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The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle

The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle

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BRÜSTLE, Berit, Sabine KREISSL, Donald L. MYKLES, Werner RATHMAYER, 2001. The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle. In: Journal of experimental biology. 204(15), pp. 2627-2635

@article{Brustle2001neuro-16257, title={The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle}, year={2001}, 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} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/16257"> <dc:creator>Kreißl, Sabine</dc:creator> <dc:contributor>Kreißl, Sabine</dc:contributor> <dc:contributor>Mykles, Donald L.</dc:contributor> <dcterms:title>The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle</dcterms:title> <dc:creator>Rathmayer, Werner</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-10-10T08:11:11Z</dcterms:available> <dc:language>eng</dc:language> <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:creator>Mykles, Donald L.</dc:creator> <dcterms:issued>2001</dcterms:issued> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/16257"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-10-10T08:11:11Z</dc:date> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dcterms:bibliographicCitation>Fist publ. in: Journal of experimental biology ; 204 (2001), 15. - pp. 2627-2635</dcterms:bibliographicCitation> <dc:contributor>Rathmayer, Werner</dc:contributor> <dc:contributor>Brüstle, Berit</dc:contributor> <dc:creator>Brüstle, Berit</dc:creator> <dc:rights>deposit-license</dc:rights> </rdf:Description> </rdf:RDF>

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