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Volumn 112, Issue 4, 1996, Pages 1531-1540

Structure-function relationship of monocot mannose-binding lectins

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EID: 0030452169     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.112.4.1531     Document Type: Article
Times cited : (111)

References (50)
  • 1
    • 0026532965 scopus 로고
    • The mannose-specific plant lectins from Cymbidium hybrid and Epipactis helleborine and the (N-acetylglucosamine)-specific plant lectin from Urtica dioica are potent and selective inhibitors of human immunodeficiency virus and cytomegalovirus replication in vitro
    • Balzarini J, Neyts J, Schols D, Hosoya M, Van Damme EJM, Peumans WJ, De Clercq E (1992) The mannose-specific plant lectins from Cymbidium hybrid and Epipactis helleborine and the (N-acetylglucosamine)-specific plant lectin from Urtica dioica are potent and selective inhibitors of human immunodeficiency virus and cytomegalovirus replication in vitro. Antiviral Res 18: 191-207
    • (1992) Antiviral Res , vol.18 , pp. 191-207
    • Balzarini, J.1    Neyts, J.2    Schols, D.3    Hosoya, M.4    Van Damme, E.J.M.5    Peumans, W.J.6    De Clercq, E.7
  • 2
    • 0026020005 scopus 로고
    • α-(1-3)- and α-(1-6)-D-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro
    • Balzarini J, Schols D, Neyts J, Van Damme EJM, Peumans WJ, De Clercq E (1991) α-(1-3)- and α-(1-6)-D-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro. Antimicrob Agents Chemother 35: 410-416
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 410-416
    • Balzarini, J.1    Schols, D.2    Neyts, J.3    Van Damme, E.J.M.4    Peumans, W.J.5    De Clercq, E.6
  • 4
    • 0028773158 scopus 로고
    • Interaction of a legume lectin with the human lactotransferrin N2 fragment or with the isolated biantennary glycopeptide: Role of the fucose moiety
    • Bourne Y, Mazurier J, Legrand D, Rougé P, Montreuil J, Spik G, Cambillau C (1994) Interaction of a legume lectin with the human lactotransferrin N2 fragment or with the isolated biantennary glycopeptide: role of the fucose moiety. Structure 2: 209-219
    • (1994) Structure , vol.2 , pp. 209-219
    • Bourne, Y.1    Mazurier, J.2    Legrand, D.3    Rougé, P.4    Montreuil, J.5    Spik, G.6    Cambillau, C.7
  • 5
    • 0025133314 scopus 로고
    • X-ray structure of α(α-Man(1-3)α-Man(1-4)GlcNAc)-lectin complex at 2.1 Å resolution. the role of water in sugar-lectin interaction
    • Bourne Y, Rougé P, Cambillau C (1990) X-ray structure of α(α-Man(1-3)α-Man(1-4)GlcNAc)-lectin complex at 2.1 Å resolution. The role of water in sugar-lectin interaction. J Biol Chem 265: 18161-18165
    • (1990) J Biol Chem , vol.265 , pp. 18161-18165
    • Bourne, Y.1    Rougé, P.2    Cambillau, C.3
  • 6
    • 0026500777 scopus 로고
    • X-ray structure of a biantennary octasaccharide-lectin complex refined at 2.3 Å resolution
    • Bourne Y, Rougé P, Cambillau C (1992) X-ray structure of a biantennary octasaccharide-lectin complex refined at 2.3 Å 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
  • 8
    • 0019572737 scopus 로고
    • Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins
    • Debray H, Decout D, Strecker G, Spik G, Montreuil J (1981) Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins. Eur J Biochem 117: 41-55
    • (1981) Eur J Biochem , vol.117 , pp. 41-55
    • Debray, H.1    Decout, D.2    Strecker, G.3    Spik, G.4    Montreuil, J.5
  • 9
    • 0006957511 scopus 로고
    • The fine sugar specificity of the Lathyrus ochrus seed lectin and isolectins
    • Debray H, Rougé P (1984) The fine sugar specificity of the Lathyrus ochrus seed lectin and isolectins. FEBS Lett 176: 120-124
    • (1984) FEBS Lett , vol.176 , pp. 120-124
    • Debray, H.1    Rougé, P.2
  • 10
    • 0028825850 scopus 로고
    • Picogram detection levels of asialofetuin via the carbohydrate moieties using the light addressable potentiometric sensor
    • Dill K, Olson JD (1995) Picogram detection levels of asialofetuin via the carbohydrate moieties using the light addressable potentiometric sensor. Glycoconjugate Journal 12: 660-663
    • (1995) Glycoconjugate Journal , vol.12 , pp. 660-663
    • Dill, K.1    Olson, J.D.2
  • 11
    • 0029064070 scopus 로고
    • Multiplicity of lectin-carbohydrate interactions
    • Drickamer K (1995) Multiplicity of lectin-carbohydrate interactions. Nature Struct Biol 2: 437-439
    • (1995) Nature Struct Biol , vol.2 , pp. 437-439
    • Drickamer, K.1
  • 12
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gaboriaud C, Bissery V, Benchetrit T, Mornon JP (1987) Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett 224: 149-155
    • (1987) FEBS Lett , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 13
    • 0029008975 scopus 로고
    • Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family
    • Hester G, Kaku H, Goldstein IJ, Wright CS (1995) Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family. Nature Struct Biol 2: 472-479
    • (1995) Nature Struct Biol , vol.2 , pp. 472-479
    • Hester, G.1    Kaku, H.2    Goldstein, I.J.3    Wright, C.S.4
  • 15
    • 0000448982 scopus 로고
    • Prediction of protein antigenic determinants from amino acid sequences
    • Hopp TP, Woods KR (1981) Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 78: 3824-3828
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3824-3828
    • Hopp, T.P.1    Woods, K.R.2
  • 16
    • 0018784438 scopus 로고
    • Surface and inside volumes in globular proteins
    • Janin J (1979) Surface and inside volumes in globular proteins. Nature 277: 491-492
    • (1979) Nature , vol.277 , pp. 491-492
    • Janin, J.1
  • 17
    • 0025333981 scopus 로고
    • Carbohydrate-binding specificity of the daffodil (Narcissus pseudonarcissus) and amaryllis (Hippeastrum hybr.) bulb lectins
    • Kaku H, Van Damme EJM, Peumans WJ, Goldstein IJ (1990) Carbohydrate-binding specificity of the daffodil (Narcissus pseudonarcissus) and amaryllis (Hippeastrum hybr.) bulb lectins. Arch Biochem Biophys 279: 298-304
    • (1990) Arch Biochem Biophys , vol.279 , pp. 298-304
    • Kaku, H.1    Van Damme, E.J.M.2    Peumans, W.J.3    Goldstein, I.J.4
  • 18
    • 0026868276 scopus 로고
    • New mannose-specific lectins from garlic (Allium sativum) and ramsons (Allium ursinum) bulbs
    • Kaku H, Van Damme EJM, Peumans WJ, Goldstein IJ (1992) New mannose-specific lectins from garlic (Allium sativum) and ramsons (Allium ursinum) bulbs. Carbohydr Res 229: 347-353
    • (1992) Carbohydr Res , vol.229 , pp. 347-353
    • Kaku, H.1    Van Damme, E.J.M.2    Peumans, W.J.3    Goldstein, I.J.4
  • 19
    • 0021918946 scopus 로고
    • Prediction of chain flexibility in proteins
    • Karplus PA, Schulz GE (1985) Prediction of chain flexibility in proteins. Naturwissenschaften 72: 212
    • (1985) Naturwissenschaften , vol.72 , pp. 212
    • Karplus, P.A.1    Schulz, G.E.2
  • 20
    • 0028978737 scopus 로고
    • The complete amino acid sequence of a mannose-binding lectin from "Kidachi aloe" (Aloe arborescens var. Natalensis Berger)
    • Koike T, Titani K, Suzuki M, Beppu H, Kuzuya H, Maruta K, Shimpo K, Fujita K (1995) The complete amino acid sequence of a mannose-binding lectin from "Kidachi aloe" (Aloe arborescens var. Natalensis Berger). Biochem Biophys Res Commun 214: 163-170
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 163-170
    • Koike, T.1    Titani, K.2    Suzuki, M.3    Beppu, H.4    Kuzuya, H.5    Maruta, K.6    Shimpo, K.7    Fujita, K.8
  • 21
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 22
    • 0025129872 scopus 로고
    • Hydrophobic cluster analysis: Procedure to derive structural and functional information from 2-D-representation of protein sequences
    • Lemesle-Varloot L, Henrissat B, Gaboriaud C, Bissery V, Morgat A, Mornon JP (1990) Hydrophobic cluster analysis: procedure to derive structural and functional information from 2-D-representation of protein sequences. Biochimie 72: 555-574
    • (1990) Biochimie , vol.72 , pp. 555-574
    • Lemesle-Varloot, L.1    Henrissat, B.2    Gaboriaud, C.3    Bissery, V.4    Morgat, A.5    Mornon, J.P.6
  • 24
    • 0023055775 scopus 로고
    • New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: Correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites
    • Parker JMR, Guo D, Hodges RS (1986) New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites. Biochemistry 25: 5425-5432
    • (1986) Biochemistry , vol.25 , pp. 5425-5432
    • Parker, J.M.R.1    Guo, D.2    Hodges, R.S.3
  • 29
    • 0027384516 scopus 로고
    • The alpha-mannosyl-binding lectin from leaves of the orchid twayblade (Listera ovata): Application to separation of α-D-mannans from α-D-glucans
    • Saito K, Komae A, Kakuta M, Van Damme EJM, Peumans WJ, Goldstein IJ, Misaki A (1993) The alpha-mannosyl-binding lectin from leaves of the orchid twayblade (Listera ovata): application to separation of α-D-mannans from α-D-glucans. Eur J Biochem 217: 677-681
    • (1993) Eur J Biochem , vol.217 , pp. 677-681
    • Saito, K.1    Komae, A.2    Kakuta, M.3    Van Damme, E.J.M.4    Peumans, W.J.5    Goldstein, I.J.6    Misaki, A.7
  • 30
    • 0025222989 scopus 로고
    • Legume lectins - A large family of homologous proteins
    • Sharon N, Lis H (1990) Legume lectins - a large family of homologous proteins. FASEB J 4: 3198-3208
    • (1990) FASEB J , vol.4 , pp. 3198-3208
    • Sharon, N.1    Lis, H.2
  • 31
    • 0024286486 scopus 로고
    • Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb
    • Shibuya N, Goldstein IJ, Van Damme EJM, Peumans WJ (1988) Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb. J Biol Chem 263: 728-734
    • (1988) J Biol Chem , vol.263 , pp. 728-734
    • Shibuya, N.1    Goldstein, I.J.2    Van Damme, E.J.M.3    Peumans, W.J.4
  • 32
    • 0028300654 scopus 로고
    • Kinetic measurement of the interaction between an oligosaccharide and lectins by a biosensor based on surface plasmon resonance
    • Shinohara Y, Kim F, Shimizu M, Goto M, Tosu M, Hasegawa Y (1994) Kinetic measurement of the interaction between an oligosaccharide and lectins by a biosensor based on surface plasmon resonance. Eur J Biochem 223: 189-194
    • (1994) Eur J Biochem , vol.223 , pp. 189-194
    • Shinohara, Y.1    Kim, F.2    Shimizu, M.3    Goto, M.4    Tosu, M.5    Hasegawa, Y.6
  • 33
    • 0028143192 scopus 로고
    • Comparative study of the post-translational processing of the mannose-binding lectins in the bulbs of garlic (Allium sativum) and ramsons (Allium ursinum)
    • Smeets K, Van Damme EJM, Peumans WJ (1994) Comparative study of the post-translational processing of the mannose-binding lectins in the bulbs of garlic (Allium sativum) and ramsons (Allium ursinum). Glycoconjugate Journal 11: 309-320
    • (1994) Glycoconjugate Journal , vol.11 , pp. 309-320
    • Smeets, K.1    Van Damme, E.J.M.2    Peumans, W.J.3
  • 34
    • 0026610615 scopus 로고
    • 1H-NMR structural determination of the N-linked carbohydrate chains on glycopeptides obtained from the bean lectin phytohemagglutinin
    • 1H-NMR structural determination of the N-linked carbohydrate chains on glycopeptides obtained from the bean lectin phytohemagglutinin. Eur J Biochem 204: 313-316
    • (1992) Eur J Biochem , vol.204 , pp. 313-316
    • Sturm, A.1    Bergwerff, A.A.2    Vliegenthart, F.G.3
  • 35
    • 0022668738 scopus 로고
    • Location of continuous antigenic determinants in the protruding regions of proteins
    • Thornton JM, Edwards MS, Taylor WR, Barlow DJ (1986) Location of continuous antigenic determinants in the protruding regions of proteins. EMBO J 5: 409-413
    • (1986) EMBO J , vol.5 , pp. 409-413
    • Thornton, J.M.1    Edwards, M.S.2    Taylor, W.R.3    Barlow, D.J.4
  • 36
    • 0001035146 scopus 로고
    • Isolation and characterization of a lectin with exclusive specificity towards mannose from snowdrop (Galanthus nivalis) bulbs
    • Van Damme EJM, Allen AK, Peumans WJ (1987) Isolation and characterization of a lectin with exclusive specificity towards mannose from snowdrop (Galanthus nivalis) bulbs. FEBS Lett 215: 140-144
    • (1987) FEBS Lett , vol.215 , pp. 140-144
    • Van Damme, E.J.M.1    Allen, A.K.2    Peumans, W.J.3
  • 37
    • 0003034009 scopus 로고
    • Related mannose-specific lectins from different species of the family Amaryllidaceae
    • Van Damme EJM, Allen AK, Peumans WJ (1988) Related mannose-specific lectins from different species of the family Amaryllidaceae. Physiol Plant 73: 52-57
    • (1988) Physiol Plant , vol.73 , pp. 52-57
    • Van Damme, E.J.M.1    Allen, A.K.2    Peumans, W.J.3
  • 38
    • 0027973161 scopus 로고
    • The monomeric and dimeric mannose binding proteins from the Orchidaceae species Listera ovata and Epipactis helleborine: Sequence homologies and differences in biological activities
    • Van Damme EJM, Balzarini J, Smeets K, Van Leuven F, Peumans WJ (1994a) The monomeric and dimeric mannose binding proteins from the Orchidaceae species Listera ovata and Epipactis helleborine: sequence homologies and differences in biological activities. Glycoconjugate Journal 11: 321-332
    • (1994) Glycoconjugate Journal , vol.11 , pp. 321-332
    • Van Damme, E.J.M.1    Balzarini, J.2    Smeets, K.3    Van Leuven, F.4    Peumans, W.J.5
  • 39
    • 0030175540 scopus 로고    scopus 로고
    • Molecular cloning of the lectin and a lectin related protein from common Solomon's seal (Polygonatum multiflorum)
    • Van Damme EJM, Barre A, Rougé P, Van Leuven F., Balzarini J, Peumans WJ (1996a) Molecular cloning of the lectin and a lectin related protein from common Solomon's seal (Polygonatum multiflorum). Plant Mol Biol 31: 657-672
    • (1996) Plant Mol Biol , vol.31 , pp. 657-672
    • Van Damme, E.J.M.1    Barre, A.2    Rougé, P.3    Van Leuven, F.4    Balzarini, J.5    Peumans, W.J.6
  • 41
    • 0002394695 scopus 로고
    • Molecular cloning and characterization of multiple isoforms of the snowdrop (Galanthus nivalis L.) lectin
    • Van Damme EJM, Declercq N, Claessens F, Hemschoote K, Peeters B, Peumans WJ (1991a) Molecular cloning and characterization of multiple isoforms of the snowdrop (Galanthus nivalis L.) lectin. Planta 186: 35-43
    • (1991) Planta , vol.186 , pp. 35-43
    • Van Damme, E.J.M.1    Declercq, N.2    Claessens, F.3    Hemschoote, K.4    Peeters, B.5    Peumans, W.J.6
  • 42
    • 84989666997 scopus 로고
    • Lectins of members of the Amaryllidaceae are encoded by multigene families which show extensive homologies
    • Van Damme EJM, Goldstein IJ, Vercammen G, Vuylsteke J, Peumans WJ (1992a) Lectins of members of the Amaryllidaceae are encoded by multigene families which show extensive homologies. Physiol Plant 86: 245-252
    • (1992) Physiol Plant , vol.86 , pp. 245-252
    • Van Damme, E.J.M.1    Goldstein, I.J.2    Vercammen, G.3    Vuylsteke, J.4    Peumans, W.J.5
  • 45
    • 0345381033 scopus 로고
    • Biosynthesis of the snowdrop (Galanthus nivalis) lectin in ripening ovaries
    • Van Damme EJM, Peumans WJ (1988) Biosynthesis of the snowdrop (Galanthus nivalis) lectin in ripening ovaries. Plant Physiol 86: 922-926
    • (1988) Plant Physiol , vol.86 , pp. 922-926
    • Van Damme, E.J.M.1    Peumans, W.J.2
  • 47
    • 0026578451 scopus 로고
    • The closely related homomeric and heterodimeric mannose-binding lectins from garlic are encoded by one-domain and two-domain lectin genes, respectively
    • Van Damme EJM, Smeets K, Torrekens S, Van Leuven F, Goldstein IJ, Peumans WJ (1992b) The closely related homomeric and heterodimeric mannose-binding lectins from garlic are encoded by one-domain and two-domain lectin genes, respectively. Eur J Biochem 206: 413-420
    • (1992) Eur J Biochem , vol.206 , pp. 413-420
    • Van Damme, E.J.M.1    Smeets, K.2    Torrekens, S.3    Van Leuven, F.4    Goldstein, I.J.5    Peumans, W.J.6
  • 48
    • 0027359615 scopus 로고
    • The mannose-specific lectins from ramsons (Allium ursinum L.) are encoded by three sets of genes
    • Van Damme EJM, Smeets K, Torrekens S, Van Leuven F, Peumans WJ (1993b) The mannose-specific lectins from ramsons (Allium ursinum L.) are encoded by three sets of genes. Eur J Biochem 217: 123-129
    • (1993) Eur J Biochem , vol.217 , pp. 123-129
    • Van Damme, E.J.M.1    Smeets, K.2    Torrekens, S.3    Van Leuven, F.4    Peumans, W.J.5
  • 49
    • 0028355084 scopus 로고
    • Characterization and molecular cloning of the mannose binding lectins from three Orchidaceae species: Listera ovata, Epipactis helleborine and Cymbidium hybrid
    • Van Damme EJM, Smeets K, Torrekens S, Van Leuven F, Peumans WJ (1994b) Characterization and molecular cloning of the mannose binding lectins from three Orchidaceae species: Listera ovata, Epipactis helleborine and Cymbidium hybrid. Eur J Biochem 221: 769-777
    • (1994) Eur J Biochem , vol.221 , pp. 769-777
    • Van Damme, E.J.M.1    Smeets, K.2    Torrekens, S.3    Van Leuven, F.4    Peumans, W.J.5


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