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Volumn 33, Issue 4, 1997, Pages 691-698

Curculin, a sweet-tasting and taste-modifying protein, is a non-functional mannose-binding lectin

Author keywords

curculin; docking; epitopes; lectins; molecular modelling; sweet proteins

Indexed keywords

CURCULIN PROTEIN, PLANT; LECTIN; MANNOSE; MANNOSE BINDING LECTIN; PLANT LECTIN; SNOWDROP LECTIN; SWEETENING AGENT; VEGETABLE PROTEIN;

EID: 0031105098     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005704616565     Document Type: Article
Times cited : (33)

References (23)
  • 1
    • 0026588709 scopus 로고
    • Molecular cloning of curculin, a novel taste-modifying protein with a sweet taste
    • Abe K, Yamashita H, Arai S, Kurihara Y: Molecular cloning of curculin, a novel taste-modifying protein with a sweet taste. Biochim Biophys Acta 1130: 232-234 (1992).
    • (1992) Biochim Biophys Acta , vol.1130 , pp. 232-234
    • Abe, K.1    Yamashita, H.2    Arai, S.3    Kurihara, Y.4
  • 2
    • 0025138532 scopus 로고
    • Conformation-activity relationships of sweet molecules. Comparison of aspartame and naphthimidazolesulfonic acids
    • Castiglione-Morelli MA, Lelj F, Naider F, Tallon M, Tancredi T, Temussi PA: Conformation-activity relationships of sweet molecules. Comparison of aspartame and naphthimidazolesulfonic acids. J Med Chem 33: 514-520 (1990).
    • (1990) J Med Chem , vol.33 , pp. 514-520
    • Castiglione-Morelli, M.A.1    Lelj, F.2    Naider, F.3    Tallon, M.4    Tancredi, T.5    Temussi, P.A.6
  • 3
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gabroriaud C, Bissery V, Benchetrit T, Mornon JP: Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett 224: 149-155 (1987).
    • (1987) FEBS Lett , vol.224 , pp. 149-155
    • Gabroriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 4
    • 0028240193 scopus 로고
    • Crystillization and preliminary X-ray diffraction studies of curculin, a new type of sweet protein having taste-modifying action
    • Harada S, Otani H, Maeda S, Kai Y, Kasai N, Kurihara Y: Crystillization and preliminary X-ray diffraction studies of curculin, a new type of sweet protein having taste-modifying action. J Mol Biol 238: 286-287 (1994).
    • (1994) J Mol Biol , vol.238 , pp. 286-287
    • Harada, S.1    Otani, H.2    Maeda, S.3    Kai, Y.4    Kasai, N.5    Kurihara, Y.6
  • 5
    • 0029008975 scopus 로고
    • Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of anew plant lectin family
    • Hester G, Kaku H, Goldstein IJ, Wright CS: Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of anew plant lectin family. Nature Struct Biol 2: 472-479 (1995).
    • (1995) Nature Struct Biol , vol.2 , pp. 472-479
    • Hester, G.1    Kaku, H.2    Goldstein, I.J.3    Wright, C.S.4
  • 7
    • 0017883568 scopus 로고
    • Antibodies to thaumatin as a model of the sweet taste receptor
    • Hough C, Edwardson J: Antibodies to thaumatin as a model of the sweet taste receptor. Nature 271: 381-383 (1978).
    • (1978) Nature , vol.271 , pp. 381-383
    • Hough, C.1    Edwardson, J.2
  • 9
    • 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: Hydrophobic cluster analysis: procedure to derive structural and functional information from 2-D-representation of protein sequences. Biochimie 72: 555-574 (1990).
    • (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
  • 10
    • 0027530456 scopus 로고
    • Purification, complete amino acid sequence and structure characterization of the heat stable sweet protein, mabinlin II
    • Liu X, Maeda S, Hu Z, Aiuchi T, Nakaya K, Kurihara Y: Purification, complete amino acid sequence and structure characterization of the heat stable sweet protein, mabinlin II. Eur J Biochem 211: 281-287 (1993).
    • (1993) Eur J Biochem , vol.211 , pp. 281-287
    • Liu, X.1    Maeda, S.2    Hu, Z.3    Aiuchi, T.4    Nakaya, K.5    Kurihara, Y.6
  • 11
    • 0015526521 scopus 로고
    • Purification of monellin, the sweet principle of Dioscoreophyllum cumminsii
    • Morris JA, Cagan RH: Purification of monellin, the sweet principle of Dioscoreophyllum cumminsii. Biochim Biophys Acta 261: 114-122 (1972).
    • (1972) Biochim Biophys Acta , vol.261 , pp. 114-122
    • Morris, J.A.1    Cagan, R.H.2
  • 12
    • 0026516609 scopus 로고
    • An enzyme immunoassay and immunoblot analysis for curculin, a new type of taste-modifying protein/cross-reactivity of curculin and miraculin to both antibodies
    • Nakajo S, Akabane T, Nakaya K, Nakamura Y, Kurihara Y: An enzyme immunoassay and immunoblot analysis for curculin, a new type of taste-modifying protein/cross-reactivity of curculin and miraculin to both antibodies. Biochim Biophys Acta 1118: 293-297 (1992).
    • (1992) Biochim Biophys Acta , vol.1118 , pp. 293-297
    • Nakajo, S.1    Akabane, T.2    Nakaya, K.3    Nakamura, Y.4    Kurihara, Y.5
  • 13
    • 0023660834 scopus 로고
    • Crystal structure of the intensely sweet protein monellin
    • Ogata C, Hatada M, Tomlinson G, Shin WC, Kim SH: Crystal structure of the intensely sweet protein monellin. Nature 328: 739-742 (1987).
    • (1987) Nature , vol.328 , pp. 739-742
    • Ogata, C.1    Hatada, M.2    Tomlinson, G.3    Shin, W.C.4    Kim, S.H.5
  • 14
    • 0346126540 scopus 로고
    • The role of lectins in the plant's defense against insects
    • Van Driessche E, Fischer J, Beeckmans S, Bøg-Hansen TC (eds) Textop, Hellerup
    • Peumans WJ, Van Damme EJM: The role of lectins in the plant's defense against insects. In: Van Driessche E, Fischer J, Beeckmans S, Bøg-Hansen TC (eds) Lectins: Biology, Biochemistry, Clinical Biochemistry, vol. 10, pp. 128-141. Textop, Hellerup (1994).
    • (1994) Lectins: Biology, Biochemistry, Clinical Biochemistry , vol.10 , pp. 128-141
    • Peumans, W.J.1    Van Damme, E.J.M.2
  • 16
    • 0024288401 scopus 로고
    • Complete purification and characterization of the taste-modifying protein, miraculin, from miracle fruit
    • Theerasilp S, Kurihara Y: Complete purification and characterization of the taste-modifying protein, miraculin, from miracle fruit. J Biol Chem 263: 11536-11539 (1988).
    • (1988) J Biol Chem , vol.263 , pp. 11536-11539
    • Theerasilp, S.1    Kurihara, Y.2
  • 17
    • 0024533487 scopus 로고
    • Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin
    • Theerasilp S, Hitotsuya H, Nakajo S, Nakaya K, Nakamura Y, Kurihara H: Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin. J Biol Chem 264: 6655-6659 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 6655-6659
    • Theerasilp, S.1    Hitotsuya, H.2    Nakajo, S.3    Nakaya, K.4    Nakamura, Y.5    Kurihara, H.6
  • 19
    • 0002928881 scopus 로고
    • Molecular cloning of the mannose-binding lectins from Amaryllidaceae and Alliaceae species
    • Van Driessche E, Fischer J, Beeckmans S, Bøg-Hansen TC (eds) Textop, Hellerup
    • Van Damme EJM, Smeets K, Peumans WJ: Molecular cloning of the mannose-binding lectins from Amaryllidaceae and Alliaceae species. In: Van Driessche E, Fischer J, Beeckmans S, Bøg-Hansen TC (eds) Lectins: Biology, Biochemistry, Clinical Biochemistry, vol. 10, pp. 166-177. Textop, Hellerup (1994).
    • (1994) Lectins: Biology, Biochemistry, Clinical Biochemistry , vol.10 , pp. 166-177
    • Van Damme, E.J.M.1    Smeets, K.2    Peumans, W.J.3
  • 20
    • 0015494327 scopus 로고
    • Isolation and characterization of thaumatin I and II, the sweet-tasting proteins from Thaumatococcus daniellii Benth
    • Van der Wel H, Loeve K: Isolation and characterization of thaumatin I and II, the sweet-tasting proteins from Thaumatococcus daniellii Benth. Eur J Biochem 31: 221-225 (1972).
    • (1972) Eur J Biochem , vol.31 , pp. 221-225
    • Van Der Wel, H.1    Loeve, K.2
  • 21
    • 0027959475 scopus 로고
    • Brazzein, a new high-potency thermostable sweet protein from Pentadiplandra brazzeana B
    • Ming D, Hellekant G: Brazzein, a new high-potency thermostable sweet protein from Pentadiplandra brazzeana B. FEBS Lett 355: 106-108 (1994).
    • (1994) FEBS Lett , vol.355 , pp. 106-108
    • Ming, D.1    Hellekant, G.2
  • 23
    • 0025126845 scopus 로고
    • Purification and complete amino acid sequence of a new type of sweet protein with taste-modifying activity, curculin
    • Yamashita H, Theerasilp S, Aiuchi T, Nakaya K, Nakamura Y, Kurihara Y: Purification and complete amino acid sequence of a new type of sweet protein with taste-modifying activity, curculin. J Biol Chem 265: 15770-15775 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 15770-15775
    • Yamashita, H.1    Theerasilp, S.2    Aiuchi, T.3    Nakaya, K.4    Nakamura, Y.5    Kurihara, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.