Ries, Annika

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Schuette, O. M."],["dc.contributor.author","Orth, Alexander"],["dc.contributor.author","Ries, Annika"],["dc.contributor.author","Werz, Daniel B."],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2018-11-07T09:22:34Z"],["dc.date.available","2018-11-07T09:22:34Z"],["dc.date.issued","2013"],["dc.format.extent","S130"],["dc.identifier.isi","000330215300368"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29376"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Lisbon, PORTUGAL"],["dc.relation.issn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.title","Modulating the phase separation in pore-spanning lipid bilayers"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2436"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Langmuir"],["dc.bibliographiccitation.lastpage","2444"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Stefaniu, Cristina"],["dc.contributor.author","Ries, Annika"],["dc.contributor.author","Gutowski, Olof"],["dc.contributor.author","Ruett, Uta"],["dc.contributor.author","Seeberger, Peter H."],["dc.contributor.author","Werz, Daniel B."],["dc.contributor.author","Brezesinski, Gerald"],["dc.date.accessioned","2018-11-07T10:16:49Z"],["dc.date.available","2018-11-07T10:16:49Z"],["dc.date.issued","2016"],["dc.description.abstract","The molecular interactions of three biologically important galactocerebrosides have been studied in monolayers formed at the soft air/water interface as 2D model membranes. Highly surface-sensitive techniques as GIXD (grazing incidence X-ray diffraction), IRRAS (infrared reflection absorption spectroscopy), and BAM (Brewster angle microscopy) have been used. The study reveals that small differences in the chemical structure have a relevant impact on the physical chemical properties and intermolecular interactions. The presence of a 2-D-hydroxyl group in the fatty acid favored for GalCer C24:0 (2-0H) monolayers a higher hydration state of the headgroup at low lateral pressures (<25 mN/m) and a higher condensation effect above 30 mN/m. An opposite behavior was recorded for GalCer 024:0 and GalCer C24:1, for which the intermolecular interactions are defined by the weakly hydrated but strong H-bonded interconnected head groups. Additionally, the 15-cis-double bond in the fatty acid chain (nervonic acid) of GalCer C24:1 stabilized the LE phase but did not disturb the packing parameters of the LC phase as compared with the saturated compound GalCer C24:0."],["dc.identifier.doi","10.1021/acs.langmuir.5b03830"],["dc.identifier.isi","000372391600017"],["dc.identifier.pmid","26907993"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41109"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0743-7463"],["dc.title","Impact of Structural Differences in Galactocerebrosides on the Behavior of 2D Monolayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Schubert, Thomas"],["dc.contributor.author","Sych, Taras"],["dc.contributor.author","Madl, Josef"],["dc.contributor.author","Xu, Maokai"],["dc.contributor.author","Omidvar, Ramin"],["dc.contributor.author","Patalag, Lukas J."],["dc.contributor.author","Ries, Annika"],["dc.contributor.author","Kettelhoit, Katharina"],["dc.contributor.author","Brandel, Annette"],["dc.contributor.author","Mely, Yves"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Werz, Daniel B."],["dc.contributor.author","Thuenauer, Roland"],["dc.contributor.author","Römer, Winfried"],["dc.date.accessioned","2021-04-14T08:25:45Z"],["dc.date.available","2021-04-14T08:25:45Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41598-020-66522-8"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81722"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2045-2322"],["dc.title","Differential recognition of lipid domains by two Gb3-binding lectins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2775"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","2778"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Schütte, Ole Mathis"],["dc.contributor.author","Patalag, Lukas J."],["dc.contributor.author","Weber, Lucas M. C."],["dc.contributor.author","Ries, Annika"],["dc.contributor.author","Römer, Winfried"],["dc.contributor.author","Werz, Daniel B."],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:43:46Z"],["dc.date.available","2017-09-07T11:43:46Z"],["dc.date.issued","2015"],["dc.description.abstract","Shiga toxin subunit B (STxB) binding to its cellular receptor Gb(3) leads to the formation of protein-lipid clusters and bending of the membrane. A newly developed synthetic route allowed synthesizing the biologically most relevant Gb(3)-C24:1 2OH species with both, the natural (Gb(3)-R) as well as the unnatural (Gb(3)-S) configuration of the 2OH group. The derivatives bind STxB with identical nanomolar affinity, while the propensity to induce membrane tubules in giant unilamellar vesicles is more pronounced for Gb(3)-S. Fluorescence and atomic force microscopy images of phase-separated supported membranes revealed differences in the lateral organization of the protein on the membrane. Gb(3)-R favorably induces large and tightly packed protein clusters, while a lower protein density is found on Gb(3)-S doped membranes."],["dc.identifier.doi","10.1016/j.bpj.2015.05.009"],["dc.identifier.gro","3141886"],["dc.identifier.isi","000356364000008"],["dc.identifier.pmid","26083916"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2167"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","2-Hydroxy Fatty Acid Enantiomers of Gb(3) Impact Shiga Toxin Binding and Membrane Organization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]