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Edda Töpfer-Petersen

Researcher at University of Veterinary Medicine Vienna

Publications -  115
Citations -  5556

Edda Töpfer-Petersen is an academic researcher from University of Veterinary Medicine Vienna. The author has contributed to research in topics: Sperm & Zona pellucida. The author has an hindex of 46, co-authored 115 publications receiving 5376 citations. Previous affiliations of Edda Töpfer-Petersen include University of Veterinary Medicine Hanover & Hochschule Hannover.

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Spermadhesins: A new protein family. Facts, hypotheses and perspectives

TL;DR: Spermadhesins are a novel family of secretory proteins expressed in the male genital tract of pig, horse and bull and have been found to be peripherally associated to the sperm surface, suggesting that they may be involved in different steps of fertilization.
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The crystal structures of two spermadhesins reveal the CUB domain fold

TL;DR: The authors reported the crystal structures of porcine seminal plasma PSP-I/PSP-II, a heterodimer of two glycosylated spermadhesins, and bovine aSFP at 2.4 A and 1.9 A resolution respectively.
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Selective sperm binding to pig oviductal epithelium in vitro.

TL;DR: Individual differences revealed by this study and their relation to morphology and contact of spermatozoa with seminal fluid indicate a selective function of sperm-oviduct binding.
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Isolation and characterization of heparin‐ and phosphorylcholine‐binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1

TL;DR: The characterization of heparin‐ and phosphorylcholine‐binding proteins of stallion and boar seminal plasma tie in with the hypothesis that homologous proteins from different mammalian species may display distinct biological activities, which may be related to species‐specific aspects of sperm physiology.
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The role of stallion seminal proteins in fertilisation.

TL;DR: The major proteins of equine seminal plasma have been isolated and characterised regarding their expression along the male genital tract, protein structure and their functions.