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Volumn 97, Issue 2, 2002, Pages 275-279

Interaction of diocleinae lectins with glycoproteins based in surface plasmon resonance

Author keywords

Binding specificity; Interaction in real time; Lectin

Indexed keywords

GLYCOPROTEIN; PLANT LECTIN;

EID: 0013317997     PISSN: 00740276     EISSN: None     Source Type: Journal    
DOI: 10.1590/S0074-02762002000200025     Document Type: Article
Times cited : (16)

References (33)
  • 3
    • 0025133314 scopus 로고
    • X-ray structure of a (alpha-Man(1-3)beta-Man(1-4)GlcNAc)-lectin complex at 2.1-A resolution. The role of water in sugar-lectin interaction
    • Bourne Y, Rougé P, Cambillau C 1990. X-ray structure of a (alpha-Man(1-3)beta-Man(1-4)GlcNAc)-lectin complex at 2.1-A 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
  • 4
    • 0026500777 scopus 로고
    • X-ray structure of a biantennary octasaccharide-lectin complex refined at 2.3-A resolution
    • Bourne Y, Rougé P, Cambillau C 1992. X-ray structure of a biantennary octasaccharide-lectin complex refined at 2.3-A 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
  • 5
    • 0028773158 scopus 로고
    • Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: Role of the fucose moiety
    • Bourne Y, Mazurier J, Legrand D, Rouge P, Montreuil J, Spik G, Cambillau C 1994. Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an 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    Rouge, P.4    Montreuil, J.5    Spik, G.6    Cambillau, C.7
  • 6
    • 0019572737 scopus 로고
    • Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-gtycosylproteins
    • Debray H, Decout D, Strecker G, Spik G, Montreuil J 1981. Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-gtycosylproteins. 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
  • 7
    • 0008904780 scopus 로고
    • Affinity of tern insolubilized lectins towards various glycopeptides with the N-glycosylamine linkage and related oligosaccharides
    • TC Bog-Hansen, GA Spegler (eds), Walter de Gruyter, Berlin, New York
    • Debray H, Pierce-Crétel G, Spik G, Montreuil J 1983. Affinity of tern insolubilized lectins towards various glycopeptides with the N-glycosylamine linkage and related oligosaccharides. In TC Bog-Hansen, GA Spegler (eds), Lectins: Biology, Biochemistry, Clinical Biochemistry, Walter de Gruyter, Berlin, New York, p. 335-350.
    • (1983) Lectins: Biology, Biochemistry, Clinical Biochemistry , pp. 335-350
    • Debray, H.1    Pierce-Crétel, G.2    Spik, G.3    Montreuil, J.4
  • 8
    • 0027196879 scopus 로고
    • Structures of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human blood group determinant at 2.0 A resolution
    • Delbaere LTJ, Vandonselaar M, Prasad L, Quail JW, Wilson KS, Dauter Z 1993. Structures of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human blood group determinant at 2.0 A resolution. J Mol Biol 230: 950-965.
    • (1993) J Mol Biol , vol.230 , pp. 950-965
    • Delbaere, L.T.J.1    Vandonselaar, M.2    Prasad, L.3    Quail, J.W.4    Wilson, K.S.5    Dauter, Z.6
  • 9
    • 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
  • 10
    • 0029792849 scopus 로고    scopus 로고
    • Characteristics of the histamine release from hamster cheek pouch mast cells stimulated by lectins from Brazilian beans and concanavalin A
    • Ferreira RR, Cavada BS, Moreira RA, Oliveira JTA, Gomes JC 1996. Characteristics of the histamine release from hamster cheek pouch mast cells stimulated by lectins from Brazilian beans and concanavalin A. Inflamm Res 45: 442-447.
    • (1996) Inflamm Res , vol.45 , pp. 442-447
    • Ferreira, R.R.1    Cavada, B.S.2    Moreira, R.A.3    Oliveira, J.T.A.4    Gomes, J.C.5
  • 11
    • 0027634151 scopus 로고
    • Primary structures of concanavalin A-like lectins from seeds of two species of Canavalia
    • Fujimura S, Terada S, Jayavardhanan KK, Panikkar KR, Kimoto E 1993. Primary structures of concanavalin A-like lectins from seeds of two species of Canavalia. Phytochem 33: 985-987.
    • (1993) Phytochem , vol.33 , pp. 985-987
    • Fujimura, S.1    Terada, S.2    Jayavardhanan, K.K.3    Panikkar, K.R.4    Kimoto, E.5
  • 12
    • 0002199711 scopus 로고
    • Isolation, physicochemical characterization and carbohydrate-binding specificity of lectins
    • IE Liener, N Sharon, IJ Goldstein (eds), Academic Press, New York
    • Goldstein IJ, Poretz RD 1986. Isolation, physicochemical characterization and carbohydrate-binding specificity of lectins. In IE Liener, N Sharon, IJ Goldstein (eds), The Lectins, Properties, Functions, and Applications in Biology and Medicine, Academic Press, New York, p. 33-247.
    • (1986) The Lectins, Properties, Functions, and Applications in Biology and Medicine , pp. 33-247
    • Goldstein, I.J.1    Poretz, R.D.2
  • 13
    • 0028317006 scopus 로고
    • Histamine release induced by glucose (mannose)-specific lectins isolated from Brazilian beans. Comparison with concanavalin A
    • Gomes JC, Ferreira RR, Cavada BS, Moreira RA, Oliveira JTA 1994. Histamine release induced by glucose (mannose)-specific lectins isolated from Brazilian beans. Comparison with concanavalin A. Agents Actions 41: 132-135.
    • (1994) Agents Actions , vol.41 , pp. 132-135
    • Gomes, J.C.1    Ferreira, R.R.2    Cavada, B.S.3    Moreira, R.A.4    Oliveira, J.T.A.5
  • 14
    • 0033570017 scopus 로고    scopus 로고
    • Characterization of the carbohydrate binding specificity and kinetic parameters of lectins by using surface plasmon resonance
    • Haseley SR, Talaga P, Kamerling JP, Vliegenthart JFG 1999. Characterization of the carbohydrate binding specificity and kinetic parameters of lectins by using surface plasmon resonance. Anal Biochem 274: 203-210.
    • (1999) Anal Biochem , vol.274 , pp. 203-210
    • Haseley, S.R.1    Talaga, P.2    Kamerling, J.P.3    Vliegenthart, J.F.G.4
  • 15
    • 0027447478 scopus 로고
    • Purification, crystallization, and preliminary X-ray studies on the rhizome lectin from stinging nettle and its complex with NN'N"-triacetylchitotriose
    • Loris R, Thi MHD, Lisgarten J, Wyns L 1993. Purification, crystallization, and preliminary X-ray studies on the rhizome lectin from stinging nettle and its complex with NN'N"-triacetylchitotriose. Proteins 15: 205-208.
    • (1993) Proteins , vol.15 , pp. 205-208
    • Loris, R.1    Thi, M.H.D.2    Lisgarten, J.3    Wyns, L.4
  • 16
    • 0021744087 scopus 로고
    • Spatial conformation of glycans and glycoproteins
    • Montreuil J 1984. Spatial conformation of glycans and glycoproteins. Biol Cell 51: 115-132.
    • (1984) Biol Cell , vol.51 , pp. 115-132
    • Montreuil, J.1
  • 17
    • 0000926728 scopus 로고
    • Lectin from Canavalia brasiliensis (Mart.). Isolation, characterization and behavior during germination
    • Moreira RA, Cavada BS 1984. Lectin from Canavalia brasiliensis (Mart.). Isolation, characterization and behavior during germination. Biol Plantarum 26: 113-120.
    • (1984) Biol Plantarum , vol.26 , pp. 113-120
    • Moreira, R.A.1    Cavada, B.S.2
  • 18
    • 0001912262 scopus 로고
    • Isolation and characterization of a lectin from the seeds of Diolcea grandiflora (Mart.)
    • Moreira RA, Barros ACH, Stewart JC, Pusztai A 1983. Isolation and characterization of a lectin from the seeds of Diolcea grandiflora (Mart.) Planta 158: 63-69.
    • (1983) Planta , vol.158 , pp. 63-69
    • Moreira, R.A.1    Barros, A.C.H.2    Stewart, J.C.3    Pusztai, A.4
  • 19
    • 0030042401 scopus 로고    scopus 로고
    • Structural basis of trimannoside recognition by concanavalin A
    • Naismith JH, Field RA 1996. Structural basis of trimannoside recognition by concanavalin A. J Biol Chem 271: 972-976.
    • (1996) J Biol Chem , vol.271 , pp. 972-976
    • Naismith, J.H.1    Field, R.A.2
  • 20
    • 0002819333 scopus 로고
    • Isolation and partial characterization of a lectin from Cratylia floribunda Mart, seeds
    • Oliveira JTA, Cavada BS, Moreira RA 1991. Isolation and partial characterization of a lectin from Cratylia floribunda Mart, seeds. Revta brasil Bot 14: 61-66.
    • (1991) Revta Brasil Bot , vol.14 , pp. 61-66
    • Oliveira, J.T.A.1    Cavada, B.S.2    Moreira, R.A.3
  • 21
    • 0026299869 scopus 로고
    • Comparison of the amino acid sequences of the lectins from seeds of Dioclea lehmanni and Canavalia maritima
    • Perez G, Perez C, Sousa-Cavada B, Moreira RA, Richardson M 1991. Comparison of the amino acid sequences of the lectins from seeds of Dioclea lehmanni and Canavalia maritima. Phytochem 30: 2619-2621.
    • (1991) Phytochem , vol.30 , pp. 2619-2621
    • Perez, G.1    Perez, C.2    Sousa-Cavada, B.3    Moreira, R.A.4    Richardson, M.5
  • 22
    • 0029644480 scopus 로고
    • BIAcore: A microchip-based system for analyzing the formation of macromolecular complexes
    • Raghavan M, Bjorkman PM 1995. BIAcore: a microchip-based system for analyzing the formation of macromolecular complexes. Curr Biol 3: 331-333.
    • (1995) Curr Biol , vol.3 , pp. 331-333
    • Raghavan, M.1    Bjorkman, P.M.2
  • 24
    • 0030274598 scopus 로고    scopus 로고
    • The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins
    • Ramos MV, Moreira RA, Oliveira JTA, Cavada BS, Rougé P 1996b. The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins. Mem Inst Oswaldo Cruz 91: 761-766.
    • (1996) Mem Inst Oswaldo Cruz , vol.91 , pp. 761-766
    • Ramos, M.V.1    Moreira, R.A.2    Oliveira, J.T.A.3    Cavada, B.S.4    Rougé, P.5
  • 25
    • 0033955735 scopus 로고    scopus 로고
    • Advances in surface plasmon resonance biosensor analysis
    • Rich RC, Myszka DG 2000. Advances in surface plasmon resonance biosensor analysis. Curr Opin Biotech 11: 54-61.
    • (2000) Curr Opin Biotech , vol.11 , pp. 54-61
    • Rich, R.C.1    Myszka, D.G.2
  • 26
    • 0021504657 scopus 로고
    • The complete amino acid sequence of the major alpha subunit of the lectin from the seeds of Dioclea grandiflora (Mart)
    • Richardson M, Campos FDAP, Moreira RA, Ainouz IL, Begbie R, Watt WB, Pusztai A 1984. The complete amino acid sequence of the major alpha subunit of the lectin from the seeds of Dioclea grandiflora (Mart). Eur J Biochem 144: 101-111.
    • (1984) Eur J Biochem , vol.144 , pp. 101-111
    • Richardson, M.1    Campos, F.D.A.P.2    Moreira, R.A.3    Ainouz, I.L.4    Begbie, R.5    Watt, W.B.6    Pusztai, A.7
  • 28
    • 0027314952 scopus 로고
    • X-ray crystal structure of a pea lectin-trimannoside complex at 2.6 A resolution
    • Rini JM, Hardman KD, Einspahr H, Suddath FL, Carver JP 1993. X-ray crystal structure of a pea lectin-trimannoside complex at 2.6 A resolution. J Biol Chem 26R: 10126-10132.
    • (1993) J Biol Chem , vol.26 R , pp. 10126-10132
    • Rini, J.M.1    Hardman, K.D.2    Einspahr, H.3    Suddath, F.L.4    Carver, J.P.5
  • 29
    • 0026746150 scopus 로고
    • Differences in macrophage stimulation and leukocyte accumulation in response to intraperitoncal administration of glucose/mannose-binding plant lectins
    • Rodriguez D, Cavada BS, Oliveira JTA, Moreira RA, Russo M 1992. Differences in macrophage stimulation and leukocyte accumulation in response to intraperitoncal administration of glucose/mannose-binding plant lectins. Braz J Med Biol Res 25: 823-826.
    • (1992) Braz J Med Biol Res , vol.25 , pp. 823-826
    • Rodriguez, D.1    Cavada, B.S.2    Oliveira, J.T.A.3    Moreira, R.A.4    Russo, M.5
  • 30
    • 0030995894 scopus 로고    scopus 로고
    • The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A
    • Sanz-Aparicio J, Hermoso J, Grangeiro TB, Calvete JJ, Cavada BS 1997. The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A. FEBS Lett 405: 114-118.
    • (1997) FEBS Lett , vol.405 , pp. 114-118
    • Sanz-Aparicio, J.1    Hermoso, J.2    Grangeiro, T.B.3    Calvete, J.J.4    Cavada, B.S.5
  • 31
    • 0026337737 scopus 로고
    • Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose
    • Shaanan B, Lis H, Sharon N 1991. Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose. Science 254: 862-866.
    • (1991) Science , vol.254 , pp. 862-866
    • Shaanan, B.1    Lis, H.2    Sharon, N.3
  • 32
    • 0000089704 scopus 로고
    • cDNAs for canavalin and concanavalin A from Canavalia gladiata seeds. Nucleotide sequence of cDNA for canavalin and RNA blot analysis of canavalin and concanavalin A mRNAs in developing seeds
    • Yamauchi D, Nakamura K, Asahi T, Minamikawa T 1989. cDNAs for canavalin and concanavalin A from Canavalia gladiata seeds. Nucleotide sequence of cDNA for canavalin and RNA blot analysis of canavalin and concanavalin A mRNAs in developing seeds. P Cell Physiol 30: 147-150.
    • (1989) P Cell Physiol , vol.30 , pp. 147-150
    • Yamauchi, D.1    Nakamura, K.2    Asahi, T.3    Minamikawa, T.4
  • 33
    • 0027078720 scopus 로고
    • Analysis of sequence variation among legume lectins. A ring of hypervariable residues forms the perimeter of the carbohydrate-binding site
    • Young NM, Oomen RP 1992. Analysis of sequence variation among legume lectins. A ring of hypervariable residues forms the perimeter of the carbohydrate-binding site. J Mol Biol 228: 924-934.
    • (1992) J Mol Biol , vol.228 , pp. 924-934
    • Young, N.M.1    Oomen, R.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.