Pfaff, Janine

[["dc.bibliographiccitation.firstpage","11839"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","ACS Nano"],["dc.bibliographiccitation.lastpage","11846"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Chizhik, Anna M."],["dc.contributor.author","Ruhlandt, Daja"],["dc.contributor.author","Pfaff, Janine"],["dc.contributor.author","Karedla, Narain"],["dc.contributor.author","Chizhik, Alexey I."],["dc.contributor.author","Gregor, Ingo"],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.contributor.author","Enderlein, Jörg"],["dc.date.accessioned","2018-04-23T11:48:40Z"],["dc.date.available","2018-04-23T11:48:40Z"],["dc.date.issued","2017"],["dc.description.abstract","The nuclear envelope, comprising the inner and the outer nuclear membrane, separates the nucleus from the cytoplasm and plays a key role in cellular functions. Nuclear pore complexes (NPCs), which are embedded in the nuclear envelope, control transport of macromolecules between the two compartments. Here, using dual-color metal-induced energy transfer (MIET), we determine the axial distance between Lap2β and Nup358 as markers for the inner nuclear membrane and the cytoplasmic side of the NPC, respectively. Using MIET imaging, we reconstruct the 3D profile of the nuclear envelope over the whole basal area, with an axial resolution of a few nanometers. This result demonstrates that optical microscopy can achieve nanometer axial resolution in biological samples and without recourse to complex interferometric approaches."],["dc.identifier.doi","10.1021/acsnano.7b04671"],["dc.identifier.gro","3142097"],["dc.identifier.pmid","28921961"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13555"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/13"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P07: Dynamik von Proteinen der inneren Kernmembran"],["dc.relation.issn","1936-0851"],["dc.relation.workinggroup","RG Kehlenbach (Nuclear Transport)"],["dc.title","Three-Dimensional Reconstruction of Nuclear Envelope Architecture Using Dual-Color Metal-Induced Energy Transfer Imaging"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","21000"],["dc.bibliographiccitation.issue","52"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","21005"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Schulz, Olaf"],["dc.contributor.author","Pieper, Christoph"],["dc.contributor.author","Clever, Michaela"],["dc.contributor.author","Pfaff, Janine"],["dc.contributor.author","Ruhlandt, Aike"],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.contributor.author","Wouters, Fred Silvester"],["dc.contributor.author","Großhans, Jörg"],["dc.contributor.author","Bunt, Gertrude"],["dc.contributor.author","Enderlein, Jörg"],["dc.date.accessioned","2018-04-23T11:49:28Z"],["dc.date.available","2018-04-23T11:49:28Z"],["dc.date.issued","2013"],["dc.description.abstract","We demonstrate how a conventional confocal spinning-disk (CSD) microscope can be converted into a doubly resolving image scanning microscopy (ISM) system without changing any part of its optical or mechanical elements. Making use of the intrinsic properties of a CSD microscope, we illuminate stroboscopically, generating an array of excitation foci that are moved across the sample by varying the phase between stroboscopic excitation and rotation of the spinning disk. ISM then generates an image with nearly doubled resolution. Using conventional fluorophores, we have imaged single nuclear pore complexes in the nuclear membrane and aggregates of GFP-conjugated Tau protein in three dimensions. Multicolor ISM was shown on cytoskeletal-associated structural proteins and on 3D four-color images including MitoTracker and Hoechst staining. The simple adaptation of conventional CSD equipment allows superresolution investigations of a broad variety of cell biological questions."],["dc.identifier.doi","10.1073/pnas.1315858110"],["dc.identifier.gro","3142124"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13705"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.doi","10.1073/pnas.1315858110"],["dc.relation.issn","0027-8424"],["dc.title","Resolution doubling in fluorescence microscopy with confocal spinning-disk image scanning microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","502"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","516"],["dc.bibliographiccitation.volume","129"],["dc.contributor.author","Pfaff, Janine"],["dc.contributor.author","Monroy, Jhon Rivera"],["dc.contributor.author","Jamieson, Cara"],["dc.contributor.author","Rajanala, Kalpana"],["dc.contributor.author","Vilardi, Fabio"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.date.accessioned","2017-09-07T11:54:41Z"],["dc.date.available","2017-09-07T11:54:41Z"],["dc.date.issued","2016"],["dc.description.abstract","Emerin is a tail-anchored protein that is found predominantly at the inner nuclear membrane (INM), where it associates with components of the nuclear lamina. Mutations in the emerin gene cause Emery-Dreifuss muscular dystrophy (EDMD), an X-linked recessive disease. Here, we report that the TRC40/GET pathway for post-translational insertion of tail-anchored proteins into membranes is involved in emerin-trafficking. Using proximity ligation assays, we show that emerin interacts with TRC40 in situ. Emerin expressed in bacteria or in a cell-free lysate was inserted into microsomal membranes in an ATP- and TRC40-dependent manner. Dominant-negative fragments of the TRC40-receptor proteins WRB and CAML (also known as CAMLG) inhibited membrane insertion. A rapamycin-based dimerization assay revealed correct transport of wild-type emerin to the INM, whereas TRC40-binding, membrane integration and INM-targeting of emerin mutant proteins that occur in EDMD was disturbed. Our results suggest that the mode of membrane integration contributes to correct targeting of emerin to the INM."],["dc.identifier.doi","10.1242/jcs.179333"],["dc.identifier.gro","3141735"],["dc.identifier.isi","000369505600007"],["dc.identifier.pmid","26675233"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/491"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/132"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A07: Rolle der TRC40-Maschinerie im Proteostase-Netzwerk von Kardiomyozyten"],["dc.relation.issn","0021-9533"],["dc.relation.issn","1477-9137"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.title","Emery-Dreifuss muscular dystrophy mutations impair TRC40-mediated targeting of emerin to the inner nuclear membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]