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Vitellogenin C-terminal fragments participate in fertilization as egg-coat binding partners of sperm trypsin-like proteases in the ascidian Halocynthia roretzi

7 Jan 2010

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PMID: 20059971
DOI: 10.1016/j.bbrc.2010.01.006

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Related research

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Vitellogenin C-terminal fragments participate in fertilization as egg-coat binding partners of sperm trypsin-like proteases in the ascidian Halocynthia roretziPMID 20059971Read ↗

Isolated ZP-N domains constitute the N-terminal extensions of Zona Pellucida proteinsSemantic proximity Read ↗

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The Caenorhabditis elegans CPI-2a Cystatin-like Inhibitor Has an Essential Regulatory Role during Oogenesis and FertilizationSemantic proximity Read ↗

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Sperm Proteasomes Degrade Sperm Receptor on the Egg Zona Pellucida during Mammalian FertilizationSemantic proximity Read ↗

Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coatsSemantic proximity Read ↗

A Structural View of Egg Coat Architecture and Function in Fertilization1Semantic proximity Read ↗

Fundulus heteroclitus vitellogenin: The deduced primary structure of a piscine precursor to noncrystalline, liquid-phase yolk proteinSemantic proximity Read ↗

Glycosylated Chicken ZP2 Accumulates in the Egg Coat of Immature Oocytes and Remains Localized to the Germinal Disc Region of Mature Eggs1Semantic proximity Read ↗

Divergent molecular signatures in fish Bouncer proteins define cross-fertilization boundariesSemantic proximity Read ↗

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