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Volumn 30, Issue 6, 1999, Pages 579-596

Differential vitellin polypeptide processing in insect embryos

Author keywords

Embryo; Insects; Vitellin; Vitellophages; Yolk sac

Indexed keywords


EID: 0032739748     PISSN: 09684328     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-4328(99)00054-2     Document Type: Review
Times cited : (70)

References (167)
  • 1
    • 0002754395 scopus 로고
    • The development of hemimetabolous insects
    • S.J. Counce, Waddington C.H. New York: Academic Press
    • Anderson D.T. The development of hemimetabolous insects. Counce S.J., Waddington C.H. Developmental Systems: Insects. vol. 1:1972;95 Academic Press, New York.
    • (1972) Developmental Systems: Insects , vol.1 , pp. 95
    • Anderson, D.T.1
  • 2
    • 0021831871 scopus 로고
    • Tyrosine sulfation of yolk proteins 1, 2 and 3 in Drosophila melanogaster
    • Bauerle P.A., Huttner W.B. Tyrosine sulfation of yolk proteins 1, 2 and 3 in Drosophila melanogaster. Journal of Biological Chemistry. 260:1985;6434-6439.
    • (1985) Journal of Biological Chemistry , vol.260 , pp. 6434-6439
    • Bauerle, P.A.1    Huttner, W.B.2
  • 3
    • 0020794521 scopus 로고
    • Ecdysteroids in the pycnogonid Pycnogorum litorale (Strom) (Arthropoda: Pantopoda)
    • Behrens W., Bückmann D. Ecdysteroids in the pycnogonid Pycnogorum litorale (Strom) (Arthropoda: Pantopoda). General Comparative Endocrinology. 51:1983;8-14.
    • (1983) General Comparative Endocrinology , vol.51 , pp. 8-14
    • Behrens, W.1    Bückmann, D.2
  • 4
    • 0345717350 scopus 로고
    • Are yolk granules related to lysosomes?
    • Bluemink J.G. Are yolk granules related to lysosomes? Zeiss Information. 73:1969;95-99.
    • (1969) Zeiss Information , vol.73 , pp. 95-99
    • Bluemink, J.G.1
  • 6
    • 0001358480 scopus 로고
    • Expression of the genes coding for vitellogenin (yolk protein)
    • Bownes M. Expression of the genes coding for vitellogenin (yolk protein). Annual Review of Entomology. 31:1986;507-531.
    • (1986) Annual Review of Entomology , vol.31 , pp. 507-531
    • Bownes, M.1
  • 8
    • 0026655197 scopus 로고
    • Why is there sequence similarity between insect yolk proteins and vertebrate lipases?
    • Bownes M. Why is there sequence similarity between insect yolk proteins and vertebrate lipases? Journal of Lipid Research. 33:1992;777-790.
    • (1992) Journal of Lipid Research , vol.33 , pp. 777-790
    • Bownes, M.1
  • 9
    • 0030779830 scopus 로고    scopus 로고
    • Vitellogenin uptake and vitellin localization in insect follicles examined using monoclonal antibodies and confocal scanning microscopy
    • Bradley J.T., Estridge B.H. Vitellogenin uptake and vitellin localization in insect follicles examined using monoclonal antibodies and confocal scanning microscopy. Invertebrate Reproduction and Development. 32:1997;245-257.
    • (1997) Invertebrate Reproduction and Development , vol.32 , pp. 245-257
    • Bradley, J.T.1    Estridge, B.H.2
  • 10
    • 0345717349 scopus 로고    scopus 로고
    • Vitellin processing and protease activity in developing eggs of Acheta domesticus
    • Bradley J.T., Estridge B.H., Handley H.L. Vitellin processing and protease activity in developing eggs of Acheta domesticus. Molecular Biology of the Cell. 8:1997;648.
    • (1997) Molecular Biology of the Cell , vol.8 , pp. 648
    • Bradley, J.T.1    Estridge, B.H.2    Handley, H.L.3
  • 11
    • 0020020426 scopus 로고
    • The follicle cells are a major site of vitellogenin synthesis in Drosophila melanogaster
    • Brennan M.D., Weiner A.J., Goralski T.J., Mahowald A.P. The follicle cells are a major site of vitellogenin synthesis in Drosophila melanogaster. Developmental Biology. 89:1981;225-236.
    • (1981) Developmental Biology , vol.89 , pp. 225-236
    • Brennan, M.D.1    Weiner, A.J.2    Goralski, T.J.3    Mahowald, A.P.4
  • 12
    • 0000503987 scopus 로고
    • Phosphorylation of the vitellogenin polypeptides of Drosophila melanogaster
    • Brennan M.D., Mahowald A.P. Phosphorylation of the vitellogenin polypeptides of Drosophila melanogaster. Insect Biochemistry. 12:1982;669-673.
    • (1982) Insect Biochemistry , vol.12 , pp. 669-673
    • Brennan, M.D.1    Mahowald, A.P.2
  • 13
    • 0031128320 scopus 로고    scopus 로고
    • ER-associated and proteasome-mediated protein degradation: How two topologically restricted events come together
    • Brodsky J.L., McCracken A.A. ER-associated and proteasome-mediated protein degradation: how two topologically restricted events come together. Trends in Cell Biology. 7:1997;151-156.
    • (1997) Trends in Cell Biology , vol.7 , pp. 151-156
    • Brodsky, J.L.1    McCracken, A.A.2
  • 15
    • 0024587474 scopus 로고
    • Evidence of a precursor-product relationship between vitellogenin and toposome, a glycoprotein complex mediating cell adhesion
    • Cervello M., Matraga V. Evidence of a precursor-product relationship between vitellogenin and toposome, a glycoprotein complex mediating cell adhesion. Cell Differentiation and Development. 26:1989;67-76.
    • (1989) Cell Differentiation and Development , vol.26 , pp. 67-76
    • Cervello, M.1    Matraga, V.2
  • 16
    • 0025787870 scopus 로고
    • An extraovarian protein accumulated in mosquito oocytes is a carboxypeptidase activated in embryos
    • Cho W-L., Deitsch K.W., Raikhel A.S. An extraovarian protein accumulated in mosquito oocytes is a carboxypeptidase activated in embryos. Proceedings of National Academy of Science, USA. 88:1991;10 821-10 824.
    • (1991) Proceedings of National Academy of Science, USA , vol.88 , pp. 10821-10824
    • Cho, W.-L.1    Deitsch, K.W.2    Raikhel, A.S.3
  • 17
    • 0000547403 scopus 로고
    • Purification and characterization of a lysosomal aspartic protease with cathepsin D activity from the mosquito
    • Cho W.L., Dhadialla T.S., Raikhel A.S. Purification and characterization of a lysosomal aspartic protease with cathepsin D activity from the mosquito. Insect Biochemistry. 21:1991;165-176.
    • (1991) Insect Biochemistry , vol.21 , pp. 165-176
    • Cho, W.L.1    Dhadialla, T.S.2    Raikhel, A.S.3
  • 18
    • 0026806495 scopus 로고
    • Cloning of cDNA for mosquito lysosomal aspartic protease
    • Cho W.L., Raikhel A.S. Cloning of cDNA for mosquito lysosomal aspartic protease. Journal of Biological Chemistry. 267:1992;21823-21829.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 21823-21829
    • Cho, W.L.1    Raikhel, A.S.2
  • 20
    • 0019332708 scopus 로고
    • Vitellin from the crustacean Artemia salina. Biochemical analysis of lipovitellin complex from the yolk granules
    • de Chaffoy D., Kondo M. Vitellin from the crustacean Artemia salina. Biochemical analysis of lipovitellin complex from the yolk granules. Journal of Biological Chemistry. 255:1980;6727-6733.
    • (1980) Journal of Biological Chemistry , vol.255 , pp. 6727-6733
    • De Chaffoy, D.1    Kondo, M.2
  • 21
    • 0000963379 scopus 로고
    • The vitellogenin of Leucophae maderae. Synthesis as a large phosphorylated precursor
    • della Cioppa G., Engelmann F. The vitellogenin of Leucophae maderae. Synthesis as a large phosphorylated precursor. Insect Biochemistry. 17:1987;401-415.
    • (1987) Insect Biochemistry , vol.17 , pp. 401-415
    • Della Cioppa, G.1    Engelmann, F.2
  • 22
    • 0018800923 scopus 로고
    • Identification and partial purification of an ATP-stimulated alkaline protease in rat liver
    • DeMartino G.N., Goldberg A.L. Identification and partial purification of an ATP-stimulated alkaline protease in rat liver. Journal of Biological Chemistry. 254:1979;3712-3715.
    • (1979) Journal of Biological Chemistry , vol.254 , pp. 3712-3715
    • DeMartino, G.N.1    Goldberg, A.L.2
  • 25
    • 0031127642 scopus 로고    scopus 로고
    • Analysis of the mosquito lysosomal aspartic protease gene: An insect housekeeping gene with fat body-enhanced expression
    • Dittmer N.T., Raikhel A.S. Analysis of the mosquito lysosomal aspartic protease gene: an insect housekeeping gene with fat body-enhanced expression. Insect Biochemistry and Molecular Biology. 27:1997;323-335.
    • (1997) Insect Biochemistry and Molecular Biology , vol.27 , pp. 323-335
    • Dittmer, N.T.1    Raikhel, A.S.2
  • 28
    • 0003099974 scopus 로고
    • Hormones during embryogenesis in the milkweed bug Oncopeltus fasciatus
    • Dorn A. Hormones during embryogenesis in the milkweed bug Oncopeltus fasciatus. Entomolology General. 8:1983;193-214.
    • (1983) Entomolology General , vol.8 , pp. 193-214
    • Dorn, A.1
  • 29
    • 0025232804 scopus 로고
    • The proteasome (multicatalytic protease) is a component of the 1500 kDa proteolytic complex which degrades ubiquitin-conjugated proteins
    • Driscoll J., Goldberg A.L. The proteasome (multicatalytic protease) is a component of the 1500 kDa proteolytic complex which degrades ubiquitin-conjugated proteins. Journal of Biological Chemistry. 265:1990;4789-4792.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 4789-4792
    • Driscoll, J.1    Goldberg, A.L.2
  • 30
    • 0025034997 scopus 로고
    • Hormonal Control of Arthropod Reproduction
    • Wiley, New York
    • Engelmann, F., 1990. Hormonal Control of Arthropod Reproduction. Progress in Comparative Endocrinology. Wiley, New York, pp. 357-364.
    • (1990) Progress in Comparative Endocrinology , pp. 357-364
    • Engelmann, F.1
  • 31
    • 0013426814 scopus 로고
    • The trypsin-like proteinase of Artemia: Yolk localization and developmental activation
    • Ezquieta B., Vallejo C.G. The trypsin-like proteinase of Artemia: yolk localization and developmental activation. Comparative Biochemistry and Physiology. 82B:1985;731-736.
    • (1985) Comparative Biochemistry and Physiology , vol.82 , pp. 731-736
    • Ezquieta, B.1    Vallejo, C.G.2
  • 32
    • 0022806750 scopus 로고
    • Lipovitellin inhibition of Artemia trypsin-like proteinase: A role for storage protein in regulating proteinase activity during development
    • Ezquieta B., Vallejo C.G. Lipovitellin inhibition of Artemia trypsin-like proteinase: a role for storage protein in regulating proteinase activity during development. Archives of Biochemistry and Biophysics. 250:1986;410-417.
    • (1986) Archives of Biochemistry and Biophysics , vol.250 , pp. 410-417
    • Ezquieta, B.1    Vallejo, C.G.2
  • 33
    • 0025527484 scopus 로고
    • Yolk degradation in tick eggs: I. Occurrence of a cathepsin L-like acid proteinase in yolk spheres
    • Fagotto F. Yolk degradation in tick eggs: I. Occurrence of a cathepsin L-like acid proteinase in yolk spheres. Archives of Insect Biochemistry and Physiology. 14:1990a;217-235.
    • (1990) Archives of Insect Biochemistry and Physiology , vol.14 , pp. 217-235
    • Fagotto, F.1
  • 34
    • 0025529201 scopus 로고
    • Yolk degradation in tick eggs: II. Evidence that cathepsin L-like proteinase is stored as a latent, acid-activable pro-enzyme
    • Fagotto F. Yolk degradation in tick eggs: II. Evidence that cathepsin L-like proteinase is stored as a latent, acid-activable pro-enzyme. Archives of Insect Biochemistry and Physiology. 14:1990b;237-252.
    • (1990) Archives of Insect Biochemistry and Physiology , vol.14 , pp. 237-252
    • Fagotto, F.1
  • 35
    • 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. Development Growth and Differentiation. 33:1991;57-66.
    • (1991) Development Growth and Differentiation , vol.33 , pp. 57-66
    • Fagotto, F.1
  • 36
    • 0028284661 scopus 로고
    • Yolk platelets in Xenopus oocytes maintain an acidic internal pH which may be essential for sodium accumulation
    • Fagotto F., Maxfield F.R. Yolk platelets in Xenopus oocytes maintain an acidic internal pH which may be essential for sodium accumulation. Journal of Cell Biology. 125:1994a;1047-1056.
    • (1994) Journal of Cell Biology , vol.125 , pp. 1047-1056
    • Fagotto, F.1    Maxfield, F.R.2
  • 37
    • 0028587431 scopus 로고
    • Changes in yolk platelets pH during Xenopus laevis development correlate with yolk utilization. A quantitative confocal microscopy study
    • Fagotto F., Maxfield F.R. Changes in yolk platelets pH during Xenopus laevis development correlate with yolk utilization. A quantitative confocal microscopy study. Journal of Cell Science. 107:1994b;3325-3337.
    • (1994) Journal of Cell Science , vol.107 , pp. 3325-3337
    • Fagotto, F.1    Maxfield, F.R.2
  • 38
    • 0029583839 scopus 로고
    • Regulation of yolk degradation, or how to make sleepy lysosomes
    • Fagotto F. Regulation of yolk degradation, or how to make sleepy lysosomes. Journal of Cell Science. 108:1995;3645-3647.
    • (1995) Journal of Cell Science , vol.108 , pp. 3645-3647
    • Fagotto, F.1
  • 39
    • 0028286771 scopus 로고
    • An ultrastructural investigation on vitellophage invasion of the yolk mass during and after germ band formation in embryos of the stick insect Carausius morosus Br
    • Fausto A.M., Carcupino M., Mazzini M., Giorgi F. An ultrastructural investigation on vitellophage invasion of the yolk mass during and after germ band formation in embryos of the stick insect Carausius morosus Br. Development Growth and Differentiation. 36:1994;197-207.
    • (1994) Development Growth and Differentiation , vol.36 , pp. 197-207
    • Fausto, A.M.1    Carcupino, M.2    Mazzini, M.3    Giorgi, F.4
  • 40
    • 0030970360 scopus 로고    scopus 로고
    • The yolk sac in late embryonic development of the stick insect Carausius morosus (Br.)
    • Fausto A.M., Mazzini M., Cecchettini A., Giorgi F. The yolk sac in late embryonic development of the stick insect Carausius morosus (Br.). Tissue and Cell. 29:1997;257-266.
    • (1997) Tissue and Cell , vol.29 , pp. 257-266
    • Fausto, A.M.1    Mazzini, M.2    Cecchettini, A.3    Giorgi, F.4
  • 42
    • 0000922544 scopus 로고
    • Yolk protein accumulation in Locusta migratoria (R&F) (Orthoptera: Acrididae) oocytes
    • Ferenz H-J. Yolk protein accumulation in Locusta migratoria (R&F) (Orthoptera: Acrididae) oocytes. International Journal of Insect Morphology and Embryology. 22:1993;295-314.
    • (1993) International Journal of Insect Morphology and Embryology , vol.22 , pp. 295-314
    • Ferenz, H.-J.1
  • 43
    • 0019018002 scopus 로고
    • The unmasking of proteolytic activity during the early development of Artemia salina. Identification of a precursor after hatching
    • Garesse R., Perona R., Marco R., Vallejo C.G. The unmasking of proteolytic activity during the early development of Artemia salina. Identification of a precursor after hatching. European Journal of Biochemistry. 106:1980;225-231.
    • (1980) European Journal of Biochemistry , vol.106 , pp. 225-231
    • Garesse, R.1    Perona, R.2    Marco, R.3    Vallejo, C.G.4
  • 45
    • 0017366102 scopus 로고
    • Recent findings on oogenesis of Drosophila melanogaster. II. Further evidence on the origin of yolk platelets
    • Giorgi F., Jacob J. Recent findings on oogenesis of Drosophila melanogaster. II. Further evidence on the origin of yolk platelets. Journal of Embryology Experimental Morphology. 38:1977;125-138.
    • (1977) Journal of Embryology Experimental Morphology , vol.38 , pp. 125-138
    • Giorgi, F.1    Jacob, J.2
  • 46
    • 0007407022 scopus 로고
    • Coated vesicles in the oocyte
    • C.D. Ockleford, & H. Whyte. Cambridge: Cambridge University Press
    • Giorgi F. Coated vesicles in the oocyte. Ockleford C.D., Whyte H. Coated Vesicles. 1980;135 Cambridge University Press, Cambridge.
    • (1980) Coated Vesicles , pp. 135
    • Giorgi, F.1
  • 47
    • 0019247006 scopus 로고
    • Vitellogenesis in the stick insect Carausius morosus. I. Specific protein synthesis during ovarian development
    • Giorgi F., Macchi F. Vitellogenesis in the stick insect Carausius morosus. I. Specific protein synthesis during ovarian development. Journal of Cell Science. 46:1980;1-16.
    • (1980) Journal of Cell Science , vol.46 , pp. 1-16
    • Giorgi, F.1    Macchi, F.2
  • 48
    • 0008487858 scopus 로고
    • Vitellogenesis in the stick insect Carausius morosus. II. Purification and biochemical characterization of two vitellins from eggs
    • Giorgi F., Baldini G., Simonini A.L., Mengheri M. Vitellogenesis in the stick insect Carausius morosus. II. Purification and biochemical characterization of two vitellins from eggs. Insect Biochemistry. 12:1982;553-562.
    • (1982) Insect Biochemistry , vol.12 , pp. 553-562
    • Giorgi, F.1    Baldini, G.2    Simonini, A.L.3    Mengheri, M.4
  • 49
    • 38249044039 scopus 로고
    • In vivo uptake of haemolymph from a female sterile mutant into wild type ovaries of Drosophila melanogaster
    • Giorgi F., Andolfi P., Spinetti I., Masetti M., Postlethwait J.H. In vivo uptake of haemolymph from a female sterile mutant into wild type ovaries of Drosophila melanogaster. Journal of Insect Physiology. 32:1986;59-69.
    • (1986) Journal of Insect Physiology , vol.32 , pp. 59-69
    • Giorgi, F.1    Andolfi, P.2    Spinetti, I.3    Masetti, M.4    Postlethwait, J.H.5
  • 50
    • 35548981455 scopus 로고
    • An autoradiographic analysis of vitellogenin synthesis and secretion in the fat body of the stick insect Bacillus rossius
    • Giorgi F., Bradley J.T., Vignali R., Mazzini M. An autoradiographic analysis of vitellogenin synthesis and secretion in the fat body of the stick insect Bacillus rossius. Tissue and Cell. 21:1989;543-558.
    • (1989) Tissue and Cell , vol.21 , pp. 543-558
    • Giorgi, F.1    Bradley, J.T.2    Vignali, R.3    Mazzini, M.4
  • 51
    • 0025190692 scopus 로고
    • Changes in the patterns of proteins stored and synthesized by developing embryos of the stick insect Carausius morosus (Br.)
    • Giorgi F., Cecchettini A., Masetti M. Changes in the patterns of proteins stored and synthesized by developing embryos of the stick insect Carausius morosus (Br.). Comparative Biochemistry and Physiology. 95B:1990;107-113.
    • (1990) Comparative Biochemistry and Physiology , vol.95 , pp. 107-113
    • Giorgi, F.1    Cecchettini, A.2    Masetti, M.3
  • 52
    • 38249003512 scopus 로고
    • Oocyte growth, follicle cell differentiation and vitellin processing in the stick insect, Carausius morosus Br. (Phasmatodea)
    • Giorgi F., Cecchettini A., Lucchesi P., Mazzini M. Oocyte growth, follicle cell differentiation and vitellin processing in the stick insect, Carausius morosus Br. (Phasmatodea). International Journal of Insect Morphology and Embryology. 22:1993a;271-293.
    • (1993) International Journal of Insect Morphology and Embryology , vol.22 , pp. 271-293
    • Giorgi, F.1    Cecchettini, A.2    Lucchesi, P.3    Mazzini, M.4
  • 54
    • 0027533625 scopus 로고
    • Ultrastructural analysis of Drosophila ovarian follicles differing in yolk polypeptide (Yps) composition
    • Giorgi F., Lucchesi P., Morelli A., Bownes M. Ultrastructural analysis of Drosophila ovarian follicles differing in yolk polypeptide (Yps) composition. Development. 117:1993c;319-328.
    • (1993) Development , vol.117 , pp. 319-328
    • Giorgi, F.1    Lucchesi, P.2    Morelli, A.3    Bownes, M.4
  • 55
    • 0028254311 scopus 로고
    • Structure of yolk granules in oocytes and eggs of Blattella germanica and their interaction with vitellophages and endosymbiotic bacteria during granule degradation
    • Giorgi F., Nordin J.H. Structure of yolk granules in oocytes and eggs of Blattella germanica and their interaction with vitellophages and endosymbiotic bacteria during granule degradation. Journal of Insect Physiology. 40:1994;1077-1092.
    • (1994) Journal of Insect Physiology , vol.40 , pp. 1077-1092
    • Giorgi, F.1    Nordin, J.H.2
  • 57
    • 0031007042 scopus 로고    scopus 로고
    • The vitellin-processing protease of Blattella germanica is derived from a pro-protease of maternal origin
    • Giorgi F., Yin L., Cecchettini A., Nordin J.H. The vitellin-processing protease of Blattella germanica is derived from a pro-protease of maternal origin. Tissue and Cell. 29:1997b;293-303.
    • (1997) Tissue and Cell , vol.29 , pp. 293-303
    • Giorgi, F.1    Yin, L.2    Cecchettini, A.3    Nordin, J.H.4
  • 58
    • 0032462021 scopus 로고    scopus 로고
    • Vitellogenin is glycosylated in the fat body of the stick insect Carausius morosus and not further modified upon transfer to the ovarian follicle
    • Giorgi F., Cecchettini A., Falleni A., Masetti M., Gremigni V. Vitellogenin is glycosylated in the fat body of the stick insect Carausius morosus and not further modified upon transfer to the ovarian follicle. Micron. 29:1998;451-460.
    • (1998) Micron , vol.29 , pp. 451-460
    • Giorgi, F.1    Cecchettini, A.2    Falleni, A.3    Masetti, M.4    Gremigni, V.5
  • 59
    • 0026090166 scopus 로고
    • Storage, ultrastructural targeting and functions of toposomes and hyalin in sea urchin embryogenesis
    • Gratwohl E.K.M., Kellenberger L., Noll H. Storage, ultrastructural targeting and functions of toposomes and hyalin in sea urchin embryogenesis. Mechanisms of Development. 33:1991;127-138.
    • (1991) Mechanisms of Development , vol.33 , pp. 127-138
    • Gratwohl, E.K.M.1    Kellenberger, L.2    Noll, H.3
  • 60
    • 0025137462 scopus 로고
    • Asymmetrically distributed ecdysteroid-related antigens in follicles and young embryos of Drosophila melanogaster
    • Grau V., Gutzeit H.O. Asymmetrically distributed ecdysteroid-related antigens in follicles and young embryos of Drosophila melanogaster. Roux's Archives for Developmental Biology. 198:1990;295-302.
    • (1990) Roux's Archives for Developmental Biology , vol.198 , pp. 295-302
    • Grau, V.1    Gutzeit, H.O.2
  • 64
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller M.M., Finger A., Schweiger M., Wolf D.H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science. 273:1996;1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 66
    • 0345717341 scopus 로고    scopus 로고
    • Anti-ecdysone and anti-von Willebrand factor reactivity with insect vitellogenin and vitellin
    • Hitt A.M., Bradley J.T. Anti-ecdysone and anti-von Willebrand factor reactivity with insect vitellogenin and vitellin. Journal of Alabama Academy of Science. 67:1996;63.
    • (1996) Journal of Alabama Academy of Science , vol.67 , pp. 63
    • Hitt, A.M.1    Bradley, J.T.2
  • 67
    • 0345285703 scopus 로고    scopus 로고
    • Vitellin proteolysis and its relationship to ecdysteroid levels during insect embryogenesis
    • Hitt A.M., Bradley J.T. Vitellin proteolysis and its relationship to ecdysteroid levels during insect embryogenesis. Journal of Alabama Academy of Science. 68:1997;126.
    • (1997) Journal of Alabama Academy of Science , vol.68 , pp. 126
    • Hitt, A.M.1    Bradley, J.T.2
  • 69
    • 0000147161 scopus 로고
    • Purification and characterization of protease responsible for vitellin degradation of the silkworm Bombyx mori
    • Ikeda M., Sasaki T., Yamashita O. Purification and characterization of protease responsible for vitellin degradation of the silkworm Bombyx mori. Insect Biochemistry. 20:1990;725-734.
    • (1990) Insect Biochemistry , vol.20 , pp. 725-734
    • Ikeda, M.1    Sasaki, T.2    Yamashita, O.3
  • 70
    • 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., Yamashita O. cDNA cloning, sequencing and temporal expression of the protease responsible for vitellin degradation in the silkworm, Bombyx mori. Comparative Biochemistry and Physiology. 99B:1991;405-411.
    • (1991) Comparative Biochemistry and Physiology , vol.99 , pp. 405-411
    • Ikeda, M.1    Yaginuma, T.2    Kobayashi, M.3    Yamashita, O.4
  • 71
    • 0001357782 scopus 로고
    • Limited degradation of vitellin and egg-specific protein in Bombyx eggs during embryogenesis
    • Indrasith L.S., Furusawa T., Shikata M., Yamashita O. Limited degradation of vitellin and egg-specific protein in Bombyx eggs during embryogenesis. Insect Biochemistry. 17:1987;539-545.
    • (1987) Insect Biochemistry , vol.17 , pp. 539-545
    • Indrasith, L.S.1    Furusawa, T.2    Shikata, M.3    Yamashita, O.4
  • 72
    • 0023870058 scopus 로고
    • A unique protease responsible for selective degradation of a yolk protein in Bombyx mori
    • Indrasith L.S., Sasaki T., Yamashita O. A unique protease responsible for selective degradation of a yolk protein in Bombyx mori. Journal Biological Chemistry. 263:1988;1045-1051.
    • (1988) Journal Biological Chemistry , vol.263 , pp. 1045-1051
    • Indrasith, L.S.1    Sasaki, T.2    Yamashita, O.3
  • 73
    • 0025525355 scopus 로고
    • Solubilization, identification and localization of vitellogenin-binding sites in follicles of the cockroach Nauphoeta cinerea
    • Indrasith L.S., Kindle H., Lanzrein B. Solubilization, identification and localization of vitellogenin-binding sites in follicles of the cockroach Nauphoeta cinerea. Archives of Insect Biochemistry and Physiology. 15:1990;213-228.
    • (1990) Archives of Insect Biochemistry and Physiology , vol.15 , pp. 213-228
    • Indrasith, L.S.1    Kindle, H.2    Lanzrein, B.3
  • 74
    • 0002064019 scopus 로고
    • Egg-specific protein in the silkworm Bombyx mori: Purification, properties, localization and titre changes during oogenesis and embryogenesis
    • Irie K., Yamashita O. Egg-specific protein in the silkworm Bombyx mori: purification, properties, localization and titre changes during oogenesis and embryogenesis. Insect Biochemistry. 13:1983;71-80.
    • (1983) Insect Biochemistry , vol.13 , pp. 71-80
    • Irie, K.1    Yamashita, O.2
  • 76
    • 0025059406 scopus 로고
    • Purification and characterization of a cysteine proteinase from silkworm eggs
    • Kageyama T., Takahashi Y. Purification and characterization of a cysteine proteinase from silkworm eggs. European Journal of Biochemistry. 193:1990;203-210.
    • (1990) European Journal of Biochemistry , vol.193 , pp. 203-210
    • Kageyama, T.1    Takahashi, Y.2
  • 77
    • 0023050010 scopus 로고
    • Physical and chemical properties of microvitellogenin. A protein from the egg of the tobacco hornmoth, Manduca sexta
    • Kawooya J.K., Osir E.O., Law J.H. Physical and chemical properties of microvitellogenin. A protein from the egg of the tobacco hornmoth, Manduca sexta. Journal of Biological Chemistry. 261:1986;10 844-10 849.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 10844-10849
    • Kawooya, J.K.1    Osir, E.O.2    Law, J.H.3
  • 78
    • 0001891521 scopus 로고
    • Chemistry of lysosomal proteases
    • H. Glaumann, & H. Ballard. New York: Academic Press
    • Kirschke H., Barrett A.J. Chemistry of lysosomal proteases. Glaumann H., Ballard H. Lysosomes: Their Role in Protein Breakdown. 1987;222 Academic Press, New York.
    • (1987) Lysosomes: Their Role in Protein Breakdown , pp. 222
    • Kirschke, H.1    Barrett, A.J.2
  • 79
    • 84990469611 scopus 로고
    • Vitellogenin in the cockroach Nauphoeta cinerea: Separation of two classes of ovarian binding sites and calcium effects on binding and uptake
    • König R., Kindle H., Kunkel J.G., Lanzrein B. Vitellogenin in the cockroach Nauphoeta cinerea: separation of two classes of ovarian binding sites and calcium effects on binding and uptake. Archives of Insect Biochemistry and Physiology. 9:1988;323-337.
    • (1988) Archives of Insect Biochemistry and Physiology , vol.9 , pp. 323-337
    • König, R.1    Kindle, H.2    Kunkel, J.G.3    Lanzrein, B.4
  • 80
    • 0001993351 scopus 로고    scopus 로고
    • Ubiquitination of integral membrane proteins and proteins in the secretory pathway
    • J.-M. Peters, J.R. Harris, & D. Finley. New York: Plenum Press
    • Kopito R.R. Ubiquitination of integral membrane proteins and proteins in the secretory pathway. Peters J.-M., Harris J.R., Finley D. Ubiquitin and the Biology of the Cell. 1998;389 Plenum Press, New York.
    • (1998) Ubiquitin and the Biology of the Cell , pp. 389
    • Kopito, R.R.1
  • 81
    • 0004921022 scopus 로고
    • Purification and properties of protease inhibitors from developing embryos of Hemileuca oliviae
    • Kucera M., Turner R.B. Purification and properties of protease inhibitors from developing embryos of Hemileuca oliviae. Biochimica Biophysica Acta. 611:1981;379-383.
    • (1981) Biochimica Biophysica Acta , vol.611 , pp. 379-383
    • Kucera, M.1    Turner, R.B.2
  • 83
    • 0013363457 scopus 로고
    • Cathepsin-type proteolytic activity in the developing eggs of the African migratory locust (Locusta migratoria migratorioides R&F)
    • Kuk-Meiri S., Lichtenstein N., Shulov A., Pener M.P. Cathepsin-type proteolytic activity in the developing eggs of the African migratory locust (Locusta migratoria migratorioides R&F). Comparative Biochemistry and Physiology. 18:1966;783-795.
    • (1966) Comparative Biochemistry and Physiology , vol.18 , pp. 783-795
    • Kuk-Meiri, S.1    Lichtenstein, N.2    Shulov, A.3    Pener, M.P.4
  • 86
    • 0000747086 scopus 로고
    • Ecdysone titre and metabolism in relation to cuticulogenesis in embryos of Locusta migratoria
    • Lagueux M., Hetru C., Goltzene F., Kappler C., Hoffmann J.A. Ecdysone titre and metabolism in relation to cuticulogenesis in embryos of Locusta migratoria. Journal of Insect Physiology. 25:1979;709-723.
    • (1979) Journal of Insect Physiology , vol.25 , pp. 709-723
    • Lagueux, M.1    Hetru, C.2    Goltzene, F.3    Kappler, C.4    Hoffmann, J.A.5
  • 89
    • 0023192604 scopus 로고
    • Involvement of ecdysone in the control of meiotic reinitiation in oocytes of Locusta migratoria (Insecta: Orthoptera)
    • Lanot R., Thiebold J., Goltzene F., Hoffman J.A. Involvement of ecdysone in the control of meiotic reinitiation in oocytes of Locusta migratoria (Insecta: orthoptera). Developmental Biology. 121:1988;174-181.
    • (1988) Developmental Biology , vol.121 , pp. 174-181
    • Lanot, R.1    Thiebold, J.2    Goltzene, F.3    Hoffman, J.A.4
  • 91
    • 38249042703 scopus 로고
    • Ubiquitin in the blowfly Calliphora vicina. Partial characterization, titers during the life cycle and relation to calliphorin breakdown
    • Levenbook L., Bauer A.C., Chou J.Y. Ubiquitin in the blowfly Calliphora vicina. Partial characterization, titers during the life cycle and relation to calliphorin breakdown. Insect Biochemistry. 16:1986;509-515.
    • (1986) Insect Biochemistry , vol.16 , pp. 509-515
    • Levenbook, L.1    Bauer, A.C.2    Chou, J.Y.3
  • 92
    • 0345285700 scopus 로고
    • Proteolytic enzymes of insects. II. Proteases of the eggs of the Moroccan locust (Dociostaurus maroccanus Thnbg.)
    • Lichthenstein N., Bodenheimer F.S., Shulov A. Proteolytic enzymes of insects. II. Proteases of the eggs of the Moroccan locust (Dociostaurus maroccanus Thnbg.). Enzymologia. 13:1949;276-280.
    • (1949) Enzymologia , vol.13 , pp. 276-280
    • Lichthenstein, N.1    Bodenheimer, F.S.2    Shulov, A.3
  • 94
    • 0031605181 scopus 로고    scopus 로고
    • Localization of the proenzyme form of the vitellin-processing protease in Blattella germanica by affinity-purified antibodies
    • Liu X.D., Nordin J.H. Localization of the proenzyme form of the vitellin-processing protease in Blattella germanica by affinity-purified antibodies. Archives of Insect Biochemistry and Physiology. 38:1998;109-118.
    • (1998) Archives of Insect Biochemistry and Physiology , vol.38 , pp. 109-118
    • Liu, X.D.1    Nordin, J.H.2
  • 95
    • 0018770618 scopus 로고
    • Membrane production and yolk degradation in the early fly embryo (Calliphora erythrocephala Meig.): An ultrastructural analsyis
    • Lundquist A., Emanuelsson H. Membrane production and yolk degradation in the early fly embryo (Calliphora erythrocephala Meig.): an ultrastructural analsyis. Journal of Morphogy. 161:1979;53-78.
    • (1979) Journal of Morphogy , vol.161 , pp. 53-78
    • Lundquist, A.1    Emanuelsson, H.2
  • 97
    • 0031200975 scopus 로고    scopus 로고
    • Purification and characterization of a protease degrading 30 kDa yolk proteins of the silkworm Bombyx mori
    • Maki N., Yamashita O. Purification and characterization of a protease degrading 30 kDa yolk proteins of the silkworm Bombyx mori. Insect Biochemistry and Molecular Biology. 27:1997;721-728.
    • (1997) Insect Biochemistry and Molecular Biology , vol.27 , pp. 721-728
    • Maki, N.1    Yamashita, O.2
  • 98
    • 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., Valdizan M.C., Lennarz W.J. Proteolysis of the major yolk glycoproteins is regulated by acidification of the yolk platelets in sea urchin embryos. Journal of Cell Biology. 117:1992;1211-1221.
    • (1992) Journal of Cell Biology , vol.117 , pp. 1211-1221
    • Mallya, S.K.1    Partin, J.S.2    Valdizan, M.C.3    Lennarz, W.J.4
  • 99
    • 0342718553 scopus 로고    scopus 로고
    • Production and extraovarian processing of vitellogenin in ovariectomized Blattella germanica (L) (Dictyoptera: Blattellidae)
    • Martin D., Piulachs M.D., Belles X. Production and extraovarian processing of vitellogenin in ovariectomized Blattella germanica (L) (Dictyoptera: Blattellidae). Journal of Insect Physiology. 42:1996;101-105.
    • (1996) Journal of Insect Physiology , vol.42 , pp. 101-105
    • Martin, D.1    Piulachs, M.D.2    Belles, X.3
  • 100
    • 38249023667 scopus 로고
    • Vitellin degradation in developing embryos of the stick insect Carausius morosus
    • Masetti M., Giorgi F. Vitellin degradation in developing embryos of the stick insect Carausius morosus. Journal of Insect Physiology. 35:1989;689-697.
    • (1989) Journal of Insect Physiology , vol.35 , pp. 689-697
    • Masetti, M.1    Giorgi, F.2
  • 101
    • 0032428775 scopus 로고    scopus 로고
    • Mono- And polyclonal antibodies as probes to study vitellin processing in embryos of the stick insect Carausius morosus
    • Masetti M., Cecchettini A., Giorgi F. Mono- and polyclonal antibodies as probes to study vitellin processing in embryos of the stick insect Carausius morosus. Comparative Biochemistry and Physiology. 120B:1998;625-631.
    • (1998) Comparative Biochemistry and Physiology , vol.120 , pp. 625-631
    • Masetti, M.1    Cecchettini, A.2    Giorgi, F.3
  • 102
    • 0344854375 scopus 로고
    • The secretory pathway of vitellogenin in the fat body of the stick insect Bacillus rossius: An ultrastructural and immunocytochemical study
    • Mazzini M., Burrini A., Giorgi F. The secretory pathway of vitellogenin in the fat body of the stick insect Bacillus rossius: an ultrastructural and immunocytochemical study. Tissue and Cell. 21:1989;609-624.
    • (1989) Tissue and Cell , vol.21 , pp. 609-624
    • Mazzini, M.1    Burrini, A.2    Giorgi, F.3
  • 103
    • 0017346299 scopus 로고
    • Amino acid composition, degradation and utilization of locust vitellogenin during embryogenesis
    • McGregor D.A., Loughton B.G. Amino acid composition, degradation and utilization of locust vitellogenin during embryogenesis. Wilhelm Roux's Archives. 181:1977;113-122.
    • (1977) Wilhelm Roux's Archives , vol.181 , pp. 113-122
    • McGregor, D.A.1    Loughton, B.G.2
  • 104
    • 0003918492 scopus 로고
    • A serine proteinase in Drosophila embryos: Yolk degradation and developmental activation
    • Medina M., Vallejo C.G. A serine proteinase in Drosophila embryos: yolk degradation and developmental activation. Insect Biochemistry. 19:1989;687-691.
    • (1989) Insect Biochemistry , vol.19 , pp. 687-691
    • Medina, M.1    Vallejo, C.G.2
  • 105
    • 0023938526 scopus 로고
    • Drosophila cathepsin B-like proteinase: A suggested role in yolk degradation
    • Medina M., Leon P., Vallejo C.G. Drosophila cathepsin B-like proteinase: a suggested role in yolk degradation. Archives of Biochemistry and Biophysics. 263:1988;355-363.
    • (1988) Archives of Biochemistry and Biophysics , vol.263 , pp. 355-363
    • Medina, M.1    Leon, P.2    Vallejo, C.G.3
  • 106
    • 84987589290 scopus 로고
    • Yolk proteins in developing follicle of the house cricket Acheta domesticus (L.)
    • Nicolaro M.L., Bradley J.T. Yolk proteins in developing follicle of the house cricket Acheta domesticus (L.). Journal of Experimental Zoology. 212:1980;225-232.
    • (1980) Journal of Experimental Zoology , vol.212 , pp. 225-232
    • Nicolaro, M.L.1    Bradley, J.T.2
  • 108
    • 84990469668 scopus 로고
    • Acidification of yolk granules in Blattella germanica eggs coincides with proteolytic processing of vitellin
    • Nordin J.H., Beaudoin E.L., Liu X.D. Acidification of yolk granules in Blattella germanica eggs coincides with proteolytic processing of vitellin. Archives of Insect Biochemistry and Physiology. 18:1991;177-192.
    • (1991) Archives of Insect Biochemistry and Physiology , vol.18 , pp. 177-192
    • Nordin, J.H.1    Beaudoin, E.L.2    Liu, X.D.3
  • 110
    • 0017389329 scopus 로고
    • Biosynthesis of ecdysone in isolated abdomens of the silkworm Bombyx mori
    • Ohnishi E., Chatani F. Biosynthesis of ecdysone in isolated abdomens of the silkworm Bombyx mori. Development Growth and Differentiation. 19:1977;67-70.
    • (1977) Development Growth and Differentiation , vol.19 , pp. 67-70
    • Ohnishi, E.1    Chatani, F.2
  • 111
    • 0019186898 scopus 로고
    • Differential post-endocytotic compartmentation in Xenopus oocytes is mediated by a specifically bound ligand
    • Opresko L., Wiley H.S., Wallace R.A. Differential post-endocytotic compartmentation in Xenopus oocytes is mediated by a specifically bound ligand. Cell. 22:1980;47-57.
    • (1980) Cell , vol.22 , pp. 47-57
    • Opresko, L.1    Wiley, H.S.2    Wallace, R.A.3
  • 112
    • 38249041579 scopus 로고
    • Studies on the carbohydrate moiety of vitellogenin from the tobacco hornworm Manduca sexta
    • Osir E.O., Anderson D.R., Grimes W.J., Law J.H. Studies on the carbohydrate moiety of vitellogenin from the tobacco hornworm Manduca sexta. Insect Biochemistry. 16:1986;471-478.
    • (1986) Insect Biochemistry , vol.16 , pp. 471-478
    • Osir, E.O.1    Anderson, D.R.2    Grimes, W.J.3    Law, J.H.4
  • 113
    • 0000526993 scopus 로고
    • Vitellogenic blood protein synthesis by insect fat body
    • Pan M.L., Bell W.J., Telfer W.H. Vitellogenic blood protein synthesis by insect fat body. Science. 165:1969;393-394.
    • (1969) Science , vol.165 , pp. 393-394
    • Pan, M.L.1    Bell, W.J.2    Telfer, W.H.3
  • 114
    • 0020485737 scopus 로고
    • The lysosomal proteinase of Artemia. Purification and characterization
    • Perona R., Vallejo C.G. The lysosomal proteinase of Artemia. Purification and characterization. European Journal of Biochemistry. 124:1982;357-362.
    • (1982) European Journal of Biochemistry , vol.124 , pp. 357-362
    • Perona, R.1    Vallejo, C.G.2
  • 116
    • 0001195162 scopus 로고
    • Origin and development of the vitellophages during embryogenesis of the migratory locust Locusta migratoria L. (Orthoptera: Acrididae)
    • Petavy G. Origin and development of the vitellophages during embryogenesis of the migratory locust Locusta migratoria L. (Orthoptera: Acrididae). International Journal of Insect Morphology and Embryology. 14:1985;361-379.
    • (1985) International Journal of Insect Morphology and Embryology , vol.14 , pp. 361-379
    • Petavy, G.1
  • 117
    • 0001227887 scopus 로고
    • Contribution of the vitellophages to yolk digestion and cytophagocytosis during embryogenesis of the migratory locust Locusta migratoria L. (Orthoptera: Acrididae)
    • Petavy G. Contribution of the vitellophages to yolk digestion and cytophagocytosis during embryogenesis of the migratory locust Locusta migratoria L. (Orthoptera: Acrididae). International Journal of Insect Morphology and Embryology. 15:1986;343-361.
    • (1986) International Journal of Insect Morphology and Embryology , vol.15 , pp. 343-361
    • Petavy, G.1
  • 119
    • 84990442708 scopus 로고
    • Yolk hydrolase activities associated with polypeptide and oligosaccharide processing of Blattella germanica vitellin
    • Purcell J.P., Kunkel J.G., Nordin J.H. Yolk hydrolase activities associated with polypeptide and oligosaccharide processing of Blattella germanica vitellin. Archives of Insect Biochemistry and Physiology. 8:1988;39-58.
    • (1988) Archives of Insect Biochemistry and Physiology , vol.8 , pp. 39-58
    • Purcell, J.P.1    Kunkel, J.G.2    Nordin, J.H.3
  • 120
    • 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.K., Nordin J.H. Correlation of yolk phosphatase expression with the programmed proteolysis of vitellin in Blattella germanica during embryonic development. Archives of Insect Biochemistry and Physiology. 8:1988;237-251.
    • (1988) Archives of Insect Biochemistry and Physiology , vol.8 , pp. 237-251
    • Purcell, J.P.1    Quinn, T.M.2    Kunkel, J.K.3    Nordin, J.H.4
  • 121
    • 0029788023 scopus 로고    scopus 로고
    • Degradation of a mutant secretory protein α1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
    • Qu D., Teckman J.H., Omura S., Perlmutter D.H. Degradation of a mutant secretory protein α1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. Journal of Biological Chemistry. 271:1996;22 791-22 795.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 22791-22795
    • Qu, D.1    Teckman, J.H.2    Omura, S.3    Perlmutter, D.H.4
  • 122
    • 0021739236 scopus 로고
    • The accumulative pathway of vitellogenin in the mosquito oocytes; A high resolution immuno and cytochemical study
    • Raikhel A.S. The accumulative pathway of vitellogenin in the mosquito oocytes; a high resolution immuno and cytochemical study. Journal of Ultrastructural Research. 87:1984;285-302.
    • (1984) Journal of Ultrastructural Research , vol.87 , pp. 285-302
    • Raikhel, A.S.1
  • 123
    • 0022482666 scopus 로고
    • The specific ligand, vitellogenin, directs internalized proteins into accumulative compartments of mosquito oocytes
    • Raikhel A.S., Lea A.O. The specific ligand, vitellogenin, directs internalized proteins into accumulative compartments of mosquito oocytes. Tissue and Cell. 18:1986;559-574.
    • (1986) Tissue and Cell , vol.18 , pp. 559-574
    • Raikhel, A.S.1    Lea, A.O.2
  • 124
    • 0023072512 scopus 로고
    • Monoclonal antibodies as probes for processing of yolk protein: A high resolution immunolocalization of secretory and accumulative pathways
    • Raikhel A.S. Monoclonal antibodies as probes for processing of yolk protein: a high resolution immunolocalization of secretory and accumulative pathways. Tissue and Cell. 19:1987;515-529.
    • (1987) Tissue and Cell , vol.19 , pp. 515-529
    • Raikhel, A.S.1
  • 131
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A.L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 78:1994;761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 134
    • 0029328486 scopus 로고
    • Mosquito vitellogenin receptor: Purification, developmental and biochemical characterization
    • Sappington T.W., Hays A.R., Raikhel A.S. Mosquito vitellogenin receptor: purification, developmental and biochemical characterization. Insect Biochemistry and Molecular Biology. 25:1995;807-817.
    • (1995) Insect Biochemistry and Molecular Biology , vol.25 , pp. 807-817
    • Sappington, T.W.1    Hays, A.R.2    Raikhel, A.S.3
  • 135
    • 0029808992 scopus 로고    scopus 로고
    • Molecular characterization of the mosquito vitellogenin receptor reveals unexpected high homology to the Drosophila yolk protein receptor
    • Sappington T.W., Kokoza V.A., Cho W.L., Raikhel A.S. Molecular characterization of the mosquito vitellogenin receptor reveals unexpected high homology to the Drosophila yolk protein receptor. Proceedings of National Academy of Science, USA. 93:1996;8934-8939.
    • (1996) Proceedings of National Academy of Science, USA , vol.93 , pp. 8934-8939
    • Sappington, T.W.1    Kokoza, V.A.2    Cho, W.L.3    Raikhel, A.S.4
  • 136
    • 0026934508 scopus 로고
    • Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the golgi complex
    • Saraste J., Kuismanen E. Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the golgi complex. Seminars in Cell Biology. 3:1992;343-355.
    • (1992) Seminars in Cell Biology , vol.3 , pp. 343-355
    • Saraste, J.1    Kuismanen, E.2
  • 137
    • 0001091619 scopus 로고
    • Synthesis and secretion of egg-specific protein from follicle cells of the silkworm Bombyx mori
    • Sato Y., Yamashita O. Synthesis and secretion of egg-specific protein from follicle cells of the silkworm Bombyx mori. Insect Biochemistry. 21:1991;233-238.
    • (1991) Insect Biochemistry , vol.21 , pp. 233-238
    • Sato, Y.1    Yamashita, O.2
  • 138
    • 0029873463 scopus 로고    scopus 로고
    • Vitellogenin receptors: Oocyte-specific members of the low-density lipoprotein receptor supergene family
    • Schneider W.J. Vitellogenin receptors: oocyte-specific members of the low-density lipoprotein receptor supergene family. International Review of Cytology. 166:1996;103-137.
    • (1996) International Review of Cytology , vol.166 , pp. 103-137
    • Schneider, W.J.1
  • 139
    • 0028964133 scopus 로고
    • The Drosophila yolkless gene encodes a vitellogenin receptor belonging to the low density lipoprotein receptor superfamily
    • Schoonbaum C.P., Lee S., Mahowald A.P. The Drosophila yolkless gene encodes a vitellogenin receptor belonging to the low density lipoprotein receptor superfamily. Proceedings of National Academy of Science USA. 92:1995;1485-1489.
    • (1995) Proceedings of National Academy of Science USA , vol.92 , pp. 1485-1489
    • Schoonbaum, C.P.1    Lee, S.2    Mahowald, A.P.3
  • 140
    • 0024513147 scopus 로고
    • Structure of a major yolk glycoprotein and its processing pathway by limited proteolysis are conserved in echinods
    • Scott L.B., Lennarz W.J. Structure of a major yolk glycoprotein and its processing pathway by limited proteolysis are conserved in echinods. Developmental Biology. 132:1989;91-102.
    • (1989) Developmental Biology , vol.132 , pp. 91-102
    • Scott, L.B.1    Lennarz, W.J.2
  • 141
    • 0345717337 scopus 로고
    • Proteolytic enzymes in various embryonic stages of the eggs of Locusta migratoria migratorioides (R&F.)
    • Shulov A., Pener M.P., Kuk-Meiri S., Lichtenstein N. Proteolytic enzymes in various embryonic stages of the eggs of Locusta migratoria migratorioides (R&F.). Journal of Insect Physiology. 1:1957;279-285.
    • (1957) Journal of Insect Physiology , vol.1 , pp. 279-285
    • Shulov, A.1    Pener, M.P.2    Kuk-Meiri, S.3    Lichtenstein, N.4
  • 142
    • 0000659213 scopus 로고
    • Regulation of ecdysteroid titer: Synthesis
    • L.I. Gilbert, & G.A. Kerkut. Oxford: Pergamon Press
    • Smith S.L. Regulation of ecdysteroid titer: synthesis. Gilbert L.I., Kerkut G.A. Comprehensive Insect Physiology, Biochemistry and Pharmacology. 1985;295 Pergamon Press, Oxford.
    • (1985) Comprehensive Insect Physiology, Biochemistry and Pharmacology , pp. 295
    • Smith, S.L.1
  • 143
    • 0030781011 scopus 로고    scopus 로고
    • Secretory and internalization pathways of mosquito yolk protein precursors
    • Snigirevskaya E.S., Hays A.R., Raikhel A.S. Secretory and internalization pathways of mosquito yolk protein precursors. Cell and Tissue Research. 290:1997;129-142.
    • (1997) Cell and Tissue Research , vol.290 , pp. 129-142
    • Snigirevskaya, E.S.1    Hays, A.R.2    Raikhel, A.S.3
  • 144
    • 0030829955 scopus 로고    scopus 로고
    • Internalization and recycling of vitellogenin receptor in the mosquito oocyte
    • Snigirevskaya E.S., Sappington T.W., Raikhel A.S. Internalization and recycling of vitellogenin receptor in the mosquito oocyte. Cell and Tissue Research. 290:1997;175-183.
    • (1997) Cell and Tissue Research , vol.290 , pp. 175-183
    • Snigirevskaya, E.S.1    Sappington, T.W.2    Raikhel, A.S.3
  • 145
    • 0006604522 scopus 로고
    • Structure and embryonic degradation of two native vitellins in the cockroach Periplaneta americana
    • Storella J.R., Wojchowski D.M., Kunkel J.G. Structure and embryonic degradation of two native vitellins in the cockroach Periplaneta americana. Insect Biochemistry. 15:1985;259-275.
    • (1985) Insect Biochemistry , vol.15 , pp. 259-275
    • Storella, J.R.1    Wojchowski, D.M.2    Kunkel, J.G.3
  • 146
    • 0001424774 scopus 로고
    • Studies on the phosphorylation of ovarian proteins from the silkworm Bombyx mori
    • Takahashi S. Studies on the phosphorylation of ovarian proteins from the silkworm Bombyx mori. Insect Biochemistry. 17:1987;141-152.
    • (1987) Insect Biochemistry , vol.17 , pp. 141-152
    • Takahashi, S.1
  • 147
    • 0001573128 scopus 로고
    • Acid cysteine proteinase from the eggs of silkmoth Bombyx mori: Tissue distribution, developmental changes and the sites of synthesis for the enzyme
    • Takahashi S.Y., Zhao X., Kageyama T., Yamamoto Y. Acid cysteine proteinase from the eggs of silkmoth Bombyx mori: tissue distribution, developmental changes and the sites of synthesis for the enzyme. Insect Biochemistry and Molecular Biology. 22:1992;369-377.
    • (1992) Insect Biochemistry and Molecular Biology , vol.22 , pp. 369-377
    • Takahashi, S.Y.1    Zhao, X.2    Kageyama, T.3    Yamamoto, Y.4
  • 148
    • 0027177631 scopus 로고
    • Cysteine proteinase from the eggs of the silkmoth Bombyx mori: Indication of a latent enzyme and characterization of activation and proteolytic processing in vivo and in vitro
    • Takahashi S.Y., Yamamoto Y., Shionoya Y., Kageyama T. Cysteine proteinase from the eggs of the silkmoth Bombyx mori: indication of a latent enzyme and characterization of activation and proteolytic processing in vivo and in vitro. Journal of Biochemistry. 114:1993;267-272.
    • (1993) Journal of Biochemistry , vol.114 , pp. 267-272
    • Takahashi, S.Y.1    Yamamoto, Y.2    Shionoya, Y.3    Kageyama, T.4
  • 151
    • 0023009780 scopus 로고
    • A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution
    • Tanaka K., Ii I., Ichihara A., Waxman L., Goldberg A.L. A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution. Journal of Biological Chemistry. 261:1986;15 197-15203.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 15197-15203
    • Tanaka, K.1    Ii, I.2    Ichihara, A.3    Waxman, L.4    Goldberg, A.L.5
  • 152
    • 0001461651 scopus 로고
    • Arylphorin, a new protein from Hyalophora cecropia: Comparisons with caliphorin and manducin
    • Telfer W.H., Keim P.S., Law J.H. Arylphorin, a new protein from Hyalophora cecropia: comparisons with caliphorin and manducin. Insect Biochemistry. 13:1983;601-613.
    • (1983) Insect Biochemistry , vol.13 , pp. 601-613
    • Telfer, W.H.1    Keim, P.S.2    Law, J.H.3
  • 153
    • 84990424240 scopus 로고
    • Adsorptive endocytosis of vitellogenin, lipophorin and microvitellogenin during yolk formation in Hyalophora
    • Telfer W.H., Pan M. Adsorptive endocytosis of vitellogenin, lipophorin and microvitellogenin during yolk formation in Hyalophora. Archives of Insect Biochemistry and Physiology. 9:1988;339-355.
    • (1988) Archives of Insect Biochemistry and Physiology , vol.9 , pp. 339-355
    • Telfer, W.H.1    Pan, M.2
  • 154
    • 0006589570 scopus 로고
    • The embryonic development of the stick insect Carausius morosus
    • Thomas A.J. The embryonic development of the stick insect Carausius morosus. Quarterly Journal of Microscopical Sciences. 78:1936;487-511.
    • (1936) Quarterly Journal of Microscopical Sciences , vol.78 , pp. 487-511
    • Thomas, A.J.1
  • 156
    • 0027502883 scopus 로고
    • Purification and characterization of a multiprotein component of the Drosophila 26S (1500 kDa) proteolytic complex
    • Udvardy A. Purification and characterization of a multiprotein component of the Drosophila 26S (1500 kDa) proteolytic complex. Journal of Biological Chemistry. 268:1993;9055-9062.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 9055-9062
    • Udvardy, A.1
  • 157
    • 0027756943 scopus 로고
    • Immunocytochemical localization of a follicle specific protein of the hawkmoth Manduca sexta
    • Van Antwerpen R., Law J.H. Immunocytochemical localization of a follicle specific protein of the hawkmoth Manduca sexta. Tissue and Cell. 25:1993;885-892.
    • (1993) Tissue and Cell , vol.25 , pp. 885-892
    • Van Antwerpen, R.1    Law, J.H.2
  • 159
    • 0031281273 scopus 로고    scopus 로고
    • Cloning and characterization of three Musca domestica yolk protein genes
    • White N.M., Bownes M. Cloning and characterization of three Musca domestica yolk protein genes. Insect Molecular Biology. 6:1997;329-341.
    • (1997) Insect Molecular Biology , vol.6 , pp. 329-341
    • White, N.M.1    Bownes, M.2
  • 160
    • 0019888345 scopus 로고
    • The structure of vitellogenin. Multiple vitellogenins in Xenopus laevis give rise to multiple forms of the yolk proteins
    • Wiley H.S., Wallace R.A. The structure of vitellogenin. Multiple vitellogenins in Xenopus laevis give rise to multiple forms of the yolk proteins. Journal of Biological Chemistry. 256:1981;8626-8634.
    • (1981) Journal of Biological Chemistry , vol.256 , pp. 8626-8634
    • Wiley, H.S.1    Wallace, R.A.2
  • 161
    • 0022762494 scopus 로고
    • Processing of provitellogenin in insect fat body: A role for high mannose oligosaccharide
    • Wojchowski D.M., Parsons P.P., Nordin J.H., Kunkel J.G. Processing of provitellogenin in insect fat body: a role for high mannose oligosaccharide. Developmental Biology. 116:1986;422-429.
    • (1986) Developmental Biology , vol.116 , pp. 422-429
    • Wojchowski, D.M.1    Parsons, P.P.2    Nordin, J.H.3    Kunkel, J.G.4
  • 163
    • 0027218436 scopus 로고
    • Cysteine proteinase from Bombyx eggs: Role in programmed degradation of yolk proteins during embryogenesis
    • Yamamoto Y., Takahashi S.Y. Cysteine proteinase from Bombyx eggs: role in programmed degradation of yolk proteins during embryogenesis. Comparative Biochemistry and Physiology, 106B. 1993;35-45.
    • (1993) Comparative Biochemistry and Physiology, 106B , pp. 35-45
    • Yamamoto, Y.1    Takahashi, S.Y.2
  • 164
    • 0028069204 scopus 로고
    • Cysteine proteinase from the eggs of the silkmoth Bombyx mori: Site of synthesis and a suggested role in yolk degradation
    • Yamamoto Y., Zhao X., Suzuki A., Takahashi S.Y. Cysteine proteinase from the eggs of the silkmoth Bombyx mori: site of synthesis and a suggested role in yolk degradation. Journal of Insect Physiology. 40:1994;447-454.
    • (1994) Journal of Insect Physiology , vol.40 , pp. 447-454
    • Yamamoto, Y.1    Zhao, X.2    Suzuki, A.3    Takahashi, S.Y.4
  • 165
  • 167
    • 0000433235 scopus 로고
    • Characterization of vitellin, egg-specific protein and 30 kDa protein from Bombyx eggs, and their fate during oogenesis and embryogenesis
    • Zhu J., Indrasith L.S., Yamashita O. Characterization of vitellin, egg-specific protein and 30 kDa protein from Bombyx eggs, and their fate during oogenesis and embryogenesis. Biochimica Biophysica Acta. 882:1986;427-436.
    • (1986) Biochimica Biophysica Acta , vol.882 , pp. 427-436
    • Zhu, J.1    Indrasith, L.S.2    Yamashita, O.3


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