메뉴 건너뛰기




Volumn 42, Issue 5, 2004, Pages 355-365

The eight-cysteine motif, a versatile structure in plant proteins

Author keywords

2S albumins; Cereal protease inhibitors; Eight cysteine motif; HyPRPs; LTPs

Indexed keywords

COMPLEMENTARY DNA; VEGETABLE PROTEIN;

EID: 3042539813     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2004.03.009     Document Type: Short Survey
Times cited : (155)

References (79)
  • 1
    • 0034637651 scopus 로고    scopus 로고
    • Lipid transfer proteins are encoded by a small multigene family in Arabidopsis thaliana
    • Arondel V., Vergnolle Ch., Cantrel C., Kader J.-C. Lipid transfer proteins are encoded by a small multigene family in Arabidopsis thaliana. Plant Sci. 157:2000;1-12
    • (2000) Plant Sci. , vol.157 , pp. 1-12
    • Arondel, V.1    Vergnolle, Ch.2    Cantrel, C.3    Kader, J.-C.4
  • 2
    • 52849098721 scopus 로고    scopus 로고
    • Minireview: Analysis of rape seed napin structure and potential roles of the storage protein
    • Barciszewski J., Szymanski M., Haertlé T. Minireview: analysis of rape seed napin structure and potential roles of the storage protein. J. Protein Chem. 19:2000;249-254
    • (2000) J. Protein Chem. , vol.19 , pp. 249-254
    • Barciszewski, J.1    Szymanski, M.2    Haertlé, T.3
  • 3
    • 0027202271 scopus 로고
    • Crystal structure of hydrophobic protein from soybean; A member of a new cysteine-rich family
    • Baud F., Pebay-Peyroula E., Cohen-Addad C., Odani S., Lehmann M.S. Crystal structure of hydrophobic protein from soybean; a member of a new cysteine-rich family. J. Mol. Biol. 231:1993;877-887
    • (1993) J. Mol. Biol. , vol.231 , pp. 877-887
    • Baud, F.1    Pebay-Peyroula, E.2    Cohen-Addad, C.3    Odani, S.4    Lehmann, M.S.5
  • 4
    • 0032480808 scopus 로고    scopus 로고
    • Structural determinants of the bifunctional corn Hageman Factor inhibitor: X-ray crystal structure at 1.95 Å resolution
    • Behnke C.A., Yee V.C., Le Trong I., Pedersen L.C., Stenkamp R.E., Kim S.-S., Reeck G.R., Teller D.C. Structural determinants of the bifunctional corn Hageman Factor inhibitor: X-ray crystal structure at 1.95 Å resolution. Biochemistry. 37:1998;15277-15288
    • (1998) Biochemistry , vol.37 , pp. 15277-15288
    • Behnke, C.A.1    Yee, V.C.2    Le Trong, I.3    Pedersen, L.C.4    Stenkamp, R.E.5    Kim, S.-S.6    Reeck, G.R.7    Teller, D.C.8
  • 5
    • 0036634210 scopus 로고    scopus 로고
    • From elicitins to lipid-transfer proteins: A new insight in cell signalling involved in plant defence mechanisms
    • Blein J.P., Coutos-Thévenot P., Marion D., Ponchet M. From elicitins to lipid-transfer proteins: a new insight in cell signalling involved in plant defence mechanisms. Trends Plant Sci. 7:2002;293-296
    • (2002) Trends Plant Sci. , vol.7 , pp. 293-296
    • Blein, J.P.1    Coutos-Thévenot, P.2    Marion, D.3    Ponchet, M.4
  • 6
    • 0034615564 scopus 로고    scopus 로고
    • Structural basis of the endoproteinase-protein inhibitor interaction
    • Bode W., Huber R. Structural basis of the endoproteinase-protein inhibitor interaction. Biochim. Biophys. Acta. 1447:2000;241-252
    • (2000) Biochim. Biophys. Acta , vol.1447 , pp. 241-252
    • Bode, W.1    Huber, R.2
  • 7
    • 0001709760 scopus 로고
    • Leaf-specific thionins of barley a novel class of cell wall proteins toxic to plant-pathogenic fungi and possibly involved in the defence mechanism of plants
    • Bohlmann H., Clausen S., Behnke S., Giese H., Hiller C., Reimann-Philipp U., Schrader G., Barkholt V., Apel K. Leaf-specific thionins of barley a novel class of cell wall proteins toxic to plant-pathogenic fungi and possibly involved in the defence mechanism of plants. EMBO J. 7:1988;1559-1565
    • (1988) EMBO J. , vol.7 , pp. 1559-1565
    • Bohlmann, H.1    Clausen, S.2    Behnke, S.3    Giese, H.4    Hiller, C.5    Reimann-Philipp, U.6    Schrader, G.7    Barkholt, V.8    Apel, K.9
  • 8
    • 0035983610 scopus 로고    scopus 로고
    • Prediction of glycosylphoshati dylinositol-anchored proteins in Arabidopsis. A genomic analysis
    • Borner G.H.H., Sherrier J., Stevens T.J., Arkin I.T., Dupree P. Prediction of glycosylphoshati dylinositol-anchored proteins in Arabidopsis. A genomic analysis. Plant Physiol. 129:2002;486-499
    • (2002) Plant Physiol. , vol.129 , pp. 486-499
    • Borner, G.H.H.1    Sherrier, J.2    Stevens, T.J.3    Arkin, I.T.4    Dupree, P.5
  • 11
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defense system
    • Broekaert W.F., Terras F.R.G., Cammue B.P.A., Osborn R.W. Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol. 108:1995;1353-1358
    • (1995) Plant Physiol. , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.G.2    Cammue, B.P.A.3    Osborn, R.W.4
  • 14
    • 0023609276 scopus 로고
    • Interaction of trypsin, β-factor XIIa, and plasma Kallikrein with a trypsin inhibitor isolated from barley seeds: A comparison with the corn inhibitor of activated Hageman factor
    • Chong G.L., Reeck G.R. Interaction of trypsin, β-factor XIIa, and plasma Kallikrein with a trypsin inhibitor isolated from barley seeds: a comparison with the corn inhibitor of activated Hageman factor. Thrombosis Res. 48:1987;211-221
    • (1987) Thrombosis Res. , vol.48 , pp. 211-221
    • Chong, G.L.1    Reeck, G.R.2
  • 15
    • 0032982195 scopus 로고    scopus 로고
    • Cell-specific expression of genes of the lipid transfer protein family from Arabidopsis thaliana
    • Clark A.M., Bohnert H.J. Cell-specific expression of genes of the lipid transfer protein family from Arabidopsis thaliana. Plant Cell Physiol. 40:1999;69-76
    • (1999) Plant Cell Physiol. , vol.40 , pp. 69-76
    • Clark, A.M.1    Bohnert, H.J.2
  • 16
    • 0000939457 scopus 로고
    • The three-dimensional structure of α1-purothionin in solution: Combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics
    • Clore G.M., Nilges M., Sukumaran D.K., Brnnger A.T., Karplus M., Gronenborn A.M. The three-dimensional structure of α1-purothionin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J. 5:1986;2729-2735
    • (1986) EMBO J. , vol.5 , pp. 2729-2735
    • Clore, G.M.1    Nilges, M.2    Sukumaran, D.K.3    Brnnger, A.T.4    Karplus, M.5    Gronenborn, A.M.6
  • 17
    • 0030569330 scopus 로고    scopus 로고
    • Disulphide structure of a sunflower seed albumin: Conserved and variant disulphide bonds in the cereal prolamin superfamily
    • Egorov T.A., Odintsova T.I., Kh. Musolyamov A., Fido R., Tatham A.S., Shewry P.R. Disulphide structure of a sunflower seed albumin: conserved and variant disulphide bonds in the cereal prolamin superfamily. FEBS Lett. 396:1996;285-288
    • (1996) FEBS Lett. , vol.396 , pp. 285-288
    • Egorov, T.A.1    Odintsova, T.I.2    Kh. Musolyamov, A.3    Fido, R.4    Tatham, A.S.5    Shewry, P.R.6
  • 18
    • 0030725285 scopus 로고    scopus 로고
    • Three-dimensional solution structure of β cryptogein, a β elicitin secreted by a phytopathogenic fungus Phytophthora cryptogea
    • Fefeu S., Bouaziz S., Huet J.C., Pernollet J.-C., Guittet E. Three-dimensional solution structure of β cryptogein, a β elicitin secreted by a phytopathogenic fungus Phytophthora cryptogea. Protein Sci. 6:1997;2279-2284
    • (1997) Protein Sci. , vol.6 , pp. 2279-2284
    • Fefeu, S.1    Bouaziz, S.2    Huet, J.C.3    Pernollet, J.-C.4    Guittet, E.5
  • 21
    • 0028518533 scopus 로고
    • Thionins: Properties, possible biological roles and mechanisms of action
    • Florack D.E.A., Stiekema W.J. Thionins: properties, possible biological roles and mechanisms of action. Plant Mol. Biol. 26:1994;25-37
    • (1994) Plant Mol. Biol. , vol.26 , pp. 25-37
    • Florack, D.E.A.1    Stiekema, W.J.2
  • 22
    • 0028833949 scopus 로고
    • The defensive role of non-specific lipid-transfer proteins in plants
    • Garcia-Olmedo F., Molina A., Segura A., Moreno M. The defensive role of non-specific lipid-transfer proteins in plants. Trends Microbiol. 3:1995;72-74
    • (1995) Trends Microbiol. , vol.3 , pp. 72-74
    • Garcia-Olmedo, F.1    Molina, A.2    Segura, A.3    Moreno, M.4
  • 24
    • 0028406286 scopus 로고
    • Triticum aestivum puroindolines, two basic cysteine-rich seed proteins: CDNA sequence analysis and developmental gene expression
    • Gautier M.-F., Aleman M.-E., Guirao A., Marion D., Joudrier P. Triticum aestivum puroindolines, two basic cysteine-rich seed proteins: cDNA sequence analysis and developmental gene expression. Plant Mol. Biol. 25:1994;43-57
    • (1994) Plant Mol. Biol. , vol.25 , pp. 43-57
    • Gautier, M.-F.1    Aleman, M.-E.2    Guirao, A.3    Marion, D.4    Joudrier, P.5
  • 25
    • 0034646623 scopus 로고    scopus 로고
    • Puroindoline genes are highly conserved in diploid ancestor wheats and related species but absent in tetraploid Triticum species
    • Gautier M.F., Cosson P., Guirao A., Alary R., Joudrier P. Puroindoline genes are highly conserved in diploid ancestor wheats and related species but absent in tetraploid Triticum species. Science. 153:2000;81-91
    • (2000) Science , vol.153 , pp. 81-91
    • Gautier, M.F.1    Cosson, P.2    Guirao, A.3    Alary, R.4    Joudrier, P.5
  • 26
    • 0033180533 scopus 로고    scopus 로고
    • Hydrophobic protein synthesized in the pod endocarp adheres to the seed surface
    • Gijzen M., Miller S., Kuflu K., Buzzell R.I., Miki B.L.A. Hydrophobic protein synthesized in the pod endocarp adheres to the seed surface. Plant Physiol. 120:1999;951-959
    • (1999) Plant Physiol. , vol.120 , pp. 951-959
    • Gijzen, M.1    Miller, S.2    Kuflu, K.3    Buzzell, R.I.4    Miki, B.L.A.5
  • 28
    • 0030005766 scopus 로고    scopus 로고
    • Solution structure and lipid binding of a non-specific lipid transfer protein extracted from maize seeds
    • Gomar J., Ch. Petit M., Sodano P., Sy D., Marion D., Kader J.C., Vovelle F., Ptak M. Solution structure and lipid binding of a non-specific lipid transfer protein extracted from maize seeds. Protein Sci. 5:1996;565-577
    • (1996) Protein Sci. , vol.5 , pp. 565-577
    • Gomar, J.1    Ch. Petit, M.2    Sodano, P.3    Sy, D.4    Marion, D.5    Kader, J.C.6    Vovelle, F.7    Ptak, M.8
  • 29
    • 0029055249 scopus 로고
    • Soybean hydrophobic protein and soybean hull allergy
    • Gonzalez R., Varela J., Carreira J., Polo F. Soybean hydrophobic protein and soybean hull allergy. Lancet. 346:1995;48-49
    • (1995) Lancet , vol.346 , pp. 48-49
    • Gonzalez, R.1    Varela, J.2    Carreira, J.3    Polo, F.4
  • 30
    • 0345148433 scopus 로고    scopus 로고
    • Selection of Arabidopsis genes encoding secreted and plasma membrane proteins
    • Goo J.H., Park A.R., Park W.J., Park O.K. Selection of Arabidopsis genes encoding secreted and plasma membrane proteins. Plant Mol. Biol. 41:1999;415-423
    • (1999) Plant Mol. Biol. , vol.41 , pp. 415-423
    • Goo, J.H.1    Park, A.R.2    Park, W.J.3    Park, O.K.4
  • 31
    • 0034098039 scopus 로고    scopus 로고
    • Structure of the bifunctional inhibitor of trypsin and α-amylase from ragi seeds at 2.2 Å resolution
    • Gourinath S., Alam N., Srinivasan A., Betzel Ch., Singh T.P. Structure of the bifunctional inhibitor of trypsin and α-amylase from ragi seeds at 2.2 Å resolution. Acta Crystallogr. Sect. D. 56:2000;287-293
    • (2000) Acta Crystallogr. Sect. D , vol.56 , pp. 287-293
    • Gourinath, S.1    Alam, N.2    Srinivasan, A.3    Betzel, Ch.4    Singh, T.P.5
  • 32
    • 0000995388 scopus 로고
    • Differential expression of the Arabidopsis 2S-albumin genes and the effect of increasing gene family size
    • Guerche P., Tire Ch., de Sa F.G., De Clerq A., Van Montagu M., Krebbers E. Differential expression of the Arabidopsis 2S-albumin genes and the effect of increasing gene family size. Plant Cell. 2:1990;469-478
    • (1990) Plant Cell , vol.2 , pp. 469-478
    • Guerche, P.1    Tire, Ch.2    De Sa, F.G.3    De Clerq, A.4    Van Montagu, M.5    Krebbers, E.6
  • 34
    • 0024116660 scopus 로고
    • Hydrophobic-cluster analysis of plant protein sequences
    • Henrissat B., Popineau Y., Kader J.-C. Hydrophobic-cluster analysis of plant protein sequences. Biochem. J. 255:1988;901-905
    • (1988) Biochem. J. , vol.255 , pp. 901-905
    • Henrissat, B.1    Popineau, Y.2    Kader, J.-C.3
  • 35
    • 0037826923 scopus 로고    scopus 로고
    • Structure of petunia hybrida defensin 1, a novel plant defensin with five disulfide bonds
    • Janssen B.J., Schirra H.J., Lay F.T., Anderson M.A., Craik D.J. Structure of petunia hybrida defensin 1, a novel plant defensin with five disulfide bonds. Biochemistry. 42:2003;8214-8222
    • (2003) Biochemistry , vol.42 , pp. 8214-8222
    • Janssen, B.J.1    Schirra, H.J.2    Lay, F.T.3    Anderson, M.A.4    Craik, D.J.5
  • 36
    • 34250079623 scopus 로고
    • Characterization of the wheat Mr 15 000 "grain softness protein" and analysis of the relationship between its accumulation in the whole seed and grain softness
    • Jolly C.J., Rahman S., Kortt A.A., Higgins T.J.V. Characterization of the wheat Mr 15 000 "grain softness protein" and analysis of the relationship between its accumulation in the whole seed and grain softness. Theor. Appl. Genet. 86:1993;589-597
    • (1993) Theor. Appl. Genet. , vol.86 , pp. 589-597
    • Jolly, C.J.1    Rahman, S.2    Kortt, A.A.3    Higgins, T.J.V.4
  • 38
    • 0026847660 scopus 로고
    • A maize embryo-specific gene encodes a proline-rich and hydrophobic protein
    • Josè-Estanyol M., Ruiz-Avila L., Puigdomènech P. A maize embryo-specific gene encodes a proline-rich and hydrophobic protein. Plant Cell. 4:1992;413-423
    • (1992) Plant Cell , vol.4 , pp. 413-423
    • Josè-Estanyol, M.1    Ruiz-Avila, L.2    Puigdomènech, P.3
  • 40
    • 0032104150 scopus 로고    scopus 로고
    • Homology modelling and molecular dynamics aided analysis of ligand complexes demonstrates functional properties of lipid-transfer proteins encoded by the barley low-temperature-inducible gene family, blt4
    • Keresztessy Z., Hughes M.A. Homology modelling and molecular dynamics aided analysis of ligand complexes demonstrates functional properties of lipid-transfer proteins encoded by the barley low-temperature-inducible gene family, blt4. Plant J. 14:1998;523-533
    • (1998) Plant J. , vol.14 , pp. 523-533
    • Keresztessy, Z.1    Hughes, M.A.2
  • 41
    • 0034637684 scopus 로고    scopus 로고
    • Characterization of MZm3-3, a Zea mays tapetum-specific transcript
    • Lauga B., Charbonnel-Campaa L., Combes D. Characterization of MZm3-3, a Zea mays tapetum-specific transcript. Plant Sci. 157:2000;65-75
    • (2000) Plant Sci. , vol.157 , pp. 65-75
    • Lauga, B.1    Charbonnel-Campaa, L.2    Combes, D.3
  • 42
    • 0346665520 scopus 로고    scopus 로고
    • Isolation and properties of floral defensins from ornamental tobacco and petunia
    • Lay F.T., Brugliera F., Anderson M.A. Isolation and properties of floral defensins from ornamental tobacco and petunia. Plant Physiol. 131:2003;1283-1293
    • (2003) Plant Physiol. , vol.131 , pp. 1283-1293
    • Lay, F.T.1    Brugliera, F.2    Anderson, M.A.3
  • 43
    • 0032548996 scopus 로고    scopus 로고
    • Rice non-specific lipid transfer protein: The 1.6 Å crystal structure in the unliganded state reveals a small hydrophobic cavity
    • Lee J.Y., Min K., Cha H., Shin D.H., Hwang K.Y., Suh S.W. Rice non-specific lipid transfer protein: the 1.6 Å crystal structure in the unliganded state reveals a small hydrophobic cavity. J. Mol. Biol. 276:1998;437-448
    • (1998) J. Mol. Biol. , vol.276 , pp. 437-448
    • Lee, J.Y.1    Min, K.2    Cha, H.3    Shin, D.H.4    Hwang, K.Y.5    Suh, S.W.6
  • 44
    • 0031568810 scopus 로고    scopus 로고
    • Barley lipid-transfer protein complexed with palmitoyl CoA: The structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands
    • Lerche M.H., Kragelund B.B., Bech L.M., Poulsen F.M. Barley lipid-transfer protein complexed with palmitoyl CoA: the structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands. Structure. 5:1997;291-306
    • (1997) Structure , vol.5 , pp. 291-306
    • Lerche, M.H.1    Kragelund, B.B.2    Bech, L.M.3    Poulsen, F.M.4
  • 46
    • 0033067345 scopus 로고    scopus 로고
    • Isolation and characterization of cDNA clones corresponding with mRNAs that accumulate during auxin-induced lateral root formation
    • Neuteboom L.W., Ng J.M.Y., Kuyper M., Clijdesdale O.R., Hooykaas P.J.J., van der Zaal B.J. Isolation and characterization of cDNA clones corresponding with mRNAs that accumulate during auxin-induced lateral root formation. Plant Mol. Biol. 39:1999;273-287
    • (1999) Plant Mol. Biol. , vol.39 , pp. 273-287
    • Neuteboom, L.W.1    Ng, J.M.Y.2    Kuyper, M.3    Clijdesdale, O.R.4    Hooykaas, P.J.J.5    Van Der Zaal, B.J.6
  • 47
    • 0030815231 scopus 로고    scopus 로고
    • Tertiary and quaternary structures of 0.19 α-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 Å resolution
    • Oda Y., Matsunaga T., Fukuyama K., Miyazaki T., Morimoto T. Tertiary and quaternary structures of 0.19 α-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 Å resolution. Biochemistry. 36:1997;13503-13511
    • (1997) Biochemistry , vol.36 , pp. 13503-13511
    • Oda, Y.1    Matsunaga, T.2    Fukuyama, K.3    Miyazaki, T.4    Morimoto, T.5
  • 48
    • 0023641901 scopus 로고
    • Soybean hydrophobic protein. Isolation, partial characterization and the complete primary structure
    • Odani S., Koide T., Ono T., Seto Y., Tanaka T. Soybean hydrophobic protein. Isolation, partial characterization and the complete primary structure. Eur. J. Biochem. 162:1987;485-491
    • (1987) Eur. J. Biochem. , vol.162 , pp. 485-491
    • Odani, S.1    Koide, T.2    Ono, T.3    Seto, Y.4    Tanaka, T.5
  • 50
    • 0036105450 scopus 로고    scopus 로고
    • Recombinant pronapin precursor produced in Pichia pastoris displays structural and immunological equivalent properties to its mature product isolated from rapeseed
    • Palomares O., Monsalve R., Rodriguez R., Villalba M. Recombinant pronapin precursor produced in Pichia pastoris displays structural and immunological equivalent properties to its mature product isolated from rapeseed. Eur. J. Biochem. 269:2002;2538-2545
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2538-2545
    • Palomares, O.1    Monsalve, R.2    Rodriguez, R.3    Villalba, M.4
  • 51
    • 0344011459 scopus 로고    scopus 로고
    • Solution structure of RicC3, a 2S-albumin storage protein from Ricinus communis
    • Pantoja-Uceda D., Bruix M., Giménez-Gallego G., Rico M., Santero J. Solution structure of RicC3, a 2S-albumin storage protein from Ricinus communis. Biochemistry. 42:2003;13839-13847
    • (2003) Biochemistry , vol.42 , pp. 13839-13847
    • Pantoja-Uceda, D.1    Bruix, M.2    Giménez-Gallego, G.3    Rico, M.4    Santero, J.5
  • 54
    • 0026889350 scopus 로고
    • The isolation and characterisation of the tapetum-specific Arabidopsis thaliana A9 gene
    • Paul W., Hodge R., Smartt S., Draper J., Scott R. The isolation and characterisation of the tapetum-specific Arabidopsis thaliana A9 gene. Plant Mol. Biol. 19:1992;611-622
    • (1992) Plant Mol. Biol. , vol.19 , pp. 611-622
    • Paul, W.1    Hodge, R.2    Smartt, S.3    Draper, J.4    Scott, R.5
  • 55
    • 0033082341 scopus 로고    scopus 로고
    • Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins
    • Poznanski J., Sodano P., Suh S.W., Lee J.Y., Ptak M., Vovelle F. Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins. Eur. J. Biochem. 259:1999;692-708
    • (1999) Eur. J. Biochem. , vol.259 , pp. 692-708
    • Poznanski, J.1    Sodano, P.2    Suh, S.W.3    Lee, J.Y.4    Ptak, M.5    Vovelle, F.6
  • 56
    • 0001483359 scopus 로고
    • PEARLI1 (Accession No. L43080): An Arabidopsis member of a conserved gene family
    • Richards K.D., Gardner R.C. pEARLI1 (Accession No. L43080): an Arabidopsis member of a conserved gene family. Plant Physiol. 109:1995;1497
    • (1995) Plant Physiol. , vol.109 , pp. 1497
    • Richards, K.D.1    Gardner, R.C.2
  • 57
    • 0001144526 scopus 로고
    • Seed storage proteins: The enzyme inhibitors
    • Rogers L.J. London: Academic Press
    • Richardson M. Seed storage proteins: the enzyme inhibitors. Rogers L.J. Methods in Plant Biochemistry. 5:1991;259-305 Academic Press, London
    • (1991) Methods in Plant Biochemistry , vol.5 , pp. 259-305
    • Richardson, M.1
  • 59
    • 0000180578 scopus 로고
    • Proteinase inhibitors in plants: Genes for improving defenses against insects and pathogens
    • Ryan C.A. Proteinase inhibitors in plants: genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 28:1990;425-449
    • (1990) Annu. Rev. Phytopathol. , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 60
    • 0026511503 scopus 로고
    • Wheat and barley allergens associated with baker's asthma. Glycosylated subunits of the α-amylase-inhibitor family have enhanced IgE-binding capacity
    • Sanchez-Monge R., Gomez L., Barber D., Lopez-Otin C., Armentia A., Salcedo G. Wheat and barley allergens associated with baker's asthma. Glycosylated subunits of the α-amylase-inhibitor family have enhanced IgE-binding capacity. Biochem. J. 281:1992;401-405
    • (1992) Biochem. J. , vol.281 , pp. 401-405
    • Sanchez-Monge, R.1    Gomez, L.2    Barber, D.3    Lopez-Otin, C.4    Armentia, A.5    Salcedo, G.6
  • 61
    • 0029328357 scopus 로고
    • Seed storage proteins: Structures and biosynthesis
    • Shewry P.R., Napier J.A., Tatham A.S. Seed storage proteins: structures and biosynthesis. Plant Cell. 7:1995;945-956
    • (1995) Plant Cell , vol.7 , pp. 945-956
    • Shewry, P.R.1    Napier, J.A.2    Tatham, A.S.3
  • 62
    • 0025357314 scopus 로고
    • The prolamin storage proteins of cereal seeds: Structure and evolution
    • Shewry P.R., Tatham A.S. The prolamin storage proteins of cereal seeds: structure and evolution. Biochem. J. 267:1990;1-12
    • (1990) Biochem. J. , vol.267 , pp. 1-12
    • Shewry, P.R.1    Tatham, A.S.2
  • 63
    • 0029643949 scopus 로고
    • High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings
    • Shin D.H., Lee J.Y., Hwang K.Y., Kim K.K., Suh S.W. High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings. Structure. 3:1995;189-199
    • (1995) Structure , vol.3 , pp. 189-199
    • Shin, D.H.1    Lee, J.Y.2    Hwang, K.Y.3    Kim, K.K.4    Suh, S.W.5
  • 65
    • 0030613687 scopus 로고    scopus 로고
    • 1H NMR and fluorescence studies of the complexation of DMPG by wheat non-specific lipid transfer protein. Global fold of the complex
    • 1H NMR and fluorescence studies of the complexation of DMPG by wheat non-specific lipid transfer protein. Global fold of the complex. FEBS Lett. 416:1997;130-134
    • (1997) FEBS Lett. , vol.416 , pp. 130-134
    • Sodano, P.1    Caille, A.2    Sy, D.3    De Person, G.4    Marion, D.5    Ptak, M.6
  • 67
    • 0032528247 scopus 로고    scopus 로고
    • A novel strategy for inhibition of α-amylases: Yellow meal worm α-amylase in complex with the Ragi bifunctional inhibitor at 2.5 Å resolution
    • Strobl S., Maskos K., Wiegand G., Huber R., Gomis-Rüth F.X., Glockshuber R. A novel strategy for inhibition of α-amylases: yellow meal worm α-amylase in complex with the Ragi bifunctional inhibitor at 2.5 Å resolution. Structure. 6:1998;911-921
    • (1998) Structure , vol.6 , pp. 911-921
    • Strobl, S.1    Maskos, K.2    Wiegand, G.3    Huber, R.4    Gomis-Rüth, F.X.5    Glockshuber, R.6
  • 68
    • 0016174105 scopus 로고
    • Crystal structure of the complex of porcine trypsin soybean trypsin inhibitor (Kunitz) at 2.6 Å resolution
    • Sweet R.M., Wright H.T., Janin J., Chotia C.H., Blow D.M. Crystal structure of the complex of porcine trypsin soybean trypsin inhibitor (Kunitz) at 2.6 Å resolution. Biochemistry. 13:1974;4212-4228
    • (1974) Biochemistry , vol.13 , pp. 4212-4228
    • Sweet, R.M.1    Wright, H.T.2    Janin, J.3    Chotia, C.H.4    Blow, D.M.5
  • 69
    • 0032539972 scopus 로고    scopus 로고
    • Solution structure of Ace-AMP1, a potent antimicrobial protein extracted from onion seeds. Structural analogies with plant non-specific lipid transfer proteins
    • Tassin S., Broekaert W.F., Marion D., Acland D.P., Ptack M., Vovelle F., Sodano P. Solution structure of Ace-AMP1, a potent antimicrobial protein extracted from onion seeds. Structural analogies with plant non-specific lipid transfer proteins. Biochemistry. 37:1998;3623-3637
    • (1998) Biochemistry , vol.37 , pp. 3623-3637
    • Tassin, S.1    Broekaert, W.F.2    Marion, D.3    Acland, D.P.4    Ptack, M.5    Vovelle, F.6    Sodano, P.7
  • 70
    • 0002436112 scopus 로고
    • Conformational studies of peptides derived by the enzymic hydrolysis of a gamma-type gliadin
    • Tatham A.S., Masson P., Popineau Y. Conformational studies of peptides derived by the enzymic hydrolysis of a gamma-type gliadin. J. Cereal Sci. 11:1990;1-13
    • (1990) J. Cereal Sci. , vol.11 , pp. 1-13
    • Tatham, A.S.1    Masson, P.2    Popineau, Y.3
  • 71
    • 0001469527 scopus 로고
    • In vitro antifungal activity of a radish (Raphanus sativus L.) seed protein homologous to nonspecific lipid transfer proteins
    • Terras F.R.G., Goderis I.J., Van Leuven F., Vanderleyden J., Cammue B.P.A., Broekaert W.F. In vitro antifungal activity of a radish (Raphanus sativus L.) seed protein homologous to nonspecific lipid transfer proteins. Plant Physiol. 100:1992;1055-1058
    • (1992) Plant Physiol. , vol.100 , pp. 1055-1058
    • Terras, F.R.G.1    Goderis, I.J.2    Van Leuven, F.3    Vanderleyden, J.4    Cammue, B.P.A.5    Broekaert, W.F.6
  • 72
    • 0028428501 scopus 로고
    • Tissue-specific expression of a gene encoding a cell wall-localized lipid transfer protein from Arabidopsis
    • Thoma S., Hecht U., Kippers A., Botella J., De Vries S., Somerville C. Tissue-specific expression of a gene encoding a cell wall-localized lipid transfer protein from Arabidopsis. Plant Physiol. 105:1994;35-45
    • (1994) Plant Physiol. , vol.105 , pp. 35-45
    • Thoma, S.1    Hecht, U.2    Kippers, A.3    Botella, J.4    De Vries, S.5    Somerville, C.6
  • 73
    • 0027568154 scopus 로고
    • A non-specific lipid transfer protein from Arabidopsis is a cell wall protein
    • Thoma S., Kaneko Y., Somerville C. A non-specific lipid transfer protein from Arabidopsis is a cell wall protein. Plant J. 3:1993;427-436
    • (1993) Plant J. , vol.3 , pp. 427-436
    • Thoma, S.1    Kaneko, Y.2    Somerville, C.3
  • 74
    • 0028981209 scopus 로고
    • How glycosyl-phosphatidy linositol-anchored membrane proteins are made
    • Udenfriend S., Kodukula K. How glycosyl-phosphatidy linositol-anchored membrane proteins are made. Annu. Rev. Biochem. 64:1995;563-591
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 563-591
    • Udenfriend, S.1    Kodukula, K.2
  • 75
    • 0032524130 scopus 로고    scopus 로고
    • Barley α-amylase bound to its endogenous protein inhibitor BASI: Crystal structure of the complex at 1.9 Å resolution
    • Vallée F., Kadziola A., Bourne Y., Juy M., Rodenburg K.W., Svensson B., Haser R. Barley α-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 Å resolution. Structure. 6:1998;649-659
    • (1998) Structure , vol.6 , pp. 649-659
    • Vallée, F.1    Kadziola, A.2    Bourne, Y.3    Juy, M.4    Rodenburg, K.W.5    Svensson, B.6    Haser, R.7
  • 77
    • 0030814238 scopus 로고    scopus 로고
    • Rice lipid transfer protein (LTP) genes belong to a complex multigene family and are differentially regulated
    • Vignols F., Wigger M., Garcia Garrido J.M., Grellet F., Kader J.C., Delseny M. Rice lipid transfer protein (LTP) genes belong to a complex multigene family and are differentially regulated. Gene. 195:1997;177-186
    • (1997) Gene , vol.195 , pp. 177-186
    • Vignols, F.1    Wigger, M.2    Garcia Garrido, J.M.3    Grellet, F.4    Kader, J.C.5    Delseny, M.6
  • 78
    • 0029658121 scopus 로고    scopus 로고
    • Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation
    • Voss R.H., Ermler U., Essen L.-O., Wenzl G., Kim Y.-M., Flecker P. Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation. Eur. J. Biochem. 242:1996;122-131
    • (1996) Eur. J. Biochem. , vol.242 , pp. 122-131
    • Voss, R.H.1    Ermler, U.2    Essen, L.-O.3    Wenzl, G.4    Kim, Y.-M.5    Flecker, P.6
  • 79
    • 0034764976 scopus 로고    scopus 로고
    • Genomics analysis of genes expressed in maize endosperm identifies novel seed proteins and clarifies patterns of zein gene expression
    • Woo Y.-M., Hu D.W.-N., Larkins B.A., Jung R. Genomics analysis of genes expressed in maize endosperm identifies novel seed proteins and clarifies patterns of zein gene expression. Plant Cell. 13:2001;2297-2317
    • (2001) Plant Cell , vol.13 , pp. 2297-2317
    • Woo, Y.-M.1    Hu, D.W.-N.2    Larkins, B.A.3    Jung, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.