Koch, Philipp

[["dc.bibliographiccitation.firstpage","1473"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","European Journal of Pediatrics"],["dc.bibliographiccitation.lastpage","1478"],["dc.bibliographiccitation.volume","168"],["dc.contributor.author","Lenk, Christian"],["dc.contributor.author","Koch, Philipp"],["dc.contributor.author","Zappel, Hildegard"],["dc.contributor.author","Wiesemann, Claudia"],["dc.date.accessioned","2017-10-16T10:54:26Z"],["dc.date.available","2017-10-16T10:54:26Z"],["dc.date.issued","2009"],["dc.description.abstract","ff-label drug use in paediatrics is associated with an increased risk of adverse drug reactions. Any risk-benefit analysis has to be based on value judgments that should include parents' views. However, nothing is known so far about the parents' perspective on this critical issue. Therefore, a quantitative survey with parents of healthy and chronically ill children was carried out (n = 94). Knowledge about the practise of off-label use is generally poor in both groups. Surprisingly, this is also true for the parents of children with chronic disease. Nine percent of the parents of chronically ill children and 20% of the parents of healthy children would refuse treatment with an off-label drug. Parents who have poor knowledge about the practise of off-label use tend to refuse to volunteer their child for study participation. Therefore, the information of parents on the off-label use of drugs is important to meet ethical standards and to increase the parents' acceptance of medical studies with children."],["dc.identifier.doi","10.1007/s00431-009-0956-6"],["dc.identifier.gro","3146729"],["dc.identifier.pmid","19277709"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3759"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/9402"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","public"],["dc.relation.issn","0340-6199"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Off-label, off-limits? Parental awareness and attitudes towards off-label use in paediatrics"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","525"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Acta Neuropathologica"],["dc.bibliographiccitation.lastpage","537"],["dc.bibliographiccitation.volume","131"],["dc.contributor.author","Kumar, Sathish"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Stueber, Kathrin"],["dc.contributor.author","Wunderlich, Patrick"],["dc.contributor.author","Koch, Philipp"],["dc.contributor.author","Theil, Sandra"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Bruestle, Oliver"],["dc.contributor.author","Thal, Dietmar Rudolf"],["dc.contributor.author","Walter, Jochen"],["dc.date.accessioned","2018-11-07T10:16:30Z"],["dc.date.available","2018-11-07T10:16:30Z"],["dc.date.issued","2016"],["dc.description.abstract","Aggregation and toxicity of the amyloid beta-peptide (A beta) are considered as critical events in the initiation and progression of Alzheimer's disease (AD). Recent evidence indicated that soluble oligomeric A beta assemblies exert pronounced toxicity, rather than larger fibrillar aggregates that deposit in the forms of extracellular plaques. While some rare mutations in the A beta sequence that cause early-onset AD promote the oligomerization, molecular mechanisms that induce the formation or stabilization of oligomers of the wild-type A beta remain unclear. Here, we identified an A beta variant phosphorylated at Ser26 residue (pSer26A beta) in transgenic mouse models of AD and in human brain that shows contrasting spatio-temporal distribution as compared to non-phosphorylated A beta (npA beta) or other modified A beta species. pSer26A beta is particularly abundant in intraneuronal deposits at very early stages of AD, but much less in extracellular plaques. pSer26A beta assembles into a specific oligomeric form that does not proceed further into larger fibrillar aggregates, and accumulates in characteristic intracellular compartments of granulovacuolar degeneration together with TDP-43 and phosphorylated tau. Importantly, pSer26A beta oligomers exert increased toxicity in human neurons as compared to other known A beta species. Thus, pSer26A beta could represent a critical species in the neurodegeneration during AD pathogenesis."],["dc.identifier.doi","10.1007/s00401-016-1546-0"],["dc.identifier.isi","000372297500003"],["dc.identifier.pmid","26898910"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13216"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41051"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","1432-0533"],["dc.relation.issn","0001-6322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Phosphorylation of the amyloid beta-peptide at Ser26 stabilizes oligomeric assembly and increases neurotoxicity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]