Jakobs, Stefan

[["dc.bibliographiccitation.firstpage","131"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","FEBS Letters"],["dc.bibliographiccitation.lastpage","135"],["dc.bibliographiccitation.volume","479"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Subramaniam, Vinod"],["dc.contributor.author","Schönle, Andreas"],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2017-09-07T11:46:46Z"],["dc.date.available","2017-09-07T11:46:46Z"],["dc.date.issued","2000"],["dc.description.abstract","The green fluorescent protein (GFP) has become an invaluable marker for monitoring protein localization and gene expression in vivo. Recently a new red fluorescent protein (drFP583 or DsRed), isolated from tropical corals, has been described [Matz, M.V. et al, (1999) Nature Biotech, 17, 969-973]. With emission maxima at 509 and 583 nm respectively, EGFP and DsRed are suited for almost crossover free dual color labeling upon simultaneous excitation, We imaged mixed populations of Escherichia coli expressing either EGFP or DsRed by one-photon confocal and by two-photon microscopy, Both excitation modes proved to be suitable for imaging cells expressing either of the fluorescent proteins. DsRed had an extended maturation time and E, coli expressing this fluorescent protein were significantly smaller than those expressing EGFP, In aging bacterial cultures DsRed appeared to aggregate within the cells, accompanied by a strong reduction in its fluorescence lifetime as determined by fluorescence lifetime imaging microscopy, (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0014-5793(00)01896-2"],["dc.identifier.gro","3144363"],["dc.identifier.isi","000088963900011"],["dc.identifier.pmid","10981721"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1979"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0014-5793"],["dc.title","EGFP and DsRed expressing cultures of Escherichia coli imaged by confocal, two-photon and fluorescence lifetime microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","4762"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Kamper, Maria"],["dc.contributor.author","Ta, Haisen"],["dc.contributor.author","Jensen, Nickels A."],["dc.contributor.author","Hell, Stefan W."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2019-07-09T11:50:56Z"],["dc.date.available","2019-07-09T11:50:56Z"],["dc.date.issued","2018"],["dc.description.abstract","The near infrared (NIR) optical window between the cutoff for hemoglobin absorption at 650 nm and the onset of increased water absorption at 900 nm is an attractive, yet largely unexplored, spectral regime for diffraction-unlimited super-resolution fluorescence microscopy (nanoscopy). We developed the NIR fluorescent protein SNIFP, a bright and photostable bacteriophytochrome, and demonstrate its use as a fusion tag in live-cell microscopy and STED nanoscopy. We further demonstrate dual color red-confocal/NIR-STED imaging by co-expressing SNIFP with a conventional red fluorescent protein."],["dc.identifier.doi","10.1038/s41467-018-07246-2"],["dc.identifier.pmid","30420676"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16027"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59855"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Near-infrared STED nanoscopy with an engineered bacterial phytochrome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1072"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","1075"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Ostersehlt, Lynn M."],["dc.contributor.author","Jans, Daniel C."],["dc.contributor.author","Wittek, Anna"],["dc.contributor.author","Keller-Findeisen, Jan"],["dc.contributor.author","Inamdar, Kaushik"],["dc.contributor.author","Sahl, Steffen J."],["dc.contributor.author","Hell, Stefan W."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2022-10-04T10:21:07Z"],["dc.date.available","2022-10-04T10:21:07Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\n MINimal fluorescence photon FLUXes (MINFLUX) nanoscopy, providing photon-efficient fluorophore localizations, has brought about three-dimensional resolution at nanometer scales. However, by using an intrinsic on–off switching process for single fluorophore separation, initial MINFLUX implementations have been limited to two color channels. Here we show that MINFLUX can be effectively combined with sequentially multiplexed DNA-based labeling (DNA-PAINT), expanding MINFLUX nanoscopy to multiple molecular targets. Our method is exemplified with three-color recordings of mitochondria in human cells."],["dc.identifier.doi","10.1038/s41592-022-01577-1"],["dc.identifier.pii","1577"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114334"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-600"],["dc.relation.eissn","1548-7105"],["dc.relation.issn","1548-7091"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","DNA-PAINT MINFLUX nanoscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","7368"],["dc.bibliographiccitation.firstpage","204"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","208"],["dc.bibliographiccitation.volume","478"],["dc.contributor.author","Grotjohann, Tim"],["dc.contributor.author","Testa, Ilaria"],["dc.contributor.author","Leutenegger, Marcel"],["dc.contributor.author","Bock, Hannes"],["dc.contributor.author","Urban, Nicolai T."],["dc.contributor.author","Lavoie-Cardinal, Flavie"],["dc.contributor.author","Willig, Katrin I."],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2017-09-07T11:43:21Z"],["dc.date.available","2017-09-07T11:43:21Z"],["dc.date.issued","2011"],["dc.description.abstract","Lens-based optical microscopy failed to discern fluorescent features closer than 200 nm for decades, but the recent breaking of the diffraction resolution barrier by sequentially switching the fluorescence capability of adjacent features on and off is making nanoscale imaging routine. Reported fluorescence nanoscopy variants switch these features either with intense beams at defined positions or randomly, molecule by molecule. Here we demonstrate an optical nanoscopy that records raw data images from living cells and tissues with low levels of light. This advance has been facilitated by the generation of reversibly switchable enhanced green fluorescent protein (rsEGFP), a fluorescent protein that can be reversibly photoswitched more than a thousand times. Distributions of functional rsEGFP-fusion proteins in living bacteria and mammalian cells are imaged at <40-nanometre resolution. Dendritic spines in living brain slices are super-resolved with about a million times lower light intensities than before. The reversible switching also enables all-optical writing of features with subdiffraction size and spacings, which can be used for data storage."],["dc.identifier.doi","10.1038/nature10497"],["dc.identifier.gro","3142644"],["dc.identifier.isi","000295782800041"],["dc.identifier.pmid","21909116"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0028-0836"],["dc.title","Diffraction-unlimited all-optical imaging and writing with a photochromic GFP"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","L67"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","L69"],["dc.bibliographiccitation.volume","92"],["dc.contributor.author","Donnert, Gerald"],["dc.contributor.author","Keller, Jan"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Westphal, Volker"],["dc.contributor.author","Schoenle, Andreas"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:49:49Z"],["dc.date.available","2017-09-07T11:49:49Z"],["dc.date.issued","2007"],["dc.description.abstract","We demonstrate two-color fluorescence microscopy with nanoscale spatial resolution by applying stimulated emission depletion on fluorophores differing in their absorption and emission spectra. Green- and red-emitting fluorophores are selectively excited and quenched using dedicated beam pairs. The stimulated emission depletion beams deliver a lateral resolution of < 30 nm and 65 nm for the green and the red color channel, respectively. The similar to 5 nm alignment accuracy of the two images establishes the precision with which differently labeled proteins are correlated in space. Colocalized nanoscopy is demonstrated with endosomal protein patterns and by resolving nanoclusters of a mitochondrial outer membrane protein, Tom20, in relation with the F(1)F(0)ATP synthase. The joint improvement of resolution and colocalization demonstrates the emerging potential of far-field fluorescence nanoscopy to study the spatial organization of macromolecules in cells."],["dc.identifier.doi","10.1529/biophysj.107.104497"],["dc.identifier.gro","3143514"],["dc.identifier.isi","000245164000003"],["dc.identifier.pmid","17307826"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1037"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-3495"],["dc.title","Two-color far-field fluorescence nanoscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13005"],["dc.bibliographiccitation.issue","32"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","13009"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Andresen, Martin"],["dc.contributor.author","Stiel, Andre C."],["dc.contributor.author","Trowitzsch, Simon"],["dc.contributor.author","Weber, Gert"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Wahl, Markus C."],["dc.contributor.author","Hell, Stefan W."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:49:26Z"],["dc.date.available","2017-09-07T11:49:26Z"],["dc.date.issued","2007"],["dc.description.abstract","Dronpa is a novel GFP-like fluorescent protein with exceptional light-controlled switching properties. It may be reversibly switched between a fluorescent on-state and a nonfluorescent off-state by irradiation with light. To elucidate the molecular basis of the switching mechanism, we generated reversibly switchable Dronpa protein crystals. Using these crystals we determined the elusive dark-state structure of Dronpa at 1.95-angstrom resolution. We found that the photoswitching results in a cis-trans isomerization of the chromophore accompanied by complex structural rearrangements of four nearby amino acid residues. Because of this cascade of intramolecular events, the chromophore is exposed to distinct electrostatic surface potentials, which are likely to influence the protonation equilibria at the chromophore. We suggest a comprehensive model for the light-induced switching mechanism, connecting a cascade of structural rearrangements with different protonation states of the chromophore."],["dc.identifier.doi","10.1073/pnas.0700629104"],["dc.identifier.gro","3143453"],["dc.identifier.isi","000248650300011"],["dc.identifier.pmid","17646653"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/969"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Structural basis for reversible photoswitching in Dronpa"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","European biophysics journal : with biophysics letters"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Andresen, Martin"],["dc.contributor.author","Brakemann, Tanja"],["dc.contributor.author","Stiel, Andre C."],["dc.contributor.author","Testa, Ilaria"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:45:52Z"],["dc.date.available","2017-09-07T11:45:52Z"],["dc.date.issued","2011"],["dc.identifier.gro","3145539"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3248"],["dc.notes.intern","lifescience"],["dc.notes.status","public"],["dc.notes.submitter","oschaef1"],["dc.publisher","Springer"],["dc.relation.conference","8th EBSA European Biophysics Congress"],["dc.relation.eissn","1432-1017"],["dc.relation.eventend","2011-08-27"],["dc.relation.eventlocation","Budapest, Hungary"],["dc.relation.eventstart","2011-08-23"],["dc.relation.issn","0175-7571"],["dc.title","A new class of reversibly switchable fluorescent proteins"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3598"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Angewandte Chemie"],["dc.bibliographiccitation.lastpage","3602"],["dc.bibliographiccitation.volume","122"],["dc.contributor.author","Belov, Vladimir N."],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Boyarskiy, Vadim P."],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:53:02Z"],["dc.date.available","2017-09-07T11:53:02Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1002/ange.201000150"],["dc.identifier.gro","3145021"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2711"],["dc.language.iso","de"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0044-8249"],["dc.title","Rhodamine NN: eine neue Klasse maskierter Fluoreszenzfarbstoffe"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3370"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","3375"],["dc.bibliographiccitation.volume","99"],["dc.contributor.author","Egner, Alexander"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:45:55Z"],["dc.date.available","2017-09-07T11:45:55Z"],["dc.date.issued","2002"],["dc.description.abstract","By introducing beam-scanning multifocal multiphoton 4Pi-confocal microscopy, we have attained fast fluorescence imaging of live cells with axial super resolution. Rapid scanning of up to 64 pairs of interfering high-angle fields and subsequent confocal detection enabled us to perform three to five times finer optical sectioning than confocal microscopy. In conjunction with nonlinear image restoration, we demonstrate, to our knowledge for the first time, three-dimensional imaging of live eukaryotic cells at an equilateral resolution of approximate to100 nm. This imaging mode allowed us to reveal the morphology and size of the green fluorescent protein-labeled mitochondrial compartment of live Saccharomyces cerevisiae (bakers' yeast) growing on different carbon sources. Our studies show that mitochondria of cells grown on medium containing glycerol as the only carbon source, as opposed to glucose-grown cells, exhibit a strongly branched tubular reticulum. We determine the average tubular diameter and find that it increases from 339 +/- 5 nm to 360 +/- 4 nm when changing from glucose to glycerol, that is, from a fermentable to a nonfermentable carbon source. Moreover, this change is associated with a 2.8-fold increase of the surface of the reticulum, resulting in an average increase in volume of the mitochondrial compartment by a factor of 3.0 +/- 0.2."],["dc.identifier.doi","10.1073/pnas.052545099"],["dc.identifier.gro","3144210"],["dc.identifier.isi","000174511000006"],["dc.identifier.pmid","11904401"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1809"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Fast 100-nm resolution three-dimensional microscope reveals structural plasticity of mitochondria in live yeast"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","943"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","945"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Fölling, Jonas"],["dc.contributor.author","Bossi, Mariano"],["dc.contributor.author","Bock, Hannes"],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Wurm, Christian A."],["dc.contributor.author","Hein, Birka"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2017-09-07T11:48:10Z"],["dc.date.available","2017-09-07T11:48:10Z"],["dc.date.issued","2008"],["dc.description.abstract","We introduce far-field fluorescence nanoscopy with ordinary fluorophores based on switching the majority of them to a metastable dark state, such as the triplet, and calculating the position of those left or those that spontaneously returned to the ground state. Continuous widefield illumination by a single laser and a continuously operating camera yielded dual-color images of rhodamine-and fluorescent protein-labeled (living) samples, proving a simple yet powerful super-resolution approach."],["dc.identifier.doi","10.1038/nmeth.1257"],["dc.identifier.gro","3143218"],["dc.identifier.isi","000260532500012"],["dc.identifier.pmid","18794861"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/708"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1548-7091"],["dc.title","Fluorescence nanoscopy by ground-state depletion and single-molecule return"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]