Butkevich, Alexey N.

[["dc.bibliographiccitation.journal","Nature Photonics"],["dc.contributor.author","Weber, Michael"],["dc.contributor.author","Leutenegger, Marcel"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Mihaila, Tiberiu S."],["dc.contributor.author","Butkevich, Alexey N."],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2021-04-14T08:28:37Z"],["dc.date.available","2021-04-14T08:28:37Z"],["dc.date.issued","2021"],["dc.description.abstract","We introduce MINSTED, a fluorophore localization and super-resolution microscopy concept based on stimulated emission depletion (STED) that provides spatial precision and resolution down to the molecular scale. In MINSTED, the intensity minimum of the STED doughnut, and hence the point of minimal STED, serves as a movable reference coordinate for fluorophore localization. As the STED rate, the background and the required number of fluorescence detections are low compared with most other STED microscopy and localization methods, MINSTED entails substantially less fluorophore bleaching. In our implementation, 200–1,000 detections per fluorophore provide a localization precision of 1–3 nm in standard deviation, which in conjunction with independent single fluorophore switching translates to a ~100-fold improvement in far-field microscopy resolution over the diffraction limit. The performance of MINSTED nanoscopy is demonstrated by imaging the distribution of Mic60 proteins in the mitochondrial inner membrane of human cells."],["dc.identifier.doi","10.1038/s41566-021-00774-2"],["dc.identifier.pmid","33953795"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82664"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/279"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1749-4893"],["dc.relation.haserratum","/handle/2/103523"],["dc.relation.issn","1749-4885"],["dc.relation.workinggroup","RG Hell"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.rights","CC BY 4.0"],["dc.title","MINSTED fluorescence localization and nanoscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","12319"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.lastpage","15"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Mitronova, Gyuzel Y."],["dc.contributor.author","Lukinavičius, Gražvydas"],["dc.contributor.author","Butkevich, Alexey N."],["dc.contributor.author","Kohl, Tobias"],["dc.contributor.author","Belov, Vladimir N."],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2018-01-17T13:30:31Z"],["dc.date.available","2018-01-17T13:30:31Z"],["dc.date.issued","2017"],["dc.description.abstract","Visualization of the G-protein coupled receptor (GPCR) is of great importance for studying its function in a native cell. We have synthesized a series of red-emitting fluorescent probes targeting β-adrenergic receptor (βAR) that are compatible with confocal and Stimulated Emission Depletion (STED) microscopy as well as with Time-Resolved Fluorescence Resonance Energy Transfer (TR-FRET) binding assay in living cells. The probe based on the agonist BI-167107 and fluorescent dye KK114 demonstrates nanomolar binding affinity and up to nine-fold β2AR selectivity over β1AR. Carazolol-derived probes are fluorogenic and allow no-wash imaging experiments. STED microscopy of β2ARs stained at the native expression level on pancreatic CAPAN cells provides two-fold improvement in lateral optical resolution over confocal mode and reveals the formation of receptor microdomains. These probes retain their functional (agonist or antagonist) properties, allowing simultaneous modulation of cyclic adenosine monophosphate (cAMP) levels and receptor internalization as well as imaging receptor localization."],["dc.identifier.doi","10.1038/s41598-017-12468-3"],["dc.identifier.pmid","28951558"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14939"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11716"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","High-Affinity Functional Fluorescent Ligands for Human β-Adrenoceptors"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]