메뉴 건너뛰기




Volumn 30, Issue 1-3, 1996, Pages 265-281

Bombyx acid cysteine proteinase

Author keywords

BCP; Pro cysteine proteinase; Yolk protein degradation

Indexed keywords

BOMBYX; BOMBYX MORI;

EID: 0030433850     PISSN: 07924259     EISSN: None     Source Type: Journal    
DOI: 10.1080/07924259.1996.9672553     Document Type: Article
Times cited : (24)

References (61)
  • 1
    • 0015523287 scopus 로고
    • Kinetics and mechanism of pepsinogen
    • Al-Janabi, J., Hartsuck, J.A. and Tang, J., Kinetics and mechanism of pepsinogen. J. Biol. Chem., 247 (1972) 4628-4632.
    • (1972) J. Biol. Chem. , vol.247 , pp. 4628-4632
    • Al-Janabi, J.1    Hartsuck, J.A.2    Tang, J.3
  • 3
    • 0001358480 scopus 로고
    • Expression of genes coding for vitellogenin (yolk proteins)
    • Bownes, M., Expression of genes coding for vitellogenin (yolk proteins). Annu. Rev. Entomol., 31 (1986) 507-531.
    • (1986) Annu. Rev. Entomol. , vol.31 , pp. 507-531
    • Bownes, M.1
  • 4
    • 0017480648 scopus 로고
    • Accumulation and degradation of three major yolk proteins in Drosophila melanogaster
    • Bownes, M and Hames, B.D., Accumulation and degradation of three major yolk proteins in Drosophila melanogaster. J. Exp. Zool., 220 (1977) 149-156.
    • (1977) J. Exp. Zool. , vol.220 , pp. 149-156
    • Bownes, M.1    Hames, B.D.2
  • 5
    • 0023968631 scopus 로고
    • Evidence that insect embryogenesis is regulated by ecdysteroids released from yolk proteins
    • Bownes, M., Shirras, A., Blair, M., Collins, J. and Coulson, A. Evidence that insect embryogenesis is regulated by ecdysteroids released from yolk proteins. Proc. Natl. Acad. Sci. U.S.A., 85 (1988) 1554-1557.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 1554-1557
    • Bownes, M.1    Shirras, A.2    Blair, M.3    Collins, J.4    Coulson, A.5
  • 6
    • 0025787870 scopus 로고
    • Extraovarian protein accumulated in mosquito oocytes is a carboxypeptidase activated in embryos
    • Cho, W-L., Deitsch, K.W. and Raikhel, A.S., Extraovarian protein accumulated in mosquito oocytes is a carboxypeptidase activated in embryos. Proc. Natl. Acad. Sci. U.S.A., 88 (1991) 10821-10824.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10821-10824
    • Cho, W.-L.1    Deitsch, K.W.2    Raikhel, A.S.3
  • 7
    • 0025977159 scopus 로고
    • Three-dimensional structure of porcine procarboxypeptidase B: A structural basis of its inactivity
    • Coll, M., Guasch, A., Aviles, F.X. and Huber, R., Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity. EMBO J., 10 (1991) 1-9.
    • (1991) EMBO J. , vol.10 , pp. 1-9
    • Coll, M.1    Guasch, A.2    Aviles, F.X.3    Huber, R.4
  • 8
    • 0027134699 scopus 로고
    • Cloning and analysis of the locus for mosquito vitellogenic carboxypeptidase
    • Deitsch, K.W. and Raikhel, A.S., Cloning and analysis of the locus for mosquito vitellogenic carboxypeptidase. Insect Molec. Biol., 2 (1993) 205-213.
    • (1993) Insect Molec. Biol. , vol.2 , pp. 205-213
    • Deitsch, K.W.1    Raikhel, A.S.2
  • 9
    • 3242852016 scopus 로고
    • Chemistry and enzymology of pancreatic enndiopeptidases
    • P. Desnuelle, H. Sjostrom and O. Noren (eds.), Elsevier Science, Amsterdam
    • Desnuelle, P., Chemistry and enzymology of pancreatic enndiopeptidases. In: Molecular and Cellular Basis of Digestion, P. Desnuelle, H. Sjostrom and O. Noren (eds.), Elsevier Science, Amsterdam, 1986, pp. 195-211.
    • (1986) Molecular and Cellular Basis of Digestion , pp. 195-211
    • Desnuelle, P.1
  • 10
    • 0024442681 scopus 로고
    • Visualization under ultraviolet light enhances 100-fold the sensitivity of peroxidase-stained blots
    • Domingo, A. and Marco, R., Visualization under ultraviolet light enhances 100-fold the sensitivity of peroxidase-stained blots. Analyt. Biochem., 182 (1989) 176-181.
    • (1989) Analyt. Biochem. , vol.182 , pp. 176-181
    • Domingo, A.1    Marco, R.2
  • 11
    • 0026386871 scopus 로고
    • Cyclic protein-2, a secretory product of rat sertori cells, is the proenzyme form of cathepsin L
    • Erickson-Lawrence, M., Zabludoff, S.D. and Wright, W.W., Cyclic protein-2, a secretory product of rat sertori cells, is the proenzyme form of cathepsin L. Mol. Endocorinol., 5 (1991) 1789-1798.
    • (1991) Mol. Endocorinol. , vol.5 , pp. 1789-1798
    • Erickson-Lawrence, M.1    Zabludoff, S.D.2    Wright, W.W.3
  • 12
    • 0025527484 scopus 로고
    • Yolk degradation in tick eggs: I Occurrence of a cathepsin L-like acid cysteine proteinase in yolk spheres
    • Fagotto, F., Yolk degradation in tick eggs: I Occurrence of a cathepsin L-like acid cysteine proteinase in yolk spheres. Arch. Insect Biochem. Physiol., 14 (1990) 217-235.
    • (1990) Arch. Insect Biochem. Physiol. , vol.14 , pp. 217-235
    • Fagotto, F.1
  • 13
    • 0026035346 scopus 로고
    • Yolk degradation in tick eggs: III Developmentally regulated acidification of the yolk spheres
    • Fagotto, F., Yolk degradation in tick eggs: III Developmentally regulated acidification of the yolk spheres. Develop. Growth Differ., 33 (1991) 57-66.
    • (1991) Develop. Growth Differ. , vol.33 , pp. 57-66
    • Fagotto, F.1
  • 14
    • 0025135576 scopus 로고
    • In vitro translation and processing of cathepsin B of Schistosoma mamsoni
    • Falleisen, R. and Klinkert, M.-Q., In vitro translation and processing of cathepsin B of Schistosoma mamsoni. EMBO J., 9 (1990) 371-377.
    • (1990) EMBO J. , vol.9 , pp. 371-377
    • Falleisen, R.1    Klinkert, M.-Q.2
  • 15
    • 0000193630 scopus 로고
    • Vitellogenin and vitellin in insects
    • Hagedorn, H.H. and Kunkel, J.G., Vitellogenin and vitellin in insects. Annu. Rev. Entomol., 24 (1979) 475-505.
    • (1979) Annu. Rev. Entomol. , vol.24 , pp. 475-505
    • Hagedorn, H.H.1    Kunkel, J.G.2
  • 16
    • 0025147952 scopus 로고
    • A novel protein produced by the vitellogenic fat body and accumulated in mosquito oocytes
    • Hays, A.R. and Raikhel, A.S., A novel protein produced by the vitellogenic fat body and accumulated in mosquito oocytes. Roux's Arch. Dev. Biol., 199 (1990) 114-121.
    • (1990) Roux's Arch. Dev. Biol. , vol.199 , pp. 114-121
    • Hays, A.R.1    Raikhel, A.S.2
  • 17
    • 0001600705 scopus 로고
    • Proaleyrain vacuolar targeting is mediated by short contiguous peptide interactions
    • Holwerda, B.C., Galvin, N.J., Baranski, T.J. and Rogers, J.C., Proaleyrain vacuolar targeting is mediated by short contiguous peptide interactions. Plant Cell, 2 (1990) 1091-1106.
    • (1990) Plant Cell , vol.2 , pp. 1091-1106
    • Holwerda, B.C.1    Galvin, N.J.2    Baranski, T.J.3    Rogers, J.C.4
  • 19
    • 0000147161 scopus 로고
    • Purification and characterization of protease responsible for vitellin degradation of the silkworm, Bombyx mori
    • Ikeda, M., Sasaki, T. and Yamashita, O., Purification and characterization of protease responsible for vitellin degradation of the silkworm, Bombyx mori. Insect Biochem., 20 (1990) 725-734.
    • (1990) Insect Biochem. , vol.20 , pp. 725-734
    • Ikeda, M.1    Sasaki, T.2    Yamashita, O.3
  • 20
    • 0025905535 scopus 로고
    • CDNA cloning, sequencing and temporal expression of the protease responsible for vitellin degradation in the silkworm, Bombyx mori
    • Ikeda, M., Yaginuma, T., Kobayashi, M. and Yamashita, O., cDNA cloning, sequencing and temporal expression of the protease responsible for vitellin degradation in the silkworm, Bombyx mori. Comp. Biochem. Physiol., 99B, (1991) 405-411.
    • (1991) Comp. Biochem. Physiol. , vol.99 B , pp. 405-411
    • Ikeda, M.1    Yaginuma, T.2    Kobayashi, M.3    Yamashita, O.4
  • 21
    • 0023870058 scopus 로고
    • A unique protease responsible for selective degradation of a yolk protein in Bombyx mori
    • Indrasith, L.S., Sasaki, T. and Yamashita, O., A unique protease responsible for selective degradation of a yolk protein in Bombyx mori. J. Biol. Chem., 263 (1988) 1045-1051.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1045-1051
    • Indrasith, L.S.1    Sasaki, T.2    Yamashita, O.3
  • 22
    • 0027962778 scopus 로고
    • Yolk proteins from insect eggs: Structure, biosynthesis and programmed degradation during embryogenesis
    • Izumi, S., Yano, K., Yamamoto, Y. and Takahashi, S.Y., Yolk proteins from insect eggs: structure, biosynthesis and programmed degradation during embryogenesis. Insect Physiology, 40 (1994) 735-746.
    • (1994) Insect Physiology , vol.40 , pp. 735-746
    • Izumi, S.1    Yano, K.2    Yamamoto, Y.3    Takahashi, S.Y.4
  • 23
    • 0024331359 scopus 로고
    • Molecular cloning and characterization of a progesterone-dependent cat endometrial secretory protein complementary deoxyribonucleic acid
    • Jaffe, R.C., Donnely, K.M., Mavrogians, P.A. and Verhage, H.G., Molecular cloning and characterization of a progesterone-dependent cat endometrial secretory protein complementary deoxyribonucleic acid. Mol. Endocrinol., 3 (1989) 1807-1814.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1807-1814
    • Jaffe, R.C.1    Donnely, K.M.2    Mavrogians, P.A.3    Verhage, H.G.4
  • 24
    • 0022643093 scopus 로고
    • Molecular structure of an asparatic protease zymogen, porcine pepsinogen, at 1.8A resolution
    • James, M.N.G. and Sielecki, A.R., Molecular structure of an asparatic protease zymogen, porcine pepsinogen, at 1.8A resolution. Nature, 319 (1986) 33-38.
    • (1986) Nature , vol.319 , pp. 33-38
    • James, M.N.G.1    Sielecki, A.R.2
  • 25
    • 0023688890 scopus 로고
    • Analysis of the activation of pepsinogen in the presence of protein substrates and estimation of the intrinsic proteolytic activity of pepsinogen
    • Kageyama, T., Analysis of the activation of pepsinogen in the presence of protein substrates and estimation of the intrinsic proteolytic activity of pepsinogen. Eur. J. Biochem., 176 (1988) 543-549.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 543-549
    • Kageyama, T.1
  • 26
    • 0025059406 scopus 로고
    • Purification and characterization of a cysteine proteinase from silkworm eggs
    • Kageyama, T. and Takahashi, S.Y., Purification and characterization of a cysteine proteinase from silkworm eggs. Eur. J. Biochem., 193 (1990) 203-210.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 203-210
    • Kageyama, T.1    Takahashi, S.Y.2
  • 27
    • 0001455778 scopus 로고
    • Time interval measuring enzyme for resumption of embryonic development in the silkworm, Bombyx mori
    • Kai, H., Kotani, Y., Miao, Y. and Azuma, M., Time interval measuring enzyme for resumption of embryonic development in the silkworm, Bombyx mori. J. Insect Physiol., 41 (1995) 905-910.
    • (1995) J. Insect Physiol. , vol.41 , pp. 905-910
    • Kai, H.1    Kotani, Y.2    Miao, Y.3    Azuma, M.4
  • 29
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease gene
    • Karrer, K.M., Peiffer, S.L. and DiTomas, M.E., Two distinct gene subfamilies within the family of cysteine protease gene. Proc. Natl. Acad. Sci. USA, 90 (1993) 3063-3067.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffer, S.L.2    DiTomas, M.E.3
  • 30
    • 0015917607 scopus 로고
    • Zymogens of proteolytic enzymes
    • Kassel, B. and Kay, J., Zymogens of proteolytic enzymes. Science, 180 (1973) 1022-1027.
    • (1973) Science , vol.180 , pp. 1022-1027
    • Kassel, B.1    Kay, J.2
  • 33
    • 0026654988 scopus 로고
    • Proteolysis of the major yolk glycoproteins is regulated by acidification of the yolk platelets in sea urchin embryos
    • Mallya, S.K., Partin, J.S., Validizan, M.C. and Lennarz, W.J., Proteolysis of the major yolk glycoproteins is regulated by acidification of the yolk platelets in sea urchin embryos. J. Cell Biol., 117 (1992) 1211-1221.
    • (1992) J. Cell Biol. , vol.117 , pp. 1211-1221
    • Mallya, S.K.1    Partin, J.S.2    Validizan, M.C.3    Lennarz, W.J.4
  • 34
    • 0142020463 scopus 로고
    • CDNA sequence encoding the 16-kDa proteolipid of chromaffin granules implies gene duplication in the evolution of H-ATPases
    • Mandel, M., Moriyama, Y., Hulmes, J.D., Pan, Y-C.E., Nelson, H. and Nelson, N:, cDNA sequence encoding the 16-kDa proteolipid of chromaffin granules implies gene duplication in the evolution of H-ATPases. Proc. Natl. Acad. Sci. U.S.A., 85 (1988) 5521-5524.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 5521-5524
    • Mandel, M.1    Moriyama, Y.2    Hulmes, J.D.3    Pan, Y.-C.E.4    Nelson, H.5    Nelson, N.6
  • 35
    • 38249023667 scopus 로고
    • Vitellin degradation in developing embryos of the stick insect, Carausius morosus
    • Masetti, M. and Giorgi, F., Vitellin degradation in developing embryos of the stick insect, Carausius morosus. J. Insect Physiol., 35 (1989) 689-697.
    • (1989) J. Insect Physiol. , vol.35 , pp. 689-697
    • Masetti, M.1    Giorgi, F.2
  • 36
    • 0023938526 scopus 로고
    • Drosophila cathepsin B-like proteinase: A suggested role in yolk degradation
    • Medina, M., Leon, P. and Vallejo, C.G., Drosophila cathepsin B-like proteinase: a suggested role in yolk degradation. Arch. Biochem. Biophys., 263 (1988) 355-363.
    • (1988) Arch. Biochem. Biophys. , vol.263 , pp. 355-363
    • Medina, M.1    Leon, P.2    Vallejo, C.G.3
  • 37
  • 38
    • 0022346135 scopus 로고
    • Characterization of toposomes from sea urchin blastula cells: A cell organelle mediating cell adhesion and expressing positional information
    • Noll, H., Matranga, V., Cervello, M., Humphreys, T., Kuwasaki, B. and Adelson, D., Characterization of toposomes from sea urchin blastula cells: A cell organelle mediating cell adhesion and expressing positional information. Proc. Natl. Acad. Sci. U.S.A., 82 (1985) 8062-8066.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 8062-8066
    • Noll, H.1    Matranga, V.2    Cervello, M.3    Humphreys, T.4    Kuwasaki, B.5    Adelson, D.6
  • 39
    • 0022163293 scopus 로고
    • Vitellogenesis in insects
    • W.L. Browder (ed.), Oogenesis, Plenum Press, New York
    • Postlethwait, J.H. and Giorgi, F., Vitellogenesis in insects. In Developmental Biology. A Comprehensive Synthesis, Vol.1, W.L. Browder (ed.), Oogenesis, Plenum Press, New York, 1985, pp. 85-126.
    • (1985) Developmental Biology. A Comprehensive Synthesis , vol.1 , pp. 85-126
    • Postlethwait, J.H.1    Giorgi, F.2
  • 40
    • 84990436167 scopus 로고
    • Correlation of yolk phosphatase expression with the programmed proteolysis of vitellin in Blattella germanica during embryonic development
    • Purcell, J.P., Quinn, T.M., Kunkel, J.G. and Nordin, J.H., Correlation of yolk phosphatase expression with the programmed proteolysis of vitellin in Blattella germanica during embryonic development. Arch. Insect Biochem. Physiol., 9 (1988) 237-251.
    • (1988) Arch. Insect Biochem. Physiol. , vol.9 , pp. 237-251
    • Purcell, J.P.1    Quinn, T.M.2    Kunkel, J.G.3    Nordin, J.H.4
  • 41
    • 0026449642 scopus 로고
    • Accumulation of yolk proteins in insect oocytes
    • Raikhel, A.S. and Dhadialla, T.S., Accumulation of yolk proteins in insect oocytes. Annu. Rev. Entomol., 37 (1992) 217-251.
    • (1992) Annu. Rev. Entomol. , vol.37 , pp. 217-251
    • Raikhel, A.S.1    Dhadialla, T.S.2
  • 42
    • 0000648105 scopus 로고
    • Cathepsin B and acid phosphatase activities during Musca domestica embryogenesis
    • Ribolla, P.E.M., Daffre, S. and De Bianchi, A.G., Cathepsin B and acid phosphatase activities during Musca domestica embryogenesis. Insect Biochem. Molec. Biol., 23 (1993) 217-223.
    • (1993) Insect Biochem. Molec. Biol. , vol.23 , pp. 217-223
    • Ribolla, P.E.M.1    Daffre, S.2    De Bianchi, A.G.3
  • 43
    • 0000865736 scopus 로고
    • Receptor mediated endocytosis of yolk proteins by insect oocytes
    • E. Ohnishi, S.Y. Takahashi and H. Sonobe (eds.), Nagoya University Press, Nagoya, Japan
    • Sappington, T.W. and Raikhel, A.S., Receptor mediated endocytosis of yolk proteins by insect oocytes. In: Recent Advances in Insect Biochemistry and Molecular Biology, E. Ohnishi, S.Y. Takahashi and H. Sonobe (eds.), Nagoya University Press, Nagoya, Japan, 1995, pp. 235-257.
    • (1995) Recent Advances in Insect Biochemistry and Molecular Biology , pp. 235-257
    • Sappington, T.W.1    Raikhel, A.S.2
  • 44
    • 0024513147 scopus 로고
    • Structure of a major glycoprotein and its processing pathway by limited proteolysis are conserved in echinoids
    • Scott, L.B. and Lennarz, W.J., Structure of a major glycoprotein and its processing pathway by limited proteolysis are conserved in echinoids. Dev. Biol., 132 (1989) 91-102.
    • (1989) Dev. Biol. , vol.132 , pp. 91-102
    • Scott, L.B.1    Lennarz, W.J.2
  • 45
    • 0024331466 scopus 로고
    • Activity and deletion analysis of recombinant human cathepsin L expressed in E. coli
    • Smith, S.M. and Gottesman, M.M., Activity and deletion analysis of recombinant human cathepsin L expressed in E. coli. J. Biol. Chem., 264 (1989) 20487-20495.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20487-20495
    • Smith, S.M.1    Gottesman, M.M.2
  • 46
    • 0006604522 scopus 로고
    • Structure and embryonic degradation of two native vitellin in the cockroach, Periplaneta americana
    • Storella, J.R., Wejchowski, D.M. and Kunkel, J.G., Structure and embryonic degradation of two native vitellin in the cockroach, Periplaneta americana. Insect Biochem., 15 (1985) 65-76.
    • (1985) Insect Biochem. , vol.15 , pp. 65-76
    • Storella, J.R.1    Wejchowski, D.M.2    Kunkel, J.G.3
  • 47
    • 0001573128 scopus 로고
    • Acid cysteine proteinase from the eggs of ailkmoth, Bombyx mori: Tissue distribution, developmental changes and the sites of synthesis of the enzyme
    • Takahashi, S.Y., Zhao, X., Kageyama, T. and Yamamoto, Y., Acid cysteine proteinase from the eggs of ailkmoth, Bombyx mori: tissue distribution, developmental changes and the sites of synthesis of the enzyme. Insect Biochem. Molec. Biol., 22 (1992a) 369-377.
    • (1992) Insect Biochem. Molec. Biol. , vol.22 , pp. 369-377
    • Takahashi, S.Y.1    Zhao, X.2    Kageyama, T.3    Yamamoto, Y.4
  • 48
    • 0026702779 scopus 로고
    • Guanosine 3′,5′-monophosphate-dependent protein kinase from the silkmoth, Bombyx mori: Further evidence for the involvement of kinase in the phosphorylation of vitellin and the effect of phosphorylation on the susceptibility of vitellin to a cysteine proteinase in the egg
    • Takahashi, S.Y., Fujiwara, M., Ohoka, T. and Yamamoto, Y., Guanosine 3′,5′-monophosphate-dependent protein kinase from the silkmoth, Bombyx mori: further evidence for the involvement of kinase in the phosphorylation of vitellin and the effect of phosphorylation on the susceptibility of vitellin to a cysteine proteinase in the egg. Comp. Biochem. Physiol., 103B (1992b) 71-79.
    • (1992) Comp. Biochem. Physiol. , vol.103 B , pp. 71-79
    • Takahashi, S.Y.1    Fujiwara, M.2    Ohoka, T.3    Yamamoto, Y.4
  • 49
    • 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., 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 (Tokyo), 114 (1993) 267-272.
    • (1993) J. Biochem (Tokyo) , vol.114 , pp. 267-272
    • Takahashi, S.Y.1    Yamamoto, Y.2    Shionoya, Y.3    Kageyama, T.4
  • 52
    • 0000422371 scopus 로고
    • Major plasma proteins of Bombyx mori
    • Tomino, S., Major plasma proteins of Bombyx mori. Zool. Sci., 2 (1985) 293-303.
    • (1985) Zool. Sci. , vol.2 , pp. 293-303
    • Tomino, S.1
  • 53
    • 0023656232 scopus 로고
    • Sequence and expresssion of the cDNA for MEP (Major excreted protein), a transformation regulated secreted cathepsin
    • Troen, B.R., Gal, S. and Gottesmann, M.M., Sequence and expresssion of the cDNA for MEP (Major excreted protein), a transformation regulated secreted cathepsin. Biochem. J., 246 (1987) 731-735.
    • (1987) Biochem. J. , vol.246 , pp. 731-735
    • Troen, B.R.1    Gal, S.2    Gottesmann, M.M.3
  • 54
    • 0027218436 scopus 로고
    • Cysteine proteinase from Bombyx eggs: Role in programmed degradation of yolk proteins during embryogenesis
    • Yamamoto, Y. and Takahashi, S.Y., Cysteine proteinase from Bombyx eggs: role in programmed degradation of yolk proteins during embryogenesis. Comp. Biochem. Physiol., 106B (1993) 35-45.
    • (1993) Comp. Biochem. Physiol. , vol.106 B , pp. 35-45
    • Yamamoto, Y.1    Takahashi, S.Y.2
  • 55
    • 0028069204 scopus 로고
    • Cysteine proteinase from the silkmoth, Bombyx mori: Site of synthesis and a suggested role in yolk protein degradation
    • Yamamoto, Y., Zhao, X., Suzuki, A.C. and Takahashi, S.Y., Cysteine proteinase from the silkmoth, Bombyx mori: site of synthesis and a suggested role in yolk protein degradation. J. Insect Physiol., 40 (1994a) 447-454.
    • (1994) J. Insect Physiol. , vol.40 , pp. 447-454
    • Yamamoto, Y.1    Zhao, X.2    Suzuki, A.C.3    Takahashi, S.Y.4
  • 56
    • 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., Molecular cloning and sequencing of cDNA that encodes cysteine proteinase in the eggs of the silkmoth, Bombyx mori. J. Biochem. (Tokyo), 116 (1994b) 1330-1335.
    • (1994) J. Biochem. (Tokyo) , 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
  • 57
    • 84985846660 scopus 로고
    • Metabolic fates of yolk proteins during embryogenesis in arthropods
    • Yamashita, O. and Indrasith, L.S., Metabolic fates of yolk proteins during embryogenesis in arthropods. Develop. Growth Differ., 30 (1988) 337-346.
    • (1988) Develop. Growth Differ. , vol.30 , pp. 337-346
    • Yamashita, O.1    Indrasith, L.S.2
  • 58
    • 0028241467 scopus 로고
    • Structure and expression of mRNA for vitellogenin in Bombyx mori
    • Yano, K., Watabe, S., Izumi, S. and Tomino, S., Structure and expression of mRNA for vitellogenin in Bombyx mori. Biochim. Biophys. Acta, 1218 (1994) 1-10.
    • (1994) Biochim. Biophys. Acta , vol.1218 , pp. 1-10
    • Yano, K.1    Watabe, S.2    Izumi, S.3    Tomino, S.4
  • 59
    • 0023880046 scopus 로고
    • Degradation of yolk proteins in sea urchin eggs and embryos
    • Yokota, Y. and Kato, H.K., Degradation of yolk proteins in sea urchin eggs and embryos. Cell Differ., 23 (1988) 191-200.
    • (1988) Cell Differ. , vol.23 , pp. 191-200
    • Yokota, Y.1    Kato, H.K.2
  • 60
    • 0029868842 scopus 로고    scopus 로고
    • Occurrence of a cathepsin B-like acid cysteine proteinase in the eggs of silkworm moth, Antheraea pernyi
    • Zhao, X., Wang, J., Yagi, N., Yamamoto, Y., Watabe, S. and Takahashi, S.Y., Occurrence of a cathepsin B-like acid cysteine proteinase in the eggs of silkworm moth, Antheraea pernyi. Comp. Biochem. Physiol., 113B (1996) 95-103.
    • (1996) Comp. Biochem. Physiol. , vol.113 B , pp. 95-103
    • Zhao, X.1    Wang, J.2    Yagi, N.3    Yamamoto, Y.4    Watabe, S.5    Takahashi, S.Y.6
  • 61
    • 0000433235 scopus 로고
    • Characterization of vitellin, egg-specific protein and 30-kDa proteins from Bombyx eggs, and their fates during oogenesis and embryogenesis
    • Zhu, J., Indrasith, L.S. and Yamashita, O., Characterization of vitellin, egg-specific protein and 30-kDa proteins from Bombyx eggs, and their fates during oogenesis and embryogenesis. Biochim. Biophys. Acta, 882 (1986) 427-436.
    • (1986) Biochim. Biophys. Acta , vol.882 , pp. 427-436
    • Zhu, J.1    Indrasith, L.S.2    Yamashita, O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.