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Volumn 124, Issue 6, 2011, Pages 940-950

ZP2 and ZP3 cytoplasmic tails prevent premature interactions and ensure incorporation into the zona pellucida

Author keywords

tectorin; Cytoplasmic tails; Extracellular matrix; Intracellular trafficking; Oocytes; Zona pellucida; ZP2; ZP3

Indexed keywords

CELL PROTEIN; PROEIN ZP2; PROTEIN ZP3; UNCLASSIFIED DRUG;

EID: 79952778368     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.079988     Document Type: Article
Times cited : (41)

References (71)
  • 2
    • 0018822414 scopus 로고
    • Structure and function of the zona pellucida: Identification and characterization of the proteins of the mouse oocyte's zona pellucida
    • Bleil, J. D. and Wassarman, P. M. (1980a). Structure and function of the zona pellucida: Identification and characterization of the proteins of the mouse oocyte's zona pellucida. Dev. Biol. 76, 185-202.
    • (1980) Dev. Biol. , vol.76 , pp. 185-202
    • Bleil, J.D.1    Wassarman, P.M.2
  • 3
    • 0018827098 scopus 로고
    • Synthesis of zona pellucida proteins by denuded and follicle-enclosed mouse oocytes during culture in vitro
    • Bleil, J. D. and Wassarman, P. M. (1980b). Synthesis of zona pellucida proteins by denuded and follicle-enclosed mouse oocytes during culture in vitro. Proc. Natl. Acad. Sci. USA 77, 1029-1033.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1029-1033
    • Bleil, J.D.1    Wassarman, P.M.2
  • 4
    • 0141557578 scopus 로고    scopus 로고
    • Structural Characterization of Native Mouse Zona Pellucida Proteins Using Mass Spectrometry
    • DOI 10.1074/jbc.M304026200
    • Boja, E. S., Hoodbhoy, T., Fales, H. M. and Dean, J. (2003). Structural characterization of native mouse zona pellucida proteins using mass spectrometry. J. Biol. Chem. 278, 34189-34202. (Pubitemid 37553261)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.36 , pp. 34189-34202
    • Boja, E.S.1    Hoodbhoy, T.2    Fales, H.M.3    Deanll, J.4
  • 5
    • 0026545275 scopus 로고
    • A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor
    • Bork, P. and 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
  • 7
    • 0000947085 scopus 로고
    • The development and morphology of the gonads of the mouse. Part III. The growth of the follicles
    • Brambell, F. W. R. (1928). The development and morphology of the gonads of the mouse. Part III. The growth of the follicles. Proc. R. Soc. Lond. B Biol. Sci. 103, 258-272.
    • (1928) Proc. R. Soc. Lond. B Biol. Sci. , vol.103 , pp. 258-272
    • Brambell, F.W.R.1
  • 9
    • 0014805929 scopus 로고
    • Transfer to the mouse oviduct of eggs with and without the zona pellucida
    • Bronson, R. A. and McLaren, A. (1970). Transfer to the mouse oviduct of eggs with and without the zona pellucida. J. Reprod. Fertil. 22, 129-137.
    • (1970) J. Reprod. Fertil. , vol.22 , pp. 129-137
    • Bronson, R.A.1    McLaren, A.2
  • 10
    • 0038664265 scopus 로고    scopus 로고
    • Analysis of the role of the membrane-spanning and cytoplasmic tail domains of herpes simplex virus type 1 glycoprotein D in membrane fusion
    • DOI 10.1099/vir.0.19039-0
    • Browne, H., Bruun, B., Whiteley, A. and Minson, T. (2003). Analysis of the role of the membrane-spanning and cytoplasmic tail domains of herpes simplex virus type 1 glycoprotein D in membrane fusion. J. Gen. Virol. 84, 1085-1089. (Pubitemid 36592600)
    • (2003) Journal of General Virology , vol.84 , Issue.5 , pp. 1085-1089
    • Browne, H.1    Bruun, B.2    Whiteley, A.3    Minson, T.4
  • 11
    • 70450176317 scopus 로고    scopus 로고
    • Polarized traffic towards the cell surface: How to find the route
    • Carmosino, M., Valenti, G., Caplan, M. and Svelto, M. (2010). Polarized traffic towards the cell surface: how to find the route. Biol. Cell 102, 75-91.
    • (2010) Biol. Cell , vol.102 , pp. 75-91
    • Carmosino, M.1    Valenti, G.2    Caplan, M.3    Svelto, M.4
  • 12
    • 0032494121 scopus 로고    scopus 로고
    • The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells
    • Chuang, J. Z. and Sung, C. H. (1998). The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells. J. Cell Biol. 142, 1245-1256.
    • (1998) J. Cell Biol. , vol.142 , pp. 1245-1256
    • Chuang, J.Z.1    Sung, C.H.2
  • 13
    • 33750919289 scopus 로고    scopus 로고
    • Extracellular matrix and inner ear development and function
    • Cosgrove, D. and Grotton, M. A. (2001). Extracellular matrix and inner ear development and function. Adv. Dev. Biol. 15, 169-201.
    • (2001) Adv. Dev. Biol. , vol.15 , pp. 169-201
    • Cosgrove, D.1    Grotton, M.A.2
  • 14
    • 70249122432 scopus 로고    scopus 로고
    • The cytoplasmic tail of the T cell receptor CD3 epsilon subunit contains a phospholipid-binding motif that regulates T cell functions
    • Deford-Watts, L. M., Tassin, T. C., Becker, A. M., Medeiros, J. J., Albanesi, J. P., Love, P. E., Wulfing, C. and van Oers, N. S. (2009). The cytoplasmic tail of the T cell receptor CD3 epsilon subunit contains a phospholipid-binding motif that regulates T cell functions. J. Immunol. 183, 1055-1064.
    • (2009) J. Immunol. , vol.183 , pp. 1055-1064
    • Deford-Watts, L.M.1    Tassin, T.C.2    Becker, A.M.3    Medeiros, J.J.4    Albanesi, J.P.5    Love, P.E.6    Wulfing, C.7    Van Oers, N.S.8
  • 15
    • 0034163775 scopus 로고    scopus 로고
    • Stimulation of cleavage of membrane proteins by calmodulin inhibitors
    • DOI 10.1042/0264-6021:3460359
    • Diaz-Rodriguez, E., Esparis-Ogando, A., Montero, J. C., Yuste, L. and Pandiella, A. (2000). Stimulation of cleavage of membrane proteins by calmodulin inhibitors. Biochem. J. 346, 359-367. (Pubitemid 30148121)
    • (2000) Biochemical Journal , vol.346 , Issue.2 , pp. 359-367
    • Diaz-Rodriguez, E.1    Esparis-Ogando, A.2    Montero, J.C.3    Yuste, L.4    Pandiella, A.5
  • 17
    • 0021329389 scopus 로고
    • Monoclonal antibodies as probes of the distribution of ZP-2, the major sulfated glycoprotein of the murine zona pellucida
    • DOI 10.1083/jcb.98.3.795
    • East, I. J. and Dean, J. (1984). Monoclonal antibodies as probes of the distribution of ZP-2, the major sulfated glycoprotein of the murine zona pellucida. J. Cell Biol. 98, 795-800. (Pubitemid 14166508)
    • (1984) Journal of Cell Biology , vol.98 , Issue.3 , pp. 795-800
    • East, I.J.1    Dean, J.2
  • 18
    • 0021855014 scopus 로고
    • Monoclonal antibodies to the murine zona pellucida protein with sperm receptor activity: Effects on fertilization and early development
    • DOI 10.1016/0012-1606(85)90454-3
    • East, I. J., Gulyas, B. J. and Dean, J. (1985). Monoclonal antibodies to the murine zona pellucida protein with sperm receptor activity: Effects on fertilization and early development. Dev. Biol. 109, 268-273. (Pubitemid 15041638)
    • (1985) Developmental Biology , vol.109 , Issue.2 , pp. 268-273
    • East, I.J.1    Gulyas, B.J.2    Dean, J.3
  • 20
    • 0036195795 scopus 로고    scopus 로고
    • Subcellular distribution of ZP1, ZP2, and ZP3 glycoproteins during folliculogenesis and demonstration of their topographical disposition within the zona matrix of mouse ovarian oocytes
    • El Mestrah, M., Castle, P. E., Borossa, G. and Kan, F. W. (2002). Subcellular distribution of ZP1, ZP2, and ZP3 glycoproteins during folliculogenesis and demonstration of their topographical disposition within the zona matrix of mouse ovarian oocytes. Biol. Reprod. 66, 866-876.
    • (2002) Biol. Reprod. , vol.66 , pp. 866-876
    • El Mestrah, M.1    Castle, P.E.2    Borossa, G.3    Kan, F.W.4
  • 21
    • 0028818844 scopus 로고
    • Mouse Zp1 encodes a zona pellucida protein homologous to egg envelope proteins in mammals and fish
    • Epifano, O., Liang, L.-F. and Dean, J. (1995a). Mouse Zp1 encodes a zona pellucida protein homologous to egg envelope proteins in mammals and fish. J. Biol. Chem. 270, 27254-27258.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27254-27258
    • Epifano, O.1    Liang, L.-F.2    Dean, J.3
  • 22
    • 0029060459 scopus 로고
    • Coordinate expression of the three zona pellucida genes during mouse oogenesis
    • Epifano, O., Liang, L.-F., Familari, M., Moos, M. C., Jr and Dean, J. (1995b). Coordinate expression of the three zona pellucida genes during mouse oogenesis. Development 121, 1947-1956.
    • (1995) Development , vol.121 , pp. 1947-1956
    • Epifano, O.1    Liang, L.-F.2    Familari, M.3    Moos Jr., M.C.4    Dean, J.5
  • 23
    • 77954600245 scopus 로고    scopus 로고
    • Gamete recognition in mice depends on the cleavage status of an egg's zona pellucida protein
    • Gahlay, G., Gauthier, L., Baibakov, B., Epifano, O. and Dean, J. (2010). Gamete recognition in mice depends on the cleavage status of an egg's zona pellucida protein. Science 329, 216-219.
    • (2010) Science , vol.329 , pp. 216-219
    • Gahlay, G.1    Gauthier, L.2    Baibakov, B.3    Epifano, O.4    Dean, J.5
  • 25
    • 0020457338 scopus 로고
    • Biosynthesis of the major zona pellucida glycoprotein secreted by oocytes during mammalian oogenesis
    • Greve, J. M., Salzmann, G. S., Roller, R. J. and Wassarman, P. M. (1982). Biosynthesis of the major zona pellucida glycoprotein secreted by oocytes during mammalian oogenesis. Cell 31, 749-759.
    • (1982) Cell , vol.31 , pp. 749-759
    • Greve, J.M.1    Salzmann, G.S.2    Roller, R.J.3    Wassarman, P.M.4
  • 26
    • 33644855363 scopus 로고    scopus 로고
    • Polarized apical sorting of guanylyl cyclase C is specified by a cytosolic signal
    • Hodson, C. A., Ambrogi, I. G., Scott, R. O., Mohler, P. J. and Milgram, S. L. (2006). Polarized apical sorting of guanylyl cyclase C is specified by a cytosolic signal. Traffic 7, 456-464.
    • (2006) Traffic , vol.7 , pp. 456-464
    • Hodson, C.A.1    Ambrogi, I.G.2    Scott, R.O.3    Mohler, P.J.4    Milgram, S.L.5
  • 28
    • 33750288538 scopus 로고    scopus 로고
    • ZP2 and ZP3 traffic independently within oocytes prior to assembly into the extracellular zona pellucida
    • DOI 10.1128/MCB.00904-06
    • Hoodbhoy, T., Aviles, M., Baibakov, B., Epifano, O., Jimenez-Movilla, M., Gauthier, L. and Dean, J. (2006). ZP2 and ZP3 traffic independently within oocytes prior to assembly into the extracellular zona pellucida. Mol. Cell. Biol. 26, 7991-7998. (Pubitemid 44630998)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.21 , pp. 7991-7998
    • Hoodbhoy, T.1    Aviles, M.2    Baibakov, B.3    Epifano, O.4    Jimenez-Movilla, M.5    Gauthier, L.6    Dean, J.7
  • 30
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C. D., Chinenov, Y. and Kerppola, T. K. (2002). Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9, 789-798.
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 31
    • 10644290857 scopus 로고    scopus 로고
    • The telling tail of L-selectin
    • DOI 10.1042/BST0321118
    • Ivetic, A. and Ridley, A. J. (2004). The telling tail of L-selectin. Biochem. Soc. Trans. 32, 1118-1121. (Pubitemid 39655563)
    • (2004) Biochemical Society Transactions , vol.32 , Issue.6 , pp. 1118-1121
    • Ivetic, A.1    Ridley, A.J.2
  • 32
    • 75449089945 scopus 로고    scopus 로고
    • Insertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion, or abrogate functions in cell fusion and viral entry
    • Jackson, J. O., Lin, E., Spear, P. G. and Longnecker, R. (2010). Insertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion, or abrogate functions in cell fusion and viral entry. J. Virol. 84, 2038-2046.
    • (2010) J. Virol. , vol.84 , pp. 2038-2046
    • Jackson, J.O.1    Lin, E.2    Spear, P.G.3    Longnecker, R.4
  • 35
    • 0032549712 scopus 로고    scopus 로고
    • Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism
    • Kahn, J., Walcheck, B., Migaki, G. I., Jutila, M. A. and Kishimoto, T. K. (1998). Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism. Cell 92, 809-818.
    • (1998) Cell , vol.92 , pp. 809-818
    • Kahn, J.1    Walcheck, B.2    Migaki, G.I.3    Jutila, M.A.4    Kishimoto, T.K.5
  • 36
    • 33745785300 scopus 로고    scopus 로고
    • Visualization of molecular interactions by fluorescence complementation
    • Kerppola, T. K. (2006). Visualization of molecular interactions by fluorescence complementation. Nat. Rev. Mol. Cell Biol. 7, 449-456.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 449-456
    • Kerppola, T.K.1
  • 37
    • 65649085856 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of molecular interactions between calmodulin, ezrin/radixin/moesin, and L-selectin
    • Killock, D. J., Parsons, M., Zarrouk, M., Ameer-Beg, S. M., Ridley, A. J., Haskard, D. O., Zvelebil, M. and Ivetic, A. (2009). In vitro and in vivo characterization of molecular interactions between calmodulin, ezrin/radixin/moesin, and L-selectin. J. Biol. Chem. 284, 8833-8845.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8833-8845
    • Killock, D.J.1    Parsons, M.2    Zarrouk, M.3    Ameer-Beg, S.M.4    Ridley, A.J.5    Haskard, D.O.6    Zvelebil, M.7    Ivetic, A.8
  • 39
    • 33748328139 scopus 로고    scopus 로고
    • The matrix reorganized: Extracellular matrix remodeling and integrin signaling
    • Larsen, M., Artym, V. V., Green, J. A. and Yamada, K. M. (2006). The matrix reorganized: extracellular matrix remodeling and integrin signaling. Curr. Opin. Cell Biol. 18, 463-471.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 463-471
    • Larsen, M.1    Artym, V.V.2    Green, J.A.3    Yamada, K.M.4
  • 40
    • 0030889074 scopus 로고    scopus 로고
    • The mouse tectorins: Modular matrix proteins of the inner ear homologous to components of the sperm-egg adhesion system
    • DOI 10.1074/jbc.272.13.8791
    • Legan, P. K., Rau, A., Keen, J. N. and Richardson, G. P. (1997). The mouse tectorins. Modular matrix proteins of the inner ear homologous to components of the sperm-egg adhesion system. J. Biol. Chem. 272, 8791-8801. (Pubitemid 27147850)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.13 , pp. 8791-8801
    • Legan, P.K.1    Rau, A.2    Keen, J.N.3    Richardson, G.P.4
  • 41
    • 0025255277 scopus 로고
    • Oocyte-specific expression of mouse Zp-2: Developmental regulation of the zona pellucida genes
    • Liang, L.-F., Chamow, S. M. and Dean, J. (1990). Oocyte-specific expression of mouse Zp-2: Developmental regulation of the zona pellucida genes. Mol. Cell. Biol. 10, 15071515.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 15071515
    • Liang, L.-F.1    Chamow, S.M.2    Dean, J.3
  • 42
    • 9344231925 scopus 로고    scopus 로고
    • Targeted disruption of the mZP3 gene results in production of eggs lacking a zona pellucida and infertility in female mice
    • Liu, C., Litscher, E. S., Mortillo, S., Sakai, Y., Kinloch, R. A., Stewart, C. L. and Wassarman, P. M. (1996). Targeted disruption of the mZP3 gene results in production of eggs lacking a zona pellucida and infertility in female mice. Proc. Natl. Acad. Sci. USA 93, 5431-5436.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5431-5436
    • Liu, C.1    Litscher, E.S.2    Mortillo, S.3    Sakai, Y.4    Kinloch, R.A.5    Stewart, C.L.6    Wassarman, P.M.7
  • 43
    • 0025301112 scopus 로고
    • Genomic mapping of murine Zp-2 and Zp-3, two oocyte-specific loci encoding zona pellucida proteins
    • DOI 10.1016/0888-7543(90)90465-7
    • Lunsford, R. D., Jenkins, N. A., Kozak, C. A., Liang, L.-F., Silan, C. M., Copeland, N. G. and Dean, J. (1990). Genomic mapping of murine Zp-2 and Zp-3, two oocyte-specific loci encoding zona pellucida proteins. Genomics 6, 184-187. (Pubitemid 20172371)
    • (1990) Genomics , vol.6 , Issue.1 , pp. 184-187
    • Lunsford, R.D.1    Jenkins, N.A.2    Kozak, C.A.3    Liang, L.-F.4    Silan, C.M.5    Copeland, N.G.6    Dean, J.7
  • 44
    • 11844252081 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: Scope and mechanism
    • DOI 10.1021/ja046699g
    • Magliery, T. J., Wilson, C. G., Pan, W., Mishler, D., Ghosh, I., Hamilton, A. D. and Regan, L. (2005). Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism. J. Am. Chem. Soc. 127, 146-157. (Pubitemid 40094379)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.1 , pp. 146-157
    • Magliery, T.J.1    Wilson, C.G.M.2    Pan, W.3    Mishler, D.4    Ghosh, I.5    Hamilton, A.D.6    Regan, L.7
  • 45
    • 0038620130 scopus 로고    scopus 로고
    • Differential distribution of low-density lipoprotein-receptor-related protein (LRP) and megalin in polarized epithelial cells is determined by their cytoplasmic domains
    • Marzolo, M. P., Yuseff, M. I., Retamal, C., Donoso, M., Ezquer, F., Farfan, P., Li, Y. and Bu, G. (2003). Differential distribution of low-density lipoprotein-receptor-related protein (LRP) and megalin in polarized epithelial cells is determined by their cytoplasmic domains. Traffic 4, 273-288. (Pubitemid 36665387)
    • (2003) Traffic , vol.4 , Issue.4 , pp. 273-288
    • Marzolo, M.-P.1    Yuseff, M.I.2    Retamal, C.3    Donoso, M.4    Ezquer, F.5    Farfan, P.6    Li, Y.7    Bu, G.8
  • 46
    • 0015126814 scopus 로고
    • An electron microscopic study of mouse eggs matured in vivo and in vitro
    • Merchant, H. and Chang, M. C. (1971). An electron microscopic study of mouse eggs matured in vivo and in vitro. Anat. Rec. 171, 21-37.
    • (1971) Anat. Rec. , vol.171 , pp. 21-37
    • Merchant, H.1    Chang, M.C.2
  • 47
    • 0026039805 scopus 로고
    • Oocyte-Specific Factors Bind a Conserved Upstream Sequence Required for Mouse Zona Pellucida Promoter Activity
    • Millar, S. E., Lader, E., Liang, L.-F. and Dean, J. (1991). Oocyte-specific factors bind a conserved upstream sequence required for mouse zona pellucida promoter activity. Mol. Cell. Biol. 12, 6197-6204. (Pubitemid 21895393)
    • (1991) Molecular and Cellular Biology , vol.11 , Issue.12 , pp. 6197-6204
    • Millar, S.E.1    Lader, E.2    Liang, L.-F.3    Dean, J.4
  • 48
    • 0014804269 scopus 로고
    • The role of the zona pellucida in the development of mouse eggs in vivo
    • Modlinski, J. A. (1970). The role of the zona pellucida in the development of mouse eggs in vivo. J. Embryol. Exp. Morphol. 23, 539-547.
    • (1970) J. Embryol. Exp. Morphol. , vol.23 , pp. 539-547
    • Modlinski, J.A.1
  • 49
    • 0028260347 scopus 로고
    • O-linked trisaccharide and N-Linked poly-N-acetyllactosaminyl glycans are present on mouse ZP2 and ZP3
    • Nagdas, S. K., Araki, Y., Chayko, C. A., Orgebin-Crist, M.-C. and Tulsiani, D. R. P. (1994). O-linked trisaccharide and N-Linked poly-N-acetyllactosaminyl glycans are present on mouse ZP2 and ZP3. Biol. Reprod. 51, 262-272.
    • (1994) Biol. Reprod. , vol.51 , pp. 262-272
    • Nagdas, S.K.1    Araki, Y.2    Chayko, C.A.3    Orgebin-Crist, M.-C.4    Tulsiani, D.R.P.5
  • 51
    • 0035675828 scopus 로고    scopus 로고
    • Molecular genetics of hearing loss
    • DOI 10.1146/annurev.genet.35.102401.091224
    • Petit, C., Levilliers, J. and Hardelin, J. P. (2001). Molecular genetics of hearing loss. Annu. Rev. Genet. 35, 589-646. (Pubitemid 34032988)
    • (2001) Annual Review of Genetics , vol.35 , pp. 589-646
    • Petit, C.1    Levilliers, J.2    Hardelin, J.-P.3
  • 52
    • 0019198150 scopus 로고
    • Surface architecture of the mouse and hamster zona pellucida and oocyte
    • DOI 10.1016/S0022-5320(80)90129-X
    • Phillips, D. M. and Shalgi, R. (1980). Surface architecture of the mouse and hamster zona pellucida and oocyte. J. Ultrastruct. Res. 72, 1-12. (Pubitemid 11232038)
    • (1980) Journal of Ultrastructure Research , vol.72 , Issue.1 , pp. 1-12
    • Phillips, D.M.1    Shalgi, R.2
  • 53
    • 0029818998 scopus 로고    scopus 로고
    • Mice homozygous for an insertional mutation in the Zp3 gene lack a zona pellucida and are infertile
    • Rankin, T., Familari, M., Lee, E., Ginsberg, A. M., Dwyer, N., Blanchette-Mackie, J., Drago, J., Westphal, H. and Dean, J. (1996). Mice homozygous for an insertional mutation in the Zp3 gene lack a zona pellucida and are infertile. Development 122, 2903-2910. (Pubitemid 26326521)
    • (1996) Development , vol.122 , Issue.9 , pp. 2903-2910
    • Rankin, T.1    Familari, M.2    Lee, E.3    Ginsberg, A.4    Dwyer, N.5    Blanchette-Mackie, J.6    Drago, J.7    Westphal, H.8    Dean, J.9
  • 54
    • 0032821285 scopus 로고    scopus 로고
    • Abnormal zonae pellucidae in mice lacking ZP1 result in early embryonic loss
    • Rankin, T., Talbot, P., Lee, E. and Dean, J. (1999). Abnormal zonae pellucidae in mice lacking ZP1 result in early embryonic loss. Development 126, 3847-3855. (Pubitemid 29440482)
    • (1999) Development , vol.126 , Issue.17 , pp. 3847-3855
    • Rankin, T.1    Talbot, P.2    Lee, E.3    Dean, J.4
  • 55
    • 0035029161 scopus 로고    scopus 로고
    • Defective zonae pellucidae in Zp2-null mice disrupt folliculogenesis, fertility and development
    • Rankin, T. L., O'Brien, M., Lee, E., Wigglesworth, K. E. J. J. and Dean, J. (2001). Defective zonae pellucidae in Zp2 null mice disrupt folliculogenesis, fertility and development. Development 128, 1119-1126. (Pubitemid 32401427)
    • (2001) Development , vol.128 , Issue.7 , pp. 1119-1126
    • Rankin, T.L.1    O'Brien, M.2    Lee, E.3    Wigglesworth, K.4    Eppig, J.5    Dean, J.6
  • 58
    • 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. and 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
  • 59
    • 0021092835 scopus 로고
    • Biosynthesis of the sperm receptor during oogenesis in the mouse
    • Salzmann, G. S., Greve, J. M., Roller, R. J. and Wassarman, P. M. (1983). Biosynthesis of the sperm receptor during oogenesis in the mouse. EMBO J. 2, 1451-1456.
    • (1983) EMBO J. , vol.2 , pp. 1451-1456
    • Salzmann, G.S.1    Greve, J.M.2    Roller, R.J.3    Wassarman, P.M.4
  • 60
    • 34248167590 scopus 로고    scopus 로고
    • Distinct Steps of Cross-linking, Self-association, and Maturation of Tropoelastin Are Necessary for Elastic Fiber Formation
    • DOI 10.1016/j.jmb.2007.03.060, PII S0022283607004251
    • Sato, F., Wachi, H., Ishida, M., Nonaka, R., Onoue, S., Urban, Z., Starcher, B. C. and Seyama, Y. (2007). Distinct steps of cross-linking, self-association, and maturation of tropoelastin are necessary for elastic fiber formation. J. Mol. Biol. 369, 841-851. (Pubitemid 46709924)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.3 , pp. 841-851
    • Sato, F.1    Wachi, H.2    Ishida, M.3    Nonaka, R.4    Onoue, S.5    Urban, Z.6    Starcher, B.C.7    Seyama, Y.8
  • 61
    • 61949278337 scopus 로고    scopus 로고
    • Analysis of uromodulin polymerization provides new insights into the mechanisms regulating ZP domain-mediated protein assembly
    • Schaeffer, C., Santambrogio, S., Perucca, S., Casari, G. and Rampoldi, L. (2009). Analysis of uromodulin polymerization provides new insights into the mechanisms regulating ZP domain-mediated protein assembly. Mol. Biol. Cell 20, 589-599.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 589-599
    • Schaeffer, C.1    Santambrogio, S.2    Perucca, S.3    Casari, G.4    Rampoldi, L.5
  • 62
    • 58149185093 scopus 로고    scopus 로고
    • Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes
    • Schoberer, J., Vavra, U., Stadlmann, J., Hawes, C., Mach, L., Steinkellner, H. and Strasser, R. (2009). Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes. Traffic 10, 101-115.
    • (2009) Traffic , vol.10 , pp. 101-115
    • Schoberer, J.1    Vavra, U.2    Stadlmann, J.3    Hawes, C.4    Mach, L.5    Steinkellner, H.6    Strasser, R.7
  • 63
    • 0020641707 scopus 로고
    • In vitro biosynthesis of three sulfated glycoproteins of murine zonae pellucidae by oocytes grown in follicle culture
    • Shimizu, S., Tsuji, M. and 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. (Pubitemid 13096508)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.9 , pp. 5858-5863
    • Shimizu, S.1    Tsuji, M.2    Dean, J.3
  • 64
  • 65
    • 72449210973 scopus 로고    scopus 로고
    • The developmental roles of the extracellular matrix: Beyond structure to regulation
    • Tsang, K. Y., Cheung, M. C., Chan, D. and Cheah, K. S. (2010). The developmental roles of the extracellular matrix: beyond structure to regulation. Cell Tissue Res. 339, 93-110.
    • (2010) Cell Tissue Res. , vol.339 , pp. 93-110
    • Tsang, K.Y.1    Cheung, M.C.2    Chan, D.3    Cheah, K.S.4
  • 66
    • 54049085798 scopus 로고    scopus 로고
    • Zona pellucida glycoproteins
    • Wassarman, P. M. (2008). Zona pellucida glycoproteins. J. Biol. Chem. 283, 24285-24289.
    • (2008) J. Biol. Chem. , vol.283 , pp. 24285-24289
    • Wassarman, P.M.1
  • 67
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • (ed. E. Knobil and J. Neil), New York: Raven Press
    • Yanagimachi, R. (1994). Mammalian fertilization. In The Physiology of Reproduction (ed. E. Knobil and J. Neil), pp. 189-317. New York: Raven Press.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 69
    • 0036234958 scopus 로고    scopus 로고
    • Conserved furin cleavage site not essential for secretion and integration of ZP3 into the extracellular egg coat of transgenic mice
    • DOI 10.1128/MCB.22.9.3111-3120.2002
    • Zhao, M., Gold, L., Ginsberg, A. M., Liang, L.-F. and Dean, J. (2002). Conserved furin cleavage site not essential for secretion and integration of ZP3 into the extracellular egg coat of transgenic mice. Mol. Cell. Biol. 22, 3111-3120. (Pubitemid 34437469)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.9 , pp. 3111-3120
    • Zhao, M.1    Gold, L.2    Ginsberg, A.M.3    Liang, L.-F.4    Dean, J.5
  • 70
    • 0344629667 scopus 로고    scopus 로고
    • Mutation of a Conserved Hydrophobic Patch Prevents Incorporation of ZP3 into the Zona Pellucida Surrounding Mouse Eggs
    • DOI 10.1128/MCB.23.24.8982-8991.2003
    • Zhao, M., Gold, L., Dorward, H., Liang, L.-F., Hoodbhoy, T., Boja, E., Fales, H. and Dean, J. (2003). Mutation of a conserved hydrophobic patch prevents incorporation of ZP3 into the zona pellucida surrounding mouse eggs. Mol. Cell. Biol. 23, 8982-8991. (Pubitemid 37499789)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.24 , pp. 8982-8991
    • Zhao, M.1    Gold, L.2    Dorward, H.3    Liang, L.-F.4    Hoodbhoy, T.5    Boja, E.S.6    Fales, H.M.7    Dean, J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.