메뉴 건너뛰기




Volumn 10, Issue , 2010, Pages

Strictosidine activation in Apocynaceae: Towards a "nuclear time bomb"?

Author keywords

[No Author keywords available]

Indexed keywords

APOCYNACEAE; BRASSICACEAE; CATHARANTHUS ROSEUS; RAUVOLFIA; RAUVOLFIA SERPENTINA;

EID: 77955670960     PISSN: None     EISSN: 14712229     Source Type: Journal    
DOI: 10.1186/1471-2229-10-182     Document Type: Article
Times cited : (124)

References (59)
  • 1
    • 0039596881 scopus 로고    scopus 로고
    • Molecular cloning and analysis of strictosidine beta-D-glucosidase, an enzyme in terpenoid indole alkaloid biosynthesis in Catharanthus roseus
    • 10.1074/jbc.275.5.3051, 10652285
    • Geerlings A, Ibanez MML, Memelink J, van der Heijden R, Verpoorte R. Molecular cloning and analysis of strictosidine beta-D-glucosidase, an enzyme in terpenoid indole alkaloid biosynthesis in Catharanthus roseus. J Biol Chem 2000, 275(5):3051-3056. 10.1074/jbc.275.5.3051, 10652285.
    • (2000) J Biol Chem , vol.275 , Issue.5 , pp. 3051-3056
    • Geerlings, A.1    Ibanez, M.M.L.2    Memelink, J.3    van der Heijden, R.4    Verpoorte, R.5
  • 2
    • 0036233184 scopus 로고    scopus 로고
    • Heterologous expression of a Rauvolfia cDNA encoding strictosidine glucosidase, a biosynthetic key to over 2000 monoterpenoid indole alkaloids
    • 10.1046/j.1432-1033.2002.02878.x, 11985599
    • Gerasimenko I, Sheludko Y, Ma XY, Stockigt J. Heterologous expression of a Rauvolfia cDNA encoding strictosidine glucosidase, a biosynthetic key to over 2000 monoterpenoid indole alkaloids. Eur J Biochem 2002, 269(8):2204-2213. 10.1046/j.1432-1033.2002.02878.x, 11985599.
    • (2002) Eur J Biochem , vol.269 , Issue.8 , pp. 2204-2213
    • Gerasimenko, I.1    Sheludko, Y.2    Ma, X.Y.3    Stockigt, J.4
  • 3
    • 35748962318 scopus 로고    scopus 로고
    • Molecular architecture of strictosidine glucosidase: The gateway to the biosynthesis of the monoterpenoid indole alkaloid family
    • 10.1105/tpc.106.045682, 2048697, 17890378
    • Barleben L, Panjikar S, Ruppert M, Koepke J, Stockigt J. Molecular architecture of strictosidine glucosidase: The gateway to the biosynthesis of the monoterpenoid indole alkaloid family. Plant Cell 2007, 19(9):2886-2897. 10.1105/tpc.106.045682, 2048697, 17890378.
    • (2007) Plant Cell , vol.19 , Issue.9 , pp. 2886-2897
    • Barleben, L.1    Panjikar, S.2    Ruppert, M.3    Koepke, J.4    Stockigt, J.5
  • 4
    • 44949127129 scopus 로고    scopus 로고
    • Alkaloid biosynthesis: metabolism and trafficking
    • 10.1146/annurev.arplant.59.032607.092730, 18251710
    • Ziegler J, Facchini PJ. Alkaloid biosynthesis: metabolism and trafficking. Annu Rev Plant Biol 2008, 59:735-769. 10.1146/annurev.arplant.59.032607.092730, 18251710.
    • (2008) Annu Rev Plant Biol , vol.59 , pp. 735-769
    • Ziegler, J.1    Facchini, P.J.2
  • 6
    • 1642263128 scopus 로고    scopus 로고
    • The Catharanthus alkaloids: Pharmacognosy and biotechnology
    • 10.2174/0929867043455846, 15032608
    • van der Heijden R, Jacobs DI, Snoeijer W, Hallard D, Verpoorte R. The Catharanthus alkaloids: Pharmacognosy and biotechnology. Curr Med Chem 2004, 11(5):607-628. 10.2174/0929867043455846, 15032608.
    • (2004) Curr Med Chem , vol.11 , Issue.5 , pp. 607-628
    • van der Heijden, R.1    Jacobs, D.I.2    Snoeijer, W.3    Hallard, D.4    Verpoorte, R.5
  • 7
    • 0005347443 scopus 로고
    • Phagodeterrency induced by leaves and leaf extracts of Catharanthus roseus in the larva of Spodoptera littoralis (Lepidoptera, Noctuidae)
    • Meisner J, Weissenberg M, Palevitch D, Aharonson N. Phagodeterrency induced by leaves and leaf extracts of Catharanthus roseus in the larva of Spodoptera littoralis (Lepidoptera, Noctuidae). Journal of Economic Entomology 1981, 74(2):131-135.
    • (1981) Journal of Economic Entomology , vol.74 , Issue.2 , pp. 131-135
    • Meisner, J.1    Weissenberg, M.2    Palevitch, D.3    Aharonson, N.4
  • 8
    • 2542505933 scopus 로고
    • Impact of the extract of Catharanthus roseus on feeding and enzymatic digestive activities of Spodoptera litura
    • Chockalingam S, Sundari MSN, Thenmozhi S. Impact of the extract of Catharanthus roseus on feeding and enzymatic digestive activities of Spodoptera litura. Journal of Environmental Biology 1989, 10(3):303-307.
    • (1989) Journal of Environmental Biology , vol.10 , Issue.3 , pp. 303-307
    • Chockalingam, S.1    Sundari, M.S.N.2    Thenmozhi, S.3
  • 9
    • 0029795353 scopus 로고    scopus 로고
    • Involvement of strictosidine as a defensive chemical in Catharanthus roseus
    • Luijendijk TJC, van der Meijden E, Verpoorte R. Involvement of strictosidine as a defensive chemical in Catharanthus roseus. J Chem Ecol 1996, 22(8):1355-1366.
    • (1996) J Chem Ecol , vol.22 , Issue.8 , pp. 1355-1366
    • Luijendijk, T.J.C.1    van der Meijden, E.2    Verpoorte, R.3
  • 10
    • 0019322070 scopus 로고
    • Glucosidases involved in indole alkaloid biosynthesis of Catharanthus cell cultures
    • 10.1016/0014-5793(80)80069-X, 6768587
    • Hemscheidt T, Zenk MH. Glucosidases involved in indole alkaloid biosynthesis of Catharanthus cell cultures. Febs Lett 1980, 110(2):187-191. 10.1016/0014-5793(80)80069-X, 6768587.
    • (1980) Febs Lett , vol.110 , Issue.2 , pp. 187-191
    • Hemscheidt, T.1    Zenk, M.H.2
  • 11
    • 0025044913 scopus 로고
    • Nucleotide sequence of a cDNA encoding the vacuolar protein strictosidine synthase from Catharanthus roseus
    • 10.1093/nar/18.16.4939, 332004, 2395663
    • McKnight TD, Roessner CA, Devagupta R, Scott AI, Nessler CL. Nucleotide sequence of a cDNA encoding the vacuolar protein strictosidine synthase from Catharanthus roseus. Nucleic Acids Res 1990, 18(16):4939-4939. 10.1093/nar/18.16.4939, 332004, 2395663.
    • (1990) Nucleic Acids Res , vol.18 , Issue.16 , pp. 4939-4939
    • McKnight, T.D.1    Roessner, C.A.2    Devagupta, R.3    Scott, A.I.4    Nessler, C.L.5
  • 12
    • 0026841089 scopus 로고
    • Coordinated regulation of 2 indole alkaloid biosynthetic genes from Catharanthus roseus by auxin and elicitors
    • 10.1007/BF00047715, 1600148
    • Pasquali G, Goddijn OJM, Dewaal A, Verpoorte R, Schilperoort RA, Hoge JHC, Memelink J. Coordinated regulation of 2 indole alkaloid biosynthetic genes from Catharanthus roseus by auxin and elicitors. Plant Molecular Biology 1992, 18(6):1121-1131. 10.1007/BF00047715, 1600148.
    • (1992) Plant Molecular Biology , vol.18 , Issue.6 , pp. 1121-1131
    • Pasquali, G.1    Goddijn, O.J.M.2    Dewaal, A.3    Verpoorte, R.4    Schilperoort, R.A.5    Hoge, J.H.C.6    Memelink, J.7
  • 13
    • 0024285106 scopus 로고
    • The cDNA clone for strictosidine synthase from Rauvolfia serpentina - DNA sequence determination and expression in Escherichia coli
    • 10.1016/0014-5793(88)80167-4, 3049153
    • Kutchan TM, Hampp N, Lottspeich F, Beyreuther K, Zenk MH. The cDNA clone for strictosidine synthase from Rauvolfia serpentina - DNA sequence determination and expression in Escherichia coli. Febs Lett 1988, 237(1-2):40-44. 10.1016/0014-5793(88)80167-4, 3049153.
    • (1988) Febs Lett , vol.237 , Issue.1-2 , pp. 40-44
    • Kutchan, T.M.1    Hampp, N.2    Lottspeich, F.3    Beyreuther, K.4    Zenk, M.H.5
  • 15
    • 0343262657 scopus 로고    scopus 로고
    • Myrosinase: gene family evolution and herbivore defense in Brassicaceae
    • 10.1023/A:1006380021658, 10688132
    • Rask L, Andreasson E, Ekbom B, Eriksson S, Pontoppidan B, Meijer J. Myrosinase: gene family evolution and herbivore defense in Brassicaceae. Plant Mol Biol 2000, 42(1):93-113. 10.1023/A:1006380021658, 10688132.
    • (2000) Plant Mol Biol , vol.42 , Issue.1 , pp. 93-113
    • Rask, L.1    Andreasson, E.2    Ekbom, B.3    Eriksson, S.4    Pontoppidan, B.5    Meijer, J.6
  • 16
    • 0036615409 scopus 로고    scopus 로고
    • Glucosinolate research in the Arabidopsis era
    • 10.1016/S1360-1385(02)02273-2, 12049923
    • Wittstock U, Halkier BA. Glucosinolate research in the Arabidopsis era. Trends Plant Sci 2002, 7(6):263-270. 10.1016/S1360-1385(02)02273-2, 12049923.
    • (2002) Trends Plant Sci , vol.7 , Issue.6 , pp. 263-270
    • Wittstock, U.1    Halkier, B.A.2
  • 17
    • 18044373501 scopus 로고    scopus 로고
    • The glucosinolate-myrosinase system in an ecological and evolutionary context
    • 10.1016/j.pbi.2005.03.002, 15860423
    • Kliebenstein DJ, Kroymann J, Mitchell-Olds T. The glucosinolate-myrosinase system in an ecological and evolutionary context. Curr Opin Plant Biol 2005, 8(3):264-271. 10.1016/j.pbi.2005.03.002, 15860423.
    • (2005) Curr Opin Plant Biol , vol.8 , Issue.3 , pp. 264-271
    • Kliebenstein, D.J.1    Kroymann, J.2    Mitchell-Olds, T.3
  • 18
    • 58149335088 scopus 로고    scopus 로고
    • The 'mustard oil bomb': not so easy to assemble?! Localization, expression and distribution of the components of the myrosinase enzyme system
    • Kissen R, Rossiter JT, Bones AM. The 'mustard oil bomb': not so easy to assemble?! Localization, expression and distribution of the components of the myrosinase enzyme system. Phytochemistry Reviews 2009, 8(1):69-86.
    • (2009) Phytochemistry Reviews , vol.8 , Issue.1 , pp. 69-86
    • Kissen, R.1    Rossiter, J.T.2    Bones, A.M.3
  • 19
    • 0033529748 scopus 로고    scopus 로고
    • Enzymatic activation of oleuropein: a protein crosslinker used as a chemical defense in the privet tree
    • 10.1073/pnas.96.16.9159, 17749, 10430912
    • Konno K, Hirayama C, Yasui H, Nakamura M. Enzymatic activation of oleuropein: a protein crosslinker used as a chemical defense in the privet tree. Proc Natl Acad Sci USA 1999, 96(16):9159-9164. 10.1073/pnas.96.16.9159, 17749, 10430912.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.16 , pp. 9159-9164
    • Konno, K.1    Hirayama, C.2    Yasui, H.3    Nakamura, M.4
  • 20
    • 0030059263 scopus 로고    scopus 로고
    • Reaction for the localization of strictosidine glucosidase activity on polyacrylamide gels
    • Luijendijk TJC, Stevens LH, Verpoorte R. Reaction for the localization of strictosidine glucosidase activity on polyacrylamide gels. Phytochem Analysis 1996, 7(1):16-19.
    • (1996) Phytochem Analysis , vol.7 , Issue.1 , pp. 16-19
    • Luijendijk, T.J.C.1    Stevens, L.H.2    Verpoorte, R.3
  • 21
    • 1842430598 scopus 로고    scopus 로고
    • Co-expression of three MEP pathway genes and geraniol 10-hydroxylase in internal phloem parenchyma of Catharanthus roseus implicates multicellular translocation of intermediates during the biosynthesis of monoterpene indole alkaloids and isoprenoid-derived primary metabolites
    • 10.1111/j.1365-313X.2004.02030.x, 15053766
    • Burlat V, Oudin A, Courtois M, Rideau M, St-Pierre B. Co-expression of three MEP pathway genes and geraniol 10-hydroxylase in internal phloem parenchyma of Catharanthus roseus implicates multicellular translocation of intermediates during the biosynthesis of monoterpene indole alkaloids and isoprenoid-derived primary metabolites. Plant J 2004, 38(1):131-141. 10.1111/j.1365-313X.2004.02030.x, 15053766.
    • (2004) Plant J , vol.38 , Issue.1 , pp. 131-141
    • Burlat, V.1    Oudin, A.2    Courtois, M.3    Rideau, M.4    St-Pierre, B.5
  • 22
    • 13944258804 scopus 로고    scopus 로고
    • Characterisation of CaaX-prenyltransferases in Catharanthus roseus: Relationships with the expression of genes involved in the early stages of monoterpenoid biosynthetic pathway
    • Courdavault V, Burlat V, St-Pierre B, Giglioli-Guivarc'h N. Characterisation of CaaX-prenyltransferases in Catharanthus roseus: Relationships with the expression of genes involved in the early stages of monoterpenoid biosynthetic pathway. Plant Sci 2005, 168(4):1097-1107.
    • (2005) Plant Sci , vol.168 , Issue.4 , pp. 1097-1107
    • Courdavault, V.1    Burlat, V.2    St-Pierre, B.3    Giglioli-Guivarc'h, N.4
  • 23
    • 17144406401 scopus 로고    scopus 로고
    • Purification, molecular cloning, and cell-specific gene expression of the alkaloid-accumulation associated protein CrPS in Catharanthus roseus
    • 10.1093/jxb/eri116, 15737982
    • Leménager D, Ouelhazi L, Mahroug S, Veau B, St-Pierre B, Rideau M, Aguirreolea J, Burlat V, Clastre M. Purification, molecular cloning, and cell-specific gene expression of the alkaloid-accumulation associated protein CrPS in Catharanthus roseus. J Exp Bot 2005, 56(414):1221-1228. 10.1093/jxb/eri116, 15737982.
    • (2005) J Exp Bot , vol.56 , Issue.414 , pp. 1221-1228
    • Leménager, D.1    Ouelhazi, L.2    Mahroug, S.3    Veau, B.4    St-Pierre, B.5    Rideau, M.6    Aguirreolea, J.7    Burlat, V.8    Clastre, M.9
  • 24
    • 69449106943 scopus 로고    scopus 로고
    • Optimization of the transient transformation of Catharanthus roseus cells by particle bombardment and its application to the subcellular localization of hydroxymethylbutenyl 4-diphosphate synthase and geraniol 10-hydroxylase
    • 10.1007/s00299-009-0722-2, 19504099
    • Guirimand G, Burlat V, Oudin A, Lanoue A, St-Pierre B, Courdavault V. Optimization of the transient transformation of Catharanthus roseus cells by particle bombardment and its application to the subcellular localization of hydroxymethylbutenyl 4-diphosphate synthase and geraniol 10-hydroxylase. Plant Cell Rep 2009, 28(8):1215-1234. 10.1007/s00299-009-0722-2, 19504099.
    • (2009) Plant Cell Rep , vol.28 , Issue.8 , pp. 1215-1234
    • Guirimand, G.1    Burlat, V.2    Oudin, A.3    Lanoue, A.4    St-Pierre, B.5    Courdavault, V.6
  • 25
    • 34547838647 scopus 로고    scopus 로고
    • Spatial distribution and hormonal regulation of gene products from methyl erythritol phosphate and monoterpene-secoiridoid pathways in Catharanthus roseus
    • 10.1007/s11103-007-9190-7, 17611800
    • Oudin A, Mahroug S, Courdavault V, Hervouet N, Zelwer C, Rodriguez-Concepcion M, St-Pierre B, Burlat V. Spatial distribution and hormonal regulation of gene products from methyl erythritol phosphate and monoterpene-secoiridoid pathways in Catharanthus roseus. Plant Molecular Biology 2007, 65(1-2):13-30. 10.1007/s11103-007-9190-7, 17611800.
    • (2007) Plant Molecular Biology , vol.65 , Issue.1-2 , pp. 13-30
    • Oudin, A.1    Mahroug, S.2    Courdavault, V.3    Hervouet, N.4    Zelwer, C.5    Rodriguez-Concepcion, M.6    St-Pierre, B.7    Burlat, V.8
  • 26
    • 0034490132 scopus 로고    scopus 로고
    • Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P450CYP72A1 as secologanin synthase
    • 10.1046/j.1365-313x.2000.00922.x, 11135113
    • Irmler S, Schroder G, St-Pierre B, Crouch NP, Hotze M, Schmidt J, Strack D, Matern U, Schroder J. Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P450CYP72A1 as secologanin synthase. Plant J 2000, 24(6):797-804. 10.1046/j.1365-313x.2000.00922.x, 11135113.
    • (2000) Plant J , vol.24 , Issue.6 , pp. 797-804
    • Irmler, S.1    Schroder, G.2    St-Pierre, B.3    Crouch, N.P.4    Hotze, M.5    Schmidt, J.6    Strack, D.7    Matern, U.8    Schroder, J.9
  • 27
    • 33646414497 scopus 로고    scopus 로고
    • Epidermis is a pivotal site of at least four secondary metabolic pathways in Catharanthus roseus aerial organs
    • 10.1007/s00425-005-0167-y, 16322983
    • Mahroug S, Courdavault V, Thiersault M, St-Pierre B, Burlat V. Epidermis is a pivotal site of at least four secondary metabolic pathways in Catharanthus roseus aerial organs. Planta 2006, 223(6):1191-1200. 10.1007/s00425-005-0167-y, 16322983.
    • (2006) Planta , vol.223 , Issue.6 , pp. 1191-1200
    • Mahroug, S.1    Courdavault, V.2    Thiersault, M.3    St-Pierre, B.4    Burlat, V.5
  • 28
    • 0032720893 scopus 로고    scopus 로고
    • Multicellular compartmentation of Catharanthus roseus alkaloid biosynthesis predicts intercellular translocation of a pathway intermediate
    • 10.1105/tpc.11.5.887, 144229, 10330473
    • St-Pierre B, Vazquez-Flota FA, De Luca V. Multicellular compartmentation of Catharanthus roseus alkaloid biosynthesis predicts intercellular translocation of a pathway intermediate. Plant Cell 1999, 11(5):887-900. 10.1105/tpc.11.5.887, 144229, 10330473.
    • (1999) Plant Cell , vol.11 , Issue.5 , pp. 887-900
    • St-Pierre, B.1    Vazquez-Flota, F.A.2    De Luca, V.3
  • 29
    • 48249155450 scopus 로고    scopus 로고
    • The leaf epidermome of Catharanthus roseus reveals its biochemical specialization
    • 10.1105/tpc.107.056630, 2329939, 18326827
    • Murata J, Roepke J, Gordon H, De Luca V. The leaf epidermome of Catharanthus roseus reveals its biochemical specialization. Plant Cell 2008, 20(3):524-542. 10.1105/tpc.107.056630, 2329939, 18326827.
    • (2008) Plant Cell , vol.20 , Issue.3 , pp. 524-542
    • Murata, J.1    Roepke, J.2    Gordon, H.3    De Luca, V.4
  • 30
    • 0000331036 scopus 로고
    • Subcellular localization of enzymes involved in indole alkaloid biosynthesis in Catharanthus roseus
    • 10.1104/pp.85.4.1099, 1054401, 16665811
    • De Luca V, Cutler AJ. Subcellular localization of enzymes involved in indole alkaloid biosynthesis in Catharanthus roseus. Plant Physiology 1987, 85(4):1099-1102. 10.1104/pp.85.4.1099, 1054401, 16665811.
    • (1987) Plant Physiology , vol.85 , Issue.4 , pp. 1099-1102
    • De Luca, V.1    Cutler, A.J.2
  • 31
    • 0000688846 scopus 로고
    • Expression of enzymatically active and correctly targeted strictosidine synthase in transgenic Tobacco plants
    • McKnight TD, Bergey DR, Burnett RJ, Nessler CL. Expression of enzymatically active and correctly targeted strictosidine synthase in transgenic Tobacco plants. Planta 1991, 185(2):148-152.
    • (1991) Planta , vol.185 , Issue.2 , pp. 148-152
    • McKnight, T.D.1    Bergey, D.R.2    Burnett, R.J.3    Nessler, C.L.4
  • 32
    • 0001754861 scopus 로고
    • Sucellular localization of tryptophan decarboxylase, strictosidine synthase and strictosidine glucosidase in suspension cultured cells of Catharanthus roseus and Tabernaemontana divaricata
    • Stevens LH, Blom TJM, Verpoorte R. Sucellular localization of tryptophan decarboxylase, strictosidine synthase and strictosidine glucosidase in suspension cultured cells of Catharanthus roseus and Tabernaemontana divaricata. Plant Cell Rep 1993, 12(10):573-576.
    • (1993) Plant Cell Rep , vol.12 , Issue.10 , pp. 573-576
    • Stevens, L.H.1    Blom, T.J.M.2    Verpoorte, R.3
  • 33
    • 0032966917 scopus 로고    scopus 로고
    • Cis-elements of protein transport to the plant vacuoles
    • Matsuoka K, Neuhaus JM. Cis-elements of protein transport to the plant vacuoles. J Exp Bot 1999, 50(331):165-174.
    • (1999) J Exp Bot , vol.50 , Issue.331 , pp. 165-174
    • Matsuoka, K.1    Neuhaus, J.M.2
  • 34
    • 0033379217 scopus 로고    scopus 로고
    • Large alkyl side-chains of isoleucine and leucine in the NPIRL region constitute the core of the vacuolar sorting determinant of sporamin precursor
    • 10.1023/A:1006357413084, 10737147
    • Matsuoka K, Nakamura K. Large alkyl side-chains of isoleucine and leucine in the NPIRL region constitute the core of the vacuolar sorting determinant of sporamin precursor. Plant Molecular Biology 1999, 41(6):825-835. 10.1023/A:1006357413084, 10737147.
    • (1999) Plant Molecular Biology , vol.41 , Issue.6 , pp. 825-835
    • Matsuoka, K.1    Nakamura, K.2
  • 35
    • 0024237306 scopus 로고
    • Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum
    • Fujiwara T, Oda K, Yokota S, Takatsuki A, Ikehara Y. Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J Biol Chem 1988, 263(34):18545-18552.
    • (1988) J Biol Chem , vol.263 , Issue.34 , pp. 18545-18552
    • Fujiwara, T.1    Oda, K.2    Yokota, S.3    Takatsuki, A.4    Ikehara, Y.5
  • 36
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence - Identification of a class of bipartite nuclear targeting sequence
    • 10.1016/0092-8674(91)90245-T, 1991323
    • Robbins J, Dilworth SM, Laskey RA, Dingwall C. Two interdependent basic domains in nucleoplasmin nuclear targeting sequence - Identification of a class of bipartite nuclear targeting sequence. Cell 1991, 64(3):615-623. 10.1016/0092-8674(91)90245-T, 1991323.
    • (1991) Cell , vol.64 , Issue.3 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 37
    • 0032104144 scopus 로고    scopus 로고
    • Purification and characterisation of strictosidine beta-D-glucosidase from Catharanthus roseus cell suspension cultures
    • Luijendijk TJC, Stevens LH, Verpoorte R. Purification and characterisation of strictosidine beta-D-glucosidase from Catharanthus roseus cell suspension cultures. Plant Physiol Bioch 1998, 36(6):419-425.
    • (1998) Plant Physiol Bioch , vol.36 , Issue.6 , pp. 419-425
    • Luijendijk, T.J.C.1    Stevens, L.H.2    Verpoorte, R.3
  • 38
    • 7044229949 scopus 로고    scopus 로고
    • Visualization of protein interactions in living plant cells using bimolecular fluorescence complementation
    • 10.1111/j.1365-313X.2004.02219.x, 15469500
    • Walter M, Chaban C, Schutze K, Batistic O, Weckermann K, Nake C, Blazevic D, Grefen C, Schumacher K, Oecking C, et al. Visualization of protein interactions in living plant cells using bimolecular fluorescence complementation. Plant J 2004, 40(3):428-438. 10.1111/j.1365-313X.2004.02219.x, 15469500.
    • (2004) Plant J , vol.40 , Issue.3 , pp. 428-438
    • Walter, M.1    Chaban, C.2    Schutze, K.3    Batistic, O.4    Weckermann, K.5    Nake, C.6    Blazevic, D.7    Grefen, C.8    Schumacher, K.9    Oecking, C.10
  • 39
    • 34147143885 scopus 로고    scopus 로고
    • Maize beta-glucosidase-aggregating factor is a polyspecific jacalin-related chimeric lectin, and its lectin domain is responsible for beta-glucosidase aggregation
    • 10.1074/jbc.M607417200, 17210577
    • Kittur FS, Lalgondar M, Yu HY, Bevan DR, Esen A. Maize beta-glucosidase-aggregating factor is a polyspecific jacalin-related chimeric lectin, and its lectin domain is responsible for beta-glucosidase aggregation. J Biol Chem 2007, 282(10):7299-7311. 10.1074/jbc.M607417200, 17210577.
    • (2007) J Biol Chem , vol.282 , Issue.10 , pp. 7299-7311
    • Kittur, F.S.1    Lalgondar, M.2    Yu, H.Y.3    Bevan, D.R.4    Esen, A.5
  • 41
    • 0000449964 scopus 로고
    • The stromacenter in Avena plastids: an aggregation of beta-glucosidase responsible for the activation of oat-leaf saponins
    • Nisius A. The stromacenter in Avena plastids: an aggregation of beta-glucosidase responsible for the activation of oat-leaf saponins. Planta 1988, 173(4):474-481.
    • (1988) Planta , vol.173 , Issue.4 , pp. 474-481
    • Nisius, A.1
  • 42
    • 33749678036 scopus 로고    scopus 로고
    • Cell and tissue localization of beta-glucosidase during the ripening of olive fruit (Olea europaea) by in situ activity assay
    • Mazzuca S, Spadafora A, Innocenti AM. Cell and tissue localization of beta-glucosidase during the ripening of olive fruit (Olea europaea) by in situ activity assay. Plant Sci 2006, 171(6):726-733.
    • (2006) Plant Sci , vol.171 , Issue.6 , pp. 726-733
    • Mazzuca, S.1    Spadafora, A.2    Innocenti, A.M.3
  • 43
    • 36749014563 scopus 로고    scopus 로고
    • Different mechanisms for phytoalexin induction by pathogen and wound signals in Medicago truncatula
    • 10.1073/pnas.0708697104, 2084270, 17971436
    • Naoumkina M, Farag MA, Sumner LW, Tang YH, Liu CJ, Dixon RA. Different mechanisms for phytoalexin induction by pathogen and wound signals in Medicago truncatula. Proc Natl Acad Sci USA 2007, 104(46):17909-17915. 10.1073/pnas.0708697104, 2084270, 17971436.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.46 , pp. 17909-17915
    • Naoumkina, M.1    Farag, M.A.2    Sumner, L.W.3    Tang, Y.H.4    Liu, C.J.5    Dixon, R.A.6
  • 44
    • 21244501422 scopus 로고    scopus 로고
    • Nuclear localization of flavonoid enzymes in Arabidopsis
    • 10.1074/jbc.M413506200, 15817473
    • Saslowsky DE, Warek U, Winkel BSJ. Nuclear localization of flavonoid enzymes in Arabidopsis. J Biol Chem 2005, 280(25):23735-23740. 10.1074/jbc.M413506200, 15817473.
    • (2005) J Biol Chem , vol.280 , Issue.25 , pp. 23735-23740
    • Saslowsky, D.E.1    Warek, U.2    Winkel, B.S.J.3
  • 45
    • 58049206258 scopus 로고    scopus 로고
    • The New β-D-Glucosidase in Terpenoid-Isoquinoline Alkaloid Biosynthesis in Psychotria ipecacuanha
    • 10.1074/jbc.M806953200, 18927081
    • Nomura T, Quesada AL, Kutchan TM. The New β-D-Glucosidase in Terpenoid-Isoquinoline Alkaloid Biosynthesis in Psychotria ipecacuanha. J Biol Chem 2008, 283(50):34650-34659. 10.1074/jbc.M806953200, 18927081.
    • (2008) J Biol Chem , vol.283 , Issue.50 , pp. 34650-34659
    • Nomura, T.1    Quesada, A.L.2    Kutchan, T.M.3
  • 46
    • 0035853772 scopus 로고    scopus 로고
    • Identification of beta-glucosidase aggregating factor (BGAF) and mapping of BGAF binding regions on maize beta-glucosidase
    • 10.1074/jbc.M008872200, 11096099
    • Blanchard DJ, Cicek M, Chen JL, Esen A. Identification of beta-glucosidase aggregating factor (BGAF) and mapping of BGAF binding regions on maize beta-glucosidase. J Biol Chem 2001, 276(15):11895-11901. 10.1074/jbc.M008872200, 11096099.
    • (2001) J Biol Chem , vol.276 , Issue.15 , pp. 11895-11901
    • Blanchard, D.J.1    Cicek, M.2    Chen, J.L.3    Esen, A.4
  • 47
    • 25444452649 scopus 로고    scopus 로고
    • Activation of an ER-body-localized beta-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana
    • 10.1093/pcp/pci126, 15919674
    • Nagano AJ, Matsushima R, Hara-Nishimura I. Activation of an ER-body-localized beta-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana. Plant and Cell Physiology 2005, 46(7):1140-1148. 10.1093/pcp/pci126, 15919674.
    • (2005) Plant and Cell Physiology , vol.46 , Issue.7 , pp. 1140-1148
    • Nagano, A.J.1    Matsushima, R.2    Hara-Nishimura, I.3
  • 48
    • 0028535437 scopus 로고
    • Avenacosidase from oat: Purification, sequence analysis and biochemical characterization of a new member of the BGA family of beta-glucosidases
    • 10.1007/BF00028858, 8000004
    • Gus-Mayer S, Brunner H, Schneider-Poetsch HAW, Rüdiger W. Avenacosidase from oat: Purification, sequence analysis and biochemical characterization of a new member of the BGA family of beta-glucosidases. Plant Molecular Biology 1994, 26(3):909-921. 10.1007/BF00028858, 8000004.
    • (1994) Plant Molecular Biology , vol.26 , Issue.3 , pp. 909-921
    • Gus-Mayer, S.1    Brunner, H.2    Schneider-Poetsch, H.A.W.3    Rüdiger, W.4
  • 50
    • 33846811280 scopus 로고    scopus 로고
    • Evidence of protease in the saliva of the butterfly Heliconius melpomene (L.) (Nymphalidae, Lepidoptera)
    • 10.1016/j.jinsphys.2006.11.001, 17210163
    • Eberhard SH, Hrassnigg N, Crailsheim K, Krenn HW. Evidence of protease in the saliva of the butterfly Heliconius melpomene (L.) (Nymphalidae, Lepidoptera). Journal of Insect Physiology 2007, 53(2):126-131. 10.1016/j.jinsphys.2006.11.001, 17210163.
    • (2007) Journal of Insect Physiology , vol.53 , Issue.2 , pp. 126-131
    • Eberhard, S.H.1    Hrassnigg, N.2    Crailsheim, K.3    Krenn, H.W.4
  • 51
    • 0029905732 scopus 로고    scopus 로고
    • Drugs, ionophoric peptides, and steroids as substrates of the yeast multidrug transporter Pdr5p
    • 10.1074/jbc.271.49.31543, 8940170
    • Kolaczkowski M, vanderRest M, Cybularz-Kolaczkowska A, Soumillion JP, Konings WN, Goffeau A. Drugs, ionophoric peptides, and steroids as substrates of the yeast multidrug transporter Pdr5p. J Biol Chem 1996, 271(49):31543-31548. 10.1074/jbc.271.49.31543, 8940170.
    • (1996) J Biol Chem , vol.271 , Issue.49 , pp. 31543-31548
    • Kolaczkowski, M.1    vanderRest, M.2    Cybularz-Kolaczkowska, A.3    Soumillion, J.P.4    Konings, W.N.5    Goffeau, A.6
  • 53
    • 0017626067 scopus 로고
    • Indole alkaloid biosynthesis - Partial purification of ajmalicine synthetase from Catharanthus roseus
    • 10.1016/0006-291X(77)91481-4, 861021
    • Scott AI, Lee SL, Wan W. Indole alkaloid biosynthesis - Partial purification of ajmalicine synthetase from Catharanthus roseus. Biochemical and Biophysical Research Communications 1977, 75(4):1004-1009. 10.1016/0006-291X(77)91481-4, 861021.
    • (1977) Biochemical and Biophysical Research Communications , vol.75 , Issue.4 , pp. 1004-1009
    • Scott, A.I.1    Lee, S.L.2    Wan, W.3
  • 54
    • 0035169918 scopus 로고    scopus 로고
    • Selective secretion of free glycine, a neutralizer against a plant defense chemical, in the digestive juice of the privet moth larvae
    • 10.1016/S0022-1910(01)00135-4, 12770151
    • Konno K, Okada S, Hirayama C. Selective secretion of free glycine, a neutralizer against a plant defense chemical, in the digestive juice of the privet moth larvae. J Insect Physiol 2001, 47(12):1451-1457. 10.1016/S0022-1910(01)00135-4, 12770151.
    • (2001) J Insect Physiol , vol.47 , Issue.12 , pp. 1451-1457
    • Konno, K.1    Okada, S.2    Hirayama, C.3
  • 55
    • 0001407651 scopus 로고
    • Induced responses in three alkaloid-containing plant species
    • van Dam NM, van der Meijden E, Verpoorte R. Induced responses in three alkaloid-containing plant species. Oecologia 1993, 95(3):425-430.
    • (1993) Oecologia , vol.95 , Issue.3 , pp. 425-430
    • van Dam, N.M.1    van der Meijden, E.2    Verpoorte, R.3
  • 56
    • 72849117553 scopus 로고    scopus 로고
    • De novo biosynthesis of defense root exudates in response to Fusarium attack in barley
    • 10.1111/j.1469-8137.2009.03066.x, 19878462
    • Lanoue A, Burlat V, Henkes GJ, Koch I, Schurr U, Röse USR. De novo biosynthesis of defense root exudates in response to Fusarium attack in barley. New Phytologist 2010, 185:577-588. 10.1111/j.1469-8137.2009.03066.x, 19878462.
    • (2010) New Phytologist , vol.185 , pp. 577-588
    • Lanoue, A.1    Burlat, V.2    Henkes, G.J.3    Koch, I.4    Schurr, U.5    Röse, U.S.R.6
  • 57
    • 54349105689 scopus 로고    scopus 로고
    • Multicolor bimolecular fluorescence complementation reveals simultaneous formation of alternative CBL/CIPK complexes in planta
    • 10.1111/j.1365-313X.2008.03612.x, 18643980
    • Waadt R, Schmidt LK, Lohse M, Hashimoto K, Bock R, Kudla J. Multicolor bimolecular fluorescence complementation reveals simultaneous formation of alternative CBL/CIPK complexes in planta. Plant J 2008, 56(3):505-516. 10.1111/j.1365-313X.2008.03612.x, 18643980.
    • (2008) Plant J , vol.56 , Issue.3 , pp. 505-516
    • Waadt, R.1    Schmidt, L.K.2    Lohse, M.3    Hashimoto, K.4    Bock, R.5    Kudla, J.6
  • 58
    • 34548487513 scopus 로고    scopus 로고
    • A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants
    • 10.1111/j.1365-313X.2007.03212.x, 17666025
    • Nelson BK, Cai X, Nebenfuhr A. A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants. Plant J 2007, 51(6):1126-1136. 10.1111/j.1365-313X.2007.03212.x, 17666025.
    • (2007) Plant J , vol.51 , Issue.6 , pp. 1126-1136
    • Nelson, B.K.1    Cai, X.2    Nebenfuhr, A.3
  • 59
    • 21244502626 scopus 로고    scopus 로고
    • CaaX-prenyltransferases are essential for expression of genes involvedin the early stages of monoterpenoid biosynthetic pathwayin Catharanthus roseus cells
    • 10.1007/s11103-005-3095-0, 15952070
    • Courdavault V, Thiersault M, Courtois M, Gantet P, Oudin A, Doireau P, St-Pierre B, Giglioli-Guivarc'h N. CaaX-prenyltransferases are essential for expression of genes involvedin the early stages of monoterpenoid biosynthetic pathwayin Catharanthus roseus cells. Plant Molecular Biology 2005, 57(6):855-870. 10.1007/s11103-005-3095-0, 15952070.
    • (2005) Plant Molecular Biology , vol.57 , Issue.6 , pp. 855-870
    • Courdavault, V.1    Thiersault, M.2    Courtois, M.3    Gantet, P.4    Oudin, A.5    Doireau, P.6    St-Pierre, B.7    Giglioli-Guivarc'h, N.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.