메뉴 건너뛰기




Volumn 8, Issue 6, 2013, Pages

Cyclotides Suppress Human T-Lymphocyte Proliferation by an Interleukin 2-Dependent Mechanism

Author keywords

cyclotide; cytokine; immunosuppression; lymphocytes; peptide; plant; proliferation

Indexed keywords

CYCLOSPORIN A; CYCLOTIDE; CYTOKINE; GAMMA INTERFERON; IMMUNOSUPPRESSIVE AGENT; INTERLEUKIN 2; INTERLEUKIN 2 RECEPTOR; KALATA B1; MUTANT PROTEIN; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84879484015     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0068016     Document Type: Article
Times cited : (66)

References (53)
  • 1
    • 17644396349 scopus 로고    scopus 로고
    • Immunology of multiple sclerosis
    • doi:10.1146/annurev.immunol.23.021704.115707
    • Sospedra M, Martin R, (2005) Immunology of multiple sclerosis. Annu Rev Immunol 23: 683-747. doi:10.1146/annurev.immunol.23.021704.115707. PubMed: 15771584.
    • (2005) Annu Rev Immunol , vol.23 , pp. 683-747
    • Sospedra, M.1    Martin, R.2
  • 2
    • 0034045947 scopus 로고    scopus 로고
    • Mechanisms of action of cyclosporine
    • doi:10.1016/S0162-3109(00)00192-2
    • Matsuda S, Koyasu S, (2000) Mechanisms of action of cyclosporine. Immunopharmacology 47: 119-125. doi:10.1016/S0162-3109(00)00192-2. PubMed: 10878286.
    • (2000) Immunopharmacology , vol.47 , pp. 119-125
    • Matsuda, S.1    Koyasu, S.2
  • 3
    • 0026030568 scopus 로고
    • Chemistry and Biology of the immunophilins and their immunosuppressive ligands
    • doi:10.1126/science.1702904. PubMed: 1702904
    • Schreiber SL, (1991) Chemistry and Biology of the immunophilins and their immunosuppressive ligands. Science 251: 283-287. doi:10.1126/science.1702904. PubMed: 1702904.
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 4
    • 0033979599 scopus 로고    scopus 로고
    • Nephrotoxicity of immunosuppressive drugs: Long-term consequences and challenges for the future
    • 10.1016/S0272-6386(00)70348-9
    • de Mattos AM, Olyaei AJ, Bennett WM, (2000) Nephrotoxicity of immunosuppressive drugs: Long-term consequences and challenges for the future. Am J Kidney Dis 35: 333-346. doi:10.1016/S0272-6386(00)70348-9. PubMed: 10676738.
    • (2000) Am J Kidney Dis , vol.35 , pp. 333-346
    • de Mattos, A.M.1    Olyaei, A.J.2    Bennett, W.M.3
  • 5
    • 51149119689 scopus 로고    scopus 로고
    • Colutellin A, an immunosuppressive peptide from Colletotrichum dematium
    • doi: 10.1099/mic.0.2008/017954-0
    • Ren Y, Strobel GA, Graff JC, Jutila M, Park SG, et al. (2008) Colutellin A, an immunosuppressive peptide from Colletotrichum dematium. Microbiology 154: 1973-1979. doi:10.1099/mic.0.2008/017954-0. PubMed: 18599825.
    • (2008) Microbiology , vol.154 , pp. 1973-1979
    • Ren, Y.1    Strobel, G.A.2    Graff, J.C.3    Jutila, M.4    Park, S.G.5
  • 6
    • 80052943523 scopus 로고    scopus 로고
    • Cyclolinopeptide derivatives modify methotrexate-induced suppression of the humoral immune response in mice
    • doi: 10.1016/j.ejmech.2011.07.040
    • Katarzyńska J, Mazur A, Rudzińska E, Artym J, Zimecki M, et al. (2011) Cyclolinopeptide derivatives modify methotrexate-induced suppression of the humoral immune response in mice. Eur J Med Chem 46: 4608-4617. doi:10.1016/j.ejmech.2011.07.040. PubMed: 21839548.
    • (2011) Eur J Med Chem , vol.46 , pp. 4608-4617
    • Katarzyńska, J.1    Mazur, A.2    Rudzińska, E.3    Artym, J.4    Zimecki, M.5
  • 7
    • 0037653363 scopus 로고    scopus 로고
    • Immunosuppressive effects of a Kv1.3 inhibitor
    • doi: 10.1016/S0008-8749(03)00063-7
    • Shah K, Tom Blake J, Huang C, Fischer P, Koo GC, (2003) Immunosuppressive effects of a Kv1.3 inhibitor. Cell Immunol 221: 100-106. doi:10.1016/S0008-8749(03)00063-7. PubMed: 12747950.
    • (2003) Cell Immunol , vol.221 , pp. 100-106
    • Shah, K.1    Tom Blake, J.2    Huang, C.3    Fischer, P.4    Koo, G.C.5
  • 8
    • 84865267824 scopus 로고    scopus 로고
    • Vm24, a natural immunosuppressive peptide, potently and selectively blocks Kv1.3 potassium channels of human T cells
    • doi: 10.1124/mol.112.078006
    • Varga Z, Gurrola-Briones G, Papp F, Rodríguez de la Vega RC, Pedraza-Alva G, et al. (2012) Vm24, a natural immunosuppressive peptide, potently and selectively blocks Kv1.3 potassium channels of human T cells. Mol Pharmacol 82: 372-382. doi:10.1124/mol.112.078006. PubMed: 22622363.
    • (2012) Mol Pharmacol , vol.82 , pp. 372-382
    • Varga, Z.1    Gurrola-Briones, G.2    Papp, F.3    Rodríguez de la Vega, R.C.4    Pedraza-Alva, G.5
  • 9
    • 84861164829 scopus 로고    scopus 로고
    • Structure, function, and chemical synthesis of Vaejovis mexicanus peptide 24: a novel potent blocker of Kv1.3 potassium channels of human T lymphocytes
    • doi: 10.1021/bi300060n
    • Gurrola GB, Hernández-López RA, Rodríguez de la Vega RC, Varga Z, Batista CV, et al. (2012) Structure, function, and chemical synthesis of Vaejovis mexicanus peptide 24: a novel potent blocker of Kv1.3 potassium channels of human T lymphocytes. Biochemistry 51: 4049-4061. doi:10.1021/bi300060n. PubMed: 22540187.
    • (2012) Biochemistry , vol.51 , pp. 4049-4061
    • Gurrola, G.B.1    Hernández-López, R.A.2    Rodríguez de la Vega, R.C.3    Varga, Z.4    Batista, C.V.5
  • 10
    • 78649853209 scopus 로고    scopus 로고
    • Ligand-based peptide design and combinatorial peptide libraries to target G protein-coupled receptors
    • doi: 10.2174/138161210793292474
    • Gruber CW, Muttenthaler M, Freissmuth M, (2010) Ligand-based peptide design and combinatorial peptide libraries to target G protein-coupled receptors. Curr Pharm Des 16: 3071-3088. doi:10.2174/138161210793292474. PubMed: 20687879.
    • (2010) Curr Pharm Des , vol.16 , pp. 3071-3088
    • Gruber, C.W.1    Muttenthaler, M.2    Freissmuth, M.3
  • 11
    • 84857591939 scopus 로고    scopus 로고
    • Do plant cyclotides have potential as immunosuppressant peptides?
    • doi: 10.1021/np200722w
    • Gründemann C, Koehbach J, Huber R, Gruber CW, (2012) Do plant cyclotides have potential as immunosuppressant peptides? J Nat Prod 75: 167-174. doi:10.1021/np200722w. PubMed: 22272797.
    • (2012) J Nat Prod , vol.75 , pp. 167-174
    • Gründemann, C.1    Koehbach, J.2    Huber, R.3    Gruber, C.W.4
  • 12
    • 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, Waine C, (1999) Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. J Mol Biol 294: 1327-1336. doi:10.1006/jmbi.1999.3383. PubMed: 10600388.
    • (1999) J Mol Biol , vol.294 , pp. 1327-1336
    • Craik, D.J.1    Daly, N.L.2    Bond, T.3    Waine, C.4
  • 13
    • 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, (2004) Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: the importance of the cyclic cystine knot. Biochemistry 43: 5965-5975. doi:10.1021/bi049711q. PubMed: 15147180.
    • (2004) Biochemistry , vol.43 , pp. 5965-5975
    • Colgrave, M.L.1    Craik, D.J.2
  • 15
    • 35748954039 scopus 로고    scopus 로고
    • An asparaginyl endopeptidase mediates in vivo protein backbone cyclization
    • doi: 10.1074/jbc.M705185200
    • Saska I, Gillon AD, Hatsugai N, Dietzgen RG, Hara-Nishimura I, et al. (2007) An asparaginyl endopeptidase mediates in vivo protein backbone cyclization. J Biol Chem 282: 29721-29728. doi:10.1074/jbc.M705185200. PubMed: 17698845.
    • (2007) J Biol Chem , vol.282 , pp. 29721-29728
    • Saska, I.1    Gillon, A.D.2    Hatsugai, N.3    Dietzgen, R.G.4    Hara-Nishimura, I.5
  • 16
    • 34547098170 scopus 로고    scopus 로고
    • A novel plant protein-disulfide isomerase involved in the oxidative folding of cystine knot defense proteins
    • doi: 10.1074/jbc.M700018200
    • Gruber CW, Cemazar M, Clark RJ, Horibe T, Renda RF, et al. (2007) A novel plant protein-disulfide isomerase involved in the oxidative folding of cystine knot defense proteins. J Biol Chem 282: 20435-20446. doi:10.1074/jbc.M700018200. PubMed: 17522051.
    • (2007) J Biol Chem , vol.282 , pp. 20435-20446
    • Gruber, C.W.1    Cemazar, M.2    Clark, R.J.3    Horibe, T.4    Renda, R.F.5
  • 17
    • 33746298040 scopus 로고    scopus 로고
    • Protein disulfide isomerase: the structure of oxidative folding
    • doi: 10.1016/j.tibs.2006.06.001
    • Gruber CW, Cemazar M, Heras B, Martin JL, Craik DJ, (2006) Protein disulfide isomerase: the structure of oxidative folding. Trends Biochem Sci 31: 455-464. doi:10.1016/j.tibs.2006.06.001. PubMed: 16815710.
    • (2006) Trends Biochem Sci , vol.31 , pp. 455-464
    • Gruber, C.W.1    Cemazar, M.2    Heras, B.3    Martin, J.L.4    Craik, D.J.5
  • 18
    • 0015723952 scopus 로고
    • On the effect of a polypeptide isolated from "Kalata-Kalata" (Oldenlandia affinis DC) on the oestrogen dominated uterus
    • Gran L, (1973) On the effect of a polypeptide isolated from "Kalata-Kalata" (Oldenlandia affinis DC) on the oestrogen dominated uterus. Acta Pharmacol Toxicol 33: 400-408.
    • (1973) Acta Pharmacol Toxicol , vol.33 , pp. 400-408
    • Gran, L.1
  • 19
    • 57749113081 scopus 로고    scopus 로고
    • Distribution and evolution of circular miniproteins in flowering plants
    • doi: 10.1105/tpc.108.062331
    • Gruber CW, Elliott AG, Ireland DC, Delprete PG, Dessein S, et al. (2008) Distribution and evolution of circular miniproteins in flowering plants. Plant Cell 20: 2471-2483. doi:10.1105/tpc.108.062331. PubMed: 18827180.
    • (2008) Plant Cell , vol.20 , pp. 2471-2483
    • Gruber, C.W.1    Elliott, A.G.2    Ireland, D.C.3    Delprete, P.G.4    Dessein, S.5
  • 20
    • 0027177567 scopus 로고
    • Hämolytisch aktive komponenten aus Viola tricolor L. und Viola arvensis Murray
    • Schöpke T, Hasan Agha MI, Kraft R, Otto A, Hiller K, (1993) Hämolytisch aktive komponenten aus Viola tricolor L. und Viola arvensis Murray. Sci Pharm 61: 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
  • 21
    • 33645033202 scopus 로고    scopus 로고
    • A Continent of Plant Defense Peptide Diversity: Cyclotides in Australian Hybanthus (Violaceae)
    • doi: 10.1105/tpc.105.034678
    • Simonsen SM, Sando L, Ireland DC, Colgrave ML, Bharathi R, et al. (2005) A Continent of Plant Defense Peptide Diversity: Cyclotides in Australian Hybanthus (Violaceae). Plant Cell 17: 3176-3189. doi:10.1105/tpc.105.034678. PubMed: 16199617.
    • (2005) Plant Cell , vol.17 , pp. 3176-3189
    • Simonsen, S.M.1    Sando, L.2    Ireland, D.C.3    Colgrave, M.L.4    Bharathi, R.5
  • 22
    • 0034674028 scopus 로고    scopus 로고
    • Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure
    • doi: 10.1021/bi9929756
    • Hernandez JF, Gagnon J, Chiche L, Nguyen TM, Andrieu JP, et al. (2000) Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure. Biochemistry 39: 5722-5730. doi:10.1021/bi9929756. PubMed: 10801322.
    • (2000) Biochemistry , vol.39 , pp. 5722-5730
    • Hernandez, J.F.1    Gagnon, J.2    Chiche, L.3    Nguyen, T.M.4    Andrieu, J.P.5
  • 23
    • 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
    • doi: 10.1021/cb100388j
    • Poth AG, Colgrave ML, Philip R, Kerenga B, Daly NL, et al. (2011) Discovery of cyclotides in the fabaceae plant family provides new insights into the cyclization, evolution, and distribution of circular proteins. ACS Chem Biol 6: 345-355. doi:10.1021/cb100388j. PubMed: 21194241.
    • (2011) ACS Chem Biol , vol.6 , pp. 345-355
    • Poth, A.G.1    Colgrave, M.L.2    Philip, R.3    Kerenga, B.4    Daly, N.L.5
  • 24
    • 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
    • doi: 10.1074/jbc.M111.229922
    • Nguyen GK, Zhang S, Nguyen NT, Nguyen PQ, Chiu MS, et al. (2011) 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 286: 24275-24287. doi:10.1074/jbc.M111.229922. PubMed: 21596752.
    • (2011) J Biol Chem , vol.286 , pp. 24275-24287
    • Nguyen, G.K.1    Zhang, S.2    Nguyen, N.T.3    Nguyen, P.Q.4    Chiu, M.S.5
  • 25
    • 84864551708 scopus 로고    scopus 로고
    • Cyclotides associate with leaf vasculature and are the products of a novel precursor in petunia (Solanaceae)
    • doi: 10.1074/jbc.M112.370841
    • Poth AG, Mylne JS, Grassl J, Lyons RE, Millar AH, et al. (2012) Cyclotides associate with leaf vasculature and are the products of a novel precursor in petunia (Solanaceae). J Biol Chem 287: 27033-27046. doi:10.1074/jbc.M112.370841. PubMed: 22700981.
    • (2012) J Biol Chem , vol.287 , pp. 27033-27046
    • Poth, A.G.1    Mylne, J.S.2    Grassl, J.3    Lyons, R.E.4    Millar, A.H.5
  • 26
    • 33749235154 scopus 로고    scopus 로고
    • Discovery of cyclotide-like protein sequences in graminaceous crop plants: ancestral precursors of circular proteins?
    • doi: 10.1105/tpc.106.042812
    • Mulvenna JP, Mylne JS, Bharathi R, Burton RA, Shirley NJ, et al. (2006) Discovery of cyclotide-like protein sequences in graminaceous crop plants: ancestral precursors of circular proteins? Plant Cell 18: 2134-2144. doi:10.1105/tpc.106.042812. PubMed: 16935986.
    • (2006) Plant Cell , vol.18 , pp. 2134-2144
    • Mulvenna, J.P.1    Mylne, J.S.2    Bharathi, R.3    Burton, R.A.4    Shirley, N.J.5
  • 27
    • 84873301841 scopus 로고    scopus 로고
    • Discovery of Linear Cyclotides in Monocot Plant Panicum laxum of Poaceae Family Provides New Insights into Evolution and Distribution of Cyclotides in Plants
    • doi: 10.1074/jbc.M112.415356
    • Nguyen GK, Lian Y, Pang EW, Nguyen PQ, Tran TD, et al. (2013) Discovery of Linear Cyclotides in Monocot Plant Panicum laxum of Poaceae Family Provides New Insights into Evolution and Distribution of Cyclotides in Plants. J Biol Chem 288: 3370-3380. doi:10.1074/jbc.M112.415356. PubMed: 23195955.
    • (2013) J Biol Chem , vol.288 , pp. 3370-3380
    • Nguyen, G.K.1    Lian, Y.2    Pang, E.W.3    Nguyen, P.Q.4    Tran, T.D.5
  • 28
    • 2542593981 scopus 로고    scopus 로고
    • Variations in cyclotide expression in viola species
    • doi: 10.1021/np034068e
    • Trabi M, Svangård E, Herrmann A, Göransson U, Claeson P, et al. (2004) Variations in cyclotide expression in viola species. J Nat Prod 67: 806-810. doi:10.1021/np034068e. PubMed: 15165141.
    • (2004) J Nat Prod , vol.67 , pp. 806-810
    • Trabi, M.1    Svangård, E.2    Herrmann, A.3    Göransson, U.4    Claeson, P.5
  • 29
    • 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, (2006) Structural plasticity of the cyclic-cystine-knot framework: implications for biological activity and drug design. Biochem J 394: 85-93. doi:10.1042/BJ20051691. PubMed: 16300479.
    • (2006) Biochem J , vol.394 , pp. 85-93
    • Clark, R.J.1    Daly, N.L.2    Craik, D.J.3
  • 30
    • 79954612403 scopus 로고    scopus 로고
    • Global cyclotide adventure: a journey dedicated to the discovery of circular peptides from flowering plants
    • doi: 10.1002/bip.21414
    • Gruber CW, (2010) Global cyclotide adventure: a journey dedicated to the discovery of circular peptides from flowering plants. Biopolymers 94: 565-572. doi:10.1002/bip.21414. PubMed: 20564015.
    • (2010) Biopolymers , vol.94 , pp. 565-572
    • Gruber, C.W.1
  • 31
    • 84878368742 scopus 로고    scopus 로고
    • Characterizing circular peptides in mixtures: sequence fragment assembly of cyclotides from a violet plant by MALDI-TOF/TOF mass spectrometry
    • 22890611
    • Hashempour H, Koehbach J, Daly NL, Ghassempour A, Gruber CW, (2013) Characterizing circular peptides in mixtures: sequence fragment assembly of cyclotides from a violet plant by MALDI-TOF/TOF mass spectrometry. Amino Acids 44: 581-595. PubMed: 22890611.
    • (2013) Amino Acids , vol.44 , pp. 581-595
    • Hashempour, H.1    Koehbach, J.2    Daly, N.L.3    Ghassempour, A.4    Gruber, C.W.5
  • 32
    • 84861615565 scopus 로고    scopus 로고
    • Orally active peptidic bradykinin B1 receptor antagonists engineered from a cyclotide scaffold for inflammatory pain treatment
    • doi: 10.1002/anie.201200984
    • Wong CT, Rowlands DK, Wong CH, Lo TW, Nguyen GK, et al. (2012) Orally active peptidic bradykinin B1 receptor antagonists engineered from a cyclotide scaffold for inflammatory pain treatment. Angew Chem Int Ed Engl 51: 5620-5624. doi:10.1002/anie.201200984. PubMed: 22532483.
    • (2012) Angew Chem Int Ed Engl , vol.51 , pp. 5620-5624
    • Wong, C.T.1    Rowlands, D.K.2    Wong, C.H.3    Lo, T.W.4    Nguyen, G.K.5
  • 33
    • 0034793341 scopus 로고    scopus 로고
    • Plant cyclotides: circular, knotted peptide toxins
    • doi: 10.1016/S0041-0101(01)00129-5
    • Craik DJ, (2001) Plant cyclotides: circular, knotted peptide toxins. Toxicon 39: 1809-1813. doi:10.1016/S0041-0101(01)00129-5. PubMed: 11600141.
    • (2001) Toxicon , vol.39 , pp. 1809-1813
    • Craik, D.J.1
  • 35
    • 33646248365 scopus 로고    scopus 로고
    • The cyclotide family of circular miniproteins: Nature's combinatorial peptide template
    • doi: 10.1002/bip.20451
    • Craik DJ, Cemazar M, Wang CK, Daly NL, (2006) The cyclotide family of circular miniproteins: Nature's combinatorial peptide template. Biopolymers 84: 250-266. doi:10.1002/bip.20451. PubMed: 16440288.
    • (2006) Biopolymers , vol.84 , pp. 250-266
    • Craik, D.J.1    Cemazar, M.2    Wang, C.K.3    Daly, N.L.4
  • 36
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • doi: 10.1016/S0041-0101(00)00160-4
    • Craik DJ, Daly NL, Waine C, (2001) The cystine knot motif in toxins and implications for drug design. Toxicon 39: 43-60. doi:10.1016/S0041-0101(00)00160-4. PubMed: 10936622.
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 37
    • 77951247943 scopus 로고    scopus 로고
    • Lysine-scanning mutagenesis reveals an amendable face of the cyclotide kalata B1 for the optimization of nematocidal activity
    • doi: 10.1074/jbc.M109.089854
    • Huang YH, Colgrave ML, Clark RJ, Kotze AC, Craik DJ, (2010) Lysine-scanning mutagenesis reveals an amendable face of the cyclotide kalata B1 for the optimization of nematocidal activity. J Biol Chem 285: 10797-10805. doi:10.1074/jbc.M109.089854. PubMed: 20103593.
    • (2010) J Biol Chem , vol.285 , pp. 10797-10805
    • Huang, Y.H.1    Colgrave, M.L.2    Clark, R.J.3    Kotze, A.C.4    Craik, D.J.5
  • 38
    • 43949138210 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of the prototypic cyclotide reveals a cluster of residues essential for bioactivity
    • doi: 10.1074/jbc.M709303200
    • Simonsen SM, Sando L, Rosengren KJ, Wang CK, Colgrave ML, et al. (2008) Alanine scanning mutagenesis of the prototypic cyclotide reveals a cluster of residues essential for bioactivity. J Biol Chem 283: 9805-9813. doi:10.1074/jbc.M709303200. PubMed: 18258598.
    • (2008) J Biol Chem , vol.283 , pp. 9805-9813
    • Simonsen, S.M.1    Sando, L.2    Rosengren, K.J.3    Wang, C.K.4    Colgrave, M.L.5
  • 39
    • 77951245192 scopus 로고    scopus 로고
    • Cyclotide interactions with the nematode external surface
    • doi: 10.1128/AAC.01306-09
    • Colgrave ML, Huang YH, Craik DJ, Kotze AC, (2010) Cyclotide interactions with the nematode external surface. Antimicrob Agents Chemother 54: 2160-2166. doi:10.1128/AAC.01306-09. PubMed: 20211894.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 2160-2166
    • Colgrave, M.L.1    Huang, Y.H.2    Craik, D.J.3    Kotze, A.C.4
  • 40
    • 41949097030 scopus 로고    scopus 로고
    • The biology of interleukin-2
    • doi: 10.1146/annurev.immunol.26.021607.090357
    • Malek TR, (2008) The biology of interleukin-2. Annu Rev Immunol 26: 453-479. doi:10.1146/annurev.immunol.26.021607.090357. PubMed: 18062768.
    • (2008) Annu Rev Immunol , vol.26 , pp. 453-479
    • Malek, T.R.1
  • 41
    • 0022377177 scopus 로고
    • Effect of cyclosporin A on the early activation of human T helper lymphocytes: inhibition of RNA-synthesis and modification of the expression of activation antigens
    • doi: 10.1016/S0171-2985(85)80067-X
    • Bettens F, Walker C, Bonnard GD, de Weck AL, (1985) Effect of cyclosporin A on the early activation of human T helper lymphocytes: inhibition of RNA-synthesis and modification of the expression of activation antigens. Immunobiology 170: 434-447. doi:10.1016/S0171-2985(85)80067-X. PubMed: 2419244.
    • (1985) Immunobiology , vol.170 , pp. 434-447
    • Bettens, F.1    Walker, C.2    Bonnard, G.D.3    de Weck, A.L.4
  • 42
    • 0021867018 scopus 로고
    • On the partial suppression of IL-2 receptor expression and the prevention of lectin-induced lymphoblast formation by cyclosporine A
    • 3926357
    • Solbach W, Heeg K, Von Steldern DU, Röllinghoff M, Wagner H, (1985) On the partial suppression of IL-2 receptor expression and the prevention of lectin-induced lymphoblast formation by cyclosporine A. Clin Exp Immunol 60: 501-508. PubMed: 3926357.
    • (1985) Clin Exp Immunol , vol.60 , pp. 501-508
    • Solbach, W.1    Heeg, K.2    Von Steldern, D.U.3    Röllinghoff, M.4    Wagner, H.5
  • 43
    • 0022330032 scopus 로고
    • The effects of cyclosporin A on the immune system
    • doi: 10.1146/annurev.iy.03.040185.002145
    • Shevach EM, (1985) The effects of cyclosporin A on the immune system. Annu Rev Immunol 3: 397-423. doi:10.1146/annurev.iy.03.040185.002145. PubMed: 3933532.
    • (1985) Annu Rev Immunol , vol.3 , pp. 397-423
    • Shevach, E.M.1
  • 44
    • 84857126819 scopus 로고    scopus 로고
    • Polyfunctional responses by human T cells result from sequential release of cytokines
    • doi: 10.1073/pnas.1117194109
    • Han Q, Bagheri N, Bradshaw EM, Hafler DA, Lauffenburger DA, et al. (2012) Polyfunctional responses by human T cells result from sequential release of cytokines. Proc Natl Acad Sci U S A 109: 1607-1612. doi:10.1073/pnas.1117194109. PubMed: 22160692.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 1607-1612
    • Han, Q.1    Bagheri, N.2    Bradshaw, E.M.3    Hafler, D.A.4    Lauffenburger, D.A.5
  • 45
    • 84863217498 scopus 로고    scopus 로고
    • Cyclosporin A and tacrolimus reduce T-cell polyfunctionality but not interferon-γ responses directed at cytomegalovirus
    • doi: 10.1111/j.1365-2567.2012.03594.x
    • Fuhrmann S, Lachmann R, Streitz M, Hetzer R, Volk HD, et al. (2012) Cyclosporin A and tacrolimus reduce T-cell polyfunctionality but not interferon-γ responses directed at cytomegalovirus. Immunology 136: 408-413. doi:10.1111/j.1365-2567.2012.03594.x. PubMed: 22533718.
    • (2012) Immunology , vol.136 , pp. 408-413
    • Fuhrmann, S.1    Lachmann, R.2    Streitz, M.3    Hetzer, R.4    Volk, H.D.5
  • 46
    • 84864538298 scopus 로고    scopus 로고
    • Biological synthesis of circular polypeptides
    • doi: 10.1074/jbc.R111.305508
    • Aboye TL, Camarero JA, (2012) Biological synthesis of circular polypeptides. J Biol Chem 287: 27026-27032. doi:10.1074/jbc.R111.305508. PubMed: 22707722.
    • (2012) J Biol Chem , vol.287 , pp. 27026-27032
    • Aboye, T.L.1    Camarero, J.A.2
  • 47
    • 84874819064 scopus 로고    scopus 로고
    • Expression of fluorescent cyclotides using protein trans-splicing for easy monitoring of cyclotide-protein interactions
    • doi: 10.1002/anie.201209219
    • Jagadish K, Borra R, Lacey V, Majumder S, Shekhtman A, et al. (2013) Expression of fluorescent cyclotides using protein trans-splicing for easy monitoring of cyclotide-protein interactions. Angew Chem Int Ed Engl 52: 3126-3131. doi:10.1002/anie.201209219. PubMed: 23322720.
    • (2013) Angew Chem Int Ed Engl , vol.52 , pp. 3126-3131
    • Jagadish, K.1    Borra, R.2    Lacey, V.3    Majumder, S.4    Shekhtman, A.5
  • 48
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • 1478777
    • Schnölzer M, Alewood P, Jones A, Alewood D, Kent SB, (1992) In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences. Int J Pept Protein Res 40: 180-193. PubMed: 1478777.
    • (1992) Int J Pept Protein Res , vol.40 , pp. 180-193
    • Schnölzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.5
  • 49
    • 84866943858 scopus 로고    scopus 로고
    • Phosphatidylethanolamine binding is a conserved feature of cyclotide-membrane interactions
    • doi: 10.1074/jbc.M112.372011
    • Henriques ST, Huang YH, Castanho MA, Bagatolli LA, Sonza S, et al. (2012) Phosphatidylethanolamine binding is a conserved feature of cyclotide-membrane interactions. J Biol Chem 287: 33629-33643. doi:10.1074/jbc.M112.372011. PubMed: 22854971.
    • (2012) J Biol Chem , vol.287 , pp. 33629-33643
    • Henriques, S.T.1    Huang, Y.H.2    Castanho, M.A.3    Bagatolli, L.A.4    Sonza, S.5
  • 50
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • doi: 10.1126/science.7973629
    • Dawson PE, Muir TW, Clark-Lewis I, Kent SB, (1994) Synthesis of proteins by native chemical ligation. Science 266: 776-779. doi:10.1126/science.7973629. PubMed: 7973629.
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.4
  • 51
    • 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, (2003) Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides. J Biol Chem 278: 6314-6322. doi:10.1074/jbc.M210492200. PubMed: 12482862.
    • (2003) J Biol Chem , vol.278 , pp. 6314-6322
    • Daly, N.L.1    Clark, R.J.2    Craik, D.J.3
  • 52
    • 39649085345 scopus 로고    scopus 로고
    • Oxidation by hypochlorite converts protective HDL into a potent platelet agonist
    • doi: 10.1016/j.febslet.2008.02.001
    • Assinger A, Schmid W, Eder S, Schmid D, Koller E, et al. (2008) Oxidation by hypochlorite converts protective HDL into a potent platelet agonist. FEBS Lett 582: 778-784. doi:10.1016/j.febslet.2008.02.001. PubMed: 18267121.
    • (2008) FEBS Lett , vol.582 , pp. 778-784
    • Assinger, A.1    Schmid, W.2    Eder, S.3    Schmid, D.4    Koller, E.5
  • 53
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • doi: 10.1016/0022-2836(84)90309-7
    • Eisenberg D, Schwarz E, Komaromy M, Wall R, (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J Mol Biol 179: 125-142. doi:10.1016/0022-2836(84)90309-7. PubMed: 6502707.
    • (1984) J Mol Biol , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.