. A computational procedure for determining energetically favorable binding sites on biologically important molecules. J. Med. Chem. 28: 849-57
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.A.1
  • 49
    • 0024288712 scopus 로고
    • A revised potential-energy surface for molecular mechanics studies of carbohydrates
    • 49. Ha SH, Giammona A, Field M, Brady JW. 1988. A revised potential-energy surface for molecular mechanics studies of carbohydrates. Carbohydr. Res. 180:207-21
    • (1988) Carbohydr. Res. , vol.180 , pp. 207-221
    • Ha, S.H.1    Giammona, A.2    Field, M.3    Brady, J.W.4
  • 50
    • 0031031483 scopus 로고    scopus 로고
    • Conformational analysis and molecular dynamics simulation of α-(1 → 2) and α-(1 → 3) linked rhamnose oligosaccharides: Reconciliation with optical rotation and NMR experiments
    • 50. Hardy B, Slavomir B, Kovac P, Widmalm G. 1997. Conformational analysis and molecular dynamics simulation of α-(1 → 2) and α-(1 → 3) linked rhamnose oligosaccharides: reconciliation with optical rotation and NMR experiments. Biopolymers 41:83-96
    • (1997) Biopolymers , vol.41 , pp. 83-96
    • Hardy, B.1    Slavomir, B.2    Kovac, P.3    Widmalm, G.4
  • 52
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • 52. Helenius A. 1994. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5:253-65
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 53
    • 0002653578 scopus 로고
    • Oligosaccharide conformations: Application of NMR and energy calculations
    • 53. Homans SW. 1990. Oligosaccharide conformations: application of NMR and energy calculations. Prog. Nucl. Magn. Reson. Spectrosc. 22:55-81
    • (1990) Prog. Nucl. Magn. Reson. Spectrosc. , vol.22 , pp. 55-81
    • Homans, S.W.1
  • 54
    • 0025050372 scopus 로고
    • A molecular mechanical force-field for the conformational analysis of oligosaccharides: Comparison of theoretical and crystal structures of Man α(1 → 3) Man β(1 → 4)GlcNAc
    • 54. Homans SW. 1990. A molecular mechanical force-field for the conformational analysis of oligosaccharides: comparison of theoretical and crystal structures of Man α(1 → 3) Man β(1 → 4)GlcNAc. Biochemistry 29:10-18
    • (1990) Biochemistry , vol.29 , pp. 10-18
    • Homans, S.W.1
  • 55
    • 0026505975 scopus 로고
    • Homonuclear three-dimensional NMR methods for the complete assignment of proton NMR spectra of oligosaccharides. Application to Ga1 β (1 → 4) Fuc α(1 → 3) GlcNAc β(1 → 3) Gal β(1 → 4)Glc
    • 55. Homans SW. 1992. Homonuclear three-dimensional NMR methods for the complete assignment of proton NMR spectra of oligosaccharides. Application to Ga1 β (1 → 4) Fuc α(1 → 3) GlcNAc β(1 → 3) Gal β(1 → 4)Glc. Glycobiology 2:153-59
    • (1992) Glycobiology , vol.2 , pp. 153-159
    • Homans, S.W.1
  • 56
    • 0027717805 scopus 로고
    • Conformation and dynamics of oligosaccharides in solution
    • 56. Homans SW. 1993. Conformation and dynamics of oligosaccharides in solution. Glycobiology 3:551-55
    • (1993) Glycobiology , vol.3 , pp. 551-555
    • Homans, S.W.1
  • 57
    • 0028877320 scopus 로고
    • Conformational analysis of heparin epoxide in aqueous solution, an NMR relaxation study
    • 57. Hricovini M, Guerrini G, Torri S, Piani S, Ungarelli F. 1995. Conformational analysis of heparin epoxide in aqueous solution, an NMR relaxation study. Carbohydr. Res. 277:11-23
    • (1995) Carbohydr. Res. , vol.277 , pp. 11-23
    • Hricovini, M.1    Guerrini, G.2    Torri, S.3    Piani, S.4    Ungarelli, F.5
  • 58
    • 0032080288 scopus 로고    scopus 로고
    • Derivation of class II force fields. VI. Carbohydrate compounds and anomeric effects
    • 58. Hwang M-J, Ni X, Waldman M, Ewig CS, Hagler AT. 1998. Derivation of class II force fields. VI. Carbohydrate compounds and anomeric effects. Biopolymers 45:435-68
    • (1998) Biopolymers , vol.45 , pp. 435-468
    • Hwang, M.-J.1    Ni, X.2    Waldman, M.3    Ewig, C.S.4    Hagler, A.T.5
  • 59
    • 0001263889 scopus 로고
    • Cross relaxation without TOCSY: Transverse rotating-frame Overhauser effect spectroscopy
    • 59. Hwang TL, Shaka AJ. 1992. Cross relaxation without TOCSY: transverse rotating-frame Overhauser effect spectroscopy. J. Am. Chem. Soc. 114:3157-59
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3157-3159
    • Hwang, T.L.1    Shaka, A.J.2
  • 60
    • 0030834858 scopus 로고    scopus 로고
    • Oligosaccharide structures: Theory versus experiment
    • 60. Imberty A. 1997. Oligosaccharide structures: theory versus experiment. Curr. Opin. Struct. Biol. 7:617-23
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 617-623
    • Imberty, A.1
  • 62
    • 0026341012 scopus 로고
    • Molecular modelling of protein-carbohydrate interactions. Docking of monosaccharides in the binding site of concanavalin A
    • 62. Imberty A, Hardman KD, Carver JP, Pérez S. 1991. Molecular modelling of protein-carbohydrate interactions. Docking of monosaccharides in the binding site of concanavalin A. Glycobiology 1:631-42
    • (1991) Glycobiology , vol.1 , pp. 631-642
    • Imberty, A.1    Hardman, K.D.2    Carver, J.P.3    Pérez, S.4
  • 63
    • 0028895099 scopus 로고
    • Stereochemistry of the N-glycosylation sites in glycoproteins
    • 63. Imberty A, Pérez S. 1995. Stereochemistry of the N-glycosylation sites in glycoproteins. Protein Eng. 8:699-709
    • (1995) Protein Eng. , vol.8 , pp. 699-709
    • Imberty, A.1    Pérez, S.2
  • 65
    • 84986439431 scopus 로고
    • Relaxed potential energy surface of N-linked oligosaccharides: The mannose-α (1 → 3)-mannose case
    • 65. Imberty A, Tran V, Pérez S. 1989. Relaxed potential energy surface of N-linked oligosaccharides: the mannose-α (1 → 3)-mannose case. J. Comput. Chem. 11:205-16
    • (1989) J. Comput. Chem. , vol.11 , pp. 205-216
    • Imberty, A.1    Tran, V.2    Pérez, S.3
  • 66
    • 0013625296 scopus 로고
    • Conformation and dynamics of surface carbohydrates in lipid membranes
    • 66. Jarrell HC, Winsborrow BG. 1994. Conformation and dynamics of surface carbohydrates in lipid membranes. Adv. Biophys. Chem. 4:149-78
    • (1994) Adv. Biophys. Chem. , vol.4 , pp. 149-178
    • Jarrell, H.C.1    Winsborrow, B.G.2
  • 69
    • 0000832142 scopus 로고
    • Biosynthetic studies using carbon-13-COSY: The Klebsiella K3 serotype polysaccharide
    • 69. Jones DNM, Sanders JKM. 1989. Biosynthetic studies using carbon-13-COSY: the Klebsiella K3 serotype polysaccharide. J. Am. Chem. Soc. 111:5132-37
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5132-5137
    • Jones, D.N.M.1    Sanders, J.K.M.2
  • 71
    • 0028047114 scopus 로고
    • Studies on the three-dimensional behaviour of the selectin ligands Lewis a and sulphated Lewis a using NMR spectroscopy and molecular dynamics simulation
    • 71. Kogelberg H, Rutherford TJ. 1994. Studies on the three-dimensional behaviour of the selectin ligands Lewis a and sulphated Lewis a using NMR spectroscopy and molecular dynamics simulation. Glycobiology 4:49-57
    • (1994) Glycobiology , vol.4 , pp. 49-57
    • Kogelberg, H.1    Rutherford, T.J.2
  • 72
    • 0003348101 scopus 로고
    • Multiple field carbon 13 NMR relaxation study of cyclodextrin
    • 72. Kowalewski J, Widmalm G. 1994. Multiple field carbon 13 NMR relaxation study of cyclodextrin. J. Phys. Chem. 98:28-34
    • (1994) J. Phys. Chem. , vol.98 , pp. 28-34
    • Kowalewski, J.1    Widmalm, G.2
  • 73
    • 0001514617 scopus 로고
    • Crosrel: Full relaxation matrix analysis for noesy and roesy NMR spectroscopy
    • 73. Leeflang BR, Kroon-Batenburg LMJ. 1992. Crosrel: full relaxation matrix analysis for noesy and roesy NMR spectroscopy. J. Biomol. NMR 2:495-518
    • (1992) J. Biomol. NMR , vol.2 , pp. 495-518
    • Leeflang, B.R.1    Kroon-Batenburg, L.M.J.2
  • 74
    • 0021103533 scopus 로고
    • The conformational analysis of oligosaccharides by proton NMR and HSEA calculation
    • 74. Lemieux R, Bock K. 1983. The conformational analysis of oligosaccharides by proton NMR and HSEA calculation. Arch. Biochem. Biophys. 221:125-34
    • (1983) Arch. Biochem. Biophys. , vol.221 , pp. 125-134
    • Lemieux, R.1    Bock, K.2
  • 75
    • 0001347671 scopus 로고
    • The conformations of oligosaccharides related to the ABH and Lewis blood group determinants
    • 75. Lemieux RU, Bock K, Delbaere TJ, Koto S, Rao VS. 1980. The conformations of oligosaccharides related to the ABH and Lewis blood group determinants. Can. J. Chem. 58:631-53
    • (1980) Can. J. Chem. , vol.58 , pp. 631-653
    • Lemieux, R.U.1    Bock, K.2    Delbaere, T.J.3    Koto, S.4    Rao, V.S.5
  • 76
    • 0002365919 scopus 로고
    • Anomeric effect: Origin and consequences
    • ed. WA Szarek, D Horton, Washington, DC: Am. Chem. Soc.
    • 76. Lemieux RU, Koto S, Voisin D. 1979. Anomeric effect: origin and consequences. In ACS Symposium Series No. 87, ed. WA Szarek, D Horton, pp. 17-29. Washington, DC: Am. Chem. Soc.
    • (1979) ACS Symposium Series , vol.87 , pp. 17-29
    • Lemieux, R.U.1    Koto, S.2    Voisin, D.3
  • 77
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macro-molecules. Theory and range of validity
    • 77. Lipari G, Szabo A. 1982, Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macro-molecules. Theory and range of validity. J. Am. Chem. Soc. 104:4546-59
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 78
    • 0032515439 scopus 로고    scopus 로고
    • Slow dynamics of the cyclic osmoregulated periplasmic glucan of Ralstonia solanacearum as revealed by heteronuclear relaxation studies
    • 78. Lippens G, Wieruszeski J-M, Horvath D, Talaga P. Bohin J-P. 1998. Slow dynamics of the cyclic osmoregulated periplasmic glucan of Ralstonia solanacearum as revealed by heteronuclear relaxation studies. J. Am. Chem. Soc. 120:170-77
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 170-177
    • Lippens, G.1    Wieruszeski, J.-M.2    Horvath, D.3    Talaga, P.4    Bohin, J.-P.5
  • 79
    • 0029785337 scopus 로고    scopus 로고
    • Correlation between the chemical shift values and precise interglycosidic distance measurements in the cyclic glucan of Burkholderia solanacearum
    • 79. Lippens G, Wieruszeski J-M, Talaga P, Bohin J-P, Desvaux HJ. 1996. Correlation between the chemical shift values and precise interglycosidic distance measurements in the cyclic glucan of Burkholderia solanacearum. J. Am. Chem. Soc. 118:7227-28
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7227-7228
    • Lippens, G.1    Wieruszeski, J.-M.2    Talaga, P.3    Bohin, J.-P.4    Desvaux, H.J.5
  • 80
    • 11544358874 scopus 로고    scopus 로고
    • Lectins: Carbohydrate-specific proteins that mediate cellular recognition
    • 80. Lis H, Sharon N. 1998. Lectins: carbohydrate-specific proteins that mediate cellular recognition. Chem. Rev. 2:637-74
    • (1998) Chem. Rev. , vol.2 , pp. 637-674
    • Lis, H.1    Sharon, N.2
  • 83
    • 0031041314 scopus 로고    scopus 로고
    • Quantitative analysis of bacterial toxin affinity and specificity for glycolipid receptors by surface plasmon resonance
    • 83. MacKenzie CR, Hirama T, Lee KK, Altman E, Young NM. 1997. Quantitative analysis of bacterial toxin affinity and specificity for glycolipid receptors by surface plasmon resonance. J. Biol Chem. 272:5533-38
    • (1997) J. Biol Chem. , vol.272 , pp. 5533-5538
    • MacKenzie, C.R.1    Hirama, T.2    Lee, K.K.3    Altman, E.4    Young, N.M.5
  • 85
    • 0028267231 scopus 로고
    • Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide
    • 85. Merritt EA, Sarfaty S, van den Akker F, L'hoir C, Martial JA. 1994. Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide. Protein Sci. 3:166-75
    • (1994) Protein Sci. , vol.3 , pp. 166-175
    • Merritt, E.A.1    Sarfaty, S.2    Van Den Akker, F.3    L'Hoir, C.4    Martial, J.A.5
  • 86
    • 0026636166 scopus 로고
    • Solution structure of the Lewis X oligosaccharide determined by NMR spectroscopy and molecular dynamics simulations
    • 86. Miller KE, Mukhopadhyay C, Cagas P, Bush CA. 1992. Solution structure of the Lewis X oligosaccharide determined by NMR spectroscopy and molecular dynamics simulations. Biochemistry 31:6703-9
    • (1992) Biochemistry , vol.31 , pp. 6703-6709
    • Miller, K.E.1    Mukhopadhyay, C.2    Cagas, P.3    Bush, C.A.4
  • 88
    • 0031934283 scopus 로고    scopus 로고
    • Concanavalin A distorts the β-GlcNAc-(1 → 2)-Man linkage of β-GlcNAc-(1 → 2)-α-Man-(1 → 3)-[β-GlcNAc-(1 → 2)-α-Man-(1 → 6)] upon binding
    • 88. Moothoo DN, Naismith JH. 1998. Concanavalin A distorts the β-GlcNAc-(1 → 2)-Man linkage of β-GlcNAc-(1 → 2)-α-Man-(1 → 3)-[β-GlcNAc-(1 → 2)-α-Man-(1 → 6)] upon binding. Glycobiology 8:173-81
    • (1998) Glycobiology , vol.8 , pp. 173-181
    • Moothoo, D.N.1    Naismith, J.H.2
  • 89
    • 0029377157 scopus 로고
    • Complete relaxation and conformational exchange matrix (CORCEMA) analysis of NOESY spectra of interacting systems; two dimensional transferred NOESY
    • 89. Moseley HNB, Curto EV, Krishna NR. 1995. Complete relaxation and conformational exchange matrix (CORCEMA) analysis of NOESY spectra of interacting systems; two dimensional transferred NOESY. J. Magn. Reson. 108:243-61
    • (1995) J. Magn. Reson. , vol.108 , pp. 243-261
    • Moseley, H.N.B.1    Curto, E.V.2    Krishna, N.R.3
  • 90
    • 0024301063 scopus 로고
    • Long-range carbon-proton coupling constants: Application to conformational studies of oligosaccharides
    • 90. Mulloy B, Frenkiel TA, Davies DB. 1988. Long-range carbon-proton coupling constants: application to conformational studies of oligosaccharides. Carbohydr. Res. 184:39-46
    • (1988) Carbohydr. Res. , vol.184 , pp. 39-46
    • Mulloy, B.1    Frenkiel, T.A.2    Davies, D.B.3
  • 91
    • 0031315329 scopus 로고    scopus 로고
    • The application of simulated annealing to the conformational analysis of disaccharides
    • 91. Naidoo KJ, Brady JW. 1997. The application of simulated annealing to the conformational analysis of disaccharides. Chem. Phys. 224:263-73
    • (1997) Chem. Phys. , vol.224 , pp. 263-273
    • Naidoo, K.J.1    Brady, J.W.2
  • 93
    • 0031050984 scopus 로고    scopus 로고
    • Structure of a selectin-like mutant of mannose-binding protein complexed with sialylated and sulfated Lewis X oligosaccharides
    • 93. Ng KK, Weis WI. 1997. Structure of a selectin-like mutant of mannose-binding protein complexed with sialylated and sulfated Lewis X oligosaccharides. Biochemistry 36:979-88
    • (1997) Biochemistry , vol.36 , pp. 979-988
    • Ng, K.K.1    Weis, W.I.2
  • 94
    • 0028728698 scopus 로고
    • Recent developments in transferred NOE methods
    • 94. Ni E. 1994. Recent developments in transferred NOE methods. Prog. Nucl. Magn. Reson. Spectrosc. 26:517-606
    • (1994) Prog. Nucl. Magn. Reson. Spectrosc. , vol.26 , pp. 517-606
    • Ni, E.1
  • 95
    • 0030113327 scopus 로고    scopus 로고
    • Two distinct binding sites for globotriaosyl cermide on verotoxins: Identification by molecular modelling and confirmation using deoxy analog and a new glycolipid acceptor for all verotoxins
    • 95. Nyholm PG, Magnusson G, Zheng Z, Norel R, Binnington-Boyd B, et al. 1996. Two distinct binding sites for globotriaosyl cermide on verotoxins: identification by molecular modelling and confirmation using deoxy analog and a new glycolipid acceptor for all verotoxins. Chem. Biol. 3:263-75
    • (1996) Chem. Biol. , vol.3 , pp. 263-275
    • Nyholm, P.G.1    Magnusson, G.2    Zheng, Z.3    Norel, R.4    Binnington-Boyd, B.5
  • 96
    • 0030720932 scopus 로고    scopus 로고
    • X-ray crystallographic studies of unique cross-linked lattices between four isomeric biantennary oligosaccharides and soybean agglutinin
    • 96. Olsen LR, Dessen A, Gupta D, Sabesan S, Sacchettini JC, Brewer CF. 1997. X-ray crystallographic studies of unique cross-linked lattices between four isomeric biantennary oligosaccharides and soybean agglutinin. Biochemistry 36:15073-80
    • (1997) Biochemistry , vol.36 , pp. 15073-15080
    • Olsen, L.R.1    Dessen, A.2    Gupta, D.3    Sabesan, S.4    Sacchettini, J.C.5    Brewer, C.F.6
  • 97
    • 0025905006 scopus 로고
    • Molecular modeling of antibody-antigen complexes between the Brucella abortus O-chain polysaccharide and a specific monoclonal antibody
    • 97. Oomen RP, Young NM, Bundle DR. 1991. Molecular modeling of antibody-antigen complexes between the Brucella abortus O-chain polysaccharide and a specific monoclonal antibody. Protein Eng. 4:427-33
    • (1991) Protein Eng. , vol.4 , pp. 427-433
    • Oomen, R.P.1    Young, N.M.2    Bundle, D.R.3
  • 98
    • 0000438266 scopus 로고    scopus 로고
    • Parametrization of GROMOS force field for oligosaccharide and assessment of efficiency of molecular dynamics simulations
    • 98. Ott KH, Meyer B. 1996. Parametrization of GROMOS force field for oligosaccharide and assessment of efficiency of molecular dynamics simulations. J. Comput. Chem. 17:1068-84
    • (1996) J. Comput. Chem. , vol.17 , pp. 1068-1084
    • Ott, K.H.1    Meyer, B.2
  • 99
    • 0030040540 scopus 로고    scopus 로고
    • Molecular dynamics simulations of maltose in water
    • 99. Ott KH, Meyer B. 1996. Molecular dynamics simulations of maltose in water. Carbohydr. Res. 281:11-34
    • (1996) Carbohydr. Res. , vol.281 , pp. 11-34
    • Ott, K.H.1    Meyer, B.2
  • 100
    • 0024651564 scopus 로고
    • Electron crystallography of linear polysaccharides
    • 100. Pérez S, Chanzy H. 1989. Electron crystallography of linear polysaccharides. J. Electron Microsc. Tech. 11:280-85
    • (1989) J. Electron Microsc. Tech. , vol.11 , pp. 280-285
    • Pérez, S.1    Chanzy, H.2
  • 101
    • 0003014623 scopus 로고
    • Practical tools for accurate modeling of complex carbohydrates and their interactions with proteins
    • ed. A Pullman, J Jortner, B Pullman, Dordrecht, Netherlands: Kluwer
    • 101. Pérez S, Meyer C, Imberty A. 1995. Practical tools for accurate modeling of complex carbohydrates and their interactions with proteins. In Modelling of Biomolecular Structures and Mechanisms, ed. A Pullman, J Jortner, B Pullman, pp. 425-54. Dordrecht, Netherlands: Kluwer
    • (1995) Modelling of Biomolecular Structures and Mechanisms , pp. 425-454
    • Pérez, S.1    Meyer, C.2    Imberty, A.3
  • 104
    • 0001248255 scopus 로고    scopus 로고
    • Structure and dynamics of oligosaccharides: NMR and modeling studies
    • 104. Peters T, Pinto BM. 1996. Structure and dynamics of oligosaccharides: NMR and modeling studies. Curr. Opin. Struct. Biol. 6:710-20
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 710-720
    • Peters, T.1    Pinto, B.M.2
  • 106
    • 0000106306 scopus 로고
    • Nuclear magnetic resonance of hydroxyl and amido protons of oligosaccharides in aqueous solution. Evidence for a strong intramolecular hydrogen bond in sialic acid residues
    • 106. Poppe L, van Halbeek H. 1991. Nuclear magnetic resonance of hydroxyl and amido protons of oligosaccharides in aqueous solution. Evidence for a strong intramolecular hydrogen bond in sialic acid residues. J. Am. Chem. Soc. 113:363-65
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 363-365
    • Poppe, L.1    Van Halbeek, H.2
  • 107
    • 0000553524 scopus 로고
    • 1H-Detected measurements of long-range heteronuclear coupling constants. Application to a trisaccharide
    • 1H-Detected measurements of long-range heteronuclear coupling constants. Application to a trisaccharide. J. Magn. Reson. 92:636-41
    • (1991) J. Magn. Reson. , vol.92 , pp. 636-641
    • Poppe, L.1    Van Halbeek, H.2
  • 108
    • 0001633386 scopus 로고
    • Selective, inverse-detected measurements of long-range C-H coupling constants. Application to a disaccharide
    • 108. Poppe L. van Halbeek H. 1991. Selective, inverse-detected measurements of long-range C-H coupling constants. Application to a disaccharide. J. Magn. Reson. 93:214-17
    • (1991) J. Magn. Reson. , vol.93 , pp. 214-217
    • Poppe, L.1    Van Halbeek, H.2
  • 109
    • 37149031332 scopus 로고
    • The rigid-ity of sucrose. Just an illusion?
    • 109. Poppe L, van Halbeek H. 1992. The rigid-ity of sucrose. Just an illusion? J. Am. Chem. Soc. 114:1092-94
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 1092-1094
    • Poppe, L.1    Van Halbeek, H.2
  • 110
    • 0028421133 scopus 로고
    • NMR spectroscopy of hydroxyl protons in supercooled carbohydrates
    • 110. Poppe L, van Halbeek H. 1994. NMR spectroscopy of hydroxyl protons in supercooled carbohydrates. Nat. Struct. Biol. 1:215-16
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 215-216
    • Poppe, L.1    Van Halbeek, H.2
  • 111
    • 0030732929 scopus 로고    scopus 로고
    • Applications of nuclear magnetic resonance spectroscopy and molecular modeling to the study of protein-carbohydrate interactions
    • 111. Poveda A, Asensio JL, Espinosa JF, Martín-Pastor M, Canada J, et al. 1997. Applications of nuclear magnetic resonance spectroscopy and molecular modeling to the study of protein-carbohydrate interactions. J. Mol. Graph. Model. 15:9-17
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 9-17
    • Poveda, A.1    Asensio, J.L.2    Espinosa, J.F.3    Martín-Pastor, M.4    Canada, J.5
  • 114
    • 0031937458 scopus 로고    scopus 로고
    • Solution conformation and dynamics of a fungal cell-wall polysaccharide isolated from Microsporum gypseum
    • 114. Poveda A, Martín-Pastor M, Bernabé M, Leal JA, Jiménez-Barbero J. 1998. Solution conformation and dynamics of a fungal cell-wall polysaccharide isolated from Microsporum gypseum. Glycoconjug. J. 15:309-21
    • (1998) Glycoconjug. J. , vol.15 , pp. 309-321
    • Poveda, A.1    Martín-Pastor, M.2    Bernabé, M.3    Leal, J.A.4    Jiménez-Barbero, J.5
  • 115
    • 0030921687 scopus 로고    scopus 로고
    • Release of tumor necrosis factor alpha in response to Vibrio vulnificus capsular polysaccharide in in vivo and in vitro models
    • 115. Powell JL, Wright AC, Wasserman SS, Hone DM, Morris JG. 1997. Release of tumor necrosis factor alpha in response to Vibrio vulnificus capsular polysaccharide in in vivo and in vitro models. Infect. Immun. 65:3713-18
    • (1997) Infect. Immun. , vol.65 , pp. 3713-3718
    • Powell, J.L.1    Wright, A.C.2    Wasserman, S.S.3    Hone, D.M.4    Morris, J.G.5
  • 116
    • 0022349437 scopus 로고
    • Conformations of blood group H active oligosaccharides of ovarian cyst mucins
    • 116. Rao BNN, Dua VK, Bush CA. 1985. Conformations of blood group H active oligosaccharides of ovarian cyst mucins. Biopolymers 24:2207-29
    • (1985) Biopolymers , vol.24 , pp. 2207-2229
    • Rao, B.N.N.1    Dua, V.K.2    Bush, C.A.3
  • 118
    • 0025887737 scopus 로고
    • Interterminal distance and flexibility of a triamennary glycopeptide as measured by resonance energy transfer
    • 118. Rice KG, Wu P, Brand L, Lee YC. 1991. Interterminal distance and flexibility of a triamennary glycopeptide as measured by resonance energy transfer. Biochemistry 30:6646-55
    • (1991) Biochemistry , vol.30 , pp. 6646-6655
    • Rice, K.G.1    Wu, P.2    Brand, L.3    Lee, Y.C.4
  • 119
    • 0027431192 scopus 로고
    • Experimental determination of oligosaccharide three-dimensional structure
    • 119. Rice KG, Wu P, Brand L, Lee YC. 1993. Experimental determination of oligosaccharide three-dimensional structure. Curr. Opin. Struct. Biol. 3:669-74
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 669-674
    • Rice, K.G.1    Wu, P.2    Brand, L.3    Lee, Y.C.4
  • 121
    • 33751384922 scopus 로고
    • Characterization of the extent of internal motions in oligosaccharides
    • 121. Rutherford TJ, Partridge J, Weller CT, Romans SW. 1993. Characterization of the extent of internal motions in oligosaccharides. Biochemistry 32:12715-24
    • (1993) Biochemistry , vol.32 , pp. 12715-12724
    • Rutherford, T.J.1    Partridge, J.2    Weller, C.T.3    Romans, S.W.4
  • 122
    • 0000265205 scopus 로고
    • Orientation and dynamics of beta dodecyl glucopyranoside in phospholipid bilayers by oriented sample NMR and order matrix analysis
    • 122. Sanders CR, Prestegard JH. 1991. Orientation and dynamics of beta dodecyl glucopyranoside in phospholipid bilayers by oriented sample NMR and order matrix analysis. J. Am. Chem. Soc. 113:1987-96
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 1987-1996
    • Sanders, C.R.1    Prestegard, J.H.2
  • 123
    • 0001149145 scopus 로고    scopus 로고
    • NMR spectroscopy of hydroxy protons of 3,4-disubstituted methyl alpha-D-galactopyranosides in aqueous solution
    • 123. Sandstrom C, Baumann H, Kenne L. 1998. NMR spectroscopy of hydroxy protons of 3,4-disubstituted methyl alpha-D-galactopyranosides in aqueous solution. J. Chem. Soc. Perkin Trans. 2:809-16
    • (1998) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 809-816
    • Sandstrom, C.1    Baumann, H.2    Kenne, L.3
  • 124
    • 0026799307 scopus 로고
    • Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: Analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography
    • 124. Sauter NK, Hanson JE, Glick GD, Brown JH, Crowther RL, et al. 1992. Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography. Biochemistry 31:9609-21
    • (1992) Biochemistry , vol.31 , pp. 9609-9621
    • Sauter, N.K.1    Hanson, J.E.2    Glick, G.D.3    Brown, J.H.4    Crowther, R.L.5
  • 127
    • 0013607543 scopus 로고
    • Theoretical studies on the modes of binding of some of the derivatives of D-mannose to concanavalin A
    • 127. Sekharudu YC, Rao VSR. 1984. Theoretical studies on the modes of binding of some of the derivatives of D-mannose to concanavalin A. Int. J. Biol. Macromol. 6:337-45
    • (1984) Int. J. Biol. Macromol. , vol.6 , pp. 337-345
    • Sekharudu, Y.C.1    Rao, V.S.R.2
  • 128
    • 0001146841 scopus 로고    scopus 로고
    • A quantum mechanically derived all-atom force field for pyranose oligosaccharides. AMBER * parameters and free energy simulations
    • 128. Senderowitz H, Still WC. 1997. A quantum mechanically derived all-atom force field for pyranose oligosaccharides. AMBER * parameters and free energy simulations. J. Org. Chem. 62:1427-38
    • (1997) J. Org. Chem. , vol.62 , pp. 1427-1438
    • Senderowitz, H.1    Still, W.C.2
  • 129
    • 0024414280 scopus 로고
    • Lectins as cell recognition molecules
    • 129. Sharon N, Lis H. 1989. Lectins as cell recognition molecules. Science 246:227-34
    • (1989) Science , vol.246 , pp. 227-234
    • Sharon, N.1    Lis, H.2
  • 130
    • 0030839256 scopus 로고    scopus 로고
    • High-resolution structure of a polyomavirus VPI-oligosaccharide complex: Implications for assembly and receptor binding
    • 130. Stehle T, Harrison SC. 1997. High-resolution structure of a polyomavirus VPI-oligosaccharide complex: implications for assembly and receptor binding. EMBO J. 16:5139-48
    • (1997) EMBO J. , vol.16 , pp. 5139-5148
    • Stehle, T.1    Harrison, S.C.2
  • 131
    • 0003004715 scopus 로고
    • Further justification for the exo-anomeric effect. Conformational analysis based on nuclear magnetic resonance spectroscopy of oligosaccharides
    • 131. Thogersen T, Lemieux RU, Bock K, Meyer B. 1982. Further justification for the exo-anomeric effect. Conformational analysis based on nuclear magnetic resonance spectroscopy of oligosaccharides. Can. J. Chem. 60:44-57
    • (1982) Can. J. Chem. , vol.60 , pp. 44-57
    • Thogersen, T.1    Lemieux, R.U.2    Bock, K.3    Meyer, B.4
  • 132
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • 132. Tjandra N, Bax A. 1997. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278:1111-14
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 133
    • 0031044297 scopus 로고    scopus 로고
    • Selectin-ligand interactions revealed by molecular dynamics simulation in solution
    • 133. Tsujishita H, Hiramatsu Y, Kondo N, Ohmoto H, Kondo H, et al. 1997. Selectin-ligand interactions revealed by molecular dynamics simulation in solution. J. Med. Chem. 40:362-69
    • (1997) J. Med. Chem. , vol.40 , pp. 362-369
    • Tsujishita, H.1    Hiramatsu, Y.2    Kondo, N.3    Ohmoto, H.4    Kondo, H.5
  • 134
    • 0000816491 scopus 로고
    • An attempt to derive a new Karplus-type equation of vicinal proton-carbon coupling constants for C-O-C-H segments of bonded atoms
    • 134. Tvaroska l, Hricovini H, Perakova E. 1989. An attempt to derive a new Karplus-type equation of vicinal proton-carbon coupling constants for C-O-C-H segments of bonded atoms. Carbohydr. Res. 189:359-62
    • (1989) Carbohydr. Res. , vol.189 , pp. 359-362
    • Tvaroska, L.1    Hricovini, H.2    Perakova, E.3
  • 135
  • 136
    • 0028077878 scopus 로고
    • NMR developments in structural studies of carbohydrates and their complexes
    • 136. van Halbeek H. 1994. NMR developments in structural studies of carbohydrates and their complexes. Curr. Opin. Struct. Biol. 4:697-709
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 697-709
    • Van Halbeek, H.1
  • 137
    • 0026842845 scopus 로고
    • Selectins and other mammalian sialic acid binding lectins
    • 137. Varki A. 1992. Selectins and other mammalian sialic acid binding lectins. Curr. Opin. Cell Biol. 4:257-66
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 257-266
    • Varki, A.1
  • 138
    • 0001844723 scopus 로고
    • The crystal and molecular structure of O-α-D-mannopyranosyl-(1 → 3)-O-β-D-mannopyranosyl-(1 → 4)-2-acetamido-2-deoxy-α-D-glucopyranose
    • 138. Warin V, Baert F, Fouret R, Strecker G, Spik G, et al. 1979, The crystal and molecular structure of O-α-D-mannopyranosyl-(1 → 3)-O-β-D-mannopyranosyl-(1 → 4)-2-acetamido-2-deoxy-α-D-glucopyranose. Carbohydr. Res. 76:11-22
    • (1979) Carbohydr. Res. , vol.76 , pp. 11-22
    • Warin, V.1    Baert, F.2    Fouret, R.3    Strecker, G.4    Spik, G.5
  • 139
    • 0028788385 scopus 로고
    • Transferred nuclear Overhauser enhancement experiments show that the monoclonal antibody strep 9 selects a local minimum conformation of Streptococcus group A trisaccharide-hapten
    • 139. Weimar T, Harris DL, Pitner JB, Bock K, Pinto BM. 1995. Transferred nuclear Overhauser enhancement experiments show that the monoclonal antibody strep 9 selects a local minimum conformation of Streptococcus group A trisaccharide-hapten. Biochemistry 34:13672-80
    • (1995) Biochemistry , vol.34 , pp. 13672-13680
    • Weimar, T.1    Harris, D.L.2    Pitner, J.B.3    Bock, K.4    Pinto, B.M.5
  • 140
    • 0031935175 scopus 로고    scopus 로고
    • Computational carbohydrate chemistry: What theoretical methods can tell us
    • 140. Woods RJ. 1998. Computational carbohydrate chemistry: what theoretical methods can tell us. Glycoconjug. J. 15:209-16
    • (1998) Glycoconjug. J. , vol.15 , pp. 209-216
    • Woods, R.J.1
  • 141
    • 33751155339 scopus 로고
    • Molecular mechanical and molecular dynamical simulations of glycoproteins and oligosaccharides. 1. GLYCAM-93 parameter development
    • 141. Woods RJ, Dwek RA, Edge CJ. 1995. Molecular mechanical and molecular dynamical simulations of glycoproteins and oligosaccharides. 1. GLYCAM-93 parameter development. J. Am. Chem. Soc. 99:3832-46
    • (1995) J. Am. Chem. Soc. , vol.99 , pp. 3832-3846
    • Woods, R.J.1    Dwek, R.A.2    Edge, C.J.3
  • 142
    • 0029658497 scopus 로고    scopus 로고
    • The 2.0 Å structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: Evidence for two unique binding modes
    • 142. Wright CS, Hester G. 1996. The 2.0 Å structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: evidence for two unique binding modes. Structure 4:1339-52
    • (1996) Structure , vol.4 , pp. 1339-1352
    • Wright, C.S.1    Hester, G.2
  • 143
    • 0030446159 scopus 로고    scopus 로고
    • Molecular modeling of the flexible cell wall polysaccharide of Streptococcus mitis J22 on the basis of heteronuclear coupling constants
    • 143. Xu Q, Bush CA. 1996. Molecular modeling of the flexible cell wall polysaccharide of Streptococcus mitis J22 on the basis of heteronuclear coupling constants. Biochemistry 35:14521-29
    • (1996) Biochemistry , vol.35 , pp. 14521-14529
    • Xu, Q.1    Bush, C.A.2
  • 144
  • 145
    • 0031800410 scopus 로고    scopus 로고
    • Measurements of long range carbon-carbon coupling constants in a uniformly enriched complex polysaccharide
    • 145. Xu Q, Bush CA. 1998. Measurements of long range carbon-carbon coupling constants in a uniformly enriched complex polysaccharide. Carbohydr. Res. 306:335-39
    • (1998) Carbohydr. Res. , vol.306 , pp. 335-339
    • Xu, Q.1    Bush, C.A.2
  • 146
    • 0029973461 scopus 로고    scopus 로고
    • Comparison of NMR and molecular modeling results for a rigid and a flexible oligosaccharide
    • 146. Xu Q, Gitti R, Bush CA. 1996. Comparison of NMR and molecular modeling results for a rigid and a flexible oligosaccharide. Glycobiology 6:281-88
    • (1996) Glycobiology , vol.6 , pp. 281-288
    • Xu, Q.1    Gitti, R.2    Bush, C.A.3
  • 147
    • 0030044341 scopus 로고    scopus 로고
    • 1H long range coupling constants combined with molecular modeling
    • 1H long range coupling constants combined with molecular modeling. Biopolymers 38:339-53
    • (1996) Biopolymers , vol.38 , pp. 339-353
    • Xu, Q.1    Mohan, S.2    Bush, C.A.3
  • 148
    • 17744417978 scopus 로고    scopus 로고
    • The three-dimensional structures of a polysaccharide binding antibody to Cryptococcus neofarmans and its complex with a peptide from a phage display library: Implications for the identification of peptide mimotopes
    • 148. Young ACM, Valadon P, Casadevall A, Scharff MD, Sacchettini JC. 1997. The three-dimensional structures of a polysaccharide binding antibody to Cryptococcus neofarmans and its complex with a peptide from a phage display library: implications for the identification of peptide mimotopes. J. Mol. Biol. 274:622-34
    • (1997) J. Mol. Biol. , vol.274 , pp. 622-634
    • Young, A.C.M.1    Valadon, P.2    Casadevall, A.3    Scharff, M.D.4    Sacchettini, J.C.5
  • 149
    • 0028231880 scopus 로고
    • Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7 Å resolution
    • 149. Zdanov A, Li Y, Bundle DR, Deng SJ, MacKenzie CR, et al. 1994. Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7 Å resolution. Proc. Natl. Acad. Sci. USA 91:6423-27
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6423-6427
    • Zdanov, A.1    Li, Y.2    Bundle, D.R.3    Deng, S.J.4    MacKenzie, C.R.5
  • 150
    • 0013574441 scopus 로고    scopus 로고
    • Least-squares method for quantitative determination of chemical exchange and cross-relaxation rate constants from a series of two-dimensional exchange NMR spectra
    • 150. Zolnai Z, Juranic N, Macura S. 1997. Least-squares method for quantitative determination of chemical exchange and cross-relaxation rate constants from a series of two-dimensional exchange NMR spectra. J. Phys. Chem. 101:3707-10
    • (1997) J. Phys. Chem. , vol.101 , pp. 3707-3710
    • Zolnai, Z.1    Juranic, N.2    Macura, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.