메뉴 건너뛰기




Volumn 39, Issue 1, 2001, Pages 43-60

The cystine knot motif in toxins and implications for drug design

Author keywords

Cyclic cystine knot; Cyclotides; Inhibitor cystine knot; Kalata; Knotted proteins

Indexed keywords

ANTIRETROVIRUS AGENT; CIRCULIN; CIRCULIN C; CIRCULIN D; CIRCULIN E; CIRCULIN F; CYCLOVIOLIN A; CYCLOVIOLIN B; CYCLOVIOLIN C; CYCLOVIOLIN D; CYSTINE; OMEGA CONOTOXIN MVIIA; OMEGA CONOTOXIN MVIIC; TOXIN; UNCLASSIFIED DRUG;

EID: 0035239222     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(00)00160-4     Document Type: Short Survey
Times cited : (432)

References (69)
  • 1
    • 0027465807 scopus 로고
    • Disulfide bonding patterns and protein topologies
    • Benham C.J., Jafri M.S. Disulfide bonding patterns and protein topologies. Protein Sci. 2:1993;41-54.
    • (1993) Protein Sci. , vol.2 , pp. 41-54
    • Benham, C.J.1    Jafri, M.S.2
  • 4
    • 0034708453 scopus 로고    scopus 로고
    • The underlying mechanism for the diversity of disulfide folding pathways
    • Chang J.Y., Li L., Bulychev A. The underlying mechanism for the diversity of disulfide folding pathways. J. Biol. Chem. 275:2000;8287-8289.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8287-8289
    • Chang, J.Y.1    Li, L.2    Bulychev, A.3
  • 5
    • 0024846405 scopus 로고
    • Use of restrained molecular dynamics in water to determine three-dimensional protein structure: Prediction of the three-dimensional structure of Ecballium elaterium trypsin inhibitor II
    • Chiche L., Gaboriaud C., Heitz A., Mornon J.P., Castro B., Kollman P.A. Use of restrained molecular dynamics in water to determine three-dimensional protein structure: prediction of the three-dimensional structure of Ecballium elaterium trypsin inhibitor II. Proteins. 6:1989;405-417.
    • (1989) Proteins , vol.6 , pp. 405-417
    • Chiche, L.1    Gaboriaud, C.2    Heitz, A.3    Mornon, J.P.4    Castro, B.5    Kollman, P.A.6
  • 6
    • 0027423755 scopus 로고
    • Solution conformation of a synthetic bis-headed inhibitor of trypsin and carboxypeptidase A: New structural alignment between the squash inhibitors and the potato carboxypeptidase inhibitor
    • Chiche L., Heitz A., Padilla A., Le-Nguyen D., Castro B. Solution conformation of a synthetic bis-headed inhibitor of trypsin and carboxypeptidase A: new structural alignment between the squash inhibitors and the potato carboxypeptidase inhibitor. Prot. Engin. 7:1993;675-682.
    • (1993) Prot. Engin. , vol.7 , pp. 675-682
    • Chiche, L.1    Heitz, A.2    Padilla, A.3    Le-Nguyen, D.4    Castro, B.5
  • 7
    • 0032824531 scopus 로고    scopus 로고
    • The cystine knot of a squash-type protease inhibitor as a structural scaffold for Esherichia coli cell surface display of conformationally constrained peptides
    • Christmann A., Walter K., Wentzel A., Krötzner R., Kolmar H. The cystine knot of a squash-type protease inhibitor as a structural scaffold for Esherichia coli cell surface display of conformationally constrained peptides. Protein Eng. 12:1999;797-806.
    • (1999) Protein Eng. , vol.12 , pp. 797-806
    • Christmann, A.1    Walter, K.2    Wentzel, A.3    Krötzner, R.4    Kolmar, H.5
  • 9
    • 0033579483 scopus 로고    scopus 로고
    • Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif
    • Craik D.J., Daly N.L., Bond T., Waine C. Plant cyclotides: a unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. J. Mol. Biol. 294:1999;1327-1336.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1327-1336
    • Craik, D.J.1    Daly, N.L.2    Bond, T.3    Waine, C.4
  • 10
    • 0034705410 scopus 로고    scopus 로고
    • Acyclic permutants of naturally occurring cyclic proteins: Characterization of cystine knot and β-sheet formation in the macrocyclic polypeptide kalata B1
    • Daly, N.L., Craik, D.J., 2000. Acyclic permutants of naturally occurring cyclic proteins: characterization of cystine knot and β-sheet formation in the macrocyclic polypeptide kalata B1. J. Biol. Chem. 275, 19068-19075.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19068-19075
    • Daly, N.L.1    Craik, D.J.2
  • 11
    • 0033534366 scopus 로고    scopus 로고
    • Solution structure by NMR of circulin A: A macrocyclic knotted peptide having anti-HIV activity
    • Daly N.L., Koltay A., Gustafson K.R., Boyd M.R., Casas-Finet J.R., Craik D.J. Solution structure by NMR of circulin A: a macrocyclic knotted peptide having anti-HIV activity. J. Mol. Biol. 285:1999;333-345.
    • (1999) J. Mol. Biol. , vol.285 , pp. 333-345
    • Daly, N.L.1    Koltay, A.2    Gustafson, K.R.3    Boyd, M.R.4    Casas-Finet, J.R.5    Craik, D.J.6
  • 12
    • 0033543137 scopus 로고    scopus 로고
    • Chemical synthesis and folding of large cyclic polypeptides: Studies of the cystine knot polypeptide kalata B1
    • Daly N.L., Love S., Alewood P.F., Craik D.J. Chemical synthesis and folding of large cyclic polypeptides: studies of the cystine knot polypeptide kalata B1. Biochemistry. 38:1999;10606-10614.
    • (1999) Biochemistry , vol.38 , pp. 10606-10614
    • Daly, N.L.1    Love, S.2    Alewood, P.F.3    Craik, D.J.4
  • 13
    • 0033573844 scopus 로고    scopus 로고
    • A novel endogenous inhibitor of phenoloxidase form Musca domestica has a cystine motif commonly found in snail and spider toxins
    • Daquinag A.C., Sato T., Koda H., Takao T., Fukuda M., Shimonishi Y., Tsukamoto T. A novel endogenous inhibitor of phenoloxidase form Musca domestica has a cystine motif commonly found in snail and spider toxins. Biochemistry. 38:1999;2179-2188.
    • (1999) Biochemistry , vol.38 , pp. 2179-2188
    • Daquinag, A.C.1    Sato, T.2    Koda, H.3    Takao, T.4    Fukuda, M.5    Shimonishi, Y.6    Tsukamoto, T.7
  • 14
    • 0030037084 scopus 로고    scopus 로고
    • RhNGF slow unfolding is not due to proline isomerization: Possibility of a cystine knot loop-threading mechanism
    • de Young L.R., Burton L.E., Liu J., Powell M.F., Schmelzer C.H., Skelton N.J. RhNGF slow unfolding is not due to proline isomerization: possibility of a cystine knot loop-threading mechanism. Protein Sci. 5:1996;1554-1566.
    • (1996) Protein Sci. , vol.5 , pp. 1554-1566
    • De Young, L.R.1    Burton, L.E.2    Liu, J.3    Powell, M.F.4    Schmelzer, C.H.5    Skelton, N.J.6
  • 16
    • 0030727613 scopus 로고    scopus 로고
    • The structure of versutoxin (δ-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel
    • Fletcher J.I., Chapman B.E., Mackay J.P., Howden M.E.H., King G.F. The structure of versutoxin (δ-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel. Structure. 5:1997;1525-1535.
    • (1997) Structure , vol.5 , pp. 1525-1535
    • Fletcher, J.I.1    Chapman, B.E.2    Mackay, J.P.3    Howden, M.E.H.4    King, G.F.5
  • 17
  • 19
    • 0032729577 scopus 로고    scopus 로고
    • Role of disulfide bridges in the folding, structure and biological activity of omega-conotoxin GVIA
    • Flinn J.P., Pallaghy P.K., Lew M.J., Murphy R., Angus J.A., Norton R.S. Role of disulfide bridges in the folding, structure and biological activity of omega-conotoxin GVIA. Biochim. Biophys. Acta. 1434:1999;177-190.
    • (1999) Biochim. Biophys. Acta , vol.1434 , pp. 177-190
    • Flinn, J.P.1    Pallaghy, P.K.2    Lew, M.J.3    Murphy, R.4    Angus, J.A.5    Norton, R.S.6
  • 21
    • 0015858263 scopus 로고
    • Isolation of oxytocic peptides from Oldenlandia affinis by solvent extraction of tetraphenylborate complexes and chromatography on sephadex LH-20
    • Gran L. Isolation of oxytocic peptides from Oldenlandia affinis by solvent extraction of tetraphenylborate complexes and chromatography on sephadex LH-20. Lloydia. 36:1973;207-208.
    • (1973) Lloydia , vol.36 , pp. 207-208
    • Gran, L.1
  • 25
    • 0030573025 scopus 로고    scopus 로고
    • The disulfide β-cross: From cystine geometry and clustering to classification of small disulfide-rich protein folds
    • Harrison P.M., Sternberg M.J.E. The disulfide β-cross: from cystine geometry and clustering to classification of small disulfide-rich protein folds. J. Mol. Biol. 264:1996;603-623.
    • (1996) J. Mol. Biol. , vol.264 , pp. 603-623
    • Harrison, P.M.1    Sternberg, M.J.E.2
  • 26
    • 0030016085 scopus 로고    scopus 로고
    • Three-dimensional solution structure of mu-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels
    • Hill J.M., Alewood P.F., Craik D.J. Three-dimensional solution structure of mu-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels. Biochemistry. 35:1996;8824-8835.
    • (1996) Biochemistry , vol.35 , pp. 8824-8835
    • Hill, J.M.1    Alewood, P.F.2    Craik, D.J.3
  • 27
    • 0031569801 scopus 로고    scopus 로고
    • Solution structure of the sodium channel antagonist conotoxin GS: A new molecular caliper for probing sodium channel geometry
    • Hill J.M., Alewood P.F., Craik D.J. Solution structure of the sodium channel antagonist conotoxin GS: a new molecular caliper for probing sodium channel geometry. Structure. 5:1997;571-583.
    • (1997) Structure , vol.5 , pp. 571-583
    • Hill, J.M.1    Alewood, P.F.2    Craik, D.J.3
  • 29
    • 0029084407 scopus 로고
    • Three-dimensional solution structure of the calcium channel antagonist omega-agatoxin IVA: Consensus molecular folding of calcium channel blockers
    • Kim J.I., Konishi S., Iwai H., Kohno T., Gouda H., Shimada I., Sato K., Arata Y. Three-dimensional solution structure of the calcium channel antagonist omega-agatoxin IVA: consensus molecular folding of calcium channel blockers. J. Mol. Biol. 250:1995;659-671.
    • (1995) J. Mol. Biol. , vol.250 , pp. 659-671
    • Kim, J.I.1    Konishi, S.2    Iwai, H.3    Kohno, T.4    Gouda, H.5    Shimada, I.6    Sato, K.7    Arata, Y.8
  • 30
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;29-32-51-5.
    • (1996) J. Mol. Graph. , vol.14 , pp. 2932-3515
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 32
    • 0027512113 scopus 로고
    • Characterization and 2D NMR study of the stable [9-21, 15-27] 2 disulfide intermediate in the folding of the 3 disulfide trypsin inhibitor EETI II
    • Le-Nguyen D., Heitz A., Chiche L., El Hajji M., Castro B. Characterization and 2D NMR study of the stable [9-21, 15-27] 2 disulfide intermediate in the folding of the 3 disulfide trypsin inhibitor EETI II. Protein Sci. 2:1993;165-174.
    • (1993) Protein Sci. , vol.2 , pp. 165-174
    • Le-Nguyen, D.1    Heitz, A.2    Chiche, L.3    El Hajji, M.4    Castro, B.5
  • 33
    • 0024831983 scopus 로고
    • Solid phase synthesis of a trypsin inhibitor isolated from Cucurbitaceae Ecballium elaterium
    • Le-Nguyen D., Nalis D., Castro B. Solid phase synthesis of a trypsin inhibitor isolated from Cucurbitaceae Ecballium elaterium. Int. J. Peptide Protein Res. 34:1989;492-497.
    • (1989) Int. J. Peptide Protein Res. , vol.34 , pp. 492-497
    • Le-Nguyen, D.1    Nalis, D.2    Castro, B.3
  • 35
    • 0032863018 scopus 로고    scopus 로고
    • Three-dimensional structure of Selenocosmia huwena lectin-I (SHL-I) from the venom of the spider Selenocosmia huwena by 2D-NMR
    • Lu S., Liang S., Gu X. Three-dimensional structure of Selenocosmia huwena lectin-I (SHL-I) from the venom of the spider Selenocosmia huwena by 2D-NMR. J. Protein Chem. 18:1999;609-617.
    • (1999) J. Protein Chem. , vol.18 , pp. 609-617
    • Lu, S.1    Liang, S.2    Gu, X.3
  • 36
    • 0028421135 scopus 로고
    • Are there knots in proteins?
    • Mansfield M.L. Are there knots in proteins? Structural Biology. 1:1994;213-214.
    • (1994) Structural Biology , vol.1 , pp. 213-214
    • Mansfield, M.L.1
  • 37
    • 0027225341 scopus 로고
    • Topological chirality of proteins
    • Mao B. Topological chirality of proteins. Protein Science. 2:1993;1057-1059.
    • (1993) Protein Science , vol.2 , pp. 1057-1059
    • Mao, B.1
  • 38
    • 0027251256 scopus 로고
    • A structural superfamily of growth factors containing a cystine knot motif
    • McDonald N.Q., Hendrickson W.A. A structural superfamily of growth factors containing a cystine knot motif. Cell. 73:1993;421-424.
    • (1993) Cell , vol.73 , pp. 421-424
    • McDonald, N.Q.1    Hendrickson, W.A.2
  • 39
    • 0028987884 scopus 로고
    • Antagonists of neuronal calcium channels: Structure, function and therapeutic implications
    • Miljanich G.P., Ramachandran J. Antagonists of neuronal calcium channels: structure, function and therapeutic implications. Annu. Rev. Pharmacol. Toxicol. 35:1995;707-734.
    • (1995) Annu. Rev. Pharmacol. Toxicol. , vol.35 , pp. 707-734
    • Miljanich, G.P.1    Ramachandran, J.2
  • 40
    • 0012203495 scopus 로고    scopus 로고
    • Knotted structures in chemistry, biochemistry and molecular biology
    • Mislow K., Liang C. Knotted structures in chemistry, biochemistry and molecular biology. Croatica Chemica Acta. 69:1996;1385-1403.
    • (1996) Croatica Chemica Acta , vol.69 , pp. 1385-1403
    • Mislow, K.1    Liang, C.2
  • 42
    • 0028695949 scopus 로고
    • Snail and spider toxins share a similar tertiary structure and 'cystine motif'
    • Narasimhan L., Singh J., Humblet C., Guruprasad K., Blundell T. Snail and spider toxins share a similar tertiary structure and 'cystine motif'. Struct. Biol. 1:1994;850-852.
    • (1994) Struct. Biol. , vol.1 , pp. 850-852
    • Narasimhan, L.1    Singh, J.2    Humblet, C.3    Guruprasad, K.4    Blundell, T.5
  • 43
    • 0033603390 scopus 로고    scopus 로고
    • Structure-activity relationships of ω-conotoxins MVIIA, MVIIC and 14 loop splice hybrids at N and P/Q-type calcium channels
    • Nielsen K.J., Adams D., Thomas L., Bond T., Alewood P.F., Craik D.J., Lewis R.J. Structure-activity relationships of ω-conotoxins MVIIA, MVIIC and 14 loop splice hybrids at N and P/Q-type calcium channels. J. Mol. Biol. 289:1999;1405-1421.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1405-1421
    • Nielsen, K.J.1    Adams, D.2    Thomas, L.3    Bond, T.4    Alewood, P.F.5    Craik, D.J.6    Lewis, R.J.7
  • 44
    • 0030601856 scopus 로고    scopus 로고
    • A consensus structure for ω-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: Comparison of MVIIA, SVIB and SNX-202
    • Nielsen K.J., Thomas L., Lewis R.J., Alewood P.F., Craik D.J. A consensus structure for ω-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: comparison of MVIIA, SVIB and SNX-202. J. Mol. Biol. 263:1996;297-310.
    • (1996) J. Mol. Biol. , vol.263 , pp. 297-310
    • Nielsen, K.J.1    Thomas, L.2    Lewis, R.J.3    Alewood, P.F.4    Craik, D.J.5
  • 45
    • 0343506108 scopus 로고
    • Relaxation matrix refinement of the solution structure of squash trypsin inhibitor
    • Nilges M., Habazettl J., Brünger A.T., Holak T.A. Relaxation matrix refinement of the solution structure of squash trypsin inhibitor. J. Mol. Biol. 248:1991;106-124.
    • (1991) J. Mol. Biol. , vol.248 , pp. 106-124
    • Nilges, M.1    Habazettl, J.2    Brünger, A.T.3    Holak, T.A.4
  • 46
    • 0031796848 scopus 로고    scopus 로고
    • The cystine knot structure of ion channel toxins and related polypeptides
    • Norton R.S., Pallaghy P.K. The cystine knot structure of ion channel toxins and related polypeptides. Toxicon. 36:1998;573-583.
    • (1998) Toxicon , vol.36 , pp. 573-583
    • Norton, R.S.1    Pallaghy, P.K.2
  • 49
    • 0029986992 scopus 로고    scopus 로고
    • Three-dimensional structure of μ-agatoxins: Further evidence for common motifs among neurotoxins with diverse ion channel specificities
    • Omecinsky D.O., Holub K.E., Adams M.E., Reily M.D. Three-dimensional structure of μ-agatoxins: further evidence for common motifs among neurotoxins with diverse ion channel specificities. Biochemistry. 35:1996;2836-2844.
    • (1996) Biochemistry , vol.35 , pp. 2836-2844
    • Omecinsky, D.O.1    Holub, K.E.2    Adams, M.E.3    Reily, M.D.4
  • 50
    • 0032898964 scopus 로고    scopus 로고
    • Refined solution structure of omega-conotoxin GVIA: Implications for calcium channel binding
    • Pallaghy P.K., Norton R.S. Refined solution structure of omega-conotoxin GVIA: implications for calcium channel binding. J. Pept. Res. 53:1999;343-351.
    • (1999) J. Pept. Res. , vol.53 , pp. 343-351
    • Pallaghy, P.K.1    Norton, R.S.2
  • 51
    • 0031451746 scopus 로고    scopus 로고
    • Solution structure of robustoxin, the lethal neurotoxin from the funnel-web spider Atrax robustus
    • Pallaghy P.K., Alewood D., Alewood P.F., Norton R.S. Solution structure of robustoxin, the lethal neurotoxin from the funnel-web spider Atrax robustus. FEBS Lett. 419:1997;191-196.
    • (1997) FEBS Lett. , vol.419 , pp. 191-196
    • Pallaghy, P.K.1    Alewood, D.2    Alewood, P.F.3    Norton, R.S.4
  • 52
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides
    • Pallaghy P.K., Nielsen K.J., Craik D.J., Norton R.S. A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides. Protein Sci. 3:1994;1833-1839.
    • (1994) Protein Sci. , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 53
    • 0029856411 scopus 로고    scopus 로고
    • Folding of ω-conotoxins: 2. Influence of precursor sequences and protein disulfide isomerase
    • Price-Carter M., Gray W.R., Goldenberg D.P. Folding of ω-conotoxins: 2. Influence of precursor sequences and protein disulfide isomerase. Biochemistry. 35:1996;15547-15557.
    • (1996) Biochemistry , vol.35 , pp. 15547-15557
    • Price-Carter, M.1    Gray, W.R.2    Goldenberg, D.P.3
  • 54
    • 0032493315 scopus 로고    scopus 로고
    • Roles of individual disulfide bonds in the stability and folding of an ω-conotoxin
    • Price-Carter M., Salem Hull M., Goldenberg D.P. Roles of individual disulfide bonds in the stability and folding of an ω-conotoxin. Biochemistry. 37:1998;9851-9861.
    • (1998) Biochemistry , vol.37 , pp. 9851-9861
    • Price-Carter, M.1    Salem Hull, M.2    Goldenberg, D.P.3
  • 55
    • 0030791931 scopus 로고    scopus 로고
    • Proton nuclear magnetic resonance studies on huwentoxin-I from the venom of the spider Selenocosmia huwena: 2. Three-dimensional structure in solution
    • Qu Y., Liang S., Ding J., Liu X., Zhang R., Gu X. Proton nuclear magnetic resonance studies on huwentoxin-I from the venom of the spider Selenocosmia huwena: 2. Three-dimensional structure in solution. J. Protein Chem. 16:1997;565-574.
    • (1997) J. Protein Chem. , vol.16 , pp. 565-574
    • Qu, Y.1    Liang, S.2    Ding, J.3    Liu, X.4    Zhang, R.5    Gu, X.6
  • 56
    • 0020491126 scopus 로고
    • Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 Å
    • Rees D.C., Lipscomb W.N. Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 Å J. Mol. Biol. 160:1982;475-498.
    • (1982) J. Mol. Biol. , vol.160 , pp. 475-498
    • Rees, D.C.1    Lipscomb, W.N.2
  • 57
    • 0029243371 scopus 로고
    • The solution structure of omega-Aga-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta
    • Reily M.D., Thanabal V., Adams M.E. The solution structure of omega-Aga-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta. J. Biomol. NMR. 5:1995;122-132.
    • (1995) J. Biomol. NMR , vol.5 , pp. 122-132
    • Reily, M.D.1    Thanabal, V.2    Adams, M.E.3
  • 58
    • 0028927655 scopus 로고
    • Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1
    • Saether O., Craik D.J., Campbell I.D., Sletten K., Juul J., Norman D.G. Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1. Biochemistry. 34:1995;4147-4158.
    • (1995) Biochemistry , vol.34 , pp. 4147-4158
    • Saether, O.1    Craik, D.J.2    Campbell, I.D.3    Sletten, K.4    Juul, J.5    Norman, D.G.6
  • 59
    • 0031574335 scopus 로고    scopus 로고
    • Solution structure and proposed binding mechanism of a novel potassium channel toxin kappa-conotoxin PVIIA
    • Scanlon M.J., Naranjo D., Thomas L., Alewood P.F., Lewis R.J., Craik D.J. Solution structure and proposed binding mechanism of a novel potassium channel toxin kappa-conotoxin PVIIA. Structure. 5:1997;1585-1597.
    • (1997) Structure , vol.5 , pp. 1585-1597
    • Scanlon, M.J.1    Naranjo, D.2    Thomas, L.3    Alewood, P.F.4    Lewis, R.J.5    Craik, D.J.6
  • 60
    • 0027177567 scopus 로고
    • Hämolytisch aktive komponenten aus Viola tricolor L. und Viola arvensis Murray
    • Schöpke T., Hasan Agha M.I., Kraft R., Otto A., Hiller K. Hämolytisch aktive komponenten aus Viola tricolor L. und Viola arvensis Murray. Sci. Pharm. 61:1993;145-153.
    • (1993) Sci. Pharm. , vol.61 , pp. 145-153
    • Schöpke, T.1    Hasan Agha, M.I.2    Kraft, R.3    Otto, A.4    Hiller, K.5
  • 61
    • 0032571365 scopus 로고    scopus 로고
    • Small binding proteins selected from a combinatorial repertoire of knottins displayed on phage
    • Smith G.P., Patel S.U., Windass J.D., Thornton J.M., Winter G., Griffiths A.D. Small binding proteins selected from a combinatorial repertoire of knottins displayed on phage. J. Mol. Biol. 277:1998;317-332.
    • (1998) J. Mol. Biol. , vol.277 , pp. 317-332
    • Smith, G.P.1    Patel, S.U.2    Windass, J.D.3    Thornton, J.M.4    Winter, G.5    Griffiths, A.D.6
  • 63
    • 0031822610 scopus 로고    scopus 로고
    • A biomimetic strategy in the synthesis, fragmentation of cyclic protein
    • Tam J.P., Lu Y.-A. A biomimetic strategy in the synthesis, fragmentation of cyclic protein. Protein Sci. 7:1998;1583-1592.
    • (1998) Protein Sci. , vol.7 , pp. 1583-1592
    • Tam, J.P.1    Lu, Y.-A.2
  • 64
    • 0033529942 scopus 로고    scopus 로고
    • An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides
    • Tam J.P., Lu Y.A., Yang J.L., Chiu K.W. An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides. Proc. Natl. Acad. Sci. USA. 96:1999;8913-8918.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8913-8918
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3    Chiu, K.W.4
  • 66
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins
    • Tang Y.-Q., Yuan J., Ösapay G., Ösapay K., Tran D., Miller C.J., Ouellette A.J., Selsted M.E. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins. Science. 286:1999;498-502.
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.-Q.1    Yuan, J.2    Ösapay, G.3    Ösapay, K.4    Tran, D.5    Miller, C.J.6    Ouellette, A.J.7    Selsted, M.E.8
  • 68
    • 0033597789 scopus 로고    scopus 로고
    • Sequence requirements of the GPNG beta-turn of the Ecballium elaterium trypsin inhibitor II explored by combinatorial library screening
    • Wentzel A., Christmann A., Kratzner R., Kolmar H. Sequence requirements of the GPNG beta-turn of the Ecballium elaterium trypsin inhibitor II explored by combinatorial library screening. J. Biol. Chem. 274:1999;21037-21043.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21037-21043
    • Wentzel, A.1    Christmann, A.2    Kratzner, R.3    Kolmar, H.4
  • 69


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.