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Volumn 260, Issue 3, 1999, Pages 736-742

A 42-kDa glycoprotein from chicken egg-envelope, an avian homolog of the ZPC family glycoproteins in mammalian zona pellucida. Its first identification, cDNA cloning and granulosa cell-specific expression

Author keywords

Chicken egg; Egg envelope; Perivitelline; Zona pellucida

Indexed keywords

ENVELOPE PROTEIN; GLYCOPROTEIN;

EID: 0000442112     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00203.x     Document Type: Article
Times cited : (88)

References (54)
  • 1
    • 0001476362 scopus 로고
    • Yolk transport in the ovarian follicle of the hen (Gallus domesticus): Lipoprotein-like particles at the periphery of the oocyte in the rapid growth phase
    • Bellairs, R., Harkness, M. & Harkness, R.D. (1963) Yolk transport in the ovarian follicle of the hen (Gallus domesticus): lipoprotein-like particles at the periphery of the oocyte in the rapid growth phase. J. Ultrastructure Res. 8, 339-359.
    • (1963) J. Ultrastructure Res. , vol.8 , pp. 339-359
    • Bellairs, R.1    Harkness, M.2    Harkness, R.D.3
  • 2
    • 0018651717 scopus 로고
    • The vitelline membrane of the hen's egg: A chemical and electron microscopical study
    • Perry, M.M. & Gilbert, A.B. (1979) The vitelline membrane of the hen's egg: a chemical and electron microscopical study. J. Cell Sci. 39, 257-272.
    • (1979) J. Cell Sci. , vol.39 , pp. 257-272
    • Perry, M.M.1    Gilbert, A.B.2
  • 3
    • 0017715424 scopus 로고
    • The fine structure of the hen's ovum at ovulation
    • Bakst, M.R. & Howarth, B. Jr (1977) The fine structure of the hen's ovum at ovulation. Biol. Reprod. 17, 370-379.
    • (1977) Biol. Reprod. , vol.17 , pp. 370-379
    • Bakst, M.R.1    Howarth B., Jr.2
  • 4
    • 0002670253 scopus 로고
    • Maturation of spermatozoa and mechanism of fertilization
    • Cunningham, E.J., Lake, P.E. & Hewitt, D., eds., Longman, Harlow, UK
    • Howarth, B. Jr (1984) Maturation of spermatozoa and mechanism of fertilization. In Reproductive Biology of Poultry, pp. 161-174. (Cunningham, E.J., Lake, P.E. & Hewitt, D., eds.), Longman, Harlow, UK.
    • (1984) Reproductive Biology of Poultry , pp. 161-174
    • Howarth B., Jr.1
  • 5
    • 0023162573 scopus 로고
    • Nuclear events from fertilisation to the early cleavage stages in the domestic fowl
    • Perry, M.M. (1987) Nuclear events from fertilisation to the early cleavage stages in the domestic fowl. J. Anat. 150, 99-109.
    • (1987) J. Anat. , vol.150 , pp. 99-109
    • Perry, M.M.1
  • 6
    • 0026492396 scopus 로고
    • Preferential attachment of cock spermatozoa to the perivitelline layer directly over the germinal disc of the hen's ovum
    • Bramwell, R.K. & Howarth, B. Jr (1992) Preferential attachment of cock spermatozoa to the perivitelline layer directly over the germinal disc of the hen's ovum. Biol. Reprod. 47, 1113-1117.
    • (1992) Biol. Reprod. , vol.47 , pp. 1113-1117
    • Bramwell, R.K.1    Howarth B., Jr.2
  • 7
    • 0018178011 scopus 로고
    • The passage of spermatozoa through the vitelline membrane in the domestic fowl, Gallus gallus
    • Okumura, F. & Nishiyama, H. (1978) The passage of spermatozoa through the vitelline membrane in the domestic fowl, Gallus gallus. Cell Tissue Res. 188, 497-508.
    • (1978) Cell Tissue Res. , vol.188 , pp. 497-508
    • Okumura, F.1    Nishiyama, H.2
  • 8
    • 0018831516 scopus 로고
    • Mammalian sperm-egg interaction: Identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm
    • Bleil, J.D. & Wassarman, P.M. (1980) Mammalian sperm-egg interaction: identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm. Cell 20, 873-882.
    • (1980) Cell , vol.20 , pp. 873-882
    • Bleil, J.D.1    Wassarman, P.M.2
  • 9
    • 0025044472 scopus 로고
    • Profile of a mammalian sperm receptor
    • Wassarman, P.M. (1990) Profile of a mammalian sperm receptor. Development 108, 1-17.
    • (1990) Development , vol.108 , pp. 1-17
    • Wassarman, P.M.1
  • 10
    • 0029896017 scopus 로고    scopus 로고
    • The molecules of mammalian fertilization. 6. Preferential attachment of cock spermatozoa to the perivitelline layer directly over the germinal disc of the hen's ovum
    • Snell, W.J. & White, J.M. (1996) The molecules of mammalian fertilization. 6. Preferential attachment of cock spermatozoa to the perivitelline layer directly over the germinal disc of the hen's ovum. Cell 85, 629-637.
    • (1996) Cell , vol.85 , pp. 629-637
    • Snell, W.J.1    White, J.M.2
  • 11
    • 0027416199 scopus 로고
    • Conservation of mammalian secondary sperm receptor genes enables the promoter of the human gene to function in mouse oocytes
    • Liang, L. & Dean, J. (1993) Conservation of mammalian secondary sperm receptor genes enables the promoter of the human gene to function in mouse oocytes. Dev. Biol. 156, 399-408.
    • (1993) Dev. Biol. , vol.156 , pp. 399-408
    • Liang, L.1    Dean, J.2
  • 12
    • 0027171178 scopus 로고
    • Nucleotide sequence of cDNA encoding ZP3a, a sperm-binding glycoprotein from zona pellucida of pig oocyte
    • Yurewicz, E.C., Hibler, D., Fontenot, G.,K., Sacco, A.G. & Harris, J. (1993) Nucleotide sequence of cDNA encoding ZP3a, a sperm-binding glycoprotein from zona pellucida of pig oocyte. Biochim. Biophys. Acta 1174, 211-214.
    • (1993) Biochim. Biophys. Acta , vol.1174 , pp. 211-214
    • Yurewicz, E.C.1    Hibler, D.2    Fontenot, G.K.3    Sacco, A.G.4    Harris, J.5
  • 13
    • 0027164196 scopus 로고
    • Identification and structural characterization of the 75-kDa rabbit zona pellucida protein
    • Lee, V.H., Schwoel, E., Prasad, S., Cheung, P., Timmons, T.M., Cook, R. & Dunbar, B.S. (1993) Identification and structural characterization of the 75-kDa rabbit zona pellucida protein. J. Biol. Chem. 268, 12412-12417.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12412-12417
    • Lee, V.H.1    Schwoel, E.2    Prasad, S.3    Cheung, P.4    Timmons, T.M.5    Cook, R.6    Dunbar, B.S.7
  • 14
    • 0022573194 scopus 로고
    • The coelomic envelope to vitelline envelope conversion in eggs of Xenopus laevis
    • Gerton, G.L. & Hedrick, J.L. (1986) The coelomic envelope to vitelline envelope conversion in eggs of Xenopus laevis. J. Cell Biochem. 30, 341-350.
    • (1986) J. Cell Biochem. , vol.30 , pp. 341-350
    • Gerton, G.L.1    Hedrick, J.L.2
  • 15
    • 0030933883 scopus 로고    scopus 로고
    • Gamete interactions in Xenopus laevis: Identification of sperm binding glycoproteins in the egg vitelline envelope
    • Tian, B., Gong, H., Thomsen, G.H. & Lennarz, W.J. (1997) Gamete interactions in Xenopus laevis: identification of sperm binding glycoproteins in the egg vitelline envelope. J. Cell Biol. 136, 1099-1108.
    • (1997) J. Cell Biol. , vol.136 , pp. 1099-1108
    • Tian, B.1    Gong, H.2    Thomsen, G.H.3    Lennarz, W.J.4
  • 16
    • 0030766728 scopus 로고    scopus 로고
    • A major glycoprotein of Xenopus egg vitelline envelope, gp41, is a frog homolog of mammalian ZP3
    • Kubo, H., Kawano, T., Tsubuki, S., Kawashima, S., Katagiri, C. & Suzuki, A. (1997) A major glycoprotein of Xenopus egg vitelline envelope, gp41, is a frog homolog of mammalian ZP3. Dev. Growth Differ. 39, 405-417.
    • (1997) Dev. Growth Differ. , vol.39 , pp. 405-417
    • Kubo, H.1    Kawano, T.2    Tsubuki, S.3    Kawashima, S.4    Katagiri, C.5    Suzuki, A.6
  • 17
    • 0030814963 scopus 로고    scopus 로고
    • cDNA cloning and sequence analysis of the Xenopus leavis egg envelope glycoprotein gp43
    • Yang, J.C. & Hedrick, J.L. (1997) cDNA cloning and sequence analysis of the Xenopus leavis egg envelope glycoprotein gp43. Dev. Growth Differ. 39, 457-467.
    • (1997) Dev. Growth Differ , vol.39 , pp. 457-467
    • Yang, J.C.1    Hedrick, J.L.2
  • 19
    • 0031052253 scopus 로고    scopus 로고
    • Cloning of cDNA and estrogen-induced hepatic gene expression for choriogenin H, a precursor protein of the fish egg envelope (chorion)
    • Murata, K., Sugiyama, H., Yasumasu, S., Iuchi, I., Yasumasu, I. & Yamagami, K. (1997) Cloning of cDNA and estrogen-induced hepatic gene expression for choriogenin H, a precursor protein of the fish egg envelope (chorion). Proc. Natl Acad. Sci. USA 94, 2050-2055.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2050-2055
    • Murata, K.1    Sugiyama, H.2    Yasumasu, S.3    Iuchi, I.4    Yasumasu, I.5    Yamagami, K.6
  • 20
    • 0027493423 scopus 로고
    • Expression and structural analysis of a teleost homolog of a mammalian zona pellucida gene
    • Lyons, C.E., Payette, K.L., Price, J.L. & Huang, R.C.C. (1993) Expression and structural analysis of a teleost homolog of a mammalian zona pellucida gene. J. Biol. Chem. 268, 21351-21358.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21351-21358
    • Lyons, C.E.1    Payette, K.L.2    Price, J.L.3    Huang, R.C.C.4
  • 21
    • 0001614984 scopus 로고
    • Separation and properties of the inner and outer layers of the vitelline membrane of hen's eggs
    • Kido, S. & Doi. Y. (1988) Separation and properties of the inner and outer layers of the vitelline membrane of hen's eggs. Poultry Sci. 67, 476-486.
    • (1988) Poultry Sci. , vol.67 , pp. 476-486
    • Kido, S.1    Doi, Y.2
  • 22
    • 0028887029 scopus 로고
    • Origin of 33 kDa protein of vitelline membrane of quail egg: Immunological studies
    • Kuroki, M. & Mori, M. (1995) Origin of 33 kDa protein of vitelline membrane of quail egg: immunological studies. Dev. Growth Differ. 37, 545-550.
    • (1995) Dev. Growth Differ. , vol.37 , pp. 545-550
    • Kuroki, M.1    Mori, M.2
  • 23
    • 0020641707 scopus 로고
    • In vitro biosynthesis of three sulfated glycoproteins of murine zonae pellucidae by oocytes grown in follicle culture
    • Shimizu, S., Tsuji, M. & Dean, J. (1983) In vitro biosynthesis of three sulfated glycoproteins of murine zonae pellucidae by oocytes grown in follicle culture. J. Biol. Chem. 258, 5858-5863.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5858-5863
    • Shimizu, S.1    Tsuji, M.2    Dean, J.3
  • 24
    • 0023926939 scopus 로고
    • Molecular analysis of cDNA coding for ZP3, a sperm binding protein of the mouse zona pellucida
    • Ringuette, M.J., Chamberlin, M.E., Baur, A.W., Sobieski, D.A. & Dean, J. (1988) Molecular analysis of cDNA coding for ZP3, a sperm binding protein of the mouse zona pellucida. Dev. Biol. 127, 287-295.
    • (1988) Dev. Biol. , vol.127 , pp. 287-295
    • Ringuette, M.J.1    Chamberlin, M.E.2    Baur, A.W.3    Sobieski, D.A.4    Dean, J.5
  • 25
    • 0025255277 scopus 로고
    • Oocyte-specific expression of mouse Zp-2: Developmental regulation of the zona pellucida genes
    • Liang, L.-F., Chamow, S.M. & Dean, J. (1990) Oocyte-specific expression of mouse Zp-2: Developmental regulation of the zona pellucida genes. Mol. Cellular Biol. 10, 1507-1515.
    • (1990) Mol. Cellular Biol. , vol.10 , pp. 1507-1515
    • Liang, L.-F.1    Chamow, S.M.2    Dean, J.3
  • 26
    • 0025102002 scopus 로고
    • Human homolog of the mouse sperm receptor
    • Chamberlin, M.E. & Dean, J. (1990) Human homolog of the mouse sperm receptor. Proc. Natl Acad. Sci. USA 87, 6014-6018.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 6014-6018
    • Chamberlin, M.E.1    Dean, J.2
  • 27
    • 0027518726 scopus 로고
    • Developmental expression of the rabbit 55-kDa zona pellucida protein and messenger RNA in ovarian follicles
    • Lee, V.H. & Dunbar, B.S. (1993) Developmental expression of the rabbit 55-kDa zona pellucida protein and messenger RNA in ovarian follicles. Dev. Biol. 155, 371-382.
    • (1993) Dev. Biol. , vol.155 , pp. 371-382
    • Lee, V.H.1    Dunbar, B.S.2
  • 28
    • 0028985303 scopus 로고
    • Cloning of a cDNA coding for porcine zona pellucida glycoprotein ZP1 and its genomic organization
    • Taya, T., Yamasaki, N., Tsubamoto, H., Hasegawa, A. & Koyama, K. (1995) Cloning of a cDNA coding for porcine zona pellucida glycoprotein ZP1 and its genomic organization. Biochem. Biophys. Res. Commun, 207, 790-799.
    • (1995) Biochem. Biophys. Res. Commun , vol.207 , pp. 790-799
    • Taya, T.1    Yamasaki, N.2    Tsubamoto, H.3    Hasegawa, A.4    Koyama, K.5
  • 29
    • 0000503046 scopus 로고
    • The development of the zona pellucida of the mammalian ovum
    • Chiquoine, A.D. (1960) The development of the zona pellucida of the mammalian ovum. Am. J. Anat. 106, 149-169.
    • (1960) Am. J. Anat. , vol.106 , pp. 149-169
    • Chiquoine, A.D.1
  • 31
    • 0017355890 scopus 로고
    • A method for separating the granulosa cells, the basal lamina and the theca of the preovulatory ovarian follicle of the domestic fowl (Gallus domesticus)
    • Gilbert, A.B., Evans, A.J., Perry, M.M. & Davidson, M.H. (1977) A method for separating the granulosa cells, the basal lamina and the theca of the preovulatory ovarian follicle of the domestic fowl (Gallus domesticus). J. Reprod. Fert. 50, 179-181.
    • (1977) J. Reprod. Fert. , vol.50 , pp. 179-181
    • Gilbert, A.B.1    Evans, A.J.2    Perry, M.M.3    Davidson, M.H.4
  • 32
    • 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
  • 33
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 34
    • 0027407873 scopus 로고
    • Structural studies of a novel type of tetraantennary sialoglycan unit in a carbohydrate-rich glycopeptide isolated from the fertilized eggs of Indian Medaka fish, Oryzias melastigma
    • Taguchi, T., Seko, A., Kitajima, K., Inoue, S., Iwamatsu, T., Khoo, K.-H., Morris, H.R., Dell, A. & Inoue, Y. (1993) Structural studies of a novel type of tetraantennary sialoglycan unit in a carbohydrate-rich glycopeptide isolated from the fertilized eggs of Indian Medaka fish, Oryzias melastigma, J. Biol. Chem. 268, 2353-2362.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2353-2362
    • Taguchi, T.1    Seko, A.2    Kitajima, K.3    Inoue, S.4    Iwamatsu, T.5    Khoo, K.-H.6    Morris, H.R.7    Dell, A.8    Inoue, Y.9
  • 35
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by peptide: N-glycanase F
    • Tarentino, A.L., Gomez, C.M. & Plummer, T.H. Jr (1985) Deglycosylation of asparagine-linked glycans by peptide: N-glycanase F. Biochemistry 24, 4665-4671.
    • (1985) Biochemistry , vol.24 , pp. 4665-4671
    • Tarentino, A.L.1    Gomez, C.M.2    Plummer T.H., Jr.3
  • 37
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 38
    • 0028973205 scopus 로고
    • Carboxy-terminal cytoplasmic domain of mouse butyrophilin specifically associates with a 150-kDa protein of mammary epithelial cells and milk fat globule membrane
    • Ishii, T., Aoki, N., Noda, A., Adachi, T., Nakamura, R. & Matsuda, T. (1995) Carboxy-terminal cytoplasmic domain of mouse butyrophilin specifically associates with a 150-kDa protein of mammary epithelial cells and milk fat globule membrane. Biochim. Biophys. Acta 1245, 285-292.
    • (1995) Biochim. Biophys. Acta , vol.1245 , pp. 285-292
    • Ishii, T.1    Aoki, N.2    Noda, A.3    Adachi, T.4    Nakamura, R.5    Matsuda, T.6
  • 40
    • 0024598146 scopus 로고
    • Fast and sensitive multiple sequence alignments on a microcomputer
    • Higgins, D.G. & Sharp, P.M. (1989) Fast and sensitive multiple sequence alignments on a microcomputer. Comput Appl. Biosci 5, 151-153.
    • (1989) Comput Appl. Biosci , vol.5 , pp. 151-153
    • Higgins, D.G.1    Sharp, P.M.2
  • 41
    • 0028956002 scopus 로고
    • Molecular cloning of chick β-tectorin, an extracellular matrix molecule of the inner ear
    • Killick, R., Legan, P.K., Malenczak, C. & Richardson, G.P. (1995) Molecular cloning of chick β-tectorin, an extracellular matrix molecule of the inner ear. J. Cell Biol. 129, 535-547.
    • (1995) J. Cell Biol. , vol.129 , pp. 535-547
    • Killick, R.1    Legan, P.K.2    Malenczak, C.3    Richardson, G.P.4
  • 42
    • 0026545275 scopus 로고
    • A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor
    • Bork, P. & Sander, C. (1992) A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor. FEBS Lett. 300, 237-240.
    • (1992) FEBS Lett. , vol.300 , pp. 237-240
    • Bork, P.1    Sander, C.2
  • 43
    • 0023164968 scopus 로고
    • Structural characterization of the Mr = 55,000 antigen (ZP3) of porcine oocyte zona pellucida. Purification and characterization of alpha- and beta-glycoproteins following digestion of lactosaminoglycan with endo-beta-galactosidase
    • Yurewicz, E.C., Sacco, A.G. & Subramanian, M.G. (1987) Structural characterization of the Mr = 55,000 antigen (ZP3) of porcine oocyte zona pellucida. Purification and characterization of alpha- and beta-glycoproteins following digestion of lactosaminoglycan with endo-beta-galactosidase. J. Biol. Chem. 262, 564-571.
    • (1987) J. Biol. Chem. , vol.262 , pp. 564-571
    • Yurewicz, E.C.1    Sacco, A.G.2    Subramanian, M.G.3
  • 44
    • 0025916877 scopus 로고
    • Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway
    • Hosaka, M., Nagahama, M., Kim, W.-S., Watanabe, T., Hatsuzawa, K., Ikemizu, J., Muratami, K. & Nakayama, K. (1991) Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway. J. Biol. Chem. 266, 12127-12130.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12127-12130
    • Hosaka, M.1    Nagahama, M.2    Kim, W.-S.3    Watanabe, T.4    Hatsuzawa, K.5    Ikemizu, J.6    Muratami, K.7    Nakayama, K.8
  • 45
    • 0023463127 scopus 로고
    • Constitutive and regulated secretion of proteins
    • Burgess, T.L. & Kelly, R.B. (1987) Constitutive and regulated secretion of proteins. Ann. Rev. Cell Biol. 3, 243-293.
    • (1987) Ann. Rev. Cell Biol. , vol.3 , pp. 243-293
    • Burgess, T.L.1    Kelly, R.B.2
  • 46
    • 0023944337 scopus 로고
    • Cell-surface anchoring of proteins via glycosyl-phosphatidylinositol structures
    • Ferguson, M.A.J. & Williams, A.F. (1988) Cell-surface anchoring of proteins via glycosyl-phosphatidylinositol structures. Annu. Rev. Biochem. 57, 285-320.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 285-320
    • Ferguson, M.A.J.1    Williams, A.F.2
  • 47
    • 0343435291 scopus 로고
    • Galactose at the nonreducting terminus of O-linked oligosaccharides of mouse egg zona pellucida glycoprotein ZP3 is essential for the glycoprotein's sperm receptor activity
    • Bleil, J.D. & Wassarman, P.M. (1988) Galactose at the nonreducting terminus of O-linked oligosaccharides of mouse egg zona pellucida glycoprotein ZP3 is essential for the glycoprotein's sperm receptor activity. Proc. Natl Acad. Sci. USA 85, 6778-6782.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 6778-6782
    • Bleil, J.D.1    Wassarman, P.M.2
  • 48
    • 0026607821 scopus 로고
    • Structural analysis of the N-linked carbohydrate chains of the 55-kDa glycoprotein family (PZP3) from porcine zona pellucida
    • Noguchi, S., Hatanaka, Y., Tobita, T. & Nakano, M. (1992) Structural analysis of the N-linked carbohydrate chains of the 55-kDa glycoprotein family (PZP3) from porcine zona pellucida. Eur. J. Biochem. 204, 1089-1100.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 1089-1100
    • Noguchi, S.1    Hatanaka, Y.2    Tobita, T.3    Nakano, M.4
  • 50
    • 0025255531 scopus 로고
    • Identification of a 257-kDa protein associated with the apical surfaces of sensory hair cells in the avian inner ear
    • Richardson, G.P., Bartolami, S. & Russell, I.J. (1990) Identification of a 257-kDa protein associated with the apical surfaces of sensory hair cells in the avian inner ear. J. Cell Biol. 110, 1055-1066.
    • (1990) J. Cell Biol. , vol.110 , pp. 1055-1066
    • Richardson, G.P.1    Bartolami, S.2    Russell, I.J.3
  • 51
    • 0023759376 scopus 로고
    • The ultrastructural organization and properties of the mouse tectorial membrane matrix
    • Hasko, J.A. & Richardson, G.P. (1988) The ultrastructural organization and properties of the mouse tectorial membrane matrix. Hearing Res. 35, 21-38.
    • (1988) Hearing Res. , vol.35 , pp. 21-38
    • Hasko, J.A.1    Richardson, G.P.2
  • 52
    • 0023186834 scopus 로고
    • Oocyte-specific expression and developmental regulation of ZP3, the sperm receptor of the mouse zona pellucida
    • Philpott, C.C., Ringuette, M.J. & Dean, J. (1987) Oocyte-specific expression and developmental regulation of ZP3, the sperm receptor of the mouse zona pellucida. Dev. Biol. 121, 568-575.
    • (1987) Dev. Biol. , vol.121 , pp. 568-575
    • Philpott, C.C.1    Ringuette, M.J.2    Dean, J.3
  • 53
    • 0022480709 scopus 로고
    • Oocyte-specific gene expression: Molecular characterization of a cDNA coding for ZP-3, the sperm receptor of the mouse zona pellucida
    • Ringuette, M.J., Sobieski, D.A., Chamow, S.M. & Dean, J. (1986) Oocyte-specific gene expression: molecular characterization of a cDNA coding for ZP-3, the sperm receptor of the mouse zona pellucida. Proc. Natl Acad. Sci. USA 83, 4341-4345.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 4341-4345
    • Ringuette, M.J.1    Sobieski, D.A.2    Chamow, S.M.3    Dean, J.4
  • 54
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. & Dootittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Dootittle, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.