메뉴 건너뛰기




Volumn 15, Issue 1-2, 2010, Pages 57-64

Cyclotides as templates in drug design

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULIN; CYCLOPEPTIDE; CYCLOPSYCHOTRIDE A; CYCLOTIDE; CYCLOVIOLACIN O2; KALATA B1; NEUROTENSIN; PROTEIN MCOTI II; UNCLASSIFIED DRUG;

EID: 73749087526     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.drudis.2009.10.007     Document Type: Review
Times cited : (124)

References (68)
  • 1
    • 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., et al. 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
  • 2
    • 0035845584 scopus 로고    scopus 로고
    • Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis
    • Jennings C., et al. Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 10614-10619
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10614-10619
    • Jennings, C.1
  • 3
    • 39549108482 scopus 로고    scopus 로고
    • Plant cyclotides disrupt epithelial cells in the midgut of lepidopteran larvae
    • Barbeta B.L., et al. Plant cyclotides disrupt epithelial cells in the midgut of lepidopteran larvae. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 1221-1225
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 1221-1225
    • Barbeta, B.L.1
  • 4
    • 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
  • 5
    • 2442715239 scopus 로고    scopus 로고
    • Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: the importance of the cyclic cystine knot
    • Colgrave M.L., and Craik D.J. Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: the importance of the cyclic cystine knot. Biochemistry 43 (2004) 5965-5975
    • (2004) Biochemistry , vol.43 , pp. 5965-5975
    • Colgrave, M.L.1    Craik, D.J.2
  • 6
    • 0003064562 scopus 로고
    • Some molecular properties of kalata peptide B-1. A uterotonic polypeptide isolated from Oldenlandia affinis DC
    • Sletten K., and Gran L. Some molecular properties of kalata peptide B-1. A uterotonic polypeptide isolated from Oldenlandia affinis DC. Medd. Nor. Farm. Selsk. 7-8 (1973) 69-82
    • (1973) Medd. Nor. Farm. Selsk. , vol.7-8 , pp. 69-82
    • Sletten, K.1    Gran, L.2
  • 7
    • 0000014794 scopus 로고
    • An oxytocic principle found in Oldenlandia affinis DC
    • Gran L. An oxytocic principle found in Oldenlandia affinis DC. Medd. Nor. Farm. Selsk. 12 (1970) 173-180
    • (1970) Medd. Nor. Farm. Selsk. , vol.12 , pp. 173-180
    • Gran, L.1
  • 8
    • 0034662438 scopus 로고    scopus 로고
    • Oldenlandia affinis (R&S) DC. A plant containing uteroactive peptides used in African traditional medicine
    • Gran L., et al. Oldenlandia affinis (R&S) DC. A plant containing uteroactive peptides used in African traditional medicine. J. Ethnopharmacol. 70 (2000) 197-203
    • (2000) J. Ethnopharmacol. , vol.70 , pp. 197-203
    • Gran, L.1
  • 9
    • 0028927655 scopus 로고
    • Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1
    • Saether O., et al. 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
  • 10
    • 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., et al. 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
  • 11
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • Craik D.J., et al. The cystine knot motif in toxins and implications for drug design. Toxicon 39 (2001) 43-60
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1
  • 12
    • 0027177567 scopus 로고
    • Hämolytisch aktive komponenten aus Viola tricolor L. und Viola arvensis Murray
    • Schöpke T., et al. 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
  • 13
    • 0028598525 scopus 로고
    • Cyclopsychotride A, a biologically active, 31-residue cyclic peptide isolated from Psychotria longipes
    • Witherup K.M., et al. Cyclopsychotride A, a biologically active, 31-residue cyclic peptide isolated from Psychotria longipes. J. Nat. Prod. 57 (1994) 1619-1625
    • (1994) J. Nat. Prod. , vol.57 , pp. 1619-1625
    • Witherup, K.M.1
  • 14
    • 0028036769 scopus 로고
    • Circulins A and B: novel HIV-inhibitory macrocyclic peptides from the tropical tree Chassalia parvifolia
    • Gustafson K.R., et al. Circulins A and B: novel HIV-inhibitory macrocyclic peptides from the tropical tree Chassalia parvifolia. J. Am. Chem. Soc. 116 (1994) 9337-9338
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9337-9338
    • Gustafson, K.R.1
  • 15
    • 0038342427 scopus 로고    scopus 로고
    • Seven novel macrocyclic polypeptides from Viola arvensis
    • Göransson U., et al. Seven novel macrocyclic polypeptides from Viola arvensis. J. Nat. Prod. 62 (1999) 283-286
    • (1999) J. Nat. Prod. , vol.62 , pp. 283-286
    • Göransson, U.1
  • 16
    • 0031935354 scopus 로고    scopus 로고
    • Fractionation protocol for the isolation of polypeptides from plant biomass
    • Claeson P., et al. Fractionation protocol for the isolation of polypeptides from plant biomass. J. Nat. Prod. 61 (1998) 77-81
    • (1998) J. Nat. Prod. , vol.61 , pp. 77-81
    • Claeson, P.1
  • 17
    • 4043144831 scopus 로고    scopus 로고
    • Discovery, structure and biological activities of the cyclotides
    • Craik D.J., et al. Discovery, structure and biological activities of the cyclotides. Curr. Protein Pept. Sci. 5 (2004) 297-315
    • (2004) Curr. Protein Pept. Sci. , vol.5 , pp. 297-315
    • Craik, D.J.1
  • 18
    • 0035838357 scopus 로고    scopus 로고
    • Solution structure of the squash trypsin inhibitor MCoTI-II. A new family for cyclic knottins
    • Heitz A., et al. Solution structure of the squash trypsin inhibitor MCoTI-II. A new family for cyclic knottins. Biochemistry 40 (2001) 7973-7983
    • (2001) Biochemistry , vol.40 , pp. 7973-7983
    • Heitz, A.1
  • 19
    • 0034674028 scopus 로고    scopus 로고
    • Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure
    • Hernandez J.F., et al. Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure. Biochemistry 39 (2000) 5722-5730
    • (2000) Biochemistry , vol.39 , pp. 5722-5730
    • Hernandez, J.F.1
  • 20
    • 33646248365 scopus 로고    scopus 로고
    • The cyclotide family of circular miniproteins: nature's combinatorial peptide template
    • Craik D.J., et al. The cyclotide family of circular miniproteins: nature's combinatorial peptide template. Biopolym. Peptide Sci. 84 (2006) 250-266
    • (2006) Biopolym. Peptide Sci. , vol.84 , pp. 250-266
    • Craik, D.J.1
  • 21
    • 32944465547 scopus 로고    scopus 로고
    • Structural plasticity of the cyclic-cystine-knot framework: implications for biological activity and drug design
    • Clark R.J., et al. Structural plasticity of the cyclic-cystine-knot framework: implications for biological activity and drug design. Biochem. J. 394 (2006) 85-93
    • (2006) Biochem. J. , vol.394 , pp. 85-93
    • Clark, R.J.1
  • 22
    • 70350539308 scopus 로고    scopus 로고
    • The conserved glu in the cyclotide cycloviolacin O2 has a key structural role
    • Goransson U., et al. The conserved glu in the cyclotide cycloviolacin O2 has a key structural role. ChemBioChem 10 (2009) 2354-2360
    • (2009) ChemBioChem , vol.10 , pp. 2354-2360
    • Goransson, U.1
  • 23
    • 67449106989 scopus 로고    scopus 로고
    • Combined X-ray and NMR analysis of the stability of the cyclotide cystine knot fold that underpins its insecticidal activity and potential use as a drug scaffold
    • Wang C.K., et al. Combined X-ray and NMR analysis of the stability of the cyclotide cystine knot fold that underpins its insecticidal activity and potential use as a drug scaffold. J. Biol. Chem. 284 (2009) 10672-10683
    • (2009) J. Biol. Chem. , vol.284 , pp. 10672-10683
    • Wang, C.K.1
  • 24
    • 0037424506 scopus 로고    scopus 로고
    • Twists, knots, and rings in proteins. Structural definition of the cyclotide framework
    • Rosengren K.J., et al. Twists, knots, and rings in proteins. Structural definition of the cyclotide framework. J. Biol. Chem. 278 (2003) 8606-8616
    • (2003) J. Biol. Chem. , vol.278 , pp. 8606-8616
    • Rosengren, K.J.1
  • 25
    • 30744437130 scopus 로고    scopus 로고
    • Key role of glutamic acid for the cytotoxic activity of the cyclotide cycloviolacin O2
    • Herrmann A., et al. Key role of glutamic acid for the cytotoxic activity of the cyclotide cycloviolacin O2. Cell. Mol. Life Sci. 63 (2006) 235-245
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 235-245
    • Herrmann, A.1
  • 26
    • 43949138210 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of the prototypic cyclotide reveals a cluster of residues essential for bioactivity
    • Simonsen S.M., et al. Alanine scanning mutagenesis of the prototypic cyclotide reveals a cluster of residues essential for bioactivity. J. Biol. Chem. 283 (2008) 9805-9813
    • (2008) J. Biol. Chem. , vol.283 , pp. 9805-9813
    • Simonsen, S.M.1
  • 27
    • 35748954039 scopus 로고    scopus 로고
    • An asparaginyl endopeptidase mediates in vivo protein backbone cyclisation
    • Saska I., et al. An asparaginyl endopeptidase mediates in vivo protein backbone cyclisation. J. Biol. Chem. 282 (2007) 29721-29728
    • (2007) J. Biol. Chem. , vol.282 , pp. 29721-29728
    • Saska, I.1
  • 28
    • 38649136638 scopus 로고    scopus 로고
    • Biosynthesis of circular proteins in plants
    • Gillon A.D., et al. Biosynthesis of circular proteins in plants. Plant J. 53 (2008) 505-515
    • (2008) Plant J. , vol.53 , pp. 505-515
    • Gillon, A.D.1
  • 30
    • 4444331457 scopus 로고    scopus 로고
    • The role of the cyclic peptide backbone in the anti-HIV activity of the cyclotide kalata B1
    • Daly N.L., et al. The role of the cyclic peptide backbone in the anti-HIV activity of the cyclotide kalata B1. FEBS Lett. 574 (2004) 69-72
    • (2004) FEBS Lett. , vol.574 , pp. 69-72
    • Daly, N.L.1
  • 31
    • 31544481160 scopus 로고    scopus 로고
    • Kalata B8, a novel antiviral circular protein, exhibits conformational flexibility in the cystine knot motif
    • Daly N.L., et al. Kalata B8, a novel antiviral circular protein, exhibits conformational flexibility in the cystine knot motif. Biochem. J. 393 (2006) 619-626
    • (2006) Biochem. J. , vol.393 , pp. 619-626
    • Daly, N.L.1
  • 32
    • 20444441123 scopus 로고    scopus 로고
    • Isolation and characterization of novel cyclotides from Viola hederaceae: solution structure and anti-HIV activity of vhl-1, a leaf-specific expressed cyclotide
    • Chen B., et al. Isolation and characterization of novel cyclotides from Viola hederaceae: solution structure and anti-HIV activity of vhl-1, a leaf-specific expressed cyclotide. J. Biol. Chem. 280 (2005) 22395-22405
    • (2005) J. Biol. Chem. , vol.280 , pp. 22395-22405
    • Chen, B.1
  • 33
    • 39149114797 scopus 로고    scopus 로고
    • Cyclotides as natural anti-HIV agents
    • Ireland D.C., et al. Cyclotides as natural anti-HIV agents. Biopolym. Peptide Sci. 90 (2008) 51-60
    • (2008) Biopolym. Peptide Sci. , vol.90 , pp. 51-60
    • Ireland, D.C.1
  • 34
    • 39049116969 scopus 로고    scopus 로고
    • Anti-HIV cyclotides from the Chinese medicinal herb Viola yedoensis
    • Wang C.K., et al. Anti-HIV cyclotides from the Chinese medicinal herb Viola yedoensis. J. Nat. Prod. 71 (2008) 47-52
    • (2008) J. Nat. Prod. , vol.71 , pp. 47-52
    • Wang, C.K.1
  • 35
    • 34548288120 scopus 로고    scopus 로고
    • An update in the development of HIV entry inhibitors
    • Rusconi S., et al. An update in the development of HIV entry inhibitors. Curr. Top. Med. Chem. 7 (2007) 1273-1289
    • (2007) Curr. Top. Med. Chem. , vol.7 , pp. 1273-1289
    • Rusconi, S.1
  • 36
    • 1642494594 scopus 로고    scopus 로고
    • Putative role of membranes in the HIV fusion inhibitor enfuvirtide mode of action at the molecular level
    • Veiga S., et al. Putative role of membranes in the HIV fusion inhibitor enfuvirtide mode of action at the molecular level. Biochem. J. 377 (2004) 107-110
    • (2004) Biochem. J. , vol.377 , pp. 107-110
    • Veiga, S.1
  • 37
    • 43249117737 scopus 로고    scopus 로고
    • Sifuvirtide screens rigid membrane surfaces. Establishment of a correlation between efficacy and membrane domain selectivity among HIV fusion inhibitor peptides
    • Franquelim H.G., et al. Sifuvirtide screens rigid membrane surfaces. Establishment of a correlation between efficacy and membrane domain selectivity among HIV fusion inhibitor peptides. J. Am. Chem. Soc. 130 (2008) 6215-6223
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6215-6223
    • Franquelim, H.G.1
  • 38
    • 11844280405 scopus 로고    scopus 로고
    • Studies on the membrane interactions of the cyclotides kalata B1 and kalata B6 on model membrane systems by surface plasmon resonance
    • Kamimori H., et al. Studies on the membrane interactions of the cyclotides kalata B1 and kalata B6 on model membrane systems by surface plasmon resonance. Anal. Biochem. 337 (2005) 149-153
    • (2005) Anal. Biochem. , vol.337 , pp. 149-153
    • Kamimori, H.1
  • 39
    • 33745227238 scopus 로고    scopus 로고
    • Conformation and mode of membrane interaction in cyclotides. Spatial structure of kalata B1 bound to a dodecylphosphocholine micelle
    • Shenkarev Z.O., et al. Conformation and mode of membrane interaction in cyclotides. Spatial structure of kalata B1 bound to a dodecylphosphocholine micelle. FEBS J. 273 (2006) 2658-2672
    • (2006) FEBS J. , vol.273 , pp. 2658-2672
    • Shenkarev, Z.O.1
  • 41
    • 68949120908 scopus 로고    scopus 로고
    • The biological activity of the prototypic cyclotide kalata B1 is modulated by the formation of multimeric pores
    • Huang Y.H., et al. The biological activity of the prototypic cyclotide kalata B1 is modulated by the formation of multimeric pores. J. Biol. Chem. 284 (2009) 20699-20707
    • (2009) J. Biol. Chem. , vol.284 , pp. 20699-20707
    • Huang, Y.H.1
  • 42
    • 57749113081 scopus 로고    scopus 로고
    • Distribution and evolution of circular miniproteins in flowering plants
    • Gruber C.W., et al. Distribution and evolution of circular miniproteins in flowering plants. Plant Cell 20 (2008) 2471-2483
    • (2008) Plant Cell , vol.20 , pp. 2471-2483
    • Gruber, C.W.1
  • 43
    • 0033529942 scopus 로고    scopus 로고
    • An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides
    • Tam J.P., et al. An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8913-8918
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8913-8918
    • Tam, J.P.1
  • 44
    • 58149347521 scopus 로고    scopus 로고
    • Cyclic peptides from Oldenlandia affinis DC. Molecular and biological properties
    • Gran L., et al. Cyclic peptides from Oldenlandia affinis DC. Molecular and biological properties. Chem. Biodivers. 5 (2008) 2014-2022
    • (2008) Chem. Biodivers. , vol.5 , pp. 2014-2022
    • Gran, L.1
  • 45
    • 0033543137 scopus 로고    scopus 로고
    • Chemical synthesis and folding pathways of large cyclic polypeptides: studies of the cystine knot polypeptide kalata B1
    • Daly N.L., et al. Chemical synthesis and folding pathways 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
  • 46
    • 0001166316 scopus 로고    scopus 로고
    • Cyclotides: a novel type of cytotoxic agents
    • Lindholm P., et al. Cyclotides: a novel type of cytotoxic agents. Mol. Cancer Ther. 1 (2002) 365-369
    • (2002) Mol. Cancer Ther. , vol.1 , pp. 365-369
    • Lindholm, P.1
  • 47
    • 39149141320 scopus 로고    scopus 로고
    • The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity
    • Herrmann A., et al. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. Phytochemistry 69 (2008) 939-952
    • (2008) Phytochemistry , vol.69 , pp. 939-952
    • Herrmann, A.1
  • 48
    • 8744299791 scopus 로고    scopus 로고
    • Cytotoxic cyclotides from Viola tricolor
    • Svangard E., et al. Cytotoxic cyclotides from Viola tricolor. J. Nat. Prod. 67 (2004) 144-147
    • (2004) J. Nat. Prod. , vol.67 , pp. 144-147
    • Svangard, E.1
  • 49
    • 34249056827 scopus 로고    scopus 로고
    • Mechanism of action of cytotoxic cyclotides: cycloviolacin O2 disrupts lipid membranes
    • Svangard E., et al. Mechanism of action of cytotoxic cyclotides: cycloviolacin O2 disrupts lipid membranes. J. Nat. Prod. 70 (2007) 643-647
    • (2007) J. Nat. Prod. , vol.70 , pp. 643-647
    • Svangard, E.1
  • 50
    • 38349009178 scopus 로고    scopus 로고
    • Studies on anticancer activities of antimicrobial peptides
    • Hoskin D.W., and Ramamoorthy A. Studies on anticancer activities of antimicrobial peptides. Biochim. Biophys. Acta 1778 (2008) 357-375
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 357-375
    • Hoskin, D.W.1    Ramamoorthy, A.2
  • 51
    • 65249093640 scopus 로고    scopus 로고
    • Thermodynamics of melittin binding to lipid bilayers. Aggregation/pore formation
    • Klocek G., et al. Thermodynamics of melittin binding to lipid bilayers. Aggregation/pore formation. Biochemistry 48 (2009) 2586-2596
    • (2009) Biochemistry , vol.48 , pp. 2586-2596
    • Klocek, G.1
  • 52
    • 67649396451 scopus 로고    scopus 로고
    • Free energies of molecular bound states in lipid bilayers: lethal concentrations of antimicrobial peptides
    • Huang H.W. Free energies of molecular bound states in lipid bilayers: lethal concentrations of antimicrobial peptides. Biophys. J. 96 (2009) 3263-3272
    • (2009) Biophys. J. , vol.96 , pp. 3263-3272
    • Huang, H.W.1
  • 53
    • 0037088544 scopus 로고    scopus 로고
    • Refined structure and metal binding site of the kalata B1 peptide
    • Skjeldal L., et al. Refined structure and metal binding site of the kalata B1 peptide. Arch. Biochem. Biophys. 399 (2002) 142-148
    • (2002) Arch. Biochem. Biophys. , vol.399 , pp. 142-148
    • Skjeldal, L.1
  • 54
    • 19944431406 scopus 로고    scopus 로고
    • Isolation, solution structure, and insecticidal activity of kalata B2, a circular protein with a twist: do Mobius strips exist in nature?
    • Jennings C.V., et al. Isolation, solution structure, and insecticidal activity of kalata B2, a circular protein with a twist: do Mobius strips exist in nature?. Biochemistry 44 (2005) 851-860
    • (2005) Biochemistry , vol.44 , pp. 851-860
    • Jennings, C.V.1
  • 55
    • 47849105966 scopus 로고    scopus 로고
    • Backbone cyclised peptides from plants show molluscicidal activity against the rice pest Pomacea canaliculata (golden apple snail)
    • Plan M.R.R., et al. Backbone cyclised peptides from plants show molluscicidal activity against the rice pest Pomacea canaliculata (golden apple snail). J. Agric. Food Chem. 56 (2008) 5237-5241
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 5237-5241
    • Plan, M.R.R.1
  • 56
    • 4344584816 scopus 로고    scopus 로고
    • Reversible antifouling effect of the cyclotide cycloviolacin O2 against barnacles
    • Göransson U., et al. Reversible antifouling effect of the cyclotide cycloviolacin O2 against barnacles. J. Nat. Prod. 67 (2004) 1287-1290
    • (2004) J. Nat. Prod. , vol.67 , pp. 1287-1290
    • Göransson, U.1
  • 57
    • 43949110597 scopus 로고    scopus 로고
    • Cyclotides: natural, circular plant peptides that possess significant activity against gastrointestinal nematode parasites of sheep
    • Colgrave M.L., et al. Cyclotides: natural, circular plant peptides that possess significant activity against gastrointestinal nematode parasites of sheep. Biochemistry 47 (2008) 5581-5589
    • (2008) Biochemistry , vol.47 , pp. 5581-5589
    • Colgrave, M.L.1
  • 58
    • 54349090107 scopus 로고    scopus 로고
    • The anthelmintic activity of the cyclotides: natural variants with enhanced activity
    • Colgrave M.L., et al. The anthelmintic activity of the cyclotides: natural variants with enhanced activity. ChemBioChem 9 (2008) 1939-1945
    • (2008) ChemBioChem , vol.9 , pp. 1939-1945
    • Colgrave, M.L.1
  • 59
    • 57849088141 scopus 로고    scopus 로고
    • Anthelmintic activity of cyclotides: in vitro studies with canine and human hookworms
    • Colgrave M.L., et al. Anthelmintic activity of cyclotides: in vitro studies with canine and human hookworms. Acta Trop. 109 (2009) 163-166
    • (2009) Acta Trop. , vol.109 , pp. 163-166
    • Colgrave, M.L.1
  • 60
    • 0015723952 scopus 로고
    • On the effect of a polypeptide isolated from "Kalata-Kalata" (Oldenlandia affinis DC) on the oestrogen dominated uterus
    • Gran L. On the effect of a polypeptide isolated from "Kalata-Kalata" (Oldenlandia affinis DC) on the oestrogen dominated uterus. Acta Pharmacol. Toxicol. (Copenh.) 33 (1973) 400-408
    • (1973) Acta Pharmacol. Toxicol. (Copenh.) , vol.33 , pp. 400-408
    • Gran, L.1
  • 61
    • 32644451112 scopus 로고    scopus 로고
    • Cycloviolacin H4, a hydrophobic cyclotide from Viola hederaceae
    • Chen B., et al. Cycloviolacin H4, a hydrophobic cyclotide from Viola hederaceae. J. Nat. Prod. 69 (2006) 23-28
    • (2006) J. Nat. Prod. , vol.69 , pp. 23-28
    • Chen, B.1
  • 62
    • 33645028340 scopus 로고    scopus 로고
    • The cyclotides and related macrocyclic peptides as scaffolds in drug design
    • Craik D.J., et al. The cyclotides and related macrocyclic peptides as scaffolds in drug design. Curr. Opin. Drug Discov. Dev. 9 (2006) 251-260
    • (2006) Curr. Opin. Drug Discov. Dev. , vol.9 , pp. 251-260
    • Craik, D.J.1
  • 63
    • 58149089532 scopus 로고    scopus 로고
    • Engineering stabilized vascular endothelial growth factor-A antagonists: synthesis, structural characterization, and bioactivity of grafted analogues of cyclotides
    • Gunasekera S., et al. Engineering stabilized vascular endothelial growth factor-A antagonists: synthesis, structural characterization, and bioactivity of grafted analogues of cyclotides. J. Med. Chem. 51 (2008) 7697-7704
    • (2008) J. Med. Chem. , vol.51 , pp. 7697-7704
    • Gunasekera, S.1
  • 64
    • 41549150296 scopus 로고    scopus 로고
    • Chemical and biomimetic total syntheses of natural and engineered MCoTI cyclotides
    • Thongyoo P., et al. Chemical and biomimetic total syntheses of natural and engineered MCoTI cyclotides. Org. Biomol. Chem. 6 (2008) 1462-1470
    • (2008) Org. Biomol. Chem. , vol.6 , pp. 1462-1470
    • Thongyoo, P.1
  • 65
    • 34748922922 scopus 로고    scopus 로고
    • The cyclic cystine knot miniprotein MCoTI-II is internalized into cells by macropinocytosis
    • Greenwood K.P., et al. The cyclic cystine knot miniprotein MCoTI-II is internalized into cells by macropinocytosis. Int. J. Biochem. Cell Biol. 39 (2007) 2252-2264
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 2252-2264
    • Greenwood, K.P.1
  • 66
    • 70349506754 scopus 로고    scopus 로고
    • Extracellular proteases as targets for drug development
    • Cudic M., and Fields G.B. Extracellular proteases as targets for drug development. Curr. Protein Pept. Sci. 10 (2009) 297-307
    • (2009) Curr. Protein Pept. Sci. , vol.10 , pp. 297-307
    • Cudic, M.1    Fields, G.B.2
  • 67
    • 57349154062 scopus 로고    scopus 로고
    • Peptide-based vaccines for cancer: realizing their potential
    • Kanodia S., and Kast W.M. Peptide-based vaccines for cancer: realizing their potential. Expert Rev. Vaccines 7 (2008) 1533-1545
    • (2008) Expert Rev. Vaccines , vol.7 , pp. 1533-1545
    • Kanodia, S.1    Kast, W.M.2
  • 68
    • 70349591891 scopus 로고    scopus 로고
    • Despite a conserved cystine knot motif, different cyclotides have different membrane binding modes
    • Wang C.K., et al. Despite a conserved cystine knot motif, different cyclotides have different membrane binding modes. Biophys. J. 97 (2009) 1471-1481
    • (2009) Biophys. J. , vol.97 , pp. 1471-1481
    • Wang, C.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.