@article{8596295074cd11dbbee902004c4f4f50,
title = "The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity",
abstract = "Neuropeptides containing the C-terminal sequence Arg-Phe-NH2 (RFamide) occur throughout the Animal Kingdom and are abundant in evolutionarily 'old' nervous systems such as those of cnidarians. From the hydromedusa Polyorchis penicillatus we have previously isolated two neuropeptides, Pol-RFamide I (",
keywords = "Amino Acid Sequence, Animals, Base Sequence, Biological Evolution, Cnidaria, Endopeptidases, Gene Library, Insect Hormones, Molecular Sequence Data, Neuropeptides, Oligodeoxyribonucleotides, Protein Precursors, Protein Processing, Post-Translational, Protein Sorting Signals, Restriction Mapping, Sequence Homology, Amino Acid",
author = "C Schmutzler and D Diekhoff and Grimmelikhuijzen, {C J}",
year = "1994",
month = apr,
day = "15",
language = "English",
volume = "299 ( Pt 2)",
pages = "431--436",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "299",
}