Linked Life Data

18793139

Source:http://linkedlifedata.com/resource/pubmed/id/18793139

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 5
pubmed:dateCreated
2008-9-16
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0300-5127
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
797-801
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Ubiquitin ligase E6-AP and its role in human disease.
pubmed:affiliation
Laboratory of Cellular Biochemistry, Department of Biology, University of Konstanz, 78457 Konstanz, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't