Richter, Frank

[["dc.bibliographiccitation.firstpage","12247"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","ACS Nano"],["dc.bibliographiccitation.lastpage","12254"],["dc.bibliographiccitation.volume","2018"],["dc.contributor.author","Saal, Kim-A."],["dc.contributor.author","Richter, Frank"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.date.accessioned","2019-07-09T11:50:22Z"],["dc.date.available","2019-07-09T11:50:22Z"],["dc.date.issued","2018"],["dc.description.abstract","Recent advances in optical nanoscopy have brought the imaging resolution to the size of the individual macromolecules, thereby setting stringent requirements for the fluorescent labels. Such requirements are optimally fulfilled by the incorporation of unnatural amino acids (UAAs) in the proteins of interest (POI), followed by fluorophore conjugation via click chemistry. However, this approach has been limited to single POIs in mammalian cells. Here we solve this problem by incorporating different UAAs in different POIs, which are expressed in independent cell sets. The cells are then fused, thereby combining the different proteins and organelles, and are easily imaged by dual-color super-resolution microscopy. This procedure, which we termed Fuse2Click, is simple, requires only the well-established Amber codon, and allows the use of all previously optimized UAAs and tRNA/RS pairs. This should render it a tool of choice for multi-color click-based imaging."],["dc.identifier.doi","10.1021/acsnano.8b06047"],["dc.identifier.pmid","30525434"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15921"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59757"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/47"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/2"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/614765/EU//NEUROMOLANATOMY"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/339580/EU//MITRAC"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P09: Proteinsortierung in der Synapse: Prinzipien und molekulare Organisation"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A06: Mitochondrienfunktion und -umsatz in Synapsen"],["dc.relation.issn","1936-086X"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","573"],["dc.subject.ddc","612"],["dc.title","Combined Use of Unnatural Amino Acids Enables Dual Color Super-Resolution Imaging of Proteins via Click Chemistry"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","139"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The EMBO journal"],["dc.bibliographiccitation.lastpage","159"],["dc.bibliographiccitation.volume","37"],["dc.contributor.author","Richter, Katharina N."],["dc.contributor.author","Revelo, Natalia H."],["dc.contributor.author","Seitz, Katharina J."],["dc.contributor.author","Helm, Martin S."],["dc.contributor.author","Sarkar, Deblina"],["dc.contributor.author","Saleeb, Rebecca S."],["dc.contributor.author","d'Este, Elisa"],["dc.contributor.author","Eberle, Jessica"],["dc.contributor.author","Wagner, Eva"],["dc.contributor.author","Vogl, Christian"],["dc.contributor.author","Lazaro, Diana F."],["dc.contributor.author","Richter, Frank"],["dc.contributor.author","Coy-Vergara, Javier"],["dc.contributor.author","Coceano, Giovanna"],["dc.contributor.author","Boyden, Edward S."],["dc.contributor.author","Duncan, Rory R."],["dc.contributor.author","Hell, Stefan W."],["dc.contributor.author","Lauterbach, Marcel A."],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Moser, Tobias"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Testa, Ilaria"],["dc.contributor.author","Zapiec, Bolek"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.date.accessioned","2018-01-09T14:09:53Z"],["dc.date.available","2018-01-09T14:09:53Z"],["dc.date.issued","2018"],["dc.description.abstract","Paraformaldehyde (PFA) is the most commonly used fixative for immunostaining of cells, but has been associated with various problems, ranging from loss of antigenicity to changes in morphology during fixation. We show here that the small dialdehyde glyoxal can successfully replace PFA Despite being less toxic than PFA, and, as most aldehydes, likely usable as a fixative, glyoxal has not yet been systematically tried in modern fluorescence microscopy. Here, we tested and optimized glyoxal fixation and surprisingly found it to be more efficient than PFA-based protocols. Glyoxal acted faster than PFA, cross-linked proteins more effectively, and improved the preservation of cellular morphology. We validated glyoxal fixation in multiple laboratories against different PFA-based protocols and confirmed that it enabled better immunostainings for a majority of the targets. Our data therefore support that glyoxal can be a valuable alternative to PFA for immunostaining."],["dc.identifier.doi","10.15252/embj.201695709"],["dc.identifier.pmid","29146773"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15063"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11599"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/195"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/15"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A09: Lokale molekulare Nanodomänen-Regulation der kardialen Ryanodin-Rezeptor-Funktion"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P09: Proteinsortierung in der Synapse: Prinzipien und molekulare Organisation"],["dc.relation.eissn","1460-2075"],["dc.relation.workinggroup","RG Hell"],["dc.relation.workinggroup","RG Lehnart (Cellular Biophysics and Translational Cardiology Section)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Glyoxal as an alternative fixative to formaldehyde in immunostaining and super-resolution microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]