메뉴 건너뛰기




Volumn 63, Issue 4, 2006, Pages 777-786

Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids

Author keywords

amylase inhibitory activity; CS motif; Insecticidal activity; Plant defensin; VrD1

Indexed keywords

AMYLASE; AMYLASE INHIBITOR; ARGININE; DEFENSIN; STARCH; VEGETABLE PROTEIN;

EID: 33646807759     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1109/JMEMS.2006.878881     Document Type: Article
Times cited : (94)

References (52)
  • 1
    • 0025080513 scopus 로고
    • γ-purothionins: Amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm
    • Colilla FJ, Rocher A, Mendez E. γ-Purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. FEBS Lett 1990;270(1-2):191-194.
    • (1990) FEBS Lett , vol.270 , Issue.1-2 , pp. 191-194
    • Colilla, F.J.1    Rocher, A.2    Mendez, E.3
  • 2
    • 0025670589 scopus 로고
    • Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, γ-hordothionin, from barley endosperm
    • Mendez E, Moreno A, Colilla F, et al. Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, γ-hordothionin, from barley endosperm. Eur J Biochem 1990;194(2):533-539.
    • (1990) Eur J Biochem , vol.194 , Issue.2 , pp. 533-539
    • Mendez, E.1    Moreno, A.2    Colilla, F.3
  • 3
    • 0025976182 scopus 로고
    • A new family of small (5 kDa) protein inhibitors of insect α-amylases from seeds or sorghum (Sorghum bicolar (L) Moench) have sequence homologies with wheat ã-puro-thionins
    • Bloch C Jr, Richardson M. A new family of small (5 kDa) protein inhibitors of insect α-amylases from seeds or sorghum (Sorghum bicolar (L) Moench) have sequence homologies with wheat ã-puro-thionins. FEBS Lett 1991;279(1):101-104.
    • (1991) FEBS Lett , vol.279 , Issue.1 , pp. 101-104
    • Bloch Jr., C.1    Richardson, M.2
  • 4
    • 0034660557 scopus 로고    scopus 로고
    • Characterization of two novel defense peptides from pea (Pisum sativum) seeds
    • Almeida MS, Cabral KM, Zingali RB, Kurtenbach E. Characterization of two novel defense peptides from pea (Pisum sativum) seeds. Arch Biochem Biophys 2000;378(2):278-286.
    • (2000) Arch Biochem Biophys , vol.378 , Issue.2 , pp. 278-286
    • Almeida, M.S.1    Cabral, K.M.2    Zingali, R.B.3    Kurtenbach, E.4
  • 5
    • 0026635585 scopus 로고
    • Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds
    • Terras FR, Schoofs HM, De Bolle MF, et al. Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds. J Biol Chem 1992;267(22):15301-15309.
    • (1992) J Biol Chem , vol.267 , Issue.22 , pp. 15301-15309
    • Terras, F.R.1    Schoofs, H.M.2    De Bolle, M.F.3
  • 6
    • 0037021614 scopus 로고    scopus 로고
    • A novel defensin encoded by a mungbean cDNA exhibits insecticidal activity against bruchid
    • Chen KC, Lin CY, Kuan CC, Sung HY, Chen CS. A novel defensin encoded by a mungbean cDNA exhibits insecticidal activity against bruchid. J Agric Food Chem 2002;50(25):7258-7263.
    • (2002) J Agric Food Chem , vol.50 , Issue.25 , pp. 7258-7263
    • Chen, K.C.1    Lin, C.Y.2    Kuan, C.C.3    Sung, H.Y.4    Chen, C.S.5
  • 8
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defense system
    • Broekaert WF, Terras FR, Cammue BP, Osborn RW. Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol 1995;108(4):1353-1358.
    • (1995) Plant Physiol , vol.108 , Issue.4 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.2    Cammue, B.P.3    Osborn, R.W.4
  • 9
    • 0030758347 scopus 로고    scopus 로고
    • Purification and characterization of a new class of insect α-amylase inhibitors from barley
    • Zhang N, Jones BL, Tao HP. Purification and characterization of a new class of insect α-amylase inhibitors from barley. Cereal Chem 1997;74(2):119-122.
    • (1997) Cereal Chem , vol.74 , Issue.2 , pp. 119-122
    • Zhang, N.1    Jones, B.L.2    Tao, H.P.3
  • 10
    • 0034613541 scopus 로고    scopus 로고
    • Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin
    • Wijaya R, Neumann GM, Condron R, Hughes AB, Polya GM. Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin. Plant Sci 2000;159(2):243-255.
    • (2000) Plant Sci , vol.159 , Issue.2 , pp. 243-255
    • Wijaya, R.1    Neumann, G.M.2    Condron, R.3    Hughes, A.B.4    Polya, G.M.5
  • 11
    • 0036681427 scopus 로고    scopus 로고
    • Inhibition of trypsin by cowpea thionin: Characterization, molecular modeling, and docking
    • Melo FR, Rigden DJ, Franco OL, et al. Inhibition of trypsin by cowpea thionin: characterization, molecular modeling, and docking. Proteins 2002;48(2):311-319.
    • (2002) Proteins , vol.48 , Issue.2 , pp. 311-319
    • Melo, F.R.1    Rigden, D.J.2    Franco, O.L.3
  • 12
    • 0032436013 scopus 로고    scopus 로고
    • Functional and structural features of γ-zeathionins, a new class of sodium channel blockers
    • Kushmerick C, de Souza Castro M, Santos Cruz J, Bloch C Jr, Beirao PS. Functional and structural features of γ-zeathionins, a new class of sodium channel blockers. FEBS Lett 1998;440(3):302-306.
    • (1998) FEBS Lett , vol.440 , Issue.3 , pp. 302-306
    • Kushmerick, C.1    De Souza Castro, M.2    Santos Cruz, J.3    Bloch Jr., C.4    Beirao, P.S.5
  • 13
    • 0029897150 scopus 로고    scopus 로고
    • Primary structure of omega-hordothionin, a member of a novel family of thionins from barley endosperm, and its inhibition of protein synthesis in eukaryotic and prokaryotic cell-free systems
    • Mendez E, Rocher A, Calero M, Girbes T, Citores L, Soriano F. Primary structure of omega-hordothionin, a member of a novel family of thionins from barley endosperm, and its inhibition of protein synthesis in eukaryotic and prokaryotic cell-free systems. Eur J Biochem 1996;239(1):67-73.
    • (1996) Eur J Biochem , vol.239 , Issue.1 , pp. 67-73
    • Mendez, E.1    Rocher, A.2    Calero, M.3    Girbes, T.4    Citores, L.5    Soriano, F.6
  • 14
    • 0027395308 scopus 로고
    • 1H-NMR: A structural motif common to toxic arthropod proteins
    • 1H-NMR: a structural motif common to toxic arthropod proteins. Biochemistry 1993;32(2):715-724.
    • (1993) Biochemistry , vol.32 , Issue.2 , pp. 715-724
    • Bruix, M.1    Jimenez, M.A.2    Santoro, J.3
  • 17
    • 0037260694 scopus 로고    scopus 로고
    • The three-dimensional solution structure of NaD1, a new floral defensin from Nicotiana alata and its application to a homology model of the crop defense protein alfAFP
    • Lay FT, Schirra HJ, Scanlon MJ, Anderson MA, Craik DJ. The three-dimensional solution structure of NaD1, a new floral defensin from Nicotiana alata and its application to a homology model of the crop defense protein alfAFP. J Mol Biol 2003;325(1):175-188.
    • (2003) J Mol Biol , vol.325 , Issue.1 , pp. 175-188
    • Lay, F.T.1    Schirra, H.J.2    Scanlon, M.J.3    Anderson, M.A.4    Craik, D.J.5
  • 18
    • 0036301039 scopus 로고    scopus 로고
    • Solution structure of Pisum sativum defensin 1 by high resolution NMR: Plant defensins, identical backbone with different mechanisms of action
    • Almeida MS, Cabral KM, Kurtenbach E, Almeida FC, Valente AP. Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action. J Mol Biol 2002;315(4):749-757.
    • (2002) J Mol Biol , vol.315 , Issue.4 , pp. 749-757
    • Almeida, M.S.1    Cabral, K.M.2    Kurtenbach, E.3    Almeida, F.C.4    Valente, A.P.5
  • 19
    • 0037826923 scopus 로고    scopus 로고
    • Structure of Petunia hybrida defensin 1, a novel plant defensin with five disulfide bonds
    • Janssen BJ, Schirra HJ, Lay FT, Anderson MA, Craik DJ. Structure of Petunia hybrida defensin 1, a novel plant defensin with five disulfide bonds. Biochemistry 2003;42(27):8214-8222.
    • (2003) Biochemistry , vol.42 , Issue.27 , pp. 8214-8222
    • Janssen, B.J.1    Schirra, H.J.2    Lay, F.T.3    Anderson, M.A.4    Craik, D.J.5
  • 21
    • 0030750976 scopus 로고    scopus 로고
    • Solution structure of drosomycin, the first inducible antifungal protein from insects
    • Landon C, Sodano P, Hetru C, Hoffmann J, Ptak M. Solution structure of drosomycin, the first inducible antifungal protein from insects. Protein Sci 1997;6(9):1878-1884.
    • (1997) Protein Sci , vol.6 , Issue.9 , pp. 1878-1884
    • Landon, C.1    Sodano, P.2    Hetru, C.3    Hoffmann, J.4    Ptak, M.5
  • 22
    • 0025974392 scopus 로고
    • 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins
    • 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins. Eur J Biochem 1991;196(1):19-28.
    • (1991) Eur J Biochem , vol.196 , Issue.1 , pp. 19-28
    • Bontems, F.1    Roumestand, C.2    Boyot, P.3
  • 24
    • 1842783692 scopus 로고    scopus 로고
    • Cloning and functional expression of a mungbean defensin VrD1 in Pichia pastoris
    • Chen JJ, Chen GH, Hsu HC, Li SS, Chen CS. Cloning and functional expression of a mungbean defensin VrD1 in Pichia pastoris. J Agric Food Chem 2004;52(8):2256-2261.
    • (2004) J Agric Food Chem , vol.52 , Issue.8 , pp. 2256-2261
    • Chen, J.J.1    Chen, G.H.2    Hsu, H.C.3    Li, S.S.4    Chen, C.S.5
  • 25
    • 0029014273 scopus 로고
    • Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae
    • Osborn RW, De Samblanx GW, Thevissen K, et al. Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae. FEBS Lett 1995; 368(2):257-262.
    • (1995) FEBS Lett , vol.368 , Issue.2 , pp. 257-262
    • Osborn, R.W.1    De Samblanx, G.W.2    Thevissen, K.3
  • 26
    • 0036164521 scopus 로고    scopus 로고
    • Plant α-amylase inhibitors and their interaction with insect α-amylases
    • Franco OL, Rigden DJ, Melo FR, Grossi-De-Sa MF. Plant α-amylase inhibitors and their interaction with insect α-amylases. Eur J Biochem 2002;269(2):397-412.
    • (2002) Eur J Biochem , vol.269 , Issue.2 , pp. 397-412
    • Franco, O.L.1    Rigden, D.J.2    Melo, F.R.3    Grossi-De-Sa, M.F.4
  • 27
    • 0006750734 scopus 로고    scopus 로고
    • Specific inhibition of insect α-amylases: Yellow meal worm α-amylase in complex with the amaranth α-amylase inhibitor at 2.0 Å resolution
    • Pereira PJ, Lozanov V, Patthy A, et al. Specific inhibition of insect α-amylases: yellow meal worm α-amylase in complex with the amaranth α-amylase inhibitor at 2.0 Å resolution. Structure 1999;7(9):1079-1088.
    • (1999) Structure , vol.7 , Issue.9 , pp. 1079-1088
    • Pereira, P.J.1    Lozanov, V.2    Patthy, A.3
  • 28
    • 13044305839 scopus 로고    scopus 로고
    • A plant-seed inhibitor of two classes of α-amylases: X-ray analysis of Tenebrio molitor larvae α-amylase in complex with the bean Phaseolus vulgaris inhibitor
    • Nahoum V, Farisei F, Le-Berre-Anton V, et al. A plant-seed inhibitor of two classes of α-amylases: X-ray analysis of Tenebrio molitor larvae α-amylase in complex with the bean Phaseolus vulgaris inhibitor. Acta Crystallogr D Biol Crystallogr 1999;55(Pt 1):360-362.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , Issue.PART 1 , pp. 360-362
    • Nahoum, V.1    Farisei, F.2    Le-Berre-Anton, V.3
  • 29
    • 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-Ruth FX, 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 1998;6(7):911-921.
    • (1998) Structure , vol.6 , Issue.7 , pp. 911-921
    • Strobl, S.1    Maskos, K.2    Wiegand, G.3    Huber, R.4    Gomis-Ruth, F.X.5    Glockshuber, R.6
  • 30
    • 0016291686 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 Å resolution
    • Huber R, Kukla D, Bode W, Schwager P, Bartels K, Deisenhofer J, Steigemann W. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 Å resolution. J Mol Biol 1974;89(1):73-101.
    • (1974) J Mol Biol , vol.89 , Issue.1 , pp. 73-101
    • Huber, R.1    Kukla, D.2    Bode, W.3    Schwager, P.4    Bartels, K.5    Deisenhofer, J.6    Steigemann, W.7
  • 31
    • 0022998680 scopus 로고
    • Structure of the trypsin-binding domain of Bowman-Birk type protease inhibitor and its interaction with trypsin
    • Tsunogae Y, Tanaka I, Yamane T, et al. Structure of the trypsin-binding domain of Bowman-Birk type protease inhibitor and its interaction with trypsin. J Biochem (Tokyo) 1986;100(6):1637-1646.
    • (1986) J Biochem (Tokyo) , vol.100 , Issue.6 , pp. 1637-1646
    • Tsunogae, Y.1    Tanaka, I.2    Yamane, T.3
  • 32
    • 0024959382 scopus 로고
    • The refined 2.0 Å X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes
    • Bode W, Greyling HJ, Huber R, Otlewski J, Wilusz T. The refined 2.0 Å X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes. FEBS Lett 1989;242(2):285-292.
    • (1989) FEBS Lett , vol.242 , Issue.2 , pp. 285-292
    • Bode, W.1    Greyling, H.J.2    Huber, R.3    Otlewski, J.4    Wilusz, T.5
  • 33
    • 0033575275 scopus 로고    scopus 로고
    • Solution structure of the major α-amylase inhibitor of the crop plant amaranth
    • Lu S, Deng P, Liu X, et al. Solution structure of the major α-amylase inhibitor of the crop plant amaranth. J Biol Chem 1999;274(29):20473-20478.
    • (1999) J Biol Chem , vol.274 , Issue.29 , pp. 20473-20478
    • Lu, S.1    Deng, P.2    Liu, X.3
  • 34
    • 0004757060 scopus 로고    scopus 로고
    • San Francisco: University of California
    • Goddard TD, Kneller DG. SPARKY. San Francisco: University of California; 1999.
    • (1999) SPARKY
    • Goddard, T.D.1    Kneller, D.G.2
  • 35
    • 0021764813 scopus 로고
    • HNHα identification of helical secondary structure
    • HNHα identification of helical secondary structure. J Mol Biol 1984;180(3):741-751.
    • (1984) J Mol Biol , vol.180 , Issue.3 , pp. 741-751
    • Pardi, A.1    Billeter, M.2    Wuthrich, K.3
  • 37
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 1996;8(4):477-486.
    • (1996) J Biomol NMR , vol.8 , Issue.4 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 38
    • 0342378173 scopus 로고    scopus 로고
    • The α-amylase from the yellow meal worm: Complete primary structure, crystallization and preliminary X-ray analysis
    • Strobl S, Gomis-Ruth FX, Maskos K, Frank G, Huber R, Glockshuber R. The α-amylase from the yellow meal worm: complete primary structure, crystallization and preliminary X-ray analysis. FEBS Lett 1997;409(1):109-114.
    • (1997) FEBS Lett , vol.409 , Issue.1 , pp. 109-114
    • Strobl, S.1    Gomis-Ruth, F.X.2    Maskos, K.3    Frank, G.4    Huber, R.5    Glockshuber, R.6
  • 39
    • 0038237369 scopus 로고    scopus 로고
    • Taking geometry to its edge: Fast unbound rigid (and hinge-bent) docking
    • Schneidman-Duhovny D, Inbar Y, Polak V, et al. Taking geometry to its edge: fast unbound rigid (and hinge-bent) docking. Proteins 2003;52(1):107-112.
    • (2003) Proteins , vol.52 , Issue.1 , pp. 107-112
    • Schneidman-Duhovny, D.1    Inbar, Y.2    Polak, V.3
  • 40
    • 18744435626 scopus 로고    scopus 로고
    • Crystal structure of yellow meal worm α-amylase at 1.64 Å resolution
    • Strobl S, Maskos K, Betz M, et al. Crystal structure of yellow meal worm α-amylase at 1.64 Å resolution. J Mol Biol 1998;278(3):617-628.
    • (1998) J Mol Biol , vol.278 , Issue.3 , pp. 617-628
    • Strobl, S.1    Maskos, K.2    Betz, M.3
  • 41
    • 0033995602 scopus 로고    scopus 로고
    • Molecular modeling of substrate binding in wild-type and mutant corynebacteria 2,5-diketo-D-gluconate reductases
    • Khurana S, Sanli G, Powers DB, Anderson S, Blaber M. Molecular modeling of substrate binding in wild-type and mutant corynebacteria 2,5-diketo-D- gluconate reductases. Proteins 2000;39(1):68-75.
    • (2000) Proteins , vol.39 , Issue.1 , pp. 68-75
    • Khurana, S.1    Sanli, G.2    Powers, D.B.3    Anderson, S.4    Blaber, M.5
  • 42
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S, Thornton JM. Principles of protein-protein interactions. Proc Natl Acad Sci USA 1996;93(1):13-20.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.1 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 43
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 1995;8(2):127-134.
    • (1995) Protein Eng , vol.8 , Issue.2 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 45
    • 0036842625 scopus 로고    scopus 로고
    • Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides
    • Carlini CR, Grossi-de-Sa MF. Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides. Toxicon 2002;40(11):1515-1539.
    • (2002) Toxicon , vol.40 , Issue.11 , pp. 1515-1539
    • Carlini, C.R.1    Grossi-De-Sa, M.F.2
  • 46
    • 0028041555 scopus 로고
    • Transgenic pea seeds expressing the a-amylase inhibitor of the common bean are resistant to bruchid beetles
    • Shade RE, Schroeder HE, Pueyo JJ, et al. Transgenic pea seeds expressing the a-amylase inhibitor of the common bean are resistant to bruchid beetles. Biotechnology 1994;12:793-796.
    • (1994) Biotechnology , vol.12 , pp. 793-796
    • Shade, R.E.1    Schroeder, H.E.2    Pueyo, J.J.3
  • 47
    • 0034635993 scopus 로고    scopus 로고
    • Bean α-amylase inhibitor 1 in transgenic peas (Pisum sativum) provides complete protection from pea weevil (Bruchus pisorum) under field conditions
    • Morton RL, Schroeder HE, Bateman KS, Chrispeels MJ, Armstrong E, Higgins TJ. Bean α-amylase inhibitor 1 in transgenic peas (Pisum sativum) provides complete protection from pea weevil (Bruchus pisorum) under field conditions. Proc Natl Acad Sci USA 2000;97(8):3820-3825.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.8 , pp. 3820-3825
    • Morton, R.L.1    Schroeder, H.E.2    Bateman, K.S.3    Chrispeels, M.J.4    Armstrong, E.5    Higgins, T.J.6
  • 48
    • 0034017054 scopus 로고    scopus 로고
    • Analysis of structural and physico-chemical parameters involved in the specificity of binding between α-amylases and their inhibitors
    • Da Silva MC, de Sa MF, Chrispeels MJ, Togawa RC, Neshich G. Analysis of structural and physico-chemical parameters involved in the specificity of binding between α-amylases and their inhibitors. Protein Eng 2000;13(3):167-177.
    • (2000) Protein Eng , vol.13 , Issue.3 , pp. 167-177
    • Da Silva, M.C.1    De Sa, M.F.2    Chrispeels, M.J.3    Togawa, R.C.4    Neshich, G.5
  • 49
    • 3242737664 scopus 로고    scopus 로고
    • Mutants of common bean α-amylase inhibitor-2 as an approach to investigate binding specificity to α-amylases
    • Da Silva MC, Mello LV, Coutinho MV, et al. Mutants of common bean α-amylase inhibitor-2 as an approach to investigate binding specificity to α-amylases. Pesquisa Agropecuaria Brasileira 2004; 39(3):201-208.
    • (2004) Pesquisa Agropecuaria Brasileira , vol.39 , Issue.3 , pp. 201-208
    • Da Silva, M.C.1    Mello, L.V.2    Coutinho, M.V.3
  • 50
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22(22):4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 51
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996;14(1):51-55, 29-32.
    • (1996) J Mol Graph , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 52
    • 33646777163 scopus 로고    scopus 로고
    • San Diego, CA: Accelrys Inc.
    • DiscoveryStudio. San Diego, CA: Accelrys Inc.; 2002.
    • (2002) DiscoveryStudio


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.