Schueren, Fabian

[["dc.bibliographiccitation.firstpage","81"],["dc.bibliographiccitation.lastpage","92"],["dc.bibliographiccitation.seriesnr","1595"],["dc.contributor.author","Hofhuis, Julia"],["dc.contributor.author","Dieterle, Severin"],["dc.contributor.author","George, Rosemol"],["dc.contributor.author","Schueren, Fabian"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.editor","Schrader, M."],["dc.date.accessioned","2018-10-08T09:34:19Z"],["dc.date.available","2018-10-08T09:34:19Z"],["dc.date.issued","2017"],["dc.description.abstract","Translational readthrough, the decoding of stop codons as sense codons, leads to C-terminal extension of proteins which may lead to the formation of protein isoforms with distinct properties from the original protein. Two proteins have recently been identified that are targeted to the peroxisome via hidden peroxisomal targeting signals in their readthrough extensions. This noninduced basal translational readthrough can be distinguished from pharmacological induction of readthrough by aminoglycosides or other small molecules, which can be used for the treatment of diseases caused by premature stop (termination) codons (PTCs). Readthrough of both, natural stop codons and PTCs, can be quantified in cell culture using reporter systems. In the present article, we describe two dual reporter systems, based on combined fluorescence/luminescence measurement and flow cytometric fluorescence measurement, respectively. Further, we provide a protocol for a fast and efficient cloning procedure of reporter constructs. The dual reporter systems described here help to analyze the peroxisome-specific isoforms of readthrough enzymes as well as potential readthrough therapeutics."],["dc.fs.pkfprnr","54350"],["dc.identifier.doi","10.1007/978-1-4939-6937-1_9"],["dc.identifier.fs","632465"],["dc.identifier.pmid","28409454"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15877"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.publisher","Humana Press"],["dc.publisher.place","New York"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.eisbn","978-1-4939-6937-1"],["dc.relation.isbn","978-1-4939-6935-7"],["dc.relation.ispartof","Peroxisomes"],["dc.relation.ispartofseries","Methods in Molecular Biology;1595"],["dc.title","Dual Reporter Systems for the Analysis of Translational Readthrough in Mammals"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"],["local.message.claim","2020-08-07T08:23:16.626+0000|||rp114519|||submit_approve|||dc_contributor_author|||None"]]

[["dc.bibliographiccitation.artnumber","e03640"],["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Schueren, Fabian"],["dc.contributor.author","Lingner, Thomas"],["dc.contributor.author","George, Rosemol"],["dc.contributor.author","Hofhuis, Julia"],["dc.contributor.author","Dickel, Corinna"],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Thoms, Sven"],["dc.date.accessioned","2017-09-07T11:45:30Z"],["dc.date.available","2017-09-07T11:45:30Z"],["dc.date.issued","2014"],["dc.description.abstract","Translational readthrough gives rise to low abundance proteins with C-terminal extensions beyond the stop codon. To identify functional translational readthrough, we estimated the readthrough propensity (RTP) of all stop codon contexts of the human genome by a new regression model in silico, identified a nucleotide consensus motif for high RTP by using this model, and analyzed all readthrough extensions in silico with a new predictor for peroxisomal targeting signal type 1 (PTS1). Lactate dehydrogenase B (LDHB) showed the highest combined RTP and PTS1 probability. Experimentally we show that at least 1.6% of the total cellular LDHB getting targeted to the peroxisome by a conserved hidden PTS1. The readthrough-extended lactate dehydrogenase subunit LDHBx can also co-import LDHA, the other LDH subunit into peroxisomes. Peroxisomal LDH is conserved in mammals and likely contributes to redox equivalent regeneration in peroxisomes."],["dc.identifier.doi","10.7554/eLife.03640"],["dc.identifier.gro","3142048"],["dc.identifier.isi","000342090300002"],["dc.identifier.pmid","25247702"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11685"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3967"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elife Sciences Publications Ltd"],["dc.relation.issn","2050-084X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Peroxisomal lactate dehydrogenase is generated by translational readthrough in mammals"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"],["local.message.claim","2020-08-07T08:23:16.626+0000|||rp114519|||submit_approve|||dc_contributor_author|||None"]]