Jakobs, Stefan

[["dc.bibliographiccitation.firstpage","651"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cell Death and Differentiation"],["dc.bibliographiccitation.lastpage","661"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Meuer, K."],["dc.contributor.author","Suppanz, I. E."],["dc.contributor.author","Lingor, P."],["dc.contributor.author","Planchamp, V."],["dc.contributor.author","Göricke, B."],["dc.contributor.author","Fichtner, L."],["dc.contributor.author","Braus, G. H."],["dc.contributor.author","Dietz, G. P. H."],["dc.contributor.author","Jakobs, S."],["dc.contributor.author","Bähr, M."],["dc.contributor.author","Weishaupt, J. H."],["dc.date.accessioned","2017-09-07T11:49:50Z"],["dc.date.available","2017-09-07T11:49:50Z"],["dc.date.issued","2007"],["dc.description.abstract","Under physiological conditions, mitochondrial morphology dynamically shifts between a punctuate appearance and tubular networks. However, little is known about upstream signal transduction pathways that regulate mitochondrial morphology. We show that mitochondrial fission is a very early and kinetically invariant event during neuronal cell death, which causally contributes to cytochrome c release and neuronal apoptosis. Using a small molecule CDK5 inhibitor, as well as a dominant-negative CDK5 mutant and RNAi knockdown experiments, we identified CDK5 as an upstream signalling kinase that regulates mitochondrial fission during apoptosis of neurons. Vice versa, our study shows that mitochondrial fission is a modulator contributing to CDK5-mediated neurotoxicity. Thereby, we provide a link that allows integration of CDK5 into established neuronal apoptosis pathways."],["dc.identifier.doi","10.1038/sj.cdd.4402087"],["dc.identifier.gro","3143515"],["dc.identifier.isi","000245102900002"],["dc.identifier.pmid","17218957"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1038"],["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","1350-9047"],["dc.title","Cyclin-dependent kinase 5 is an upstream regulator of mitochondrial fission during neuronal apoptosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11288"],["dc.bibliographiccitation.issue","36"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","11293"],["dc.bibliographiccitation.volume","112"],["dc.contributor.author","Kukat, Christian"],["dc.contributor.author","Davies, Karen M."],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Spåhr, Henrik"],["dc.contributor.author","Bonekamp, Nina A."],["dc.contributor.author","Kühl, Inge"],["dc.contributor.author","Joos, Friederike"],["dc.contributor.author","Loguercio Polosa, Paola Anna Maria"],["dc.contributor.author","Park, Chan Bae"],["dc.contributor.author","Posse, Viktor"],["dc.contributor.author","Falkenberg, Maria"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Kühlbrandt, Werner"],["dc.contributor.author","Larsson, Nils-Göran"],["dc.date.accessioned","2017-09-07T11:43:32Z"],["dc.date.available","2017-09-07T11:43:32Z"],["dc.date.issued","2015"],["dc.description.abstract","Mammalian mitochondrial DNA (mtDNA) is packaged by mitochondrial transcription factor A (TFAM) into mitochondrial nucleoids that are of key importance in controlling the transmission and expression of mtDNA. Nucleoid ultrastructure is poorly defined, and therefore we used a combination of biochemistry, super-resolution microscopy, and electron microscopy to show that mitochondrial nucleoids have an irregular ellipsoidal shape and typically contain a single copy of mtDNA. Rotary shadowing electron microscopy revealed that nucleoid formation in vitro is a multistep process initiated by TFAM aggregation and cross-strand binding. Superresolution microscopy of cultivated cells showed that increased mtDNA copy number increases nucleoid numbers without altering their sizes. Electron cryo-tomography visualized nucleoids at high resolution in isolated mammalian mitochondria and confirmed the sizes observed by superresolution microscopy of cell lines. We conclude that the fundamental organizational unit of the mitochondrial nucleoid is a single copy of mtDNA compacted by TFAM, and we suggest a packaging mechanism."],["dc.identifier.doi","10.1073/pnas.1512131112"],["dc.identifier.gro","3141829"],["dc.identifier.isi","000360994900049"],["dc.identifier.pmid","26305956"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1534"],["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","Cross-strand binding of TFAM to a single mtDNA molecule forms the mitochondrial nucleoid"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.lastpage","19"],["dc.bibliographiccitation.seriesnr","124"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Neumann, Daniel"],["dc.contributor.editor","Müller, Susann"],["dc.contributor.editor","Bley, Thomas"],["dc.date.accessioned","2017-09-07T11:45:03Z"],["dc.date.available","2017-09-07T11:45:03Z"],["dc.date.issued","2011"],["dc.description.abstract","Heterogeneity in the shapes of individual multicellular organisms is a daily experience. Likewise, even a quick glance through the ocular of a light microscope reveals the morphological heterogeneities in genetically identical cultured cells, whereas heterogeneities on the level of the organelles are much less obvious. This short review focuses on intracellular heterogeneities at the example of the mitochondria and their analysis by fluorescence microscopy. The overall mitochondrial shape as well as mitochondrial dynamics can be studied by classical (fluorescence) light microscopy. However, with an organelle diameter generally close to the resolution limit of light, the heterogeneities within mitochondria cannot be resolved with conventional light microscopy. Therefore, we briefly discuss here the potential of subdiffraction light microscopy (nanoscopy) to study inner-mitochondrial heterogeneities."],["dc.identifier.doi","10.1007/10_2010_81"],["dc.identifier.gro","3142799"],["dc.identifier.isi","000288919400001"],["dc.identifier.pmid","21072702"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/243"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Springer"],["dc.publisher.place","Berlin"],["dc.relation.crisseries","Advances in Biochemical Engineering, Biotechnology"],["dc.relation.isbn","978-3-642-16886-4"],["dc.relation.ispartof","High Resolution Microbial Single Cell Analytics"],["dc.relation.ispartofseries","Advances in Biochemical Engineering, Biotechnology; 124"],["dc.relation.issn","0724-6145"],["dc.relation.issn","0724-6145"],["dc.title","Light Microscopic Analysis of Mitochondrial Heterogeneity in Cell Populations and Within Single Cells"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","247"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","257"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Alkhaja, Alwaleed K."],["dc.contributor.author","Jans, Daniel C."],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Vukotic, Milena"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Ludewig, Fabian"],["dc.contributor.author","Schliebs, Wolfgang"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Deckers, Markus"],["dc.date.accessioned","2017-09-07T11:49:01Z"],["dc.date.available","2017-09-07T11:49:01Z"],["dc.date.issued","2012"],["dc.description.abstract","The inner membrane of mitochondria is especially protein rich and displays a unique morphology characterized by large invaginations, the mitochondrial cristae, and the inner boundary membrane, which is in proximity to the outer membrane. Mitochondrial inner membrane proteins appear to be not evenly distributed in the inner membrane, but instead organize into functionally distinct subcompartments. It is unknown how the organization of the inner membrane is achieved. We identified MINOS1/MIO10 (C1orf151/YCL057C-A), a conserved mitochondrial inner membrane protein. mio10-mutant yeast cells are affected in growth on nonfermentable carbon sources and exhibit altered mitochondrial morphology. At the ultrastructural level, mutant mitochondria display loss of inner membrane organization. Proteomic analyses reveal MINOS1/Mio10 as a novel constituent of Mitofilin/Fcj1 complexes in human and yeast mitochondria. Thus our analyses reveal new insight into the composition of the mitochondrial inner membrane organizing machinery."],["dc.identifier.doi","10.1091/mbc.E11-09-0774"],["dc.identifier.gro","3142588"],["dc.identifier.isi","000299108000002"],["dc.identifier.pmid","22114354"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7823"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8955"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1059-1524"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2292"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","2301"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Hildenbeutel, Markus"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Herrmann, Johannes M."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:48:51Z"],["dc.date.available","2017-09-07T11:48:51Z"],["dc.date.issued","2012"],["dc.description.abstract","The Oxa1 protein is a well-conserved integral protein of the inner membrane of mitochondria. It mediates the insertion of both mitochondrial-and nuclear-encoded proteins from the matrix into the inner membrane. We investigated the distribution of budding yeast Oxa1 between the two subdomains of the contiguous inner membrane-the cristae membrane (CM) and the inner boundary membrane (IBM)-under different physiological conditions. We found that under fermentable growth conditions, Oxa1 is enriched in the IBM, whereas under nonfermentable (respiratory) growth conditions, it is predominantly localized in the CM. The enrichment of Oxa1 in the CM requires mitochondrial translation; similarly, deletion of the ribosome-binding domain of Oxa1 prevents an enrichment of Oxa1 in the CM. The predominant localization in the IBM under fermentable growth conditions is prevented by inhibiting mitochondrial protein import. Furthermore, overexpression of the nuclear-encoded Oxa1 substrate Mdl1 shifts the distribution of Oxa1 toward the IBM. Apparently, the availability of nuclear- and mitochondrial-encoded substrates influences the inner-membrane distribution of Oxa1. Our findings show that the distribution of Oxa1 within the inner membrane is dynamic and adapts to different physiological needs."],["dc.identifier.doi","10.1091/mbc.E11-06-0538"],["dc.identifier.gro","3142518"],["dc.identifier.isi","000306286700006"],["dc.identifier.pmid","22513091"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9497"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8878"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1059-1524"],["dc.rights","CC BY-NC-SA 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-sa/3.0"],["dc.title","The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["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.firstpage","572"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Biology"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Bollmann, Franziska"],["dc.contributor.author","Dohrke, Jan-Niklas"],["dc.contributor.author","Wurm, Christian A."],["dc.contributor.author","Jans, Daniel C."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2021-09-01T06:43:08Z"],["dc.date.available","2021-09-01T06:43:08Z"],["dc.date.issued","2021"],["dc.description.abstract","Mitochondria are highly dynamic organelles that interchange their contents mediated by fission and fusion. However, it has previously been shown that the mitochondria of cultured human epithelial cells exhibit a gradient in the relative abundance of several proteins, with the perinuclear mitochondria generally exhibiting a higher protein abundance than the peripheral mitochondria. The molecular mechanisms that are required for the establishment and the maintenance of such inner-cellular mitochondrial protein abundance gradients are unknown. We verified the existence of inner-cellular gradients in the abundance of clusters of the mitochondrial outer membrane protein Tom20 in the mitochondria of kidney epithelial cells from an African green monkey (Vero cells) using STED nanoscopy and confocal microscopy. We found that the Tom20 gradients are established immediately after cell division and require the presence of microtubules. Furthermore, the gradients are abrogated in hyperfused mitochondrial networks. Our results suggest that inner-cellular protein abundance gradients from the perinuclear to the peripheral mitochondria are established by the trafficking of individual mitochondria to their respective cellular destination."],["dc.description.abstract","Mitochondria are highly dynamic organelles that interchange their contents mediated by fission and fusion. However, it has previously been shown that the mitochondria of cultured human epithelial cells exhibit a gradient in the relative abundance of several proteins, with the perinuclear mitochondria generally exhibiting a higher protein abundance than the peripheral mitochondria. The molecular mechanisms that are required for the establishment and the maintenance of such inner-cellular mitochondrial protein abundance gradients are unknown. We verified the existence of inner-cellular gradients in the abundance of clusters of the mitochondrial outer membrane protein Tom20 in the mitochondria of kidney epithelial cells from an African green monkey (Vero cells) using STED nanoscopy and confocal microscopy. We found that the Tom20 gradients are established immediately after cell division and require the presence of microtubules. Furthermore, the gradients are abrogated in hyperfused mitochondrial networks. Our results suggest that inner-cellular protein abundance gradients from the perinuclear to the peripheral mitochondria are established by the trafficking of individual mitochondria to their respective cellular destination."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.description.sponsorship","European Research Council"],["dc.identifier.doi","10.3390/biology10070572"],["dc.identifier.pii","biology10070572"],["dc.identifier.pmid","34201436"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89225"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/146"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P01: Untersuchung der Unterschiede in der Zusammensetzung, Funktion und Position von individuellen MICOS Komplexen in einzelnen Säugerzellen"],["dc.relation.eissn","2079-7737"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.rights","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Mitochondrial Protein Abundance Gradients Require the Distribution of Separated Mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["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"]]