메뉴 건너뛰기




Volumn 121, Issue 3, 1997, Pages 464-476

Characterization of a gene family encoding cysteine proteinases of Sitophilus zeamais (maize weevil), and analysis of the protein distribution in various tissues including alimentary tract and germ cells

Author keywords

Alimentary tract; Cysteine proteinase; Gene family; Germ cells; Maize weevil

Indexed keywords

AMINO ACID; CATHEPSIN L; COMPLEMENTARY DNA; CYSTEINE PROTEINASE; MESSENGER RNA;

EID: 0030964845     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021611     Document Type: Article
Times cited : (56)

References (57)
  • 1
    • 0020688213 scopus 로고
    • Structures and functions of lysosomal thiol proteinases and their endogenous inhibitor
    • Katunuma, N. and Kominami, E. (1983) Structures and functions of lysosomal thiol proteinases and their endogenous inhibitor. Curr. Top. Cell. Regul. 22, 71-101
    • (1983) Curr. Top. Cell. Regul. , vol.22 , pp. 71-101
    • Katunuma, N.1    Kominami, E.2
  • 3
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-lβ-converting enzyme
    • Yuan, J., Shaham, S., Ledoux, S., Ellis, H.M., and Horvitz, H.R. (1993) The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-lβ-converting enzyme. Cell 75, 641-652
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 4
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3
    • Miura, M., Zhu, H., Rotello, R., Hartwieg, E.A., and Yuan, J. (1993) Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell 75, 653-660
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartwieg, E.A.4    Yuan, J.5
  • 5
    • 0029069295 scopus 로고
    • ICE-like proteases in apoptosis
    • Kumar, S. (1995) ICE-like proteases in apoptosis. Trends Biochem. Sci. 20, 198-202
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 198-202
    • Kumar, S.1
  • 6
    • 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
  • 7
    • 0028923541 scopus 로고
    • Alignment/phylogeny of the papain superfamily of cysteine proteases
    • Berti, P.J. and Storer, A.C. (1995) Alignment/phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 246, 273-283
    • (1995) J. Mol. Biol. , vol.246 , pp. 273-283
    • Berti, P.J.1    Storer, A.C.2
  • 8
    • 0344310530 scopus 로고
    • Identification of cDNA clones encoding a precursor of rat liver cathepsin B
    • Segundo, B.S., Chan, S.J., and Steiner, D.F. (1985) Identification of cDNA clones encoding a precursor of rat liver cathepsin B. Proc. Natl. Acad. Sci. USA 82, 2320-2324
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2320-2324
    • Segundo, B.S.1    Chan, S.J.2    Steiner, D.F.3
  • 11
    • 0027092035 scopus 로고
    • Sequence analysis, tissue distribution, and expression of rat cathepsin S
    • Petanceska, S. and Devi, L. (1992) Sequence analysis, tissue distribution, and expression of rat cathepsin S. J. Biol. Chem. 267, 26038-26043
    • (1992) J. Biol. Chem. , vol.267 , pp. 26038-26043
    • Petanceska, S.1    Devi, L.2
  • 13
    • 0026000497 scopus 로고
    • Molecular cloning of cDNA for rat cathepsin C
    • Ishidoh, K., Muno, D., Sato, N., and Kominami, E. (1991) Molecular cloning of cDNA for rat cathepsin C. J. Biol. Chem. 266, 16312-16317
    • (1991) J. Biol. Chem. , vol.266 , pp. 16312-16317
    • Ishidoh, K.1    Muno, D.2    Sato, N.3    Kominami, E.4
  • 14
    • 0022828086 scopus 로고
    • Cloning and sequencing of papain-encoding cDNA
    • Cohen, L.W., Coghlan, V.M., and Dihel, L.C. (1986) Cloning and sequencing of papain-encoding cDNA. Gene 48, 219-227
    • (1986) Gene , vol.48 , pp. 219-227
    • Cohen, L.W.1    Coghlan, V.M.2    Dihel, L.C.3
  • 15
    • 0011742571 scopus 로고
    • Aleurain: A barley thiol protease closely related to mammalian cathepsin H
    • Rogers, J.C., Dean, D., and Heck, G.R. (1985) Aleurain: a barley thiol protease closely related to mammalian cathepsin H. Proc. Natl. Acad. Sci. USA 82, 6512-6516
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6512-6516
    • Rogers, J.C.1    Dean, D.2    Heck, G.R.3
  • 16
    • 0026095842 scopus 로고
    • Molecular cloning and gebberellin-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 gebberellin-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
  • 17
    • 0022052044 scopus 로고
    • A developmentally regulated cysteine proteinase in Dictyostelium discoideum
    • Williams, J.G., North, M.J., and Mahbubani, H. (1985) A developmentally regulated cysteine proteinase in Dictyostelium discoideum. EMBO J. 4, 999-1006
    • (1985) EMBO J. , vol.4 , pp. 999-1006
    • Williams, J.G.1    North, M.J.2    Mahbubani, H.3
  • 18
    • 0026570815 scopus 로고
    • The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is encoded by multiple polymorphic tandemly organized gene located on different chromosomes
    • Campetella, O., Henriksson, J., Aslund, L., Frasen, A.C.C., Pettersson, U., and Cazzulo, J.J. (1992) The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is encoded by multiple polymorphic tandemly organized gene located on different chromosomes. Mol Biochem. Parasitol. 50, 225-234
    • (1992) Mol Biochem. Parasitol. , vol.50 , pp. 225-234
    • Campetella, O.1    Henriksson, J.2    Aslund, L.3    Frasen, A.C.C.4    Pettersson, U.5    Cazzulo, J.J.6
  • 19
    • 0023462882 scopus 로고
    • The identiflcation of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L
    • Mason, R.W., Gal, S., and Gottesman, M.M. (1987) The identiflcation of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L. Biochem. J. 248, 449-454
    • (1987) Biochem. J. , vol.248 , pp. 449-454
    • Mason, R.W.1    Gal, S.2    Gottesman, M.M.3
  • 22
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • Golde, T.E., Estus, S., Younkin, L.H., Selkoe, D.J., and Younkin, S.G. (1992) Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 255, 728-730
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.E.1    Estus, S.2    Younkin, L.H.3    Selkoe, D.J.4    Younkin, S.G.5
  • 23
    • 0025817602 scopus 로고
    • The cystatins: Protein inhibitors of cysteine proteinases
    • Turk, V. and Bode, W. (1991) The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett. 285, 213-219
    • (1991) FEBS Lett. , vol.285 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 24
    • 0024066065 scopus 로고
    • The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode, W., Engh, R., Musil, D., Thiele, U., Huber, R., Karshikov, A., Brzin, J., Kos, J., and Turk, V. (1988) The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7, 2593-2599
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 25
    • 0025301658 scopus 로고
    • The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction
    • Stubbs, M.T., Laber, B., Bode, W., Huber, R., Jerala, R., Lenarcic, B., and Turk, V. (1990) The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J. 9, 1939-1947
    • (1990) EMBO J. , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 26
    • 0023657047 scopus 로고
    • Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin)
    • Abe, K., Emori, Y., Kondo, H., Suzuki, K., and Arai, S. (1987) Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). J. Biol. Chem. 262, 16793-16797
    • (1987) J. Biol. Chem. , vol.262 , pp. 16793-16797
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Suzuki, K.4    Arai, S.5
  • 27
    • 0024278653 scopus 로고
    • 2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily
    • 2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily. J. Biol. Chem. 263, 7655-7659
    • (1988) J. Biol. Chem. , vol.263 , pp. 7655-7659
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Arai, S.4    Suzuki, K.5
  • 28
    • 0024424222 scopus 로고
    • Cloning and sequence analysis of the genomic DNA fragment encoding oryzacystatin
    • Kondo, H., Emori, Y., Abe, K., Suzuki, K., and Arai, S. (1989) Cloning and sequence analysis of the genomic DNA fragment encoding oryzacystatin. Gene 81, 259-265
    • (1989) Gene , vol.81 , pp. 259-265
    • Kondo, H.1    Emori, Y.2    Abe, K.3    Suzuki, K.4    Arai, S.5
  • 29
    • 0025160575 scopus 로고
    • Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases
    • Kondo, H., Abe, K., Nishimura, I., Watanabe, H., Emori, Y., and Arai, S. (1990) Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. J. Biol. Chem. 265, 15832-15837
    • (1990) J. Biol. Chem. , vol.265 , pp. 15832-15837
    • Kondo, H.1    Abe, K.2    Nishimura, I.3    Watanabe, H.4    Emori, Y.5    Arai, S.6
  • 30
    • 0026042651 scopus 로고
    • Oryzacystatins as the first well-defined cystatins of plant origin and their target proteinases in rice seeds
    • Abe, K., Kondo, H., Watanabe, H., Emori, Y., and Arai, S. (1991) Oryzacystatins as the first well-defined cystatins of plant origin and their target proteinases in rice seeds. Biomed. Biochim. Acta 50, 637-641
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 637-641
    • Abe, K.1    Kondo, H.2    Watanabe, H.3    Emori, Y.4    Arai, S.5
  • 31
    • 0026497716 scopus 로고
    • Corn kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin
    • Abe, M., Abe, K., Kuroda, M., and Arai, S. (1992) Corn kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin. Eur. J. Biochem. 209, 933-937
    • (1992) Eur. J. Biochem. , vol.209 , pp. 933-937
    • Abe, M.1    Abe, K.2    Kuroda, M.3    Arai, S.4
  • 33
    • 0027691245 scopus 로고
    • Characterization of a genomic sequence coding for potato multicystatin, an eight-domain cysteine proteinase inhibitor
    • Waldron, C., Wegrich, L.M., Merlo, P.A.O., and Walsh, T.A. (1993) Characterization of a genomic sequence coding for potato multicystatin, an eight-domain cysteine proteinase inhibitor. Plant Mol. Biol. 23, 801-812
    • (1993) Plant Mol. Biol. , vol.23 , pp. 801-812
    • Waldron, C.1    Wegrich, L.M.2    Merlo, P.A.O.3    Walsh, T.A.4
  • 34
    • 0026505938 scopus 로고
    • Inhibitory effect of oryzacystatins and a truncation mutant on the replication of poliovirus in infected Vero cells
    • Kondo, H., Ijiri, S., Abe, K., Maeda, H., and Arai, S. (1992) Inhibitory effect of oryzacystatins and a truncation mutant on the replication of poliovirus in infected Vero cells. FEBS Lett. 299, 48-50
    • (1992) FEBS Lett. , vol.299 , pp. 48-50
    • Kondo, H.1    Ijiri, S.2    Abe, K.3    Maeda, H.4    Arai, S.5
  • 35
    • 0028916483 scopus 로고
    • Antiviral effect of oryzacystatin, a proteinase inhibitor in rice, against herpes simplex virus type 1 in vitro and in vivo
    • Aoki, H., Akaike, T., Abe, K., Kuroda, M., Arai, S., Okumura, R., Negi, A., and Maeda, H. (1995) Antiviral effect of oryzacystatin, a proteinase inhibitor in rice, against herpes simplex virus type 1 in vitro and in vivo. Antimicrob. Agents Chemother. 39, 846-849
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 846-849
    • Aoki, H.1    Akaike, T.2    Abe, K.3    Kuroda, M.4    Arai, S.5    Okumura, R.6    Negi, A.7    Maeda, H.8
  • 36
    • 0030027738 scopus 로고    scopus 로고
    • Oryzacystatins exhibit growth-inhibitory and lethal effects on different species of bean insect pests, Callosobruchus chinensis (Coleoptera) and Riptortus clavatus (Hemiptera)
    • Kuroda, M., Ishimoto, M., Suzuki, K., Kondo, H., Abe, K., Kitamura, K., and Arai, S. (1996) Oryzacystatins exhibit growth-inhibitory and lethal effects on different species of bean insect pests, Callosobruchus chinensis (Coleoptera) and Riptortus clavatus (Hemiptera). Biosci. Biotech. Biochem. 60, 209-212
    • (1996) Biosci. Biotech. Biochem. , vol.60 , pp. 209-212
    • Kuroda, M.1    Ishimoto, M.2    Suzuki, K.3    Kondo, H.4    Abe, K.5    Kitamura, K.6    Arai, S.7
  • 38
    • 0027170847 scopus 로고
    • Dietary mixtures of cysteine and serine proteinase inhibitors exhibit synergistic toxicity toward the red flour beetle, Tribolium castaneum
    • Oppert, B., Morgan, T.D., Culbertson, C., and Kramer, K.J. (1993) Dietary mixtures of cysteine and serine proteinase inhibitors exhibit synergistic toxicity toward the red flour beetle, Tribolium castaneum. Comp. Biochem. Physiol. 105C, 379-385
    • (1993) Comp. Biochem. Physiol. , vol.105 C , pp. 379-385
    • Oppert, B.1    Morgan, T.D.2    Culbertson, C.3    Kramer, K.J.4
  • 39
    • 0028840144 scopus 로고
    • A putative digestive cysteine proteinase from Drosophila melanogaster is predominantly expressed in the embryonic and larval midgut
    • Matsumoto, I., Watanabe, H., Abe, K., Arai, S., and Emori, Y. (1995) A putative digestive cysteine proteinase from Drosophila melanogaster is predominantly expressed in the embryonic and larval midgut. Eur. J. Biochem. 227, 582-587
    • (1995) Eur. J. Biochem. , vol.227 , pp. 582-587
    • Matsumoto, I.1    Watanabe, H.2    Abe, K.3    Arai, S.4    Emori, Y.5
  • 40
    • 0028243651 scopus 로고
    • Purification, characterization, and cDNA cloning of procathepsin L from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrine (flesh fly), and its involvement in the differentiation of imaginal discs
    • Homma, K., Kurata, S., and Natori, S. (1994) Purification, characterization, and cDNA cloning of procathepsin L from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrine (flesh fly), and its involvement in the differentiation of imaginal discs. J. Biol. Chem. 269, 15258-15264
    • (1994) J. Biol. Chem. , vol.269 , pp. 15258-15264
    • Homma, K.1    Kurata, S.2    Natori, S.3
  • 41
    • 0028606210 scopus 로고
    • Molecular cloning and sequencing of cDNA that encodes cysteine proteinase in the eggs of the silkmoth, Bombyx mori
    • Yamamoto, Y., Takimoto, K., Izumi, S., Toriyama-Sakurai, M., Kageyama, T., and Takahashi, S.Y. (1994) Molecular cloning and sequencing of cDNA that encodes cysteine proteinase in the eggs of the silkmoth, Bombyx mori. J. Biochem. 116, 1330-1335
    • (1994) J. Biochem. , vol.116 , pp. 1330-1335
    • Yamamoto, Y.1    Takimoto, K.2    Izumi, S.3    Toriyama-Sakurai, M.4    Kageyama, T.5    Takahashi, S.Y.6
  • 42
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E.M. (1975) Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98, 503-517
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 44
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • Frohman, M.A., Dush, M.K., and Martin, G.R. (1988) Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc. Natl. Acad. Sci. USA 85, 8998-9002
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 47
    • 0027985149 scopus 로고
    • Calpain localization changes in coordination with actin-related cytoskeletal changes during early embryonic development of Drosophila
    • Emori, Y. and Saigo, K. (1994) Calpain localization changes in coordination with actin-related cytoskeletal changes during early embryonic development of Drosophila. J. Biol. Chem. 269, 25137-25142
    • (1994) J. Biol. Chem. , vol.269 , pp. 25137-25142
    • Emori, Y.1    Saigo, K.2
  • 48
    • 0028279274 scopus 로고
    • Purification of glutathione S-transferase fusion proteins as a non-degraded form by using a protease-negative E. coli strain, AD202
    • Nakano, H., Yamazaki, T., Ikeda, M., Masai, H., Miyatake, S., and Saito, T. (1994) Purification of glutathione S-transferase fusion proteins as a non-degraded form by using a protease-negative E. coli strain, AD202. Nucleic Acids Res. 22, 543-544
    • (1994) Nucleic Acids Res. , vol.22 , pp. 543-544
    • Nakano, H.1    Yamazaki, T.2    Ikeda, M.3    Masai, H.4    Miyatake, S.5    Saito, T.6
  • 49
    • 0023778543 scopus 로고
    • Isolation and sequence of a cDNA for human pro-(cathepsin L)
    • Gal, S. and Gottesman, M.M. (1988) Isolation and sequence of a cDNA for human pro-(cathepsin L). Biochem. J. 253, 303-306
    • (1988) Biochem. J. , vol.253 , pp. 303-306
    • Gal, S.1    Gottesman, M.M.2
  • 50
    • 0026001237 scopus 로고
    • Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus)
    • Laycock, M.V., MacKay, R.M., Fruscio, M.D., and Gallant, J.W. (1991) Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus). FEBS Lett. 292, 115-120
    • (1991) FEBS Lett. , vol.292 , pp. 115-120
    • Laycock, M.V.1    MacKay, R.M.2    Fruscio, M.D.3    Gallant, J.W.4
  • 51
    • 0027177631 scopus 로고
    • Cysteine proteinase from the eggs of the silkmoth, Bombyx mori: Identification of a latent enzyme and characterization of activation and proteolytic processing in vivo and in vitro
    • Takahashi, S.Y., Yamamoto, Y., Shionoya, Y., and Kageyama, T. (1993) Cysteine proteinase from the eggs of the silkmoth, Bombyx mori: identification of a latent enzyme and characterization of activation and proteolytic processing in vivo and in vitro. J. Biochem. 114, 267-272
    • (1993) J. Biochem. , vol.114 , pp. 267-272
    • Takahashi, S.Y.1    Yamamoto, Y.2    Shionoya, Y.3    Kageyama, T.4
  • 52
    • 0000782890 scopus 로고
    • Ultrastructural features of the gut of Sitophilus granarius (L.) (Coleoptera: Curculionidae) with notes on distribution of proteinases and amylases in crop and midgut
    • Baker, J. E., Woo, S.M., and Byrd, R.V. (1984) Ultrastructural features of the gut of Sitophilus granarius (L.) (Coleoptera: Curculionidae) with notes on distribution of proteinases and amylases in crop and midgut. Can. J. Zool. 62, 1251-1259
    • (1984) Can. J. Zool. , vol.62 , pp. 1251-1259
    • Baker, J.E.1    Woo, S.M.2    Byrd, R.V.3
  • 53
    • 0027218436 scopus 로고
    • Cysteine proteinase from Bombyx eggs: Role in programmed degradation of yolk proteins during embryogenesis
    • Yamamoto, Y. and Takahashi, S.Y. (1993) Cysteine proteinase from Bombyx eggs: role in programmed degradation of yolk proteins during embryogenesis. Comp. Biochem. Physiol. 106B, 35-45
    • (1993) Comp. Biochem. Physiol. , vol.106 B , pp. 35-45
    • Yamamoto, Y.1    Takahashi, S.Y.2
  • 55
    • 0026054428 scopus 로고
    • Inhibition of digestive proteinases of stored grain coleoptera by oryzacystatin, a cysteine proteinase inhibitor from rice seed
    • Liang, C., Brookhart, G., Feng, G.H., Reeck, G.R., and Kramer, K.J. (1991) Inhibition of digestive proteinases of stored grain coleoptera by oryzacystatin, a cysteine proteinase inhibitor from rice seed. FEBS Lett. 278, 139-142
    • (1991) FEBS Lett. , vol.278 , pp. 139-142
    • Liang, C.1    Brookhart, G.2    Feng, G.H.3    Reeck, G.R.4    Kramer, K.J.5
  • 56
    • 0027999854 scopus 로고
    • Insect digestive enzymes: Properties, compartmentalization and function
    • Terra, W.R. and Ferreira, C. (1994) Insect digestive enzymes: properties, compartmentalization and function. Comp. Biochem. Physiol. 109B, 1-62
    • (1994) Comp. Biochem. Physiol. , vol.109 B , pp. 1-62
    • Terra, W.R.1    Ferreira, C.2
  • 57
    • 0030019236 scopus 로고    scopus 로고
    • Transgenic rice established to express corn cystatin exhibits strong inhibitory activity against, insect gut proteinases
    • Irie, K., Hosoyama, H., Takeuchi, T., Iwabuchi, K., Watanabe, H., Abe, M., Abe, K., and Arai, S. (1996) Transgenic rice established to express corn cystatin exhibits strong inhibitory activity against, insect gut proteinases. Plant Mol. Biol. 30, 149-157
    • (1996) Plant Mol. Biol. , vol.30 , pp. 149-157
    • Irie, K.1    Hosoyama, H.2    Takeuchi, T.3    Iwabuchi, K.4    Watanabe, H.5    Abe, M.6    Abe, K.7    Arai, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.