Heitmüller, Svenja

[["dc.bibliographiccitation.firstpage","13422"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Langmuir"],["dc.bibliographiccitation.lastpage","13428"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Bernecker, Anja"],["dc.contributor.author","Ziomkowska, Joanna"],["dc.contributor.author","Heitmüller, Svenja"],["dc.contributor.author","Wieneke, Ralph"],["dc.contributor.author","Geyer, Armin"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:45:20Z"],["dc.date.available","2017-09-07T11:45:20Z"],["dc.date.issued","2010"],["dc.description.abstract","Ether lipids with alkyl chains of uniform length and varying amine headgroups were synthesized and assembled into bilayer structures in aqueous solution, which served as templates for the formation of silica in two and three dimensions produced under ambient conditions. Dynamic light scattering revealed that unilamellar vesicles of the aminolipids are formed by the extrusion method. The alkylation of the polar amine headgroup was systematically increased from a primary, secondary, and tertiary amine to a quaternary ammonium salt, and the amount of silica was quantified by the beta-silicomolybdate method as a function of the headgroup. A lysinol-connected ether lipid harboring two primary amine groups was also investigated. This variation enabled us to compare the influence of the headgroup on the properties of the precipitated silica in detail. By spreading of unilamellar aminolipid vesicles onto planar silicon substrates, two-dimensional planar bilayers can be produced. By means of ellipsometry in conjunction with atomic force microscopy, we were able to demonstrate that very thin silica layers with a thickness of a few nanometers are formed within minutes on the surface of the aminolipid bilayers. All layers are composed of silica nanospheres, and the thickness turned out to be independent of the amine headgroup."],["dc.identifier.doi","10.1021/la1021627"],["dc.identifier.gro","3142873"],["dc.identifier.isi","000280667900054"],["dc.identifier.pmid","20695587"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/325"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: VW-Stiftung [I/82 042]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0743-7463"],["dc.title","Formation of Silica Precipitates on Membrane Surfaces in Two and Three Dimensions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","453"],["dc.bibliographiccitation.journal","Metabolic Engineering"],["dc.bibliographiccitation.lastpage","462"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Heitmüller, Svenja"],["dc.contributor.author","Neumann-Staubitz, Petra"],["dc.contributor.author","Herrfurth, Cornelia"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Neumann, Heinz"],["dc.date.accessioned","2020-12-10T15:21:49Z"],["dc.date.available","2020-12-10T15:21:49Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.ymben.2018.04.022"],["dc.identifier.issn","1096-7176"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73173"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Cellular substrate limitations of lysine acetylation turnover by sirtuins investigated with engineered futile cycle enzymes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","939"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","ACS Chemical Biology"],["dc.bibliographiccitation.lastpage","944"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Wilkins, Bryan J."],["dc.contributor.author","Hahn, Liljan E."],["dc.contributor.author","Heitmüller, Svenja"],["dc.contributor.author","Frauendorf, Holm"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Neumann, Heinz"],["dc.date.accessioned","2018-09-28T07:57:34Z"],["dc.date.available","2018-09-28T07:57:34Z"],["dc.date.issued","2015"],["dc.description.abstract","Post-translational modifications of proteins are important modulators of protein function. In order to identify the specific consequences of individual modifications, general methods are required for homogeneous production of modified proteins. The direct installation of modified amino acids by genetic code expansion facilitates the production of such proteins independent of the knowledge and availability of the enzymes naturally responsible for the modification. The production of recombinant histone H4 with genetically encoded modifications has proven notoriously difficult in the past. Here, we present a general strategy to produce histone H4 with acetylation, propionylation, butyrylation, and crotonylation on lysine residues. We produce homogeneous histone H4 containing up to four simultaneous acetylations to analyze the impact of the modifications on chromatin array compaction. Furthermore, we explore the ability of antibodies to discriminate between alternative lysine acylations by incorporating these modifications in recombinant histone H4."],["dc.identifier.doi","10.1021/cb501011v"],["dc.identifier.pmid","25590375"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15833"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1554-8937"],["dc.title","Genetically encoding lysine modifications on histone H4"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]