메뉴 건너뛰기




Volumn 19, Issue 1, 1999, Pages 43-53

Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions

Author keywords

[No Author keywords available]

Indexed keywords

CELL VACUOLE; ENZYME LOCALIZATION; ENZYME REGULATION; ENZYME SYNTHESIS; ETHYLENE; GENE EXPRESSION REGULATION; GENETIC STRAIN; JASMONIC ACID; LYSIS; MATURATION; MESSENGER RNA; PROMOTER REGION; PROTEIN PROTEIN INTERACTION; REPORTER GENE; SALICYLIC ACID; SENESCENCE; TRANSGENIC PLANT; WOUND;

EID: 0033166888     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1999.00497.x     Document Type: Article
Times cited : (195)

References (50)
  • 1
    • 0002427688 scopus 로고
    • Efficient transformation of Arabidopsis thaliana: Comparison of the efficiencies with various organs, plant ecotypes and Agrobacterium strains
    • Akama, K., Shiraishi, H., Ohta, S., Nakamura, K., Okada, K. and Shimura, Y. (1992) Efficient transformation of Arabidopsis thaliana: comparison of the efficiencies with various organs, plant ecotypes and Agrobacterium strains. Plant Cell Reports, 12, 7-11.
    • (1992) Plant Cell Reports , vol.12 , pp. 7-11
    • Akama, K.1    Shiraishi, H.2    Ohta, S.3    Nakamura, K.4    Okada, K.5    Shimura, Y.6
  • 2
    • 0029379575 scopus 로고
    • A putative vacuolar processing protease is regulated by ethylene and also during fruit ripening in Citrus fruit
    • Alonso, J.M. and Granell, A. (1995) A putative vacuolar processing protease is regulated by ethylene and also during fruit ripening in Citrus fruit. Plant Physiol. 109, 541-547.
    • (1995) Plant Physiol. , vol.109 , pp. 541-547
    • Alonso, J.M.1    Granell, A.2
  • 3
    • 0001844190 scopus 로고
    • Copper enzyme in isolated chloroplasts, polyphenoloxidase in Beta vulgaris
    • Arnon, D.I. (1949) Copper enzyme in isolated chloroplasts, polyphenoloxidase in Beta vulgaris. Plant Physiol. 24, 1-15.
    • (1949) Plant Physiol. , vol.24 , pp. 1-15
    • Arnon, D.I.1
  • 4
    • 0027551083 scopus 로고
    • Proteinase inhibitors in Nicotiana alata stigmas are derived from a precursor protein which is processed into five homologous inhibitors
    • Atkinson, A.H., Heath, R.L., Simpson, R.J., Clarke, A.E. and Anderson, M.A. (1993) Proteinase inhibitors in Nicotiana alata stigmas are derived from a precursor protein which is processed into five homologous inhibitors. Plant Cell. 5, 203-213.
    • (1993) Plant Cell , vol.5 , pp. 203-213
    • Atkinson, A.H.1    Heath, R.L.2    Simpson, R.J.3    Clarke, A.E.4    Anderson, M.A.5
  • 5
    • 0019156319 scopus 로고
    • Structure of actinidin, after refinement at 1.7 a resolution
    • Baker, E.N. (1980) Structure of actinidin, after refinement at 1.7 A resolution. J. Mol. Biol, 141, 441-484.
    • (1980) J. Mol. Biol , vol.141 , pp. 441-484
    • Baker, E.N.1
  • 6
    • 0027435506 scopus 로고
    • In planta Agrobacterium mediated gene transfer by infiltration of adult Arabidopsis thaliana plants
    • Bechtold, N., Ellis, J. and Pelletier, G. (1993) In planta Agrobacterium mediated gene transfer by infiltration of adult Arabidopsis thaliana plants. C.R. Acad. Sci. Ser. III Sci. Vie. 316, 1194-1199.
    • (1993) C.r. Acad. Sci. Ser. III Sci. Vie. , vol.316 , pp. 1194-1199
    • Bechtold, N.1    Ellis, J.2    Pelletier, G.3
  • 7
    • 0028958785 scopus 로고
    • Purification, cDNA cloning and characterization of proteinase B, an asparagine-specific endopeptidase from germinating vetch (Vicia sativa L.) seeds
    • Becker, C., Shutov, A.D., Nong, V.H., Senyuk, V.I., Jung, R., Horstmann, C., Fischer, J., Nielsen, N.C. and Müntz, K. (1995) Purification, cDNA cloning and characterization of proteinase B, an asparagine-specific endopeptidase from germinating vetch (Vicia sativa L.) seeds. Eur. J. Biochem. 228, 456-462.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 456-462
    • Becker, C.1    Shutov, A.D.2    Nong, V.H.3    Senyuk, V.I.4    Jung, R.5    Horstmann, C.6    Fischer, J.7    Nielsen, N.C.8    Müntz, K.9
  • 8
    • 0001404236 scopus 로고
    • Plant pathogenesis-related proteins induced by virus infection
    • Bol, J.F. and Linthorst, J.M. (1990) Plant pathogenesis-related proteins induced by virus infection. Annu. Rev. Phytopathol. 1, 113-138.
    • (1990) Annu. Rev. Phytopathol. , vol.1 , pp. 113-138
    • Bol, J.F.1    Linthorst, J.M.2
  • 10
    • 0030087809 scopus 로고    scopus 로고
    • Isolation and analysis of cDNAs encoding tomato cysteine proteases expressed during leaf senescence
    • Drake, R., John, I., Farrell, A., Cooper, W., Schuch, W. and Grierson, D. (1996) Isolation and analysis of cDNAs encoding tomato cysteine proteases expressed during leaf senescence. Plant Mol. Biol. 30, 755-767.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 755-767
    • Drake, R.1    John, I.2    Farrell, A.3    Cooper, W.4    Schuch, W.5    Grierson, D.6
  • 11
    • 0026698279 scopus 로고
    • Tracheary element formation as a model system of cell differentiation
    • Fukuda, H. (1992) Tracheary element formation as a model system of cell differentiation. Int. Rev. Cytol. 136, 289-332.
    • (1992) Int. Rev. Cytol. , vol.136 , pp. 289-332
    • Fukuda, H.1
  • 12
    • 0022422764 scopus 로고
    • Wound-induced proteinase inhibitors from tomato leaves: I the cDNA-deduced primary structure of pre-inhibitor I and its post-translational processing
    • Graham, J.S., Pearce, G., Merryweather, J., Titani, K., Ericsson, H.L. and Ryan, C.A. (1985) Wound-induced proteinase inhibitors from tomato leaves: I The cDNA-deduced primary structure of pre-inhibitor I and its post-translational processing. J. Biol. Chem. 260, 6555-6560.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6555-6560
    • Graham, J.S.1    Pearce, G.2    Merryweather, J.3    Titani, K.4    Ericsson, H.L.5    Ryan, C.A.6
  • 13
    • 0026952853 scopus 로고
    • Temporal and spatial expression of a thiol protease gene during pea ovary senescence, and its regulation by gibberellin
    • Granell, A., Harris, N., Pisabarro, A.G. and Carbonell, J. (1992) Temporal and spatial expression of a thiol protease gene during pea ovary senescence, and its regulation by gibberellin. Plant J. 2, 907-915.
    • (1992) Plant J. , vol.2 , pp. 907-915
    • Granell, A.1    Harris, N.2    Pisabarro, A.G.3    Carbonell, J.4
  • 14
    • 0000995388 scopus 로고
    • Differential expression of the Arabidopsis 2s albumin genes and the effect of increasing gene family size
    • Guerche, P., Tire, C., Grossi De, S.A.F., De Clercq, A., Van Montagu, M. and Krebbers, E. (1990) Differential expression of the Arabidopsis 2S albumin genes and the effect of increasing gene family size. Plant Cell. 2, 469-478.
    • (1990) Plant Cell , vol.2 , pp. 469-478
    • Guerche, P.1    Tire, C.2    De Grossi, S.A.F.3    De Clercq, A.4    Van Montagu, M.5    Krebbers, E.6
  • 15
    • 0001842082 scopus 로고    scopus 로고
    • Asparaginyl endopeptidase
    • London: Academic Press
    • Hara-Nishimura, I. (1998) Asparaginyl endopeptidase. In Handbook of Proteolytic Enzymes, Vol. 37. London: Academic Press, 746-749.
    • (1998) Handbook of Proteolytic Enzymes , vol.37 , pp. 746-749
    • Hara-Nishimura, I.1
  • 16
    • 0025986480 scopus 로고
    • A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms
    • Hara-Nishimura, I., Inoue, K. and Nishimura, M. (1991) A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms. FEBS Lett. 294, 89-93.
    • (1991) FEBS Lett. , vol.294 , pp. 89-93
    • Hara-Nishimura, I.1    Inoue, K.2    Nishimura, M.3
  • 17
    • 0031842339 scopus 로고    scopus 로고
    • Vacuolar processing enzymes in protein-storage vacuoles and lytic vacuoles
    • Hara-Nishimura, I., Kinoshita, T., Hiraiwa, N. and Nishimura, M. (1998b) Vacuolar processing enzymes in protein-storage vacuoles and lytic vacuoles. J. Plant Physiol. 152, 668-674.
    • (1998) J. Plant Physiol. , vol.152 , pp. 668-674
    • Hara-Nishimura, I.1    Kinoshita, T.2    Hiraiwa, N.3    Nishimura, M.4
  • 18
    • 0000235299 scopus 로고
    • Proglobulin processing enzyme in vacuoles isolated from developing pumpkin cotyledons
    • Hara-Nishimura, I. and Nishimura, M. (1987) Proglobulin processing enzyme in vacuoles isolated from developing pumpkin cotyledons. Plant Physiol. 85, 440-445.
    • (1987) Plant Physiol. , vol.85 , pp. 440-445
    • Hara-Nishimura, I.1    Nishimura, M.2
  • 19
    • 0031795695 scopus 로고    scopus 로고
    • Transport of storage proteins to protein-storage vacuoles is mediated by large precursor-accumulating vesicles
    • Hara-Nishimura, I., Shimada, T., Hatano, K., Takeuchi, Y. and Nishimura, M. (1998a) Transport of storage proteins to protein-storage vacuoles is mediated by large precursor-accumulating vesicles. Plant Cell. 10, 825-836.
    • (1998) Plant Cell , vol.10 , pp. 825-836
    • Hara-Nishimura, I.1    Shimada, T.2    Hatano, K.3    Takeuchi, Y.4    Nishimura, M.5
  • 20
    • 0001612653 scopus 로고
    • Vacuolar processing enzyme responsible for maturation of seed proteins
    • Hara-Nishimura, I., Shimada, T., Hiraiwa, N. and Nishimura, M. (1995) Vacuolar processing enzyme responsible for maturation of seed proteins. J. Plant Physiol. 145, 632-640.
    • (1995) J. Plant Physiol. , vol.145 , pp. 632-640
    • Hara-Nishimura, I.1    Shimada, T.2    Hiraiwa, N.3    Nishimura, M.4
  • 21
    • 0027692821 scopus 로고
    • Vesicle transport and processing of the precursor to 2S albumin in pumpkin
    • Hara-Nishimura, I., Takeuchi, Y., Inoue, K. and Nishimura, M. (1993b) Vesicle transport and processing of the precursor to 2S albumin in pumpkin. Plant J. 4, 793-800.
    • (1993) Plant J. , vol.4 , pp. 793-800
    • Hara-Nishimura, I.1    Takeuchi, Y.2    Inoue, K.3    Nishimura, M.4
  • 22
    • 0027688051 scopus 로고
    • Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni
    • Hara-Nishimura, I., Takeuchi, Y. and Nishimura, M. (1993a) Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni. Plant Cell. 5, 1651-1659.
    • (1993) Plant Cell , vol.5 , pp. 1651-1659
    • Hara-Nishimura, I.1    Takeuchi, Y.2    Nishimura, M.3
  • 23
    • 0024287059 scopus 로고
    • Nucleotide sequence of cloned cDNA coding for pumpkin 11S-globulin β subunit
    • Hayashi, M., Mori, H., Nishimura, M., Akazawa, T. and Hara-Nishimura, I. (1988) Nucleotide sequence of cloned cDNA coding for pumpkin 11S-globulin β subunit. Eur. J. Biochem. 172, 627-632.
    • (1988) Eur. J. Biochem. , vol.172 , pp. 627-632
    • Hayashi, M.1    Mori, H.2    Nishimura, M.3    Akazawa, T.4    Hara-Nishimura, I.5
  • 24
    • 0027597690 scopus 로고
    • Developmental and age-related processes that influence the longevity and senescence of photosynthetic tissues in Arabidopsis
    • Hensel, L.L., Grbic, V., Baumgarten, D.A. and Bleecker, A.B. (1993) Developmental and age-related processes that influence the longevity and senescence of photosynthetic tissues in Arabidopsis. Plant Cell. 5, 553-564.
    • (1993) Plant Cell , vol.5 , pp. 553-564
    • Hensel, L.L.1    Grbic, V.2    Baumgarten, D.A.3    Bleecker, A.B.4
  • 25
    • 0026605537 scopus 로고
    • Clustal V: Improved software for multiple sequence alignment
    • Higins, D.G., Bleasby, A.J. and Fuchs, R. (1992) Clustal V: Improved software for multiple sequence alignment. Comput. Appl. Biosci. 8, 189-191.
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 189-191
    • Higins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 26
    • 0030993676 scopus 로고    scopus 로고
    • An aspartic proteinase is involved in the maturation of storage proteins in concert with the vacuolar processing enzyme
    • Hiraiwa, N., Kondo, M., Nishimura, M. and Hara-Nishimura, I. (1997a) An aspartic proteinase is involved in the maturation of storage proteins in concert with the vacuolar processing enzyme. Eur. J. Biochem. 246, 133-141.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 133-141
    • Hiraiwa, N.1    Kondo, M.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 27
    • 0031259680 scopus 로고    scopus 로고
    • Expression and activation of the vacuolar processing enzyme in Saccharomyces cerevisiae
    • Hiraiwa, N., Nishimura, M. and Hara-Nishimura, I. (1997b) Expression and activation of the vacuolar processing enzyme in Saccharomyces cerevisiae. Plant J. 12, 819-829.
    • (1997) Plant J. , vol.12 , pp. 819-829
    • Hiraiwa, N.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 28
    • 0032970657 scopus 로고    scopus 로고
    • Vacuolar processing enzyme is self-catalytically activated by sequential removal of the C-terminal and N-terminal propeptides
    • Hiraiwa, N., Nishimura, M. and Hara-Nishimura, I. (1999) Vacuolar processing enzyme is self-catalytically activated by sequential removal of the C-terminal and N-terminal propeptides. FEBS Lett. 447, 213-216.
    • (1999) FEBS Lett. , vol.447 , pp. 213-216
    • Hiraiwa, N.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 29
    • 0027139607 scopus 로고
    • A vacuolar processing enzyme in maturing and germinating seeds: Its distribution and associated changes during development
    • Hiraiwa, N., Takeuchi, Y., Nishimura, M. and Hara-Nishimura, I. (1993) A vacuolar processing enzyme in maturing and germinating seeds: Its distribution and associated changes during development. Plant Cell Physiol. 34, 1197-1204.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 1197-1204
    • Hiraiwa, N.1    Takeuchi, Y.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 30
    • 0031105674 scopus 로고    scopus 로고
    • Heterologous expression and subcellular localization of pumpkin seed tonoplast intrinsic proteins (TIP) in yeast cells
    • Inoue, K., Wada, Y., Nishimura, M. and Hara-Nishimura, I. (1997) Heterologous expression and subcellular localization of pumpkin seed tonoplast intrinsic proteins (TIP) in yeast cells. Plant Cell Physiol. 38, 366-370.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 366-370
    • Inoue, K.1    Wada, Y.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 31
    • 51249176890 scopus 로고
    • Assaying chimeric genes in plants: The GUS gene fusion system
    • Jefferson, R.A. (1987) Assaying chimeric genes in plants: The GUS gene fusion system. Plant Mol. Biol. Report, 5, 387-405.
    • (1987) Plant Mol. Biol. Report , vol.5 , pp. 387-405
    • Jefferson, R.A.1
  • 32
    • 0029310609 scopus 로고
    • Ethylene-regulated expression of a carnation cysteine proteinase during flower petal senescence
    • Jones, M.L., Larsen, P.B. and Woodson, W.R. (1995) Ethylene-regulated expression of a carnation cysteine proteinase during flower petal senescence. Plant Mol. Biol. 28, 505-512.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 505-512
    • Jones, M.L.1    Larsen, P.B.2    Woodson, W.R.3
  • 33
    • 0020338057 scopus 로고
    • PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae
    • Jones, E.W., Zubenko, G.S. and Parker, R.R. (1982) PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae. Genetics. 102, 665-677.
    • (1982) Genetics , vol.102 , pp. 665-677
    • Jones, E.W.1    Zubenko, G.S.2    Parker, R.R.3
  • 34
    • 0029379549 scopus 로고
    • Homologues of a vacuolar processing enzyme that are expressed in different organs in Arabidopsis thaliana
    • Kinoshita, T., Nishimura, M. and Hara-Nishimura, I. (1995a) Homologues of a vacuolar processing enzyme that are expressed in different organs in Arabidopsis thaliana. Plant Mol. Biol. 29, 81-89.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 81-89
    • Kinoshita, T.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 35
    • 0029588601 scopus 로고
    • The sequence and expression of the γ-VPE gene, one member of a family of three genes for vacuolar processing enzymes in Arabidopsis thaliana
    • Kinoshita, T., Nishimura, M. and Hara-Nishimura, I. (1995b) The sequence and expression of the γ-VPE gene, one member of a family of three genes for vacuolar processing enzymes in Arabidopsis thaliana. Plant Cell Physiol. 36, 1555-1562.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 1555-1562
    • Kinoshita, T.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 36
    • 0024581884 scopus 로고
    • Primary structure of sm31/32 diagnostic proteins of Schistosoma mansoni and their identification as proteases
    • Klinkert, M.-Q., Felleisen, R., Link, G., Ruppel, A. and Beck, E. (1989) Primary structure of Sm31/32 diagnostic proteins of Schistosoma mansoni and their identification as proteases. Mol. Biochem. Parasitol. 33, 113-122.
    • (1989) Mol. Biochem. Parasitol. , vol.33 , pp. 113-122
    • Klinkert, M.-Q.1    Felleisen, R.2    Link, G.3    Ruppel, A.4    Beck, E.5
  • 37
    • 0027274695 scopus 로고
    • Structure and expression of two genes that encode distinct drought-inducible cysteine proteinases in Arabidopsis thaliana
    • Koizumi, M., Yamaguchi-Shinozaki, K., Tsuji, H. and Shinozaki, K. (1993) Structure and expression of two genes that encode distinct drought-inducible cysteine proteinases in Arabidopsis thaliana. Gene, 129, 175-182.
    • (1993) Gene , vol.129 , pp. 175-182
    • Koizumi, M.1    Yamaguchi-Shinozaki, K.2    Tsuji, H.3    Shinozaki, K.4
  • 38
    • 0031128023 scopus 로고    scopus 로고
    • Programmed cell death in the root cortex of soybean root necrosis mutants
    • Kosslak, R.M., Chamberlin, M.A., Palmer, R.G. and Bowen, B.A. (1997) Programmed cell death in the root cortex of soybean root necrosis mutants. Plant J. 11, 729-745.
    • (1997) Plant J. , vol.11 , pp. 729-745
    • Kosslak, R.M.1    Chamberlin, M.A.2    Palmer, R.G.3    Bowen, B.A.4
  • 39
    • 0027690396 scopus 로고
    • Fruit developmental regulation of the kiwifruit actinidin promoter is conserved in transgenic petunia plants
    • Lin, E., Burns, D.J.W. and Gardner, R.C. (1993) Fruit developmental regulation of the kiwifruit actinidin promoter is conserved in transgenic petunia plants. Plant Mol. Biol. 23, 489-499.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 489-499
    • Lin, E.1    Burns, D.J.W.2    Gardner, R.C.3
  • 40
    • 0025091987 scopus 로고
    • Electroporation of binary Ti plasmid vector into Agrobacterium tumefaciens and Agrobacterium rhizogenes
    • Nagel, R., Elliott, A., Masel, A., Birch, R.G. and Manners, J.M. (1990) Electroporation of binary Ti plasmid vector into Agrobacterium tumefaciens and Agrobacterium rhizogenes. FEMS Microbiol. Lett 67, 325-328.
    • (1990) FEMS Microbiol. Lett , vol.67 , pp. 325-328
    • Nagel, R.1    Elliott, A.2    Masel, A.3    Birch, R.G.4    Manners, J.M.5
  • 41
    • 0029008688 scopus 로고
    • Purification of a processing enzyme (VmPe-1) that is involved in post-translational processing of a plant cysteine endopeptidase (SH-EP)
    • Okamoto, T. and Minamikawa, T. (1995) Purification of a processing enzyme (VmPE-1) that is involved in post-translational processing of a plant cysteine endopeptidase (SH-EP). Eur. J. Biochem. 231, 300-305.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 300-305
    • Okamoto, T.1    Minamikawa, T.2
  • 42
    • 0029294005 scopus 로고
    • Correct processing of the kiwifruit protease actinidin in transgenic tobacco requires the presence of the C-terminal propeptide
    • Paul, W., Amiss, J., Try, R., Praekelt, U., Scott, R. and Smith, H. (1995) Correct processing of the kiwifruit protease actinidin in transgenic tobacco requires the presence of the C-terminal propeptide. Plant Physiol. 108, 261-268.
    • (1995) Plant Physiol. , vol.108 , pp. 261-268
    • Paul, W.1    Amiss, J.2    Try, R.3    Praekelt, U.4    Scott, R.5    Smith, H.6
  • 43
    • 0028446555 scopus 로고
    • Vacuolar processing enzyme of soybean that converts proprotein to the corresponding mature forms
    • Shimada, T., Hiraiwa, N., Nishimura, M. and Hara-Nishimura, I. (1994) Vacuolar processing enzyme of soybean that converts proprotein to the corresponding mature forms. Plant Cell Physiol. 35, 713-718.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 713-718
    • Shimada, T.1    Hiraiwa, N.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 44
    • 0027572807 scopus 로고
    • Posttranslational processing of a new class of hydroxyproline-containing proteins: Prolyl hydroxylation and C-terminal cleavage of tobacco (Nicotiana tabacum) vacuolar chitinase
    • Sticher, L., Hofsteenge, J., Neuhaus, J.-M., Boller, T. and Meins, F.J. (1993) Posttranslational processing of a new class of hydroxyproline-containing proteins: Prolyl hydroxylation and C-terminal cleavage of tobacco (Nicotiana tabacum) vacuolar chitinase. Plant Physiol. 101, 1239-1247.
    • (1993) Plant Physiol. , vol.101 , pp. 1239-1247
    • Sticher, L.1    Hofsteenge, J.2    Neuhaus, J.-M.3    Boller, T.4    Meins, F.J.5
  • 45
    • 0027990302 scopus 로고
    • Isolation and analysis of cDNA encoding a precursor of Canavalia ensiformis asparaginyl endopeptidase (legumain)
    • Takeda, O., Miura, Y., Mitta, M., Matsushita, H., Kato, I., Abe, Y., Yokosawa, H. and Ishii, S.-i. (1994) Isolation and analysis of cDNA encoding a precursor of Canavalia ensiformis asparaginyl endopeptidase (legumain). J. Biochem. 116, 541-546.
    • (1994) J. Biochem. , vol.116 , pp. 541-546
    • Takeda, O.1    Miura, Y.2    Mitta, M.3    Matsushita, H.4    Kato, I.5    Abe, Y.6    Yokosawa, H.7    Ishii, S.-I.8
  • 46
    • 0023652379 scopus 로고
    • Protein sorting in yeast; the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide
    • Valls, L.A., Hunter, C.P., Rothman, J.H. and Stevens, T.H. (1987) Protein sorting in yeast; the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide. Cell, 48, 887-897.
    • (1987) Cell , vol.48 , pp. 887-897
    • Valls, L.A.1    Hunter, C.P.2    Rothman, J.H.3    Stevens, T.H.4
  • 47
    • 0029310458 scopus 로고
    • Upregulation of a cysteine protease accompanies the ethylene-insensitive senescence of daylily (Hemerocallis) flowers
    • Valpuesta, V., Lange, N.E., Guerrero, C. and Reid, M.S. (1995) Upregulation of a cysteine protease accompanies the ethylene-insensitive senescence of daylily (Hemerocallis) flowers. Plant Mol. Biol. 28, 575-582.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 575-582
    • Valpuesta, V.1    Lange, N.E.2    Guerrero, C.3    Reid, M.S.4
  • 48
    • 0025269991 scopus 로고
    • The SLP1 gene of Saccharomyces cerevisiae is essential for vacuolar morphogenesis and function
    • Wada, Y., Kitamoto, K., Kanbe, T., Tanaka, K. and Anraku, Y. (1990) The SLP1 gene of Saccharomyces cerevisiae is essential for vacuolar morphogenesis and function. Mol. Cell Biol. 10, 2214-2223.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 2214-2223
    • Wada, Y.1    Kitamoto, K.2    Kanbe, T.3    Tanaka, K.4    Anraku, Y.5
  • 49
    • 0026095842 scopus 로고
    • Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (oryzains)
    • Watanabe, H., Abe, K., Emori, Y., Hosoyama, H. and Arai, S. (1991) Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (oryzains). J. Biol. Chem. 266, 16897-16902.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16897-16902
    • Watanabe, H.1    Abe, K.2    Emori, Y.3    Hosoyama, H.4    Arai, S.5
  • 50
    • 0033593439 scopus 로고    scopus 로고
    • Multiple functional proteins are produced by cleaving Asn-Gln bonds of a single precursor by vacuolar processing enzyme
    • Yamada, K., Shimada, T., Kondo, M., Nishimura, M. and Hara-Nishimura, I. (1999) Multiple functional proteins are produced by cleaving Asn-Gln bonds of a single precursor by vacuolar processing enzyme. J. Biol. Chem. 274, 2563-2570.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2563-2570
    • Yamada, K.1    Shimada, T.2    Kondo, M.3    Nishimura, M.4    Hara-Nishimura, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.