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Volumn 252, Issue 3, 1998, Pages 416-427

Conformer selection and differential restriction of ligand mobility by a plant lectin - Conformational behaviour in the free state and complexed with galactoside-specific mistletoe lectin as revealed by random-walk and conformational-clustering molecular-mechanics calculations, molecular- dynamics simulations and nuclear Overhauser experiments

Author keywords

Agglutinin; Conformational analysis; Lectin; Molecular modelling; Nuclear Overhauser effect

Indexed keywords

AGGLUTININ; DISACCHARIDE; GALACTOSIDE; LECTIN;

EID: 7144254472     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2520416.x     Document Type: Article
Times cited : (47)

References (57)
  • 1
    • 0024414280 scopus 로고
    • Lectins as cell recognition molecules
    • Sharon, N. & Lis, H. (1989) Lectins as cell recognition molecules, Science 246, 227-234.
    • (1989) Science , vol.246 , pp. 227-234
    • Sharon, N.1    Lis, H.2
  • 2
    • 0029586586 scopus 로고
    • Protein-Zucker-Erkennung. Grundlagen und medizinische Anwendungen am Beispiel der Tumorlektinologie
    • Gabius, H.-J., Kayser, K. & Gabius, S. (1995) Protein-Zucker-Erkennung. Grundlagen und medizinische Anwendungen am Beispiel der Tumorlektinologie, Naturwissenschaften 82, 533-543.
    • (1995) Naturwissenschaften , vol.82 , pp. 533-543
    • Gabius, H.-J.1    Kayser, K.2    Gabius, S.3
  • 4
    • 0000815176 scopus 로고
    • Oligosaccharides: How can flexible molecules act as signals?
    • Carver, J. (1993) Oligosaccharides: how can flexible molecules act as signals? Pure & Appl. Chem. 65, 763-770.
    • (1993) Pure & Appl. Chem. , vol.65 , pp. 763-770
    • Carver, J.1
  • 5
    • 0000149999 scopus 로고
    • Molecular modeling: An essential component in the structure determination of oligosaccharides and polysaccharides
    • Peréz, S., Imberty, A. & Carver, J. (1994) Molecular modeling: an essential component in the structure determination of oligosaccharides and polysaccharides, Adv. Comput. Biol. 1, 147-202.
    • (1994) Adv. Comput. Biol. , vol.1 , pp. 147-202
    • Peréz, S.1    Imberty, A.2    Carver, J.3
  • 6
    • 0027996135 scopus 로고
    • Structure and energetics of protein-carbohydrate complexes
    • Toone, E. J. (1994) Structure and energetics of protein-carbohydrate complexes, Curr. Opin. Struct. Biol. 4, 719-728.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 719-728
    • Toone, E.J.1
  • 7
    • 77956795989 scopus 로고
    • The structural features of protein-carbohydrate interactions revealed by X-ray crystallography
    • Montreuil, J., Vliegenthart, J. F. G. & Schachter, H., eds Elsevier Science, Amsterdam
    • Cambillau, C. (1995) The structural features of protein-carbohydrate interactions revealed by X-ray crystallography, in Glycoproteins (Montreuil, J., Vliegenthart, J. F. G. & Schachter, H., eds) pp. 29-65, Elsevier Science, Amsterdam.
    • (1995) Glycoproteins , pp. 29-65
    • Cambillau, C.1
  • 8
    • 0003012148 scopus 로고    scopus 로고
    • How water provides the impetus for molecular recognition in aqueous solution
    • Lemieux, R. U. (1996) How water provides the impetus for molecular recognition in aqueous solution, Acc. Chem. Res. 29, 373-380.
    • (1996) Acc. Chem. Res. , vol.29 , pp. 373-380
    • Lemieux, R.U.1
  • 9
    • 0001787913 scopus 로고    scopus 로고
    • Antibody-oligosaccharide interactions determined by crystallography
    • Gabius, H.-J. & Gabius, S., eds Chapman & Hall, London, Weinheim
    • Bundle, D. R. (1997) Antibody-oligosaccharide interactions determined by crystallography, in Glycosciences: Status and perspectives (Gabius, H.-J. & Gabius, S., eds) pp. 311-331, Chapman & Hall, London, Weinheim.
    • (1997) Glycosciences: Status and Perspectives , pp. 311-331
    • Bundle, D.R.1
  • 13
    • 85007661623 scopus 로고
    • Lectinology meets mythology: Oncological future for the mistletoe lectin?
    • Gabius, H.-J. (1994) Lectinology meets mythology: oncological future for the mistletoe lectin? Trends Glycosci. Glycotechnol. 6, 229-238.
    • (1994) Trends Glycosci. Glycotechnol. , vol.6 , pp. 229-238
    • Gabius, H.-J.1
  • 14
    • 0026731763 scopus 로고
    • The immunomodulatory β-galactoside-specific Jectin from mistletoe: Partial sequence analysis, cell and tissue binding, and impact on intracellular biosignalling of monocytic leukemia cells
    • Gabius, H.-J., Walzel, H., Joshi, S. S., Kruip, J., Kojima, S., Gerke, V., Kratzin, H. & Gabius, S. (1992) The immunomodulatory β-galactoside-specific Jectin from mistletoe: partial sequence analysis, cell and tissue binding, and impact on intracellular biosignalling of monocytic leukemia cells, Anticancer Res. 12, 669-676.
    • (1992) Anticancer Res. , vol.12 , pp. 669-676
    • Gabius, H.-J.1    Walzel, H.2    Joshi, S.S.3    Kruip, J.4    Kojima, S.5    Gerke, V.6    Kratzin, H.7    Gabius, S.8
  • 15
    • 0028274275 scopus 로고
    • From ill-defined extracts to the immunomodulatory lectin: Will there be a reason for oncological application of mistletoe?
    • Gabius, H.-J., Gabius, S., Joshi, S. S., Koch, B., Schroeder, M., Manzke, W. M. & Westerhausen, M. (1994) From ill-defined extracts to the immunomodulatory lectin: will there be a reason for oncological application of mistletoe? Planta Med. 60, 2-7.
    • (1994) Planta Med. , vol.60 , pp. 2-7
    • Gabius, H.-J.1    Gabius, S.2    Joshi, S.S.3    Koch, B.4    Schroeder, M.5    Manzke, W.M.6    Westerhausen, M.7
  • 16
    • 0027095973 scopus 로고
    • Ligand-binding characteristics of the major mistletoe lectin
    • Lee, R. T., Gabius, H.-J. & Lee, Y. C. (1992) Ligand-binding characteristics of the major mistletoe lectin, J. Biol. Chem. 267, 23 722-23 727.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23722-23727
    • Lee, R.T.1    Gabius, H.-J.2    Lee, Y.C.3
  • 17
    • 0028381203 scopus 로고
    • The sugar-combining area of galaclose-specific toxic lectin of mistletoe extends beyond the terminal sugar residue: Comparison with a homologous toxic lectin, ricin
    • Lee, R. T., Gabius, H.-J. & Lee, Y. C. (1994) The sugar-combining area of galaclose-specific toxic lectin of mistletoe extends beyond the terminal sugar residue: comparison with a homologous toxic lectin, ricin, Carbohydr. Res. 254, 269-276.
    • (1994) Carbohydr. Res. , vol.254 , pp. 269-276
    • Lee, R.T.1    Gabius, H.-J.2    Lee, Y.C.3
  • 18
    • 0030445222 scopus 로고    scopus 로고
    • Comparative cross-linking activities of lactose-specific plant and animal lectins and a nalural lactose-binding immunoglobulin G fraction from human serum with asialofetuin
    • Gupta, D., Kaltner, H., Dong, X., Gabius, H.-J. & Brewer, C. F. (1996) Comparative cross-linking activities of lactose-specific plant and animal lectins and a nalural lactose-binding immunoglobulin G fraction from human serum with asialofetuin, Glycobiology 6, 843-849.
    • (1996) Glycobiology , vol.6 , pp. 843-849
    • Gupta, D.1    Kaltner, H.2    Dong, X.3    Gabius, H.-J.4    Brewer, C.F.5
  • 19
    • 0002860359 scopus 로고
    • The use of transferred nuclear Overhauser effects in the study of the conformations of small molecules bound to proteins
    • Albrand, J. P., Birdsall, B., Feeney, J., Roberts, G. C. K. & Burgen, A. S. V. (1979) The use of transferred nuclear Overhauser effects in the study of the conformations of small molecules bound to proteins, Int. J. Biol. Macromol. 1, 37-41.
    • (1979) Int. J. Biol. Macromol. , vol.1 , pp. 37-41
    • Albrand, J.P.1    Birdsall, B.2    Feeney, J.3    Roberts, G.C.K.4    Burgen, A.S.V.5
  • 20
    • 0000393431 scopus 로고
    • Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small molecules bound to proteins
    • Clore, G. M. & Gronenborn, A. M. (1982) Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small molecules bound to proteins, J. Magn. Reson. 48, 402-417.
    • (1982) J. Magn. Reson. , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 21
    • 0001342923 scopus 로고
    • Theory of the time-dependent transferred nuclear Overhauser effect: Applications of structural analysis of ligand-protein complexes in solution
    • Clore, G. M. & Gronenborn, A. M. (1983) Theory of the time-dependent transferred nuclear Overhauser effect: applications of structural analysis of ligand-protein complexes in solution, J. Magn. Reson. 53, 423-442.
    • (1983) J. Magn. Reson. , vol.53 , pp. 423-442
    • Clore, G.M.1    Gronenborn, A.M.2
  • 22
    • 0027361390 scopus 로고
    • Experimental NMR techniques for studies of protein-ligand interactions
    • Otting, G. (1993) Experimental NMR techniques for studies of protein-ligand interactions, Curr. Opin. Struct. Biol. 3, 760-768.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 760-768
    • Otting, G.1
  • 23
    • 0028728698 scopus 로고
    • Recent developments in transferred NOE methods
    • Ni, F. (1994) Recent developments in transferred NOE methods, Progr. NMR Spectr. 26, 517-606.
    • (1994) Progr. NMR Spectr. , vol.26 , pp. 517-606
    • Ni, F.1
  • 25
    • 0001248255 scopus 로고    scopus 로고
    • Structure and dynamics of oligosaccharides: NMR and modeling studies
    • Peters, T. & Pinto, B. M. (1996) Structure and dynamics of oligosaccharides: NMR and modeling studies, Curr. Opin. Struct. Biol. 5, 710-720.
    • (1996) Curr. Opin. Struct. Biol. , vol.5 , pp. 710-720
    • Peters, T.1    Pinto, B.M.2
  • 26
    • 0031029256 scopus 로고    scopus 로고
    • Animal lectins
    • Gabius, H.-J. (1997) Animal lectins, Eur. J. Biochem. 243, 543-576.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 543-576
    • Gabius, H.-J.1
  • 27
    • 0029669986 scopus 로고    scopus 로고
    • Identification of GDP-Fuc :Galβ1-3GalNAc-R (Fuc to Gal) α1-2 fucosyltransferase and a GDP-Fuc:Galβ1-4GlcNAc (Fuc to GlcNAc) α1-3 fucosyltransferase in connective tissue of the snail Lymanaea stagnalis
    • Mulder, H., Schachter, H,. Thomas, J. R., Halkes, K. M., Kamerling, J. P. & Vliegenthart, J. F. G. (1996) Identification of GDP-Fuc :Galβ1-3GalNAc-R (Fuc to Gal) α1-2 fucosyltransferase and a GDP-Fuc:Galβ1-4GlcNAc (Fuc to GlcNAc) α1-3 fucosyltransferase in connective tissue of the snail Lymanaea stagnalis, Glycoconjugate J. 13, 107-113.
    • (1996) Glycoconjugate J. , vol.13 , pp. 107-113
    • Mulder, H.1    Schachter, H.2    Thomas, J.R.3    Halkes, K.M.4    Kamerling, J.P.5    Vliegenthart, J.F.G.6
  • 28
    • 0030045734 scopus 로고    scopus 로고
    • NMR-based, molecular dynamics- and random walk molecular mechanics-supported study of conformational aspects of a carbohydrate ligand (Galβ1,2Galβ1-R) for an animal galectin in the free and in the bound state
    • Siebert, H.-C., Gilleron, M., Kaltner, H., von der Lieth, C.-W., Kozár, T., Bovin, N. V., Korchagina, E. Y., Vliegenthart, J. F. G. & Gabius, H.-J. (1996) NMR-based, molecular dynamics- and random walk molecular mechanics-supported study of conformational aspects of a carbohydrate ligand (Galβ1,2Galβ1-R) for an animal galectin in the free and in the bound state, Biochem. Biophys. Res. Commun. 219, 205-212.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 205-212
    • Siebert, H.-C.1    Gilleron, M.2    Kaltner, H.3    Von Der Lieth, C.-W.4    Kozár, T.5    Bovin, N.V.6    Korchagina, E.Y.7    Vliegenthart, J.F.G.8    Gabius, H.-J.9
  • 29
  • 30
    • 0027838025 scopus 로고
    • A CHARMm based force field for carbohydrates using the CHEAT approach: Carbohydrate hydroxyl groups represented by extended atoms
    • Grootenhuis, P. D. J. & Haasnoot, C. A. G. (1993) A CHARMm based force field for carbohydrates using the CHEAT approach: carbohydrate hydroxyl groups represented by extended atoms. Mol. Simulat. 10, 75-95.
    • (1993) Mol. Simulat. , vol.10 , pp. 75-95
    • Grootenhuis, P.D.J.1    Haasnoot, C.A.G.2
  • 31
    • 0016399124 scopus 로고
    • Energy functions for peptides and proteins. Deviation of a consistent force field including the hydrogen bond for amide crystals
    • Hagler, A. T., Huler, E. & Lifson, S. (1974) Energy functions for peptides and proteins. Deviation of a consistent force field including the hydrogen bond for amide crystals, J. Am. Chem. Soc. 96, 5316-5327.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 5316-5327
    • Hagler, A.T.1    Huler, E.2    Lifson, S.3
  • 32
    • 6344256147 scopus 로고
    • Consistent force field studies of intermolecular forces in hydrogen-bonded crystals. 2. A benchmark, for the objective comparison of alternative force fields
    • Hagler, A. T. Lifson, S. & Dauber, P. (1979) Consistent force field studies of intermolecular forces in hydrogen-bonded crystals. 2. A benchmark, for the objective comparison of alternative force fields, J. Am. Chem. Soc. 101, 5122-5130.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 5122-5130
    • Hagler, A.T.1    Lifson, S.2    Dauber, P.3
  • 34
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner, S. J., Kollman, P. A., Nguyen, D. T. & Case, D. A. (1986) An all atom force field for simulations of proteins and nucleic acids, J. Comput. Chem. 7, 230-252.
    • (1986) J. Comput. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 36
    • 0023993998 scopus 로고
    • The role of computer simulation techniques in protein engineering
    • van Gunsteren, W. F. (1988) The role of computer simulation techniques in protein engineering, Protein Eng. 2, 5-13.
    • (1988) Protein Eng. , vol.2 , pp. 5-13
    • Van Gunsteren, W.F.1
  • 37
    • 44949289714 scopus 로고
    • RAMM - a new procedure for theoretical conformational analysis of carbohydrates
    • Kozár, T., Petrak, F., Galova, Z. & Tvaroska, I. (1990) RAMM - a new procedure for theoretical conformational analysis of carbohydrates, Carbohydr. Res. 204, 27-36.
    • (1990) Carbohydr. Res. , vol.204 , pp. 27-36
    • Kozár, T.1    Petrak, F.2    Galova, Z.3    Tvaroska, I.4
  • 38
    • 0000319811 scopus 로고    scopus 로고
    • A (critical) survey of modeling protocols used to explore the conformational space of oligosaccharides
    • von der Lieth, C.-W., Kozár, T. & Hull, W. E. (1997) A (critical) survey of modeling protocols used to explore the conformational space of oligosaccharides, J. Mol. Struct. 395-396, 225-244.
    • (1997) J. Mol. Struct. , vol.395-396 , pp. 225-244
    • Von Der Lieth, C.-W.1    Kozár, T.2    Hull, W.E.3
  • 39
    • 3042988525 scopus 로고
    • Conformational analysis. MM 2. A hydrogen force field utilizing V1 and V2 torsional teen
    • Allinger, N. L. (1977) Conformational analysis. MM 2. A hydrogen force field utilizing V1 and V2 torsional teen, J. Am. Chem. Soc. 99, 8127-8134.
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 8127-8134
    • Allinger, N.L.1
  • 41
    • 7144259195 scopus 로고    scopus 로고
    • Modeling conformational properties of maltose in gas phase and solvent
    • in press
    • Kozár, T. & von der Lieth, C.-W. (1998) Modeling conformational properties of maltose in gas phase and solvent. Glycoconjugate J., in press.
    • (1998) Glycoconjugate J.
    • Kozár, T.1    Von Der Lieth, C.-W.2
  • 42
    • 0028343420 scopus 로고
    • Studies of inhibitor binding to Escherichia coli purine nucleoside phosphorylase using the transferred nuclear Overhauser effect and rotating frame nuclear Overhauser enhancement
    • Perlman, M. E., Davis, G. E., Koszalka, G. W., Tuttle, J. V. & London, R. E. (1994) Studies of inhibitor binding to Escherichia coli purine nucleoside phosphorylase using the transferred nuclear Overhauser effect and rotating frame nuclear Overhauser enhancement, Biochemistry 33, 7547-7559.
    • (1994) Biochemistry , vol.33 , pp. 7547-7559
    • Perlman, M.E.1    Davis, G.E.2    Koszalka, G.W.3    Tuttle, J.V.4    London, R.E.5
  • 44
    • 0026742506 scopus 로고
    • 3 gangliosides containing different sialic acid residues as revealed by NOE-based distance mapping, molecular mechanics, and molecular dynamics calculations
    • 3 gangliosides containing different sialic acid residues as revealed by NOE-based distance mapping, molecular mechanics, and molecular dynamics calculations, Biochemistry 31, 6962-6971.
    • (1992) Biochemistry , vol.31 , pp. 6962-6971
    • Siebert, H.-C.1    Reuter, G.2    Schauer, R.3    Von Der Lieth, C.-W.4    Dabrowski, J.5
  • 47
    • 0025007355 scopus 로고
    • 1 ganglioside revealed by distance-mapping procedure: A rotating and laboratory frame nuclear Overhauser enhancement investigation of native glycolipid in dimethyl sulfoxide and in water-dodecylphosphocholine solutions
    • 1 ganglioside revealed by distance-mapping procedure: a rotating and laboratory frame nuclear Overhauser enhancement investigation of native glycolipid in dimethyl sulfoxide and in water-dodecylphosphocholine solutions, J. Am. Chem. Soc. 112, 7772-7778.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 7772-7778
    • Acquotti, D.1    Poppe, L.2    Dabrowski, J.3    Von Der Lieth, C.-W.4    Sonnino, S.5    Tettamanti, G.6
  • 48
    • 0001048934 scopus 로고
    • Conformation on the glycolipid globoside head group in various solvents and in the micelle-bound state
    • Poppe, L., von der Lieth, C.-W. & Dabrowski, J. (1990) Conformation on the glycolipid globoside head group in various solvents and in the micelle-bound state, J. Am. Chem. Soc. 112, 7762-7771.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 7762-7771
    • Poppe, L.1    Von Der Lieth, C.-W.2    Dabrowski, J.3
  • 49
    • 0028876191 scopus 로고
    • Studies of the bound conformations of methyl α-lactoside and methyl β-allolactoside to ricin B chain using transferred NOE experiments in the laboratory and rotating frames, assisted by molecular mechanics and molecular dynamics calculations
    • Asensio, J. L., Canada, F. J. & Jiménez-Barbero, J. (1995) Studies of the bound conformations of methyl α-lactoside and methyl β-allolactoside to ricin B chain using transferred NOE experiments in the laboratory and rotating frames, assisted by molecular mechanics and molecular dynamics calculations, Eur. J. Biochem. 233, 618-630.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 618-630
    • Asensio, J.L.1    Canada, F.J.2    Jiménez-Barbero, J.3
  • 50
    • 33748734029 scopus 로고
    • Aleuria aurantia agglutinin recognizes multiple conformations of α-L-Fuc-(1-6)-β-D-GlcNAc-OMe
    • Weimar, T. & Peters, T. (1994) Aleuria aurantia agglutinin recognizes multiple conformations of α-L-Fuc-(1-6)-β-D-GlcNAc-OMe, Angew. Chem. Int. Ed. Engl. 33, 88-91.
    • (1994) Angew. Chem. Int. Ed. Engl. , vol.33 , pp. 88-91
    • Weimar, T.1    Peters, T.2
  • 52
    • 0000659890 scopus 로고    scopus 로고
    • Unterschiede zwischen den Konformationen von O- und C-Glycosiden im proteingebundenen Zustand: Ricin B. ein Galactose-bindendes Protein, erkennt unterschiedliche Konformationen von C-Lactose und dessen O-Analogon
    • Espinosa, J.-F., Cañada, F. J., Asensio, J. L., Dietrich, H., Martin-Lomas, M., Schmidt, R. R. & Jiménez-Barbero, J. (1996) Unterschiede zwischen den Konformationen von O- und C-Glycosiden im proteingebundenen Zustand: Ricin B. ein Galactose-bindendes Protein, erkennt unterschiedliche Konformationen von C-Lactose und dessen O-Analogon, Angew. Chem. 108, 323-326.
    • (1996) Angew. Chem. , vol.108 , pp. 323-326
    • Espinosa, J.-F.1    Cañada, F.J.2    Asensio, J.L.3    Dietrich, H.4    Martin-Lomas, M.5    Schmidt, R.R.6    Jiménez-Barbero, J.7
  • 53
    • 17544377102 scopus 로고    scopus 로고
    • Different architecture of the combining sites of two chicken galectins revealed by chemical-mapping studies with synthetic ligand derivatives
    • Solís, D., Romero, A., Kaltner, H., Gabíus, H.-J. & Diaz-Mauriño, T. (1996) Different architecture of the combining sites of two chicken galectins revealed by chemical-mapping studies with synthetic ligand derivatives, J. Biol. Chem. 271, 12 744-12 748.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12744-12748
    • Solís, D.1    Romero, A.2    Kaltner, H.3    Gabíus, H.-J.4    Diaz-Mauriño, T.5
  • 54
    • 0029243119 scopus 로고
    • Identification of protein-mediated indirect NOE effects in disaccharide-Fab′ complex by transferred ROESY
    • Arepalli, S. R., Glaudemans, C. P. J., Daves, G. D. Jr. Kovac, P. & Bax, A. (1995) Identification of protein-mediated indirect NOE effects in disaccharide-Fab′ complex by transferred ROESY, J. Magn. Res. 106B, 195-198.
    • (1995) J. Magn. Res. , vol.106 B , pp. 195-198
    • Arepalli, S.R.1    Glaudemans, C.P.J.2    Daves Jr., G.D.3    Kovac, P.4    Bax, A.5
  • 55
    • 0030766193 scopus 로고    scopus 로고
    • Concepts of tumor lectinology
    • Gabius, H.-J. (1997) Concepts of tumor lectinology, Cancer Invest. 15, 454-464.
    • (1997) Cancer Invest. , vol.15 , pp. 454-464
    • Gabius, H.-J.1
  • 56
    • 0031915833 scopus 로고    scopus 로고
    • The how and why of protein-carbohydrate interaction: A primer to the theoretical concept and a guide to application in drug design
    • Gabius, H.-J. (1998) The how and why of protein-carbohydrate interaction: a primer to the theoretical concept and a guide to application in drug design, Pharm. Res. 15, 24-31.
    • (1998) Pharm. Res. , vol.15 , pp. 24-31
    • Gabius, H.-J.1


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