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Volumn 7, Issue 3, 2012, Pages 179-194

Cyclotides as a basis for drug design

Author keywords

Circular proteins; Cyclic peptides; Cyclotides; Cystine knot; Drug design; Kalata B1

Indexed keywords

ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; CELL PENETRATING PEPTIDE; CIRCULIN; CYCLOPSYCHOTRIDE A; CYCLOTIDE; CYCLOTIDE MCOTI I; CYCLOTIDE MCOTI II; CYCLOTIDE VARV A; CYCLOTIDE VARV E; CYCLOTIDE VARV F; CYCLOTIDE VHL 1; CYCLOVIOLACIN O14; CYCLOVIOLACIN O15; CYCLOVIOLACIN O24; CYCLOVIOLIN A; CYCLOVIOLIN B; CYCLOVIOLIN C; CYCLOVIOLIN D; DEFENSIN; KALATA B1; KALATA B2; KALATA B8; KALLIKREIN; PALICOUREIN; RECOMBINANT PROTEIN; THETA DEFENSIN; TRYPSIN INHIBITOR; UNCLASSIFIED DRUG; UNINDEXED DRUG; UTEROTONIC AGENT; VITRI A;

EID: 84857547296     PISSN: 17460441     EISSN: 1746045X     Source Type: Journal    
DOI: 10.1517/17460441.2012.661554     Document Type: Review
Times cited : (102)

References (143)
  • 1
    • 0033579483 scopus 로고    scopus 로고
    • Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif
    • DOI 10.1006/jmbi.1999.3383
    • Craik DJ, Daly NL, Bond T, et al. Plant cyclotides: a unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. J Mol Biol 1999;294:1327-36 (Pubitemid 30008803)
    • (1999) Journal of Molecular Biology , vol.294 , Issue.5 , pp. 1327-1336
    • Craik, D.J.1    Daly, N.L.2    Bond, T.3    Waine, C.4
  • 2
    • 0028036769 scopus 로고
    • Circulins A and B: Novel HIV-inhibitory macrocyclic peptides from the tropical tree Chassalia parvifolia
    • Gustafson KR, Sowder RCI, Henderson LE, et al. Circulins A and B: novel HIV-inhibitory macrocyclic peptides from the tropical tree Chassalia parvifolia. J Am Chem Soc 1994;116:9337-8
    • (1994) J Am Chem Soc , vol.116 , pp. 9337-9338
    • Gustafson, K.R.1    Sowder, R.C.I.2    Henderson, L.E.3
  • 3
    • 0028598525 scopus 로고
    • Cyclopsychotride A, A biologically active, 31-residue cyclic peptide isolated from Psychotria longipes
    • Witherup KM, Bogusky MJ, Anderson PS, et al. Cyclopsychotride A, A biologically active, 31-residue cyclic peptide isolated from Psychotria longipes. J Nat Prod 1994;57:1619-25
    • (1994) J Nat Prod , vol.57 , pp. 1619-1625
    • Witherup, K.M.1    Bogusky, M.J.2    Anderson, P.S.3
  • 5
    • 0000014794 scopus 로고
    • An oxytocic principle found in oldenlandia affinis DC
    • Gran L. An oxytocic principle found in Oldenlandia affinis DC. Med Nor Farm Selsk 1970;12:173-80
    • (1970) Med Nor Farm Selsk , vol.12 , pp. 173-180
    • Gran, L.1
  • 6
    • 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 1973;36:207-8
    • (1973) Lloydia , vol.36 , pp. 207-208
    • Gran, L.1
  • 7
    • 0003064562 scopus 로고
    • Some molecular properties of kalatapeptide B-1. A uterotonic polypeptide isolated from oldenlandia affinis DC
    • Sletten K, Gran L. Some molecular properties of kalatapeptide B-1. A uterotonic polypeptide isolated from Oldenlandia affinis DC. Med Nor Farm Selsk 1973;7(8):69-82
    • (1973) Med Nor Farm Selsk , vol.7 , Issue.8 , pp. 69-82
    • Sletten, K.1    Gran, L.2
  • 8
    • 0028927655 scopus 로고
    • Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1
    • Saether O, Craik DJ, Campbell ID, et al. Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1. Biochemistry 1995;34:4147-58
    • (1995) Biochemistry , vol.34 , pp. 4147-4158
    • Saether, O.1    Craik, D.J.2    Campbell, I.D.3
  • 9
    • 0037424506 scopus 로고    scopus 로고
    • Twists, knots, and rings in proteins: Structural definition of the cyclotide framework
    • DOI 10.1074/jbc.M211147200
    • Rosengren KJ, Daly NL, Plan MR, et al. Twists, knots, and rings in proteins. Structural definition of the cyclotide framework. J Biol Chem 2003;278:8606-16 (Pubitemid 36800615)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 8606-8616
    • Rosengren, K.J.1    Daly, N.L.2    Plan, M.R.3    Waine, C.4    Craik, D.J.5
  • 10
    • 2442715239 scopus 로고    scopus 로고
    • Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: The importance of the cyclic cystine knot
    • DOI 10.1021/bi049711q
    • Colgrave ML, Craik DJ. Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: the importance of the cyclic cystine knot. Biochemistry 2004;43:5965-75 (Pubitemid 38669464)
    • (2004) Biochemistry , vol.43 , Issue.20 , pp. 5965-5975
    • Colgrave, M.L.1    Craik, D.J.2
  • 11
    • 77956937013 scopus 로고    scopus 로고
    • Backbone dynamics of cyclotide MCoTI-I free and complexed with trypsin
    • Puttamadappa SS, Jagadish K, Shekhtman A, et al. Backbone dynamics of cyclotide MCoTI-I free and complexed with trypsin. Angew Chem Int Ed Engl 2010;49:7030-4
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 7030-7034
    • Puttamadappa, S.S.1    Jagadish, K.2    Shekhtman, A.3
  • 12
    • 79960623078 scopus 로고    scopus 로고
    • Corrigendum: Backbone dynamics of cyclotide MCoTI-I free and complexed with trypsin
    • Puttamadappa SS, Jagadish K, Shekhtman A, et al. Corrigendum: backbone dynamics of cyclotide MCoTI-I free and complexed with trypsin. Angew Chem Int Ed Engl 2011;50:6948-9
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 6948-6949
    • Puttamadappa, S.S.1    Jagadish, K.2    Shekhtman, A.3
  • 14
    • 79959965754 scopus 로고    scopus 로고
    • Discovery of an unusual biosynthetic origin for circular proteins in legumes
    • Poth AG, Colgrave ML, Lyons RE, et al. Discovery of an unusual biosynthetic origin for circular proteins in legumes. Proc Natl Acad Sci USA 2011;108:10127-32
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 10127-10132
    • Poth, A.G.1    Colgrave, M.L.2    Lyons, R.E.3
  • 15
    • 79959864353 scopus 로고    scopus 로고
    • Discovery and characterization of novel cyclotides originated from chimeric precursors consisting of albumin-1 chain a and cyclotide domains in the Fabaceae family
    • Nguyen GK, Zhang S, Nguyen NT, et al. Discovery and characterization of novel cyclotides originated from chimeric precursors consisting of albumin-1 chain a and cyclotide domains in the Fabaceae family. J Biol Chem 2011;286:24275-87
    • (2011) J Biol Chem , vol.286 , pp. 24275-24287
    • Nguyen, G.K.1    Zhang, S.2    Nguyen, N.T.3
  • 18
    • 39149141320 scopus 로고    scopus 로고
    • The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity
    • Herrmann A, Burman R, Mylne J, et al. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity. Phytochemistry 2008;69:939-52
    • (2008) Phytochemistry , vol.69 , pp. 939-952
    • Herrmann, A.1    Burman, R.2    Mylne, J.3
  • 19
    • 65949100618 scopus 로고    scopus 로고
    • Circular proteins from melicytus violaceae refine the conserved protein and gene architecture of cyclotides
    • Trabi M, Mylne JS, Sando L, et al. Circular proteins from Melicytus Violaceae refine the conserved protein and gene architecture of cyclotides. Org Biomol Chem 2009;7:2378-88
    • (2009) Org Biomol Chem , vol.7 , pp. 2378-2388
    • Trabi, M.1    Mylne, J.S.2    Sando, L.3
  • 20
    • 58149291681 scopus 로고    scopus 로고
    • Identification of two suites of cyclotide precursor genes from metallophyte Viola baoshanensis: CDNA sequence variation, alternative RNA splicing and potential cyclotide diversity
    • Zhang J, Liao B, Craik DJ, et al. Identification of two suites of cyclotide precursor genes from metallophyte Viola baoshanensis: cDNA sequence variation, alternative RNA splicing and potential cyclotide diversity. Gene 2009;431:23-32
    • (2009) Gene , vol.431 , pp. 23-32
    • Zhang, J.1    Liao, B.2    Craik, D.J.3
  • 22
    • 48149102488 scopus 로고    scopus 로고
    • Protease-catalysed protein splicing: A new post-translational modification?
    • Saska I, Craik DJ. Protease-catalysed protein splicing: a new post-translational modification? Trends Biochem Sci 2008;33:363-8
    • (2008) Trends Biochem Sci , vol.33 , pp. 363-368
    • Saska, I.1    Craik, D.J.2
  • 24
    • 38549134937 scopus 로고    scopus 로고
    • CyBase: A database of cyclic protein sequences and structures, with applications in protein discovery and engineering
    • DOI 10.1093/nar/gkm953
    • Wang CK, Kaas Q, Chiche L, et al. CyBase: a database of cyclic protein sequences and structures, with applications in protein discovery and engineering. Nucleic Acids Res 2008;36:D206-10 (Pubitemid 351149723)
    • (2008) Nucleic Acids Research , vol.36 , Issue.SUPPL. 1
    • Wang, C.K.L.1    Kaas, Q.2    Chiche, L.3    Craik, D.J.4
  • 25
    • 33646248365 scopus 로고    scopus 로고
    • The cyclotide family of circular miniproteins: Nature's combinatorial peptide template
    • Craik DJ, Cemazar M, Wang CK, et al. The cyclotide family of circular miniproteins: nature's combinatorial peptide template. Biopolymers Pept Sci 2006;84:250-66
    • (2006) Biopolymers Pept Sci , vol.84 , pp. 250-266
    • Craik, D.J.1    Cemazar, M.2    Wang, C.K.3
  • 26
    • 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 1973;33:400-8
    • (1973) Acta Pharmacol Toxicol , vol.33 , pp. 400-408
    • Gran, L.1
  • 28
  • 31
    • 0038322581 scopus 로고    scopus 로고
    • Linearization of a naturally occurring circular protein maintains structure but eliminates hemolytic activity
    • DOI 10.1021/bi027323n
    • Barry DG, Daly NL, Clark RJ, et al. Linearization of a naturally occurring circular protein maintains structure but eliminates hemolytic activity. Biochemistry 2003;42:6688-95 (Pubitemid 36666109)
    • (2003) Biochemistry , vol.42 , Issue.22 , pp. 6688-6695
    • Barry, D.G.1    Daly, N.L.2    Clark, R.J.3    Sando, L.4    Craik, D.J.5
  • 32
    • 80052650140 scopus 로고    scopus 로고
    • Evaluation of toxicity and anti-tumour activity of cycloviolacin O2 in mice
    • Burman R, Svedlund E, Felth J, et al. Evaluation of toxicity and anti-tumour activity of cycloviolacin O2 in mice. Biopolymers Pept Sci 2010;94:626-34
    • (2010) Biopolymers Pept Sci , vol.94 , pp. 626-634
    • Burman, R.1    Svedlund, E.2    Felth, J.3
  • 33
    • 79955567660 scopus 로고    scopus 로고
    • Anticancer and chemosensitizing abilities of cycloviolacin O2 from Viola odorata and psyle cyclotides from Psychotria leptothyrsa
    • Gerlach SL, Rathinakumar R, Chakravarty G, et al. Anticancer and chemosensitizing abilities of cycloviolacin O2 from Viola odorata and psyle cyclotides from Psychotria leptothyrsa. Biopolymers Pept Sci 2010;94:617-25
    • (2010) Biopolymers Pept Sci , vol.94 , pp. 617-625
    • Gerlach, S.L.1    Rathinakumar, R.2    Chakravarty, G.3
  • 34
    • 66649136413 scopus 로고    scopus 로고
    • Circling the enemy: Cyclic proteins in plant defence
    • Craik DJ. Circling the enemy: cyclic proteins in plant defence. Trends Plant Sci 2009;14:328-35
    • (2009) Trends Plant Sci , vol.14 , pp. 328-335
    • Craik, D.J.1
  • 35
    • 33847385325 scopus 로고    scopus 로고
    • Insecticidal plant cyclotides and related cystine knot toxins
    • DOI 10.1016/j.toxicon.2006.11.018, PII S004101010600434X
    • Gruber CW, Cemazar M, Anderson MA, et al. Insecticidal plant cyclotides and related cystine knot toxins. Toxicon 2007;49:561-75 (Pubitemid 46341392)
    • (2007) Toxicon , vol.49 , Issue.4 , pp. 561-575
    • Gruber, C.W.1    Cemazar M2    Anderson, M.A.3    Craik, D.J.4
  • 36
    • 54349090107 scopus 로고    scopus 로고
    • The anthelmintic activity of the cyclotides: Natural variants with enhanced activity
    • Colgrave ML, Kotze AC, Ireland DC, et al. The anthelmintic activity of the cyclotides: natural variants with enhanced activity. ChemBioChem 2008;9:1939-45
    • (2008) ChemBioChem , vol.9 , pp. 1939-1945
    • Colgrave, M.L.1    Kotze, A.C.2    Ireland, D.C.3
  • 37
    • 57849088141 scopus 로고    scopus 로고
    • Anthelmintic activity of cyclotides: In vitro studies with canine and human hookworms
    • Colgrave ML, Kotze AC, Kopp S, et al. Anthelmintic activity of cyclotides: In vitro studies with canine and human hookworms. Acta Trop 2009;109:163-6
    • (2009) Acta Trop , vol.109 , pp. 163-166
    • Colgrave, M.L.1    Kotze, A.C.2    Kopp, S.3
  • 38
    • 47849105966 scopus 로고    scopus 로고
    • Backbone cyclised peptides from plants show molluscicidal activity against the rice pest Pomacea canaliculate (golden apple snail)
    • DOI 10.1021/jf800302f
    • Plan MR, Saska I, Cagauan AG, et al. Backbone cyclised peptides from plants show molluscicidal activity against the rice pest Pomacea canaliculata golden apple snail. J Agric Food Chem 2008;56:5237-41 (Pubitemid 352039129)
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.13 , pp. 5237-5241
    • Plan, M.R.R.1    Saska, I.2    Cagauan, A.G.3    Craik, D.J.4
  • 40
    • 68949120908 scopus 로고    scopus 로고
    • The biological activity of the prototypic cyclotide kalata B1 is modulated by the formation of multimeric pores
    • Huang YH, Colgrave ML, Daly NL, et al. The biological activity of the prototypic cyclotide kalata B1 is modulated by the formation of multimeric pores. J Biol Chem 2009;284:20699-707
    • (2009) J Biol Chem , vol.284 , pp. 20699-20707
    • Huang, Y.H.1    Colgrave, M.L.2    Daly, N.L.3
  • 41
    • 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
    • DOI 10.1016/j.ab.2004.10.028, PII S0003269704008462
    • Kamimori H, Hall K, Craik DJ, 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 2005;337:149-53 (Pubitemid 40092791)
    • (2005) Analytical Biochemistry , vol.337 , Issue.1 , pp. 149-153
    • Kamimori, H.1    Hall, K.2    Craik, D.J.3    Aguilar, M.-I.4
  • 42
    • 84857388366 scopus 로고    scopus 로고
    • A synthetic mirror image of kalata B1 reveals that cyclotide activity is independent of a protein receptor
    • Sando L, Henriques ST, Foley F, et al. A synthetic mirror image of kalata B1 reveals that cyclotide activity is independent of a protein receptor. ChemBioChem 2011;12:2456-62
    • (2011) Chem Bio Chem , vol.12 , pp. 2456-2462
    • Sando, L.1    Henriques, S.T.2    Foley, F.3
  • 43
    • 0036257686 scopus 로고    scopus 로고
    • Converting a peptide into a drug: Strategies to improve stability and bioavailability
    • Adessi C, Soto C. Converting a peptide into a drug: strategies to improve stability and bioavailability. Curr Med Chem 2002;9:963-78 (Pubitemid 34498572)
    • (2002) Current Medicinal Chemistry , vol.9 , Issue.9 , pp. 963-978
    • Adessi, C.1    Soto, C.2
  • 44
    • 0031822610 scopus 로고    scopus 로고
    • A biomimetic strategy in the synthesis and fragmentation of cyclic protein
    • Tam JP, Lu Y-A. A biomimetic strategy in the synthesis and fragmentation of cyclic protein. Protein Sci 1998;7:1583-92 (Pubitemid 28331278)
    • (1998) Protein Science , vol.7 , Issue.7 , pp. 1583-1592
    • Tam, J.P.1    Lu, Y.I.-A.N.2
  • 45
    • 0033543137 scopus 로고    scopus 로고
    • Chemical synthesis and folding pathways of large cyclic polypeptides: Studies of the cystine knot polypeptide kalata B1
    • Daly NL, Love S, Alewood PF, et al. Chemical synthesis and folding pathways of large cyclic polypeptides: studies of the cystine knot polypeptide kalata B1. Biochemistry 1999;38:10606-14
    • (1999) Biochemistry , vol.38 , pp. 10606-10614
    • Daly, N.L.1    Love, S.2    Alewood, P.F.3
  • 47
    • 0037458652 scopus 로고    scopus 로고
    • Disulfide folding pathways of cystine knot proteins: Tying the knot within the circular backbone of the cyclotides
    • DOI 10.1074/jbc.M210492200
    • Daly NL, Clark RJ, Craik DJ. Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides. J Biol Chem 2003;278:6314-22 (Pubitemid 36800889)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 6314-6322
    • Daly, N.L.1    Clark, R.J.2    Craik, D.J.3
  • 48
    • 0346220263 scopus 로고    scopus 로고
    • Disulfide mapping of the cyclotide kalata B1. Chemical proof of the cyclic cystine knot motif
    • DOI 10.1074/jbc.M308771200
    • Goransson U, Craik DJ. Disulfide mapping of the cyclotide kalata B1. Chemical proof of the cyclic cystine knot motif. J Biol Chem 2003;278:48188-96 (Pubitemid 37523272)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.48 , pp. 48188-48196
    • Goransson, U.1    Craik, D.J.2
  • 49
    • 33749128301 scopus 로고    scopus 로고
    • Chemical synthesis and biosynthesis of the cyclotide family of circular proteins
    • DOI 10.1080/15216540600889532, PII KP287U827L852077
    • Gunasekera S, Daly NL, Anderson MA, et al. Chemical synthesis and biosynthesis of the cyclotide family of circular proteins. IUBMB Life 2006;58:515-24 (Pubitemid 44470237)
    • (2006) IUBMB Life , vol.58 , Issue.9 , pp. 515-524
    • Gunasekera, S.1    Daly, N.L.2    Anderson, M.A.3    Craik, D.J.4
  • 50
    • 14844315799 scopus 로고    scopus 로고
    • Oxidative folding of the cystine knot motif in cyclotide proteins
    • DOI 10.2174/0929866053005863
    • Craik DJ, Daly NL. Oxidative folding of the cystine knot motif in cyclotide proteins. Protein Pept Lett 2005;12:147-52 (Pubitemid 40335666)
    • (2005) Protein and Peptide Letters , vol.12 , Issue.2 , pp. 147-152
    • Craik, D.J.1    Daly, N.L.2
  • 51
    • 79954569541 scopus 로고    scopus 로고
    • Discovery of cyclotides in the Fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins
    • Poth AG, Colgrave ML, Philip R, et al. Discovery of cyclotides in the Fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. ACS Chem Biol 2011;6:345-55
    • (2011) ACS Chem Biol , vol.6 , pp. 345-355
    • Poth, A.G.1    Colgrave, M.L.2    Philip, R.3
  • 52
    • 45849122826 scopus 로고    scopus 로고
    • Plant cell culture technology-harnessing a biological approach for competitive cyclotides production
    • Dornenburg H. Plant cell culture technology-harnessing a biological approach for competitive cyclotides production. Biotechnol Lett 2008;30:1311-21
    • (2008) Biotechnol Lett , vol.30 , pp. 1311-1321
    • Dornenburg, H.1
  • 53
    • 68049092854 scopus 로고    scopus 로고
    • Progress in kalata peptide production via plant cell bioprocessing
    • Dornenburg H. Progress in kalata peptide production via plant cell bioprocessing. Biotechnol J 2009;4:632-45
    • (2009) Biotechnol J , vol.4 , pp. 632-645
    • Dornenburg, H.1
  • 54
    • 80054879031 scopus 로고    scopus 로고
    • Cyclotide synthesis and supply: From plant to bioprocess
    • Dornenburg H. Cyclotide synthesis and supply: from plant to bioprocess. Biopolymers Pept Sci 2010;94:602-10
    • (2010) Biopolymers Pept Sci , vol.94 , pp. 602-610
    • Dornenburg, H.1
  • 55
    • 43049115684 scopus 로고    scopus 로고
    • Plant cell-based processes for cyclotides production
    • Dornenburg H, Frickinger P, Seydel P. Plant cell-based processes for cyclotides production. J Biotechnol 2008;135:123-6
    • (2008) J Biotechnol , vol.135 , pp. 123-126
    • Dornenburg, H.1    Frickinger, P.2    Seydel, P.3
  • 56
    • 33744953723 scopus 로고    scopus 로고
    • Establishment of in vitro plants, cell and tissue cultures from Oldenlandia affinis for the production of cyclic peptides
    • DOI 10.1007/s11240-005-9056-0
    • Seydel P, Dornenburg H. Establishment of in vitro plants, cell and tissue cultures from Oldenlandia affinis for the production of cyclic peptides. Plant Cell Tissue Organ Cult 2006;85:247-55 (Pubitemid 43854269)
    • (2006) Plant Cell, Tissue and Organ Culture , vol.85 , Issue.3 , pp. 247-255
    • Seydel, P.1    Dornenburg, H.2
  • 57
    • 35649012780 scopus 로고    scopus 로고
    • Formation of cyclotides and variations in cyclotide expression in Oldenlandia affinis suspension cultures
    • DOI 10.1007/s00253-007-1159-6
    • Seydel P, Gruber CW, Craik DJ, et al. Formation of cyclotides and variations in cyclotide expression in Oldenlandia affinis suspension cultures. Appl Microbiol Biotechnol 2007;77:275-84 (Pubitemid 350029441)
    • (2007) Applied Microbiology and Biotechnology , vol.77 , Issue.2 , pp. 275-284
    • Seydel, P.1    Gruber, C.W.2    Craik, D.J.3    Dornenburg, H.4
  • 58
    • 52949116910 scopus 로고    scopus 로고
    • Biosynthesis of the cyclotide kalata B1 by using protein splicing
    • Kimura RH, Tran A-T, Camarero JA. Biosynthesis of the cyclotide kalata B1 by using protein splicing. Angew Chem Int Ed Engl 2006;118:987-90
    • (2006) Angew Chem Int Ed Engl , vol.118 , pp. 987-990
    • Kimura, R.H.1    Tran, A.-T.2    Camarero, J.A.3
  • 59
    • 34548127744 scopus 로고    scopus 로고
    • Biosynthesis of a fully functional cyclotide inside living bacterial cells
    • DOI 10.1002/cbic.200700183
    • Camarero JA, Kimura RH, Woo Y-H, et al. Biosynthesis of a fully functional cyclotide inside living bacterial cells. Chem Bio Chem 2007;8:1363-6 (Pubitemid 47300326)
    • (2007) ChemBioChem , vol.8 , Issue.12 , pp. 1363-1366
    • Camarero, J.A.1    Kimura, R.H.2    Woo, Y.-H.3    Shekhtman, A.4    Cantor, J.5
  • 60
    • 78649987052 scopus 로고    scopus 로고
    • Cyclotides, a promising molecular scaffold for peptide-based therapeutics
    • Jagadish K, Camarero JA. Cyclotides, a promising molecular scaffold for peptide-based therapeutics. Biopolymers Pept Sci 2010;94:611-16
    • (2010) Biopolymers Pept Sci , vol.94 , pp. 611-616
    • Jagadish, K.1    Camarero, J.A.2
  • 61
    • 0038498076 scopus 로고    scopus 로고
    • Enzymatic cyclization of a potent bowman-birk protease inhibitor, sunflower trypsin inhibitor-1, and solution structure of an acyclic precursor peptide
    • DOI 10.1074/jbc.M212996200
    • Marx UC, Korsinczky ML, Schirra HJ, et al. Enzymatic cyclization of a potent Bowman-Birk protease inhibitor, sunflower trypsin inhibitor-1, and solution structure of an acyclic precursor peptide. J Biol Chem 2003;278:21782-9 (Pubitemid 36792582)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 21782-21789
    • Marx, U.C.1    Korsinczky, M.L.J.2    Schirra, H.J.3    Jones, A.4    Condie, B.5    Otvos Jr., L.6    Craik, D.J.7
  • 62
    • 34547566772 scopus 로고    scopus 로고
    • Immobilized protease-assisted synthesis of engineered cysteine-knot microproteins
    • DOI 10.1002/cbic.200700187
    • Thongyoo P, Jaulent AM, Tate EW, et al. Immobilized protease-assisted synthesis of engineered cysteine-knot microproteins. Chem Bio Chem 2007;8:1107-9 (Pubitemid 47194814)
    • (2007) ChemBioChem , vol.8 , Issue.10 , pp. 1107-1109
    • Thongyoo, P.1    Jaulent, A.M.2    Tate, E.W.3    Leatherbarrow, R.J.4
  • 63
    • 4444359659 scopus 로고    scopus 로고
    • Novel strategies for isolation and characterization of cyclotides: The discovery of bioactive macrocyclic plant polypeptides in the Violaceae
    • DOI 10.2174/1389203043379495
    • Goransson U, Svangard E, Claeson P, et al. Novel strategies for isolation and characterization of cyclotides: the discovery of bioactive macrocyclic plant polypeptides in the Violaceae. Curr Protein Pept Sci 2004;5:317-29 (Pubitemid 39200162)
    • (2004) Current Protein and Peptide Science , vol.5 , Issue.5 , pp. 317-329
    • Goransson, U.1    Svangard, E.2    Claeson, P.3    Bohlin, L.4
  • 64
    • 77957236219 scopus 로고    scopus 로고
    • Isolation, sequencing, and structure-activity relationships of cyclotides
    • Ireland DC, Clark RJ, Daly NL, et al. Isolation, sequencing, and structure-activity relationships of cyclotides. J Nat Prod 2010;73:1610-22
    • (2010) J Nat Prod , vol.73 , pp. 1610-1622
    • Ireland, D.C.1    Clark, R.J.2    Daly, N.L.3
  • 65
    • 79958826757 scopus 로고    scopus 로고
    • The chemistry of cyclotides
    • Craik DJ, Conibear AC. The chemistry of cyclotides. J Org Chem 2011;76:4805-17
    • (2011) J Org Chem , vol.76 , pp. 4805-4817
    • Craik, D.J.1    Conibear, A.C.2
  • 66
    • 33947359890 scopus 로고    scopus 로고
    • NMR as a tool for elucidating the structures of circular and knotted proteins
    • DOI 10.1039/b616856f
    • Craik DJ, Daly NL. NMR as a tool for elucidating the structures of circular and knotted proteins. Mol Biosyst 2007;3:257-65 (Pubitemid 46456310)
    • (2007) Molecular BioSystems , vol.3 , Issue.4 , pp. 257-265
    • Craik, D.J.1    Daly, N.L.2
  • 68
  • 69
    • 73749087526 scopus 로고    scopus 로고
    • Cyclotides as templates in drug design
    • Henriques ST, Craik DJ. Cyclotides as templates in drug design. Drug Discov Today 2010;15:57-64
    • (2010) Drug Discov Today , vol.15 , pp. 57-64
    • Henriques, S.T.1    Craik, D.J.2
  • 70
    • 78650009505 scopus 로고    scopus 로고
    • Biological activities of natural and engineered cyclotides, a novel molecular scaffold for peptide-based therapeutics
    • Garcia AE, Camarero JA. Biological activities of natural and engineered cyclotides, a novel molecular scaffold for peptide-based therapeutics. Curr Mol Pharmacol 2010;3:153-63
    • (2010) Curr Mol Pharmacol , vol.3 , pp. 153-163
    • Garcia, A.E.1    Camarero, J.A.2
  • 72
    • 84857602297 scopus 로고    scopus 로고
    • The University of Queensland and Hexima Ltd, assignee.
    • The University of Queensland and Hexima Ltd, assignee. Novel nucleic acid molecules. WO0134829; 2000
    • (2000) Novel Nucleic Acid Molecules. WO0134829
  • 73
    • 84857555075 scopus 로고    scopus 로고
    • The University of Queensland, assignee
    • The University of Queensland, assignee. Cystine knot molecules. US7960340; 2000
    • (2000) Cystine Knot Molecules. US7960340
  • 78
    • 84857555084 scopus 로고    scopus 로고
    • Pioneer Hi Breed International, Inc. and E.I. Du Pont De Nemours & Co., assignee
    • Pioneer Hi Breed International, Inc. and E.I. Du Pont De Nemours & Co., assignee. Maize cyclo1 gene and promoter. WO06076189; 2006
    • (2006) Maize cyclo1 Gene and Promoter. WO06076189
  • 83
    • 73749087228 scopus 로고    scopus 로고
    • Cyclotides: Macrocyclic peptides with applications in drug design and agriculture
    • Craik DJ, Mylne JS, Daly NL. Cyclotides: macrocyclic peptides with applications in drug design and agriculture. Cell Mol Life Sci 2010;67:9-16
    • (2010) Cell Mol Life Sci , vol.67 , pp. 9-16
    • Craik, D.J.1    Mylne, J.S.2    Daly, N.L.3
  • 84
    • 70349414437 scopus 로고    scopus 로고
    • Biological diversity and therapeutic potential of natural and engineered cystine knot miniproteins
    • Kolmar H. Biological diversity and therapeutic potential of natural and engineered cystine knot miniproteins. Curr Opin Pharmacol 2009;9:608-14
    • (2009) Curr Opin Pharmacol , vol.9 , pp. 608-614
    • Kolmar, H.1
  • 85
    • 43949138210 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of the prototypic cyclotide reveals a cluster of residues essential for bioactivity
    • Simonsen SM, Sando L, Rosengren KJ, et al. Alanine scanning mutagenesis of the prototypic cyclotide reveals a cluster of residues essential for bioactivity. J Biol Chem 2008;283:9805-13
    • (2008) J Biol Chem , vol.283 , pp. 9805-9813
    • Simonsen, S.M.1    Sando, L.2    Rosengren, K.J.3
  • 86
    • 77951247943 scopus 로고    scopus 로고
    • Lysine-scanning mutagenesis reveals an amendable face of the cyclotide kalata B1 for the optimization of nematocidal activity
    • Huang YH, Colgrave ML, Clark RJ, et al. Lysine-scanning mutagenesis reveals an amendable face of the cyclotide kalata B1 for the optimization of nematocidal activity. J Biol Chem 2010;285:10797-805
    • (2010) J Biol Chem , vol.285 , pp. 10797-10805
    • Huang, Y.H.1    Colgrave, M.L.2    Clark, R.J.3
  • 87
    • 0034705410 scopus 로고    scopus 로고
    • Acyclic permutants of naturally occurring cyclic proteins: Characterization of cystine knot and beta-sheet formation in the macrocyclic polypeptide kalata B1
    • DOI 10.1074/jbc.M000450200
    • Daly NL, Craik DJ. Acyclic permutants of naturally occurring cyclic proteins. Characterization of cystine knot and beta -sheet formation in the macrocyclic polypeptide kalata B1. J Biol Chem 2000;275:19068-75 (Pubitemid 30422874)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 19068-19075
    • Daly, N.L.1    Craik, D.J.2
  • 88
    • 77956502216 scopus 로고    scopus 로고
    • The engineering of an orally active conotoxin for the treatment of neuropathic pain
    • Clark RJ, Jensen J, Nevin ST, et al. The engineering of an orally active conotoxin for the treatment of neuropathic pain. Angew Chem Int Ed 2010;49:6545-8
    • (2010) Angew Chem Int Ed , vol.49 , pp. 6545-6548
    • Clark, R.J.1    Jensen, J.2    Nevin, S.T.3
  • 90
    • 67649547851 scopus 로고    scopus 로고
    • Substrate-guided design of a potent and selective kallikrein-related peptidase inhibitor for kallikrein 4
    • Swedberg JE, Nigon LV, Reid JC, et al. Substrate-guided design of a potent and selective kallikrein-related peptidase inhibitor for kallikrein 4. Chem Biol 2009;16:633-43
    • (2009) Chem Biol , vol.16 , pp. 633-643
    • Swedberg, J.E.1    Nigon, L.V.2    Reid, J.C.3
  • 91
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins
    • Tang YQ, Yuan J, Osapay G, et al. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins. Science 1999;286:498-502
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3
  • 94
    • 4444331457 scopus 로고    scopus 로고
    • The role of the cyclic peptide backbone in the anti-HIV activity of the cyclotide kalata B1
    • DOI 10.1016/j.febslet.2004.08.007, PII S001457930400986X
    • Daly NL, Gustafson KR, Craik DJ. The role of the cyclic peptide backbone in the anti-HIV activity of the cyclotide kalata B1. FEBS Lett 2004;574:69-72 (Pubitemid 39200896)
    • (2004) FEBS Letters , vol.574 , Issue.1-3 , pp. 69-72
    • Daly, N.L.1    Gustafson, K.R.2    Craik, D.J.3
  • 95
    • 79959914450 scopus 로고    scopus 로고
    • Decoding the membrane activity of the cyclotide kalata B1
    • Henriques ST, Huang Y-H, Rosengren KJ, et al. Decoding the membrane activity of the cyclotide kalata B1. J Biol Chem 2011;286:24231-41
    • (2011) J Biol Chem , vol.286 , pp. 24231-24241
    • Henriques, S.T.1    Huang, Y.-H.2    Rosengren, K.J.3
  • 97
    • 77955645237 scopus 로고    scopus 로고
    • The cyclotide cycloviolacin O2 from Viola odorata has potent bactericidal activity against Gram-negative bacteria
    • Pranting M, Loov C, Burman R, et al. The cyclotide cycloviolacin O2 from Viola odorata has potent bactericidal activity against Gram-negative bacteria. J Antimicrob Chemother 2010;65:1964-71
    • (2010) J Antimicrob Chemother , vol.65 , pp. 1964-1971
    • Pranting, M.1    Loov, C.2    Burman, R.3
  • 98
    • 32944465547 scopus 로고    scopus 로고
    • Structural plasticity of the cyclic-cystine-knot framework: Implications for biological activity and drug design
    • DOI 10.1042/BJ20051691
    • Clark RJ, Daly NL, Craik DJ. Structural plasticity of the cyclic-cystine-knot framework: implications for biological activity and drug design. Biochem J 2006;394:85-93 (Pubitemid 43259658)
    • (2006) Biochemical Journal , vol.394 , Issue.1 , pp. 85-93
    • Clark, R.J.1    Daly, N.L.2    Craik, D.J.3
  • 99
    • 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, Foley FM, Clark RJ, et al. Engineering stabilized vascular endothelial growth factor-A antagonists: synthesis, structural characterization, and bioactivity of grafted analogues of cyclotides. J Med Chem 2008;51:7697-704
    • (2008) J Med Chem , vol.51 , pp. 7697-7704
    • Gunasekera, S.1    Foley, F.M.2    Clark, R.J.3
  • 101
    • 84055177578 scopus 로고    scopus 로고
    • Engineering pro-angiogenic peptides using stable disulfide-rich cyclic scaffolds
    • Chan LY, Gunasekera S, Henriques ST, et al. Engineering pro-angiogenic peptides using stable disulfide-rich cyclic scaffolds. Blood 2011;118:6709-17
    • (2011) Blood , vol.118 , pp. 6709-6717
    • Chan, L.Y.1    Gunasekera, S.2    Henriques, S.T.3
  • 102
    • 70350059832 scopus 로고    scopus 로고
    • Potent inhibitors of beta-tryptase and human leukocyte elastase based on the MCoTI-II scaffold
    • Thongyoo P, Bonomelli C, Leatherbarrow RJ, et al. Potent inhibitors of beta-tryptase and human leukocyte elastase based on the MCoTI-II scaffold. J Med Chem 2009;52:6197-200
    • (2009) J Med Chem , vol.52 , pp. 6197-6200
    • Thongyoo, P.1    Bonomelli, C.2    Leatherbarrow, R.J.3
  • 103
    • 63149084613 scopus 로고    scopus 로고
    • Knottin cyclization: Impact on structure and dynamics
    • Heitz A, Avrutina O, Le-Nguyen D, et al. Knottin cyclization: impact on structure and dynamics. BMC Struct Biol 2008;8:54
    • (2008) BMC Struct Biol , vol.8 , pp. 54
    • Heitz, A.1    Avrutina, O.2    Le-Nguyen, D.3
  • 105
    • 80054689774 scopus 로고    scopus 로고
    • Identification and characterization of a new family of cell-penetrating peptides: Cyclic cell-penetrating peptides
    • Cascales L, Henriques ST, Kerr MC, et al. Identification and characterization of a new family of cell-penetrating peptides: cyclic cell-penetrating peptides. J Biol Chem 2011;286:36932-43
    • (2011) J Biol Chem , vol.286 , pp. 36932-36943
    • Cascales, L.1    Henriques, S.T.2    Kerr, M.C.3
  • 106
    • 80054094292 scopus 로고    scopus 로고
    • Cellular uptake of cyclotide MCoTI-I follows multiple endocytic pathways
    • Contreras J, Elnagar AYO, Hamm-Alvarez SF, et al. Cellular uptake of cyclotide MCoTI-I follows multiple endocytic pathways. J Control Release 2011;155:134-43
    • (2011) J Control Release , vol.155 , pp. 134-143
    • Contreras, J.1    Elnagar, A.Y.O.2    Hamm-Alvarez, S.F.3
  • 107
    • 71049186869 scopus 로고    scopus 로고
    • Biosynthesis and biological screening of a genetically encoded library based on the cyclotide MCoTI-I
    • Austin J, Wang W, Puttamadappa S, et al. Biosynthesis and biological screening of a genetically encoded library based on the cyclotide MCoTI-I. Chem Bio Chem 2009;10:2663-70
    • (2009) Chem Bio Chem , vol.10 , pp. 2663-2670
    • Austin, J.1    Wang, W.2    Puttamadappa, S.3
  • 108
    • 79957944066 scopus 로고    scopus 로고
    • Update 1 of: Proteases universally recognize beta strands in their active sites
    • Madala PK, Tyndall JD, Nall T, et al. Update 1 of: Proteases universally recognize beta strands in their active sites. Chem Rev 2010;110:PR1-31
    • (2010) Chem Rev , vol.110
    • Madala, P.K.1    Tyndall, J.D.2    Nall, T.3
  • 109
    • 77955373045 scopus 로고    scopus 로고
    • Kallikreins on steroids: Structure, function, and hormonal regulation of prostate-specific antigen and the extended kallikrein locus
    • Lawrence MG, Lai J, Clements JA. Kallikreins on steroids: structure, function, and hormonal regulation of prostate-specific antigen and the extended kallikrein locus. Endocr Rev 2010;31:407-46
    • (2010) Endocr Rev , vol.31 , pp. 407-446
    • Lawrence, M.G.1    Lai, J.2    Clements, J.A.3
  • 111
    • 84857560905 scopus 로고    scopus 로고
    • Non-combinatorial library screening reveals subsite cooperativity and identifies new high efficiency substrates for kallikrein-related peptidase 14
    • (in press), published on-line 9 Jan, PMID: 22148894, DOI: 10.1515/bc-2011-250
    • de Veer SJ, Swedberg JE, Parker EA, et al. Non-combinatorial library screening reveals subsite cooperativity and identifies new high efficiency substrates for kallikrein-related peptidase 14. Biol Chem (in press), published on-line 9 Jan 2012, PMID: 22148894, DOI: 10.1515/bc-2011-250
    • (2012) Biol Chem
    • De Veer, S.J.1    Swedberg, J.E.2    Parker, E.A.3
  • 112
    • 80053401993 scopus 로고    scopus 로고
    • Plasmin substrate binding site cooperativity guides the design of potent peptide aldehyde inhibitors
    • Swedberg JE, Harris JM. Plasmin substrate binding site cooperativity guides the design of potent peptide aldehyde inhibitors. Biochemistry 2011;50:8454-62
    • (2011) Biochemistry , vol.50 , pp. 8454-8462
    • Swedberg, J.E.1    Harris, J.M.2
  • 113
    • 0036479317 scopus 로고    scopus 로고
    • Homodimeric -defensins from Rhesus macaque leukocytes. Isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides
    • DOI 10.1074/jbc.M109117200
    • Tran D, Tran PA, Tang YQ, et al. Homodimeric theta-defensins from rhesus macaque leukocytes: isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides. J Biol Chem 2002;277:3079-84 (Pubitemid 34953167)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3079-3084
    • Tran, D.1    Tran, P.A.2    Tang, Y.-Q.3    Yuan, J.4    Cole, T.5    Selsted, M.E.6
  • 114
    • 70350278897 scopus 로고    scopus 로고
    • Rhesus theta-defensin prevents death in a mouse model of severe acute respiratory syndrome coronavirus pulmonary disease
    • Wohlford-Lenane CL, Meyerholz DK, Perlman S, et al. Rhesus theta-defensin prevents death in a mouse model of severe acute respiratory syndrome coronavirus pulmonary disease. J Virol 2009;83:11385-90
    • (2009) J Virol , vol.83 , pp. 11385-11390
    • Wohlford-Lenane, C.L.1    Meyerholz, D.K.2    Perlman, S.3
  • 116
    • 1042302158 scopus 로고    scopus 로고
    • Evolution of primate -defensins: A serpentine path to a sweet tooth
    • DOI 10.1016/j.peptides.2003.07.023
    • Nguyen TX, Cole AM, Lehrer RI. Evolution of primate theta-defensins: a serpentine path to a sweet tooth. Peptides 2003;24:1647-54 (Pubitemid 38198072)
    • (2003) Peptides , vol.24 , Issue.11 , pp. 1647-1654
    • Nguyen, T.X.1    Cole, A.M.2    Lehrer, R.I.3
  • 118
    • 80051809310 scopus 로고    scopus 로고
    • Humanized theta-defensins (retrocyclins) enhance macrophage performance and protect mice from experimental anthrax infections
    • Welkos S, Cote CK, Hahn U, et al. Humanized theta-defensins (retrocyclins) enhance macrophage performance and protect mice from experimental anthrax infections. Antimicrob Agents Chemother 2011;55:4238-50
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 4238-4250
    • Welkos, S.1    Cote, C.K.2    Hahn, U.3
  • 121
    • 65949105709 scopus 로고    scopus 로고
    • Reawakening retrocyclins: Ancestral human defensins active against HIV-1
    • Venkataraman N, Cole AL, Ruchala P, et al. Reawakening retrocyclins: ancestral human defensins active against HIV-1. PLoS Biol 2009;7:e95
    • (2009) PLoS Biol , vol.7
    • Venkataraman, N.1    Cole, A.L.2    Ruchala, P.3
  • 123
    • 79960947133 scopus 로고    scopus 로고
    • Retrocyclins and their activity against HIV-1
    • Penberthy WT, Chari S, Cole AL, et al. Retrocyclins and their activity against HIV-1. Cell Mol Life Sci 2011;68:2231-42
    • (2011) Cell Mol Life Sci , vol.68 , pp. 2231-2242
    • Penberthy, W.T.1    Chari, S.2    Cole, A.L.3
  • 125
    • 81355146481 scopus 로고    scopus 로고
    • Simplified theta-Defensins: Search for new antivirals
    • Ruchala P, Cho S, Cole A, et al. Simplified theta-Defensins: search for new antivirals. Int J Pept Res Ther 2011;17:325-36
    • (2011) Int J Pept Res Ther , vol.17 , pp. 325-336
    • Ruchala, P.1    Cho, S.2    Cole, A.3
  • 126
    • 78650067828 scopus 로고    scopus 로고
    • Expression and characterization of antimicrobial peptides Retrocyclin-101 and Protegrin-1 in chloroplasts to control viral and bacterial infections
    • Lee SB, Li B, Jin S, et al. Expression and characterization of antimicrobial peptides Retrocyclin-101 and Protegrin-1 in chloroplasts to control viral and bacterial infections. Plant Biotechnol J 2011;9:100-15
    • (2011) Plant Biotechnol J , vol.9 , pp. 100-115
    • Lee, S.B.1    Li, B.2    Jin, S.3
  • 127
    • 77955881150 scopus 로고    scopus 로고
    • In vivo biosynthesis of an Ala-scan library based on the cyclic peptide SFTI-1
    • Austin J, Kimura RH, Woo YH, et al. In vivo biosynthesis of an Ala-scan library based on the cyclic peptide SFTI-1. Amino Acids 2010;38:1313-22
    • (2010) Amino Acids , vol.38 , pp. 1313-1322
    • Austin, J.1    Kimura, R.H.2    Woo, Y.H.3
  • 128
    • 33645077862 scopus 로고    scopus 로고
    • Seamless proteins tie up their loose ends
    • Craik DJ. Seamless proteins tie up their loose ends. Science 2006;311:1563-4
    • (2006) Science , vol.311 , pp. 1563-1564
    • Craik, D.J.1
  • 129
    • 78049323503 scopus 로고    scopus 로고
    • Naturally occurring circular proteins: Distribution, biosynthesis and evolution
    • Cascales L, Craik DJ. Naturally occurring circular proteins: distribution, biosynthesis and evolution. Org Biomol Chem 2010;8:5035-47
    • (2010) Org Biomol Chem , vol.8 , pp. 5035-5047
    • Cascales, L.1    Craik, D.J.2
  • 131
    • 4444341077 scopus 로고    scopus 로고
    • Defensins: Cyclic antimicrobial peptides produced by binary ligation of truncated alpha-defensins
    • DOI 10.2174/1389203043379459
    • Selsted ME. Theta-defensins: cyclic antimicrobial peptides produced by binary ligation of truncated alpha-defensins. Curr Protein Pept Sci 2004;5:365-71 (Pubitemid 39200166)
    • (2004) Current Protein and Peptide Science , vol.5 , Issue.5 , pp. 365-371
    • Selsted, M.E.1
  • 132
    • 0036495674 scopus 로고    scopus 로고
    • Circular proteins - No end in sight
    • DOI 10.1016/S0968-0004(02)02057-1, PII S0968000402020571
    • Trabi M, Craik DJ. Circular proteins - no end in sight. Trends Biochem Sci 2002;27:132-8 (Pubitemid 34219323)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.3 , pp. 132-138
    • Trabi, M.1    Craik, D.J.2
  • 133
    • 79955058492 scopus 로고    scopus 로고
    • Albumins and their processing machinery are hijacked for cyclic peptides in sunflower
    • Mylne JS, Colgrave ML, Daly NL, et al. Albumins and their processing machinery are hijacked for cyclic peptides in sunflower. Nat Chem Biol 2011;7:257-9
    • (2011) Nat Chem Biol , vol.7 , pp. 257-259
    • Mylne, J.S.1    Colgrave, M.L.2    Daly, N.L.3
  • 135
    • 33751073415 scopus 로고    scopus 로고
    • A novel suite of cyclotides from Viola odorata: Sequence variation and the implications for structure, function and stability
    • DOI 10.1042/BJ20060627
    • Ireland DC, Colgrave ML, Craik DJ. A novel suite of cyclotides from Viola odorata: sequence variation and the implications for structure, function and stability. Biochem J 2006;400:1-12 (Pubitemid 44763814)
    • (2006) Biochemical Journal , vol.400 , Issue.1 , pp. 1-12
    • Ireland, D.C.1    Colgrave, M.L.2    Craik, D.J.3
  • 138
    • 31544481160 scopus 로고    scopus 로고
    • Kalata B8, a novel antiviral circular protein, exhibits conformational flexibility in the cystine knot motif
    • DOI 10.1042/BJ20051371
    • Daly NL, Clark RJ, Plan MR, et al. Kalata B8, a novel antiviral circular protein, exhibits conformational flexibility in the cystine knot motif. Biochem J 2006;393:619-26 (Pubitemid 43163802)
    • (2006) Biochemical Journal , vol.393 , Issue.3 , pp. 619-626
    • Daly, N.L.1    Clark, R.J.2    Plan, M.R.3    Craik, D.J.4
  • 140
    • 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
    • DOI 10.1074/jbc.M501737200
    • Chen B, Colgrave ML, Daly NL, 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 2005;280:22395-405 (Pubitemid 40827895)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.23 , pp. 22395-22405
    • Chen, B.1    Colgrave, M.L.2    Daly, N.L.3    Rosengren, K.J.4    Gustafson, K.R.5    Craik, D.J.6


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