The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity. / Schmutzler, C; Diekhoff, D; Grimmelikhuijzen, C J.

In: Biochemical Journal, Vol. 299 ( Pt 2), No. 299, 15.04.1994, p. 431-436.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Schmutzler, C, Diekhoff, D & Grimmelikhuijzen, CJ 1994, 'The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity', Biochemical Journal, vol. 299 ( Pt 2), no. 299, pp. 431-436.

APA

Schmutzler, C., Diekhoff, D., & Grimmelikhuijzen, C. J. (1994). The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity. Biochemical Journal, 299 ( Pt 2)(299), 431-436.

Vancouver

Schmutzler C, Diekhoff D, Grimmelikhuijzen CJ. The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity. Biochemical Journal. 1994 Apr 15;299 ( Pt 2)(299):431-436.

Author

Schmutzler, C ; Diekhoff, D ; Grimmelikhuijzen, C J. / The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity. In: Biochemical Journal. 1994 ; Vol. 299 ( Pt 2), No. 299. pp. 431-436.

Bibtex

@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",

}

RIS

TY - JOUR

T1 - The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity

AU - Schmutzler, C

AU - Diekhoff, D

AU - Grimmelikhuijzen, C J

PY - 1994/4/15

Y1 - 1994/4/15

N2 - 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 (

AB - 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 (

KW - Amino Acid Sequence

KW - Animals

KW - Base Sequence

KW - Biological Evolution

KW - Cnidaria

KW - Endopeptidases

KW - Gene Library

KW - Insect Hormones

KW - Molecular Sequence Data

KW - Neuropeptides

KW - Oligodeoxyribonucleotides

KW - Protein Precursors

KW - Protein Processing, Post-Translational

KW - Protein Sorting Signals

KW - Restriction Mapping

KW - Sequence Homology, Amino Acid

M3 - Journal article

C2 - 7909659

VL - 299 ( Pt 2)

SP - 431

EP - 436

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 299

ER -

ID: 248899