@article{Brustle2001neuro-16257,
  year={2001},
  title={The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle},
  number={15},
  volume={204},
  journal={Journal of experimental biology},
  pages={2627--2635},
  author={Brüstle, Berit and Kreißl, Sabine and Mykles, Donald L. and Rathmayer, Werner}
}

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    <dc:creator>Mykles, Donald L.</dc:creator>
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    <dc:contributor>Kreißl, Sabine</dc:contributor>
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    <dcterms:title>The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle</dcterms:title>
    <dc:contributor>Rathmayer, Werner</dc:contributor>
    <dcterms:issued>2001</dcterms:issued>
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    <dcterms:bibliographicCitation>Fist publ. in: Journal of experimental biology ; 204 (2001), 15. - pp. 2627-2635</dcterms:bibliographicCitation>
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    <dcterms:abstract xml:lang="eng">In the isopod Idotea emarginata, the neuropeptide proctolin is contained in a single pair of motoneurones located in pereion ganglion 4. The two neurones supply dorsal extensor muscle fibres of all segments. Proctolin (1μmoll−1) potentiates the amplitude of contractures of single extensor muscle fibres elicited by 10mmoll−1 caffeine. In western blots of myofibrillar proteins isolated from single muscle fibres and treated with an anti-phosphoserine antibody, a protein with an apparent molecular mass of 30kDa was consistently found. The phosphorylation of this protein was significantly increased by treating the fibres with proctolin. After separation of myofibrillar filaments, a 30kDa protein was found only in the thin filament fraction. This protein is phosphorylated and detected by an antiserum against crustacean troponin I.</dcterms:abstract>
    <dc:contributor>Mykles, Donald L.</dc:contributor>
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