메뉴 건너뛰기




Volumn 2, Issue , 2013, Pages 1852-1858

Plant C1A Cysteine Peptidases in Germination and Senescence

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84884895130     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-382219-2.00417-8     Document Type: Chapter
Times cited : (19)

References (66)
  • 2
    • 47649106761 scopus 로고    scopus 로고
    • The origin and evolution of plant cystatins and their target cysteine proteinases indicate a complex functional relationship
    • Martinez M., Diaz I. The origin and evolution of plant cystatins and their target cysteine proteinases indicate a complex functional relationship. BMC Evol. Biol. 2008, 8:198.
    • (2008) BMC Evol. Biol. , vol.8 , pp. 198
    • Martinez, M.1    Diaz, I.2
  • 3
    • 0000941909 scopus 로고
    • Gibberellic acid-induced synthesis of protease by isolated aleurone layers of barley
    • Jacobsen J.V., Varner J.E. Gibberellic acid-induced synthesis of protease by isolated aleurone layers of barley. Plant Physiol. 1967, 42:1596-1600.
    • (1967) Plant Physiol. , vol.42 , pp. 1596-1600
    • Jacobsen, J.V.1    Varner, J.E.2
  • 5
    • 70350686335 scopus 로고    scopus 로고
    • Characterization of the entire cystatin gene family in barley and their target cathepsin L-like cysteine-proteases, partners in the hordein mobilization during seed germination
    • Martinez M., Cambra I., Carrillo L., Diaz-Mendoza M., Diaz I. Characterization of the entire cystatin gene family in barley and their target cathepsin L-like cysteine-proteases, partners in the hordein mobilization during seed germination. Plant Physiol. 2009, 151:1531-1545.
    • (2009) Plant Physiol. , vol.151 , pp. 1531-1545
    • Martinez, M.1    Cambra, I.2    Carrillo, L.3    Diaz-Mendoza, M.4    Diaz, I.5
  • 6
    • 0026952853 scopus 로고
    • Temporal and spatial expression of a thiolprotease gene during pea ovary senescence, and its regulation by gibberellins
    • Granell A., Harris N., Pisabarro A.G., Carbonell J. Temporal and spatial expression of a thiolprotease gene during pea ovary senescence, and its regulation by gibberellins. Plant J. 1992, 2:907-915.
    • (1992) Plant J. , vol.2 , pp. 907-915
    • Granell, A.1    Harris, N.2    Pisabarro, A.G.3    Carbonell, J.4
  • 7
    • 0034623255 scopus 로고    scopus 로고
    • Expression of genes responsible for ethylene production and wilting are differently regulated in carnation (Dianthus caryophyllus L.) petals
    • Kosugi Y., Shibuya K., Tsuruno N., Iwazaki Y., Muchizuki A., Yoshioka T., Satoh S. Expression of genes responsible for ethylene production and wilting are differently regulated in carnation (Dianthus caryophyllus L.) petals. Plant Sci. 2000, 158:139-145.
    • (2000) Plant Sci. , vol.158 , pp. 139-145
    • Kosugi, Y.1    Shibuya, K.2    Tsuruno, N.3    Iwazaki, Y.4    Muchizuki, A.5    Yoshioka, T.6    Satoh, S.7
  • 8
    • 57649171450 scopus 로고    scopus 로고
    • Characterization and cloning of cyteine protease that is induced in green leaves of barley
    • Watanabe Y., Matsushima.S., Yamaguchi A., Shioi Y. Characterization and cloning of cyteine protease that is induced in green leaves of barley. Plant Sci. 2009, 176:264-271.
    • (2009) Plant Sci. , vol.176 , pp. 264-271
    • Watanabe, Y.1    Matsushima, S.2    Yamaguchi, A.3    Shioi, Y.4
  • 9
    • 67649482672 scopus 로고    scopus 로고
    • Functional redundancy in the Arabidopsis cathepsin B gene family contributes to basal defence, the hypersensitive response and senescence
    • McLellan H., Gilroy E.M., Yun B.W., Birch P.R.J., Loake G.J. Functional redundancy in the Arabidopsis cathepsin B gene family contributes to basal defence, the hypersensitive response and senescence. New Phytol. 2009, 183:408-418.
    • (2009) New Phytol. , vol.183 , pp. 408-418
    • McLellan, H.1    Gilroy, E.M.2    Yun, B.W.3    Birch, P.R.J.4    Loake, G.J.5
  • 11
    • 79956201615 scopus 로고    scopus 로고
    • A model of the C14-EPIC complex indicates hotspots for a protease-inhibitor arms race in the oomycete-potato interaction
    • Kaschani F., van der Hoorn R. A model of the C14-EPIC complex indicates hotspots for a protease-inhibitor arms race in the oomycete-potato interaction. Plant Signal. Behav. 2011, 6:109-112.
    • (2011) Plant Signal. Behav. , vol.6 , pp. 109-112
    • Kaschani, F.1    van der Hoorn, R.2
  • 12
    • 77954542512 scopus 로고    scopus 로고
    • A distinct subfamily of papain-like cysteine proteinases regulated by senescence and stresses in Glycine max
    • Esteban-García B., Garrido-Cardenas J.A., Lopez-Alonso D., Garcia-Maroto F. A distinct subfamily of papain-like cysteine proteinases regulated by senescence and stresses in Glycine max. J Plant Physiol. 2010, 167:1101-1108.
    • (2010) J Plant Physiol. , vol.167 , pp. 1101-1108
    • Esteban-García, B.1    Garrido-Cardenas, J.A.2    Lopez-Alonso, D.3    Garcia-Maroto, F.4
  • 13
    • 84884874268 scopus 로고    scopus 로고
    • Multifunctional role of the cathepsin F-like HvPap-1, a new cysteine-protease from barley (Hordeum vulgare L.) (Submitted).
    • Cambra, I., Martinez, M., Dader, B., Gonzalez-Melendi, P., Santamaria M.E., Diaz, I. (2012). Multifunctional role of the cathepsin F-like HvPap-1, a new cysteine-protease from barley (Hordeum vulgare L.) (Submitted).
    • (2012)
    • Cambra, I.1    Martinez, M.2    Dader, B.3    Gonzalez-Melendi, P.4    Santamaria M.E. Diaz, I.5
  • 14
    • 0032547704 scopus 로고    scopus 로고
    • Gel electrophoresis of proteolytic enzymes
    • Micahud D. Gel electrophoresis of proteolytic enzymes. Anal. Chim. Acta 1998, 372:173-185.
    • (1998) Anal. Chim. Acta , vol.372 , pp. 173-185
    • Micahud, D.1
  • 15
    • 44649165814 scopus 로고    scopus 로고
    • Cysteine proteinases regulate chloroplast protein content and composition in tobacco leaves: a model for dynamic interactions with ribulose-1,5-biphosphate carboxylase/oxydase (Rubisco) vesicular bodies
    • Prins A., van Heerden P.D.R., Olmos E., Kunert K.J., Foyer C.H. Cysteine proteinases regulate chloroplast protein content and composition in tobacco leaves: a model for dynamic interactions with ribulose-1,5-biphosphate carboxylase/oxydase (Rubisco) vesicular bodies. J. Exp. Bot. 2008, 59:1935-1950.
    • (2008) J. Exp. Bot. , vol.59 , pp. 1935-1950
    • Prins, A.1    van Heerden, P.D.R.2    Olmos, E.3    Kunert, K.J.4    Foyer, C.H.5
  • 16
    • 33744961634 scopus 로고    scopus 로고
    • Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities
    • Choe Y., Leonetti F., Greenbaum D.C., Lecaille F., Bogyo M., Brömme D., Ellman J.A., Craik C.S. Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities. J. Biol. Chem. 2006, 281:12824-12832.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12824-12832
    • Choe, Y.1    Leonetti, F.2    Greenbaum, D.C.3    Lecaille, F.4    Bogyo, M.5    Brömme, D.6    Ellman, J.A.7    Craik, C.S.8
  • 18
    • 0033759066 scopus 로고    scopus 로고
    • Prediction of protein cleavage sites by the barley cysteine endoproteases EP-A and EP-B based on the kinetics of synthetic peptide hydrolysis
    • Davy A., Sorensen M.B., Svendsen I., Cameron-Mills V., Simpson D.J. Prediction of protein cleavage sites by the barley cysteine endoproteases EP-A and EP-B based on the kinetics of synthetic peptide hydrolysis. Plant Physiol. 2000, 122:137-145.
    • (2000) Plant Physiol. , vol.122 , pp. 137-145
    • Davy, A.1    Sorensen, M.B.2    Svendsen, I.3    Cameron-Mills, V.4    Simpson, D.J.5
  • 19
    • 77952672644 scopus 로고    scopus 로고
    • Mining the active proteome in plant science and biotechnolgy
    • Kolodziejek I., van der Hoorn R. Mining the active proteome in plant science and biotechnolgy. Curr. Opini. Biotechnol. 2010, 21:225-233.
    • (2010) Curr. Opini. Biotechnol. , vol.21 , pp. 225-233
    • Kolodziejek, I.1    van der Hoorn, R.2
  • 20
    • 0022429212 scopus 로고
    • Thiol proteases. Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain
    • Kamphuis I.G., Drenth J., Baker E.N. Thiol proteases. Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain. J. Mol. Biol. 1985, 182:317-329.
    • (1985) J. Mol. Biol. , vol.182 , pp. 317-329
    • Kamphuis, I.G.1    Drenth, J.2    Baker, E.N.3
  • 22
    • 79960742147 scopus 로고    scopus 로고
    • Crystal structure of tarocystatin-papain complex: implications for the inhibition property of group-2 phytocystatins
    • Chu M.H., Liu K.L., Wu H.Y., Yeh K.W., Cheng Y.S. Crystal structure of tarocystatin-papain complex: implications for the inhibition property of group-2 phytocystatins. Planta 2011, 234:243-254.
    • (2011) Planta , vol.234 , pp. 243-254
    • Chu, M.H.1    Liu, K.L.2    Wu, H.Y.3    Yeh, K.W.4    Cheng, Y.S.5
  • 23
    • 0029175998 scopus 로고
    • Pattern of endoproteolysis following wheat grain germination
    • Dominguez F., Cejudo F.J. Pattern of endoproteolysis following wheat grain germination. Physiol. Plant. 1995, 95:253-259.
    • (1995) Physiol. Plant. , vol.95 , pp. 253-259
    • Dominguez, F.1    Cejudo, F.J.2
  • 25
    • 79954988984 scopus 로고    scopus 로고
    • Proteomes of the barley aleurone layer: A model system for plant signalling and protein secretion
    • Finnie C., Andersen B., Shahpiri A., Svensson B. Proteomes of the barley aleurone layer: A model system for plant signalling and protein secretion. Proteomics 2011, 11:1595-1605.
    • (2011) Proteomics , vol.11 , pp. 1595-1605
    • Finnie, C.1    Andersen, B.2    Shahpiri, A.3    Svensson, B.4
  • 26
    • 0000172376 scopus 로고
    • Purification and characterization of a thiol-protease induced during senescence of unpollinated ovaries of Pisum sativum
    • Cercos M., Carbonell J. Purification and characterization of a thiol-protease induced during senescence of unpollinated ovaries of Pisum sativum. Physiol. Plant. 1993, 88:267-274.
    • (1993) Physiol. Plant. , vol.88 , pp. 267-274
    • Cercos, M.1    Carbonell, J.2
  • 28
    • 0001600705 scopus 로고
    • In vitro processing of aleurain, a barley vacuolar thiol protease. Plant Cell
    • Holwerda, B.C., Galvin, N.J., Baranski, T.J., Rogers, J.C. (1990). In vitro processing of aleurain, a barley vacuolar thiol protease. Plant Cell 2, 1091-106.
    • (1990) , vol.2 , pp. 1091-106
    • Holwerda, B.C.1    Galvin, N.J.2    Baranski, T.J.3    Rogers, J.C.4
  • 30
    • 2442610018 scopus 로고    scopus 로고
    • Structure-function relationship in class CA1 cysteine peptides propeptides
    • Wiederanders B. Structure-function relationship in class CA1 cysteine peptides propeptides. Acta Biochem. Pol. 2003, 50:691-713.
    • (2003) Acta Biochem. Pol. , vol.50 , pp. 691-713
    • Wiederanders, B.1
  • 33
    • 0036005912 scopus 로고    scopus 로고
    • Activation of Arabidopsis vacuolar processing enzyme by self-catalytic removal of an auto-inhibitory domain of the C-terminal propeptide
    • Kuroyanagi M., Nishimura M., Hara-Nishimura I. Activation of Arabidopsis vacuolar processing enzyme by self-catalytic removal of an auto-inhibitory domain of the C-terminal propeptide. Plant Cell Physiol. 2002, 43:143-151.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 143-151
    • Kuroyanagi, M.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 34
    • 85047684006 scopus 로고    scopus 로고
    • A slow maturation of cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves
    • Yamada K., Mitsushima R., Nishimura.M., Hara-Nishimura I. A slow maturation of cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves. Plant Physiol. 2001, 127:1626-1634.
    • (2001) Plant Physiol. , vol.127 , pp. 1626-1634
    • Yamada, K.1    Mitsushima, R.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 35
    • 0742322084 scopus 로고    scopus 로고
    • The S8 serine, C1A cysteine and A1 aspartic protease families in Arabidopsis
    • Beers E.P., Jones A.M., Dickermann A.W. The S8 serine, C1A cysteine and A1 aspartic protease families in Arabidopsis. Phytochemistry 2004, 65:43-58.
    • (2004) Phytochemistry , vol.65 , pp. 43-58
    • Beers, E.P.1    Jones, A.M.2    Dickermann, A.W.3
  • 36
    • 0032718660 scopus 로고    scopus 로고
    • Protein storage bodies and vacuoles
    • Herman E.M., Larkins B.A. Protein storage bodies and vacuoles. Plant Cell 1999, 11:601-614.
    • (1999) Plant Cell , vol.11 , pp. 601-614
    • Herman, E.M.1    Larkins, B.A.2
  • 37
    • 0034614933 scopus 로고    scopus 로고
    • Mass transport of proform of a KDEL-tailed cysteine proteinase (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicles is involved in protein mobilization in germinating seeds
    • Toyooka K., Okamoto T., Minamikawa T. Mass transport of proform of a KDEL-tailed cysteine proteinase (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicles is involved in protein mobilization in germinating seeds. J. Cell Biol. 2000, 148:453-463.
    • (2000) J. Cell Biol. , vol.148 , pp. 453-463
    • Toyooka, K.1    Okamoto, T.2    Minamikawa, T.3
  • 38
    • 0000677652 scopus 로고
    • Purification and characterization of aleurain: a plant thiol protease functionally homologous to mammalian cathepsin H
    • Holwerda B.C., Rogers J.C. Purification and characterization of aleurain: a plant thiol protease functionally homologous to mammalian cathepsin H. Plant Physiol. 1992, 99:848-855.
    • (1992) Plant Physiol. , vol.99 , pp. 848-855
    • Holwerda, B.C.1    Rogers, J.C.2
  • 39
    • 0037338198 scopus 로고    scopus 로고
    • A cathepsin B-like cysteine protease gene from Hordeum vulgare (gene CatB) induced by GA in aleurone cells is under circadian control in leaves
    • Martinez M., Rubio-Somoza.I., Carbonero P., Diaz I. A cathepsin B-like cysteine protease gene from Hordeum vulgare (gene CatB) induced by GA in aleurone cells is under circadian control in leaves. J. Exp. Bot. 2003, 54:951-959.
    • (2003) J. Exp. Bot. , vol.54 , pp. 951-959
    • Martinez, M.1    Rubio-Somoza, I.2    Carbonero, P.3    Diaz, I.4
  • 40
    • 4644253630 scopus 로고    scopus 로고
    • Multifunctional role of plant cysteine proteinases
    • Grudkowska M., Zagdanska B. Multifunctional role of plant cysteine proteinases. Acta Biochim. Pol. 2004, 51:609-624.
    • (2004) Acta Biochim. Pol. , vol.51 , pp. 609-624
    • Grudkowska, M.1    Zagdanska, B.2
  • 41
    • 44949258132 scopus 로고    scopus 로고
    • Plant proteases: from phenotypes to molecular mechanisms
    • van der Hoorn RAL Plant proteases: from phenotypes to molecular mechanisms. Ann. Rev. Plant Biol. 2008, 59:191-223.
    • (2008) Ann. Rev. Plant Biol. , vol.59 , pp. 191-223
    • van der Hoorn, R.A.L.1
  • 42
    • 37349092681 scopus 로고    scopus 로고
    • Papain-like cysteine proteases: key players at molecular battlefields employed by both plants and their invaders
    • Shindo T., van der Hoorn R.A. Papain-like cysteine proteases: key players at molecular battlefields employed by both plants and their invaders. Mol. Plant Pathol. 2008, 9:119-125.
    • (2008) Mol. Plant Pathol. , vol.9 , pp. 119-125
    • Shindo, T.1    van der Hoorn, R.A.2
  • 43
    • 33745642719 scopus 로고    scopus 로고
    • Ternary complex formation between HvMYBS3 and other factors involved in transcriptional control in barley seeds
    • Rubio-Somoza I., Martinez M., Abraham Z., Diaz I., Carbonero P. Ternary complex formation between HvMYBS3 and other factors involved in transcriptional control in barley seeds. Plant J. 2006, 47:269-281.
    • (2006) Plant J. , vol.47 , pp. 269-281
    • Rubio-Somoza, I.1    Martinez, M.2    Abraham, Z.3    Diaz, I.4    Carbonero, P.5
  • 44
    • 34547109079 scopus 로고    scopus 로고
    • The HvDOF19 transcription factor mediates the abscisic acid-dependent repression of hydrolase genes in germinating barley aleurone
    • Moreno-Risueno M.A., Diaz I., Carrillo L., Fuentes R., Carbonero P. The HvDOF19 transcription factor mediates the abscisic acid-dependent repression of hydrolase genes in germinating barley aleurone. Plant J. 2007, 51:352-365.
    • (2007) Plant J. , vol.51 , pp. 352-365
    • Moreno-Risueno, M.A.1    Diaz, I.2    Carrillo, L.3    Fuentes, R.4    Carbonero, P.5
  • 45
    • 0036676947 scopus 로고    scopus 로고
    • Legumains and their functions in plants
    • Muntz K., Shutov A.D. Legumains and their functions in plants. Trends Plant Sci. 2004, 7:340-344.
    • (2004) Trends Plant Sci. , vol.7 , pp. 340-344
    • Muntz, K.1    Shutov, A.D.2
  • 46
    • 0000700014 scopus 로고
    • Characterization of germinated barley endoproteolytic enzymes by two-dimensional gel electrophoresis
    • Zhang N., Jones B.L. Characterization of germinated barley endoproteolytic enzymes by two-dimensional gel electrophoresis. J. Cereal Sci. 1995, 21:145-153.
    • (1995) J. Cereal Sci. , vol.21 , pp. 145-153
    • Zhang, N.1    Jones, B.L.2
  • 47
    • 58149359204 scopus 로고    scopus 로고
    • Characters of cysteine endopeptidases in wheat endosperm during seed germination and subsequent seedling growth
    • Shi C., Xu L.L. Characters of cysteine endopeptidases in wheat endosperm during seed germination and subsequent seedling growth. J. Integ. Plant Biol. 2009, 51:52-57.
    • (2009) J. Integ. Plant Biol. , vol.51 , pp. 52-57
    • Shi, C.1    Xu, L.L.2
  • 48
    • 0035028591 scopus 로고    scopus 로고
    • Differential tissue-specific expression of cysteine proteinases forms the basis for the fine-tuned mobilization of storage globulin during and after germination in legume seeds
    • Tiedemann J., Schlereth A., Muntz K. Differential tissue-specific expression of cysteine proteinases forms the basis for the fine-tuned mobilization of storage globulin during and after germination in legume seeds. Planta 2001, 212:728-738.
    • (2001) Planta , vol.212 , pp. 728-738
    • Tiedemann, J.1    Schlereth, A.2    Muntz, K.3
  • 49
    • 0036999514 scopus 로고    scopus 로고
    • Legumains - a family of asparagin-specific cysteine endopeptidases involved in propolypepttide processing and protein breakdown in plants
    • Muntz K., Blattner F.R., Shutov A.D. Legumains - a family of asparagin-specific cysteine endopeptidases involved in propolypepttide processing and protein breakdown in plants. J. Plant Physiol. 2002, 159:1281-1293.
    • (2002) J. Plant Physiol. , vol.159 , pp. 1281-1293
    • Muntz, K.1    Blattner, F.R.2    Shutov, A.D.3
  • 50
    • 66149173194 scopus 로고    scopus 로고
    • The vacuolar processing enzyme OsVPE1 is required for efficient glutelin processing in rice
    • Wang Y., Hu A., Liu S., Jiang L., Chen L., Ren L., Han X., Liu F., Ji S., Liu X., Wan J. The vacuolar processing enzyme OsVPE1 is required for efficient glutelin processing in rice. Plant J. 2009, 58:606-617.
    • (2009) Plant J. , vol.58 , pp. 606-617
    • Wang, Y.1    Hu, A.2    Liu, S.3    Jiang, L.4    Chen, L.5    Ren, L.6    Han, X.7    Liu, F.8    Ji, S.9    Liu, X.10    Wan, J.11
  • 51
    • 77954161029 scopus 로고    scopus 로고
    • Analysis of barley (Hordeum vulgare) leaf senescence and protease gene expression: a family C1A cysteine protease is specifically induced under conditions characterized by high carbohydrate, but not low to moderate nitrogen levels
    • Parrot D.L., Martin J.M., Fischer A.M. Analysis of barley (Hordeum vulgare) leaf senescence and protease gene expression: a family C1A cysteine protease is specifically induced under conditions characterized by high carbohydrate, but not low to moderate nitrogen levels. New Phytol. 2010, 187:313-331.
    • (2010) New Phytol. , vol.187 , pp. 313-331
    • Parrot, D.L.1    Martin, J.M.2    Fischer, A.M.3
  • 52
    • 0036008857 scopus 로고    scopus 로고
    • Is a cysteine protease inhibitor involved in the regulation of petal wilting in senescing carnation (Dianthus caryophyllus L.) flowers?
    • Sugawara H., Shibuya K., Yoshioka T., Hashiba T., Satoh S. Is a cysteine protease inhibitor involved in the regulation of petal wilting in senescing carnation (Dianthus caryophyllus L.) flowers?. J. Exp. Bot. 2002, 53:407-413.
    • (2002) J. Exp. Bot. , vol.53 , pp. 407-413
    • Sugawara, H.1    Shibuya, K.2    Yoshioka, T.3    Hashiba, T.4    Satoh, S.5
  • 54
    • 53649092665 scopus 로고    scopus 로고
    • Senescence-associated vacuoles are involved in the degradation of chloroplast protein in tobacco leaves
    • Martinez D.E., Costa M.L., Gomez F.M., Otegui M.S., Guiamet J.J. Senescence-associated vacuoles are involved in the degradation of chloroplast protein in tobacco leaves. Plant J. 2008, 56:196-206.
    • (2008) Plant J. , vol.56 , pp. 196-206
    • Martinez, D.E.1    Costa, M.L.2    Gomez, F.M.3    Otegui, M.S.4    Guiamet, J.J.5
  • 55
    • 70349998767 scopus 로고    scopus 로고
    • Expression of a senescence-associated cysteine protease gene related to peel pitting of navel orange (Citrus sinensis L. Osbeck)
    • Fan J., Yang Y.W., Gao X., Deng W., Falara V., Kanellis A.K., Li Z-G. Expression of a senescence-associated cysteine protease gene related to peel pitting of navel orange (Citrus sinensis L. Osbeck). Plant Cell Tiss Organ Cult. 2009, 98:281-289.
    • (2009) Plant Cell Tiss Organ Cult. , vol.98 , pp. 281-289
    • Fan, J.1    Yang, Y.W.2    Gao, X.3    Deng, W.4    Falara, V.5    Kanellis, A.K.6    Li, Z.-G.7
  • 56
    • 0033598774 scopus 로고    scopus 로고
    • Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes
    • Schmid M., Simpson D., Gietl C. Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes. Proc. Natl Acad. Sci. USA 1999, 96:14159-14164.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 14159-14164
    • Schmid, M.1    Simpson, D.2    Gietl, C.3
  • 57
    • 24044517545 scopus 로고    scopus 로고
    • Modified expression of cysteine protease affects seed germination, vegetative growth and nodule development in transgenic lines of Medicago truncatula
    • Sheokand S., Dahiya P., Vincent J.L., Brewin N.J. Modified expression of cysteine protease affects seed germination, vegetative growth and nodule development in transgenic lines of Medicago truncatula. Plant Sci. 2005, 169:966-975.
    • (2005) Plant Sci. , vol.169 , pp. 966-975
    • Sheokand, S.1    Dahiya, P.2    Vincent, J.L.3    Brewin, N.J.4
  • 58
    • 0033166888 scopus 로고    scopus 로고
    • Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions
    • Kinoshita T., Yamada K., Hiraiwa N., Kondo M., Nishimura M., Hara-Nishimura I. Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions. Plant J. 1999, 19:43-53.
    • (1999) Plant J. , vol.19 , pp. 43-53
    • Kinoshita, T.1    Yamada, K.2    Hiraiwa, N.3    Kondo, M.4    Nishimura, M.5    Hara-Nishimura, I.6
  • 59
    • 1042290220 scopus 로고    scopus 로고
    • Papain protects papaya trees from herbivorous insects: role of cysteine proteases in latex
    • Konno K., Hirayama C., Nakamura M., Tateishi K., Tamura Y., Hattori M., Kohno K. Papain protects papaya trees from herbivorous insects: role of cysteine proteases in latex. Plant J. 2004, 37:370-378.
    • (2004) Plant J. , vol.37 , pp. 370-378
    • Konno, K.1    Hirayama, C.2    Nakamura, M.3    Tateishi, K.4    Tamura, Y.5    Hattori, M.6    Kohno, K.7
  • 60
    • 79960733465 scopus 로고    scopus 로고
    • Plant latex and other exudates as plant defense systems: Roles of various defense chemicals and proteins contained therein
    • Konno K. Plant latex and other exudates as plant defense systems: Roles of various defense chemicals and proteins contained therein. Phytochemistry 2011, 72(13):1510-1530.
    • (2011) Phytochemistry , vol.72 , Issue.13 , pp. 1510-1530
    • Konno, K.1
  • 61
    • 0033868878 scopus 로고    scopus 로고
    • A unique 33-kD cysteine proteinase accumulates in response to larval feeding in maize genotypes resistant to fall armyworm and other Lepidoptera
    • Pechan T., Ye L., Chang Y., Mitra A., Lin L., Davis F.M., Williams W.P., Luthe D.S. A unique 33-kD cysteine proteinase accumulates in response to larval feeding in maize genotypes resistant to fall armyworm and other Lepidoptera. Plant Cell 2000, 12:1031-1040.
    • (2000) Plant Cell , vol.12 , pp. 1031-1040
    • Pechan, T.1    Ye, L.2    Chang, Y.3    Mitra, A.4    Lin, L.5    Davis, F.M.6    Williams, W.P.7    Luthe, D.S.8
  • 62
    • 0036790854 scopus 로고    scopus 로고
    • Insect feeding mobilizes a unique plant defense protease that disrupts the peritrophic matrix of caterpillars
    • Pechan T., Cohen A., Williams W.P., Luthe D.S. Insect feeding mobilizes a unique plant defense protease that disrupts the peritrophic matrix of caterpillars. Proc. Natl Acad. Sci. USA 2002, 99:13319-13323.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 13319-13323
    • Pechan, T.1    Cohen, A.2    Williams, W.P.3    Luthe, D.S.4
  • 65
    • 0000023298 scopus 로고
    • A major gibberellic acid-induced barley aleurone cysteine proteinase which digest hordein. Purification and characterization
    • Koehler S., Ho T.-H.D. A major gibberellic acid-induced barley aleurone cysteine proteinase which digest hordein. Purification and characterization. Plant Physiol. 1990, 94:251-258.
    • (1990) Plant Physiol. , vol.94 , pp. 251-258
    • Koehler, S.1    Ho, T.-H.D.2
  • 66
    • 34250357224 scopus 로고    scopus 로고
    • Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases
    • Martinez M., Diaz-Mendoza M., Carrillo L., Diaz I. Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases. FEBS Lett. 2007, 581:2914-2918.
    • (2007) FEBS Lett. , vol.581 , pp. 2914-2918
    • Martinez, M.1    Diaz-Mendoza, M.2    Carrillo, L.3    Diaz, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.