Stephan, Milena

[["dc.bibliographiccitation.firstpage","1987"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Analyst"],["dc.bibliographiccitation.lastpage","1992"],["dc.bibliographiccitation.volume","139"],["dc.contributor.author","Stephan, Milena"],["dc.contributor.author","Kramer, Corinna"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2017-09-07T11:46:55Z"],["dc.date.available","2017-09-07T11:46:55Z"],["dc.date.issued","2014"],["dc.description.abstract","Small molecule sensing is of great importance in pharmaceutical research. While there exist well established screening methods such as EMSA (electrophoretic motility shift assay) or biointeraction chromatography to report on successful binding interactions, there are only a few techniques that allow studying and quantifying the interaction of low molecular weight analytes with a binding partner directly. We report on a binding assay for small molecules based on the reflectivity change of a porous transparent film upon immobilisation of an absorbing substance on the pore walls. The porous matrix acts as a thin optical transparent film to produce interference fringes and accumulates molecules at the inner wall to amplify the sensor response. The benefits and limits of the assay are demonstrated by investigating the binding of biotin labelled with an atto dye to avidin physisorbed within an anodic aluminium oxide membrane."],["dc.identifier.doi","10.1039/c4an00009a"],["dc.identifier.fs","604886"],["dc.identifier.gro","3142213"],["dc.identifier.isi","000333081800024"],["dc.identifier.pmid","24599267"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11469"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5788"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: DFG [SFB 937 (A08)]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1364-5528"],["dc.relation.issn","0003-2654"],["dc.rights.access","openAccess"],["dc.title","Binding assay for low molecular weight analytes based on reflectometry of absorbing molecules in porous substrates"],["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"]]

[["dc.bibliographiccitation.artnumber","e85033"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Vilardi, Fabio"],["dc.contributor.author","Stephan, Milena"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:46:54Z"],["dc.date.available","2017-09-07T11:46:54Z"],["dc.date.issued","2014"],["dc.description.abstract","Tail-Anchored (TA) proteins are inserted into the endoplasmic reticulum (ER) membrane of yeast cells via the posttranslational Guided Entry of Tail-Anchored protein (GET) pathway. The key component of this targeting machinery is the ATPase Get3 that docks to the ER membrane by interacting with a receptor complex formed by the proteins Get1 and Get2. A conserved pathway is present in higher eukaryotes and is mediated by TRC40, homolog of Get3, and the recently identified membrane receptors WRB and CAML. Here, we used yeast lacking the GET1 and GET2 genes and substituted them with WRB and CAML. This rescued the growth phenotypes of the GET receptor mutant. We demonstrate that WRB and CAML efficiently recruit Get3 to the ER membrane and promote the targeting of the TA proteins in vivo. Our results show that the membrane spanning segments of CAML are essential to create a functional receptor with WRB and to ensure TA protein membrane insertion. Finally, we determined the binding parameters of TRC40 to the WRB/CAML receptor. We conclude that together, WRB and CAML are not only necessary but also sufficient to create a functional membrane receptor complex for TRC40. The yeast complementation assay can be used to further dissect the structure-function relationship of the WRB/CAML heteromultimer in the absence of endogenous receptor proteins."],["dc.description.sponsorship","Open-Access-Publikatinsfonds 2014"],["dc.identifier.doi","10.1371/journal.pone.0085033"],["dc.identifier.gro","3142201"],["dc.identifier.isi","000329460100086"],["dc.identifier.pmid","24392163"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9662"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5654"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: University Medicine Gottingen"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","WRB and CAML Are Necessary and Sufficient to Mediate Tail-Anchored Protein Targeting to the ER Membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]