Ubiquitin, Ubiquitin-Like Proteins, and Proteasome-Mediated Degradation

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DOHMEN, R. Jürgen, Jon M. HUIBREGTSE, Martin SCHEFFNER, 2016. Ubiquitin, Ubiquitin-Like Proteins, and Proteasome-Mediated Degradation. In: BRADSHAW, Ralph A., ed., Philip D. STAHL, ed.. Molecular Cell Biology. Waltham:Elsevier, pp. 582-595. ISBN 978-0-12-394796-3

@inbook{Dohmen2016Ubiqu-36938, title={Ubiquitin, Ubiquitin-Like Proteins, and Proteasome-Mediated Degradation}, year={2016}, doi={10.1016/B978-0-12-394447-4.10069-0}, number={1}, isbn={978-0-12-394796-3}, address={Waltham}, publisher={Elsevier}, series={Encyclopedia of Cell Biology}, pages={582--595}, editor={Bradshaw, Ralph A. and Stahl, Philip D.}, author={Dohmen, R. Jürgen and Huibregtse, Jon M. and Scheffner, Martin} }

<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/123456789/36938"> <dcterms:issued>2016</dcterms:issued> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-01-25T07:01:02Z</dcterms:available> <dc:creator>Dohmen, R. Jürgen</dc:creator> <dc:contributor>Scheffner, Martin</dc:contributor> <dc:contributor>Dohmen, R. Jürgen</dc:contributor> <dc:language>eng</dc:language> <dcterms:title>Ubiquitin, Ubiquitin-Like Proteins, and Proteasome-Mediated Degradation</dcterms:title> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/36938"/> <dc:contributor>Huibregtse, Jon M.</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-01-25T07:01:02Z</dc:date> <dc:creator>Scheffner, Martin</dc:creator> <dc:creator>Huibregtse, Jon M.</dc:creator> <dcterms:abstract xml:lang="eng">Covalent modification of eukaryotic proteins by ubiquitin and ubiquitin-like proteins is involved in the control of many – if not all – cellular processes including protein quality control, cell cycle, DNA metabolism, and signal transduction. Conjugation of ubiquitin is mediated by an elaborate enzymatic cascade and in general alters the ability of the modified proteins to interact with other biomolecules, with serving as signal for proteasome-mediated degradation being the most studied and most prevalent function. Deregulation of the ubiquitin-proteasome system (UPS) has been associated with various human diseases including cancer and neurological disorders and, thus, components of the UPS have emerged as pharmacological targets.</dcterms:abstract> </rdf:Description> </rdf:RDF>

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