Papers associated with egg (and zp3)

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	Dicalcin, a zona pellucida protein that regulates fertilization competence of the egg coat in Xenopus laevis., Miwa N., J Physiol Sci. November 1, 2015; 65 (6): 507-14.
	Fertilization competence of the egg-coating envelope is regulated by direct interaction of dicalcin and gp41, the Xenopus laevis ZP3., Miwa N., Sci Rep. August 5, 2015; 5 12672.
	Corrigendum: Fertilization competence of the egg-coating envelope is regulated by direct interaction of dicalcin and gp41, the Xenopus laevis ZP3., Miwa N., Sci Rep. January 12, 2015; 5 15303.
	Dicalcin inhibits fertilization through its binding to a glycoprotein in the egg envelope in Xenopus laevis., Miwa N., J Biol Chem. May 14, 2010; 285 (20): 15627-15636.
	Glycoproteins of the vitelline envelope of Amphibian oocyte: biological and molecular characterization of ZPC component (gp41) in Bufo arenarum., Barisone GA., Mol Reprod Dev. May 1, 2007; 74 (5): 629-40.
	Isolation and mapping the chicken zona pellucida genes: an insight into the evolution of orthologous genes in different species., Smith J., Mol Reprod Dev. February 1, 2005; 70 (2): 133-45.
	CpZPC, a newt ZPC molecule, localizes to the inner surface of the egg envelope., Makabe-Kobayashi Y., Int J Dev Biol. February 1, 2003; 47 (1): 51-8.
	Cell surface beta-1,4-galactosyltransferase-I activates G protein-dependent exocytotic signaling., Shi X., Development. March 1, 2001; 128 (5): 645-54.
	Egg envelope glycoprotein gp37 as a Xenopus homolog of mammalian ZP1, based on cDNA cloning., Kubo H., Dev Growth Differ. August 1, 2000; 42 (4): 419-27.
	Analyses of oviductal pars recta-induced fertilizability of coelomic eggs in Xenopus laevis., Katagiri C., Dev Biol. June 15, 1999; 210 (2): 269-76.
	Oviductin, the Xenopus laevis oviductal protease that processes egg envelope glycoprotein gp43, increases sperm binding to envelopes, and is translated as part of an unusual mosaic protein composed of two protease and several CUB domains., Lindsay LL., Biol Reprod. April 1, 1999; 60 (4): 989-95.
	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., Takeuchi Y., Eur J Biochem. March 1, 1999; 260 (3): 736-42.
	Molecular basis for oviductin-mediated processing from gp43 to gp41, the predominant glycoproteins of Xenopus egg envelopes., Kubo H., Dev Genet. January 1, 1999; 25 (2): 123-9.
	cDNA cloning and sequence analysis of the Xenopus laevis egg envelope glycoprotein gp43., Yang JC., Dev Growth Differ. August 1, 1997; 39 (4): 457-67.
	A major glycoprotein of Xenopus egg vitelline envelope, gp41, is a frog homolog of mammalian ZP3., Kubo H., Dev Growth Differ. August 1, 1997; 39 (4): 405-17.
	Xenopus laevis sperm-egg adhesion is regulated by modifications in the sperm receptor and the egg vitelline envelope., Tian J., Dev Biol. July 15, 1997; 187 (2): 143-53.
	Gamete interactions in Xenopus laevis: identification of sperm binding glycoproteins in the egg vitelline envelope., Tian J., J Cell Biol. March 10, 1997; 136 (5): 1099-108.
	Oviductin. Purification and properties of the oviductal protease that processes the molecular weight 43,000 glycoprotein of the Xenopus laevis egg envelope., Hardy DM., Biochemistry. May 12, 1992; 31 (18): 4466-72.

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