Ubiquitin ligase E6-AP and its role in human disease


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MATENTZOGLU, Konstantin, Martin SCHEFFNER, 2008. Ubiquitin ligase E6-AP and its role in human disease. In: Biochem Society Transactions. 36(5), pp. 797-801. ISSN 0300-5127. eISSN 1470-8752

@article{Matentzoglu2008Ubiqu-1267, title={Ubiquitin ligase E6-AP and its role in human disease}, year={2008}, doi={10.1042/BST0360797}, number={5}, volume={36}, issn={0300-5127}, journal={Biochem Society Transactions}, pages={797--801}, author={Matentzoglu, Konstantin 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/123456789/1267"> <dcterms:abstract>The ubiquitin ligase E6-AP (E6-associated protein) represents a prime example for the notion that deregulated modification of proteins with ubiquitin contributes to the development of human disease: loss of E6-AP function by mutation is responsible for the development of AS (Angelman syndrome), a neurological disorder, and unscheduled activation of E6-AP by complex formation with the E6 oncoprotein of HPVs (human papillomaviruses) contributes to cervical carcinogenesis. However, while there is a considerable amount of data concerning the oncogenic properties of the E6-E6-AP complex, only little is known about the function(s) of E6-AP in neurons. This is mainly due to the fact that although some E6-AP substrates have been identified, it is at present unclear whether deregulated modification/degradation of these proteins is involved in the pathogenesis of AS. Similarly, the cellular pathways involving E6-AP remain enigmatic. To obtain insights into the physiological functions of E6-AP, we are currently employing several strategies, including quantitative affinity proteomics and RNA interference approaches. The results obtained will eventually allow the introduction of E6-AP into functional protein networks and so reveal potential targets for molecular approaches in the treatment of E6-AP-associated diseases.</dcterms:abstract> <dc:creator>Scheffner, Martin</dc:creator> <dcterms:issued>2008</dcterms:issued> <dc:contributor>Matentzoglu, Konstantin</dc:contributor> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103416863-3868037-7"/> <dc:rights>deposit-license</dc:rights> <dc:contributor>Scheffner, Martin</dc:contributor> <dc:language>eng</dc:language> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-23T09:07:31Z</dcterms:available> <dcterms:title>Ubiquitin ligase E6-AP and its role in human disease</dcterms:title> <dcterms:bibliographicCitation>Publ. in: Biochem Society Transactions 36 (2008), pp. 797-801</dcterms:bibliographicCitation> <dc:creator>Matentzoglu, Konstantin</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-23T09:07:31Z</dc:date> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/1267"/> </rdf:Description> </rdf:RDF>

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