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Medda, Rebecca
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Medda, Rebecca
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Medda, Rebecca
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Medda, R.
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2006Journal Article Research Paper [["dc.bibliographiccitation.firstpage","11440"],["dc.bibliographiccitation.issue","31"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","11445"],["dc.bibliographiccitation.volume","103"],["dc.contributor.author","Donnert, Gerald"],["dc.contributor.author","Keller, Jan"],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Andrei, M. Alexandra"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:52:39Z"],["dc.date.available","2017-09-07T11:52:39Z"],["dc.date.issued","2006"],["dc.description.abstract","We demonstrate far-field fluorescence microscopy with a focal-plane resolution of 15-20 nm in biological samples. The 10- to 12-fold multilateral increase in resolution below the diffraction barrier has been enabled by the elimination of molecular triplet state excitation as a major source of photobleaching of a number of dyes in stimulated emission depletion microscopy. Allowing for relaxation of the triplet state between subsequent excitation-depletion cycles yields an up to 30-fold increase in total fluorescence signal as compared with reported stimulated emission depletion illumination schemes. Moreover, it enables the reduction of the effective focal spot area by up to approximate to 140-fold below that given by diffraction. Triplet-state relaxation can be realized either by reducing the repetition rate of pulsed lasers or by increasing the scanning speed such that the build-up of the triplet state is effectively prevented. This resolution in immunofluorescence imaging is evidenced by revealing nanoscale protein patterns on endosomes, the punctuated structures of intermediate filaments in neurons, and nuclear protein speckles in mammalian cells with conventional optics. The reported performance of diffraction-unlimited fluorescence microscopy opens up a pathway for addressing fundamental problems in the life sciences."],["dc.identifier.doi","10.1073/pnas.0604965103"],["dc.identifier.gro","3143651"],["dc.identifier.isi","000239616400005"],["dc.identifier.pmid","16864773"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1188"],["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","Macromolecular-scale resolution in biological fluorescence microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2007Journal Article Research Paper [["dc.bibliographiccitation.firstpage","915"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","918"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Willig, Katrin I."],["dc.contributor.author","Harke, Benjamin"],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:49:24Z"],["dc.date.available","2017-09-07T11:49:24Z"],["dc.date.issued","2007"],["dc.description.abstract","We report stimulated emission depletion (STED) fluorescence microscopy with continuous wave (CW) laser beams. Lateral fluorescence confinement from the scanning focal spot delivered a resolution of 29 - 60 nm in the focal plane, corresponding to a 5 - 8- fold improvement over the diffraction barrier. Axial spot confinement increased the axial resolution by 3.5-fold. We observed three-dimensional (3D) subdiffraction resolution in 3D image stacks. Viable for fluorophores with low triplet yield, the use of CW light sources greatly simplifies the implementation of this concept of far-field fluorescence nanoscopy."],["dc.identifier.doi","10.1038/NMETH1108"],["dc.identifier.gro","3143419"],["dc.identifier.isi","000250575700014"],["dc.identifier.pmid","17952088"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/931"],["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","STED microscopy with continuous wave beams"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2011Journal Article Research Paper [["dc.bibliographiccitation.firstpage","1651"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","1660"],["dc.bibliographiccitation.volume","101"],["dc.contributor.author","Mueller, Veronica"],["dc.contributor.author","Ringemann, Christian"],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","Schwarzmann, Guenter"],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Leuschner, Ivo"],["dc.contributor.author","Polyakova, Svetlana"],["dc.contributor.author","Belov, Vladimir N."],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Eggeling, Christian"],["dc.date.accessioned","2017-09-07T11:43:23Z"],["dc.date.available","2017-09-07T11:43:23Z"],["dc.date.issued","2011"],["dc.description.abstract","Details about molecular membrane dynamics in living cells, such as lipid-protein interactions, are often hidden from the observer because of the limited spatial resolution of conventional far-field optical microscopy. The superior spatial resolution of stimulated emission depletion (STED) nanoscopy can provide new insights into this process. The application of fluorescence correlation spectroscopy (FCS) in focal spots continuously tuned down to 30 nm in diameter distinguishes between free and anomalous molecular diffusion due to, for example, transient binding of lipids to other membrane constituents, such as lipids and proteins. We compared STED-FCS data recorded on various fluorescent lipid analogs in the plasma membrane of living mammalian cells. Our results demonstrate details about the observed transient formation of molecular complexes. The diffusion characteristics of phosphoglycerolipids without hydroxyl-containing headgroups revealed weak interactions. The strongest interactions were observed with sphingolipid analogs, which showed cholesterol-assisted and cytoskeleton-dependent binding. The hydroxyl-containing headgroup of gangliosides, galactosylceramide, and phosphoinositol assisted binding, but in a much less cholesterol- and cytoskeleton-dependent manner. The observed anomalous diffusion indicates lipid-specific transient hydrogen bonding to other membrane molecules, such as proteins, and points to a distinct connectivity of the various lipids to other membrane constituents. This strong interaction is different from that responsible for forming cholesterol-dependent, liquid-ordered domains in model membranes."],["dc.identifier.doi","10.1016/j.bpj.2011.09.006"],["dc.identifier.gro","3142651"],["dc.identifier.isi","000295661300011"],["dc.identifier.pmid","21961591"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78"],["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","0006-3495"],["dc.title","STED Nanoscopy Reveals Molecular Details of Cholesterol- and Cytoskeleton-Modulated Lipid Interactions in Living Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2007Journal Article Research Paper [["dc.bibliographiccitation.firstpage","6266"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","6270"],["dc.bibliographiccitation.volume","46"],["dc.contributor.author","Fölling, Jonas"],["dc.contributor.author","Belov, Vladimir N."],["dc.contributor.author","Kunetsky, R."],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Schoenle, Andreas"],["dc.contributor.author","Egner, Alexander"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Bossi, Mariano L."],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:49:52Z"],["dc.date.available","2017-09-07T11:49:52Z"],["dc.date.issued","2007"],["dc.description.abstract","Exciting developments: Switching individual photochromic and fluorescent rhodamine amides enables 3D far-field optical microscopy with nanoscale resolution, excellent signal-to-noise ratio, and fast acquisition times. The rhodamine amides can be switched on using two photons, which enables 3D detailed imaging of thick and densely stained samples (such as 5-μm silica beads (see image) and living cells) to be constructed."],["dc.identifier.doi","10.1002/anie.200702167"],["dc.identifier.gro","3143552"],["dc.identifier.isi","000249114700006"],["dc.identifier.pmid","17640007"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1078"],["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","1433-7851"],["dc.title","Photochromic rhodamines provide nanoscopy with optical sectioning"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2008Journal Article Research Paper [["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"]]Details DOI PMID PMC WOS2011Journal Article Research Paper [["dc.bibliographiccitation.firstpage","9055"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","The Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","9066"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Jorgačevski, Jernej"],["dc.contributor.author","Potokar, Maja"],["dc.contributor.author","Grilc, Sonja"],["dc.contributor.author","Kreft, Marko"],["dc.contributor.author","Liu, Wei"],["dc.contributor.author","Barclay, Jeff W."],["dc.contributor.author","Bückers, Johanna"],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Parpura, Vladimir"],["dc.contributor.author","Burgoyne, Robert D."],["dc.contributor.author","Zorec, Robert"],["dc.date.accessioned","2017-09-07T11:44:09Z"],["dc.date.available","2017-09-07T11:44:09Z"],["dc.date.issued","2011"],["dc.description.abstract","The release of hormones and neurotransmitters, mediated by regulated exocytosis, can be modified by regulation of the fusion pore. The fusion pore is considered stable and narrow initially, eventually leading to the complete merger of the vesicle and the plasma membranes. By using the high-resolution patch-clamp capacitance technique, we studied single vesicles and asked whether the Sec1/Munc18 proteins, interacting with the membrane fusion-mediating SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, affect fusion pore properties. Munc18-1 mutants were transfected into lactotrophs to affect the interaction of Munc18-1 with syntaxin1 (Synt1) (R39C), Rab3A (E466K), and Mints (P242S). Compared with wild-type, Munc18-1 E466K increased the frequency of the fusion event. The latter two mutants increased the fusion pore dwell-time. All the mutants stabilized narrow fusion pores and increased the amplitude of fusion events, likely via preferential fusion of larger vesicles, since overexpression of Munc18-1 R39C did not affect the average size of vesicles, as determined by stimulated emission depletion (STED) microscopy. Single-molecule atomic force microscopy experiments revealed that wild-type Munc18-1, but not Munc18-1 R39C, abrogates the interaction between synaptobrevin2 (Syb2) and Synt1 binary trans-complexes. However, neither form of Munc18-1 affected the interaction of Syb2 with the preformed binary cis-Synt1A-SNAP25B complexes. This indicates that Munc18-1 performs a proofing function by inhibiting tethering of Syb2-containing vesicles solely to Synt1 at the plasmalemma and favoring vesicular tethering to the preformed binary cis-complex of Synt1A-SNAP25B. The association of Munc18-1 with the ternary SNARE complex leads to tuning of fusion pores via multiple and converging mechanisms involving Munc18-1 interactions with Synt1A, Rab3A, and Mints."],["dc.identifier.doi","10.1523/JNEUROSCI.0185-11.2011"],["dc.identifier.gro","3142714"],["dc.identifier.isi","000291642800037"],["dc.identifier.pmid","21677188"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/149"],["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","0270-6474"],["dc.title","Munc18-1 Tuning of Vesicle Merger and Fusion Pore Properties"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2007Journal Article Research Paper [["dc.bibliographiccitation.firstpage","3285"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","3290"],["dc.bibliographiccitation.volume","93"],["dc.contributor.author","Egner, Alexander"],["dc.contributor.author","Geisler, Claudia"],["dc.contributor.author","von Middendorff, Claas"],["dc.contributor.author","Bock, Hannes"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Andresen, Martin"],["dc.contributor.author","Stiel, Andre C."],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Schoenle, Andreas"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:49:23Z"],["dc.date.available","2017-09-07T11:49:23Z"],["dc.date.issued","2007"],["dc.description.abstract","We demonstrate nanoscale resolution in far-field fluorescence microscopy using reversible photoswitching and localization of individual fluorophores at comparatively fast recording speeds and from the interior of intact cells. These advancements have become possible by asynchronously recording the photon bursts of individual molecular switching cycles. We present images from the microtubular network of an intact mammalian cell with a resolution of 40 nm."],["dc.identifier.doi","10.1529/biophysj.107.112201"],["dc.identifier.gro","3143415"],["dc.identifier.isi","000250199300033"],["dc.identifier.pmid","17660318"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/927"],["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","Fluorescence nanoscopy in whole cells by asynchronous localization of photoswitching emitters"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2007Journal Article Research Paper [["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Microscopy Research and Technique"],["dc.bibliographiccitation.lastpage","9"],["dc.bibliographiccitation.volume","70"],["dc.contributor.author","Staudt, Thorsten"],["dc.contributor.author","Lang, Marion C."],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Engelhardt, Johann"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:49:53Z"],["dc.date.available","2017-09-07T11:49:53Z"],["dc.date.issued","2007"],["dc.description.abstract","The use of high numerical aperture immersion lenses in optical microscopy is compromised by spherical aberrations induced by the refractive index mismatch between the immersion system and the embedding medium of the sample. Especially when imaging >10 mu m deep into the specimen, the refractive index mismatch results in a noticeable loss of image brightness and resolution. A solution to this problem is to adapt the index of the embedding medium to that of the immersion system. Unfortunately, not many mounting media are known that are both index tunable as well as compatible with fluorescence imaging. Here we introduce a nontoxic embedding medium, 2,2'-thiodiethanol (TDE), which, by being miscible with water at any ratio, allows fine adjustment of the average refractive index of the sample ranging from that of water (1.33) to that of immersion oil (1.52). TDE thus enables high resolution imaging deep inside fixed specimens with objective lenses of the highest available aperture angles and has the potential to render glycerol embedding redundant. The refractive index changes due to larger cellular structures, such as nuclei, are largely compensated. Additionally, as an antioxidant, TDE preserves the fluorescence quantum yield of most of the fluorophores. We present the optical and chemical properties of this new medium as well as its application to a variety of differently stained cells and cellular substructures."],["dc.identifier.doi","10.1002/jemt.20396"],["dc.identifier.gro","3143561"],["dc.identifier.isi","000243313200001"],["dc.identifier.pmid","17131355"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1088"],["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","1059-910X"],["dc.title","2,2 '-thiodiethanol: A new water soluble mounting medium for high resolution optical microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2008Journal Article Research Paper [["dc.bibliographiccitation.firstpage","21093"],["dc.bibliographiccitation.issue","25"],["dc.bibliographiccitation.journal","Optics Express"],["dc.bibliographiccitation.lastpage","21104"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Testa, Ilaria"],["dc.contributor.author","Schönle, Andreas"],["dc.contributor.author","von Middendorff, Claas"],["dc.contributor.author","Geisler, Claudia"],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Wurm, Christian A."],["dc.contributor.author","Stiel, Andre C."],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Bossi, Mariano"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Hell, Stefan W."],["dc.contributor.author","Egner, Alexander"],["dc.date.accessioned","2017-09-07T11:48:07Z"],["dc.date.available","2017-09-07T11:48:07Z"],["dc.date.issued","2008"],["dc.description.abstract","We combine far-field fluorescence nanoscopy through serialized recording of switchable emitters with polarization-sensitive fluorescence detection. In addition to imaging with nanoscale spatial resolution, this technique allows determination of the fluorescence anisotropy of each detected dipole emitter and thus an estimate of its rotational mobility. Subpopulations of fluorescent markers can thus be separated based on their interaction with the sample. We applied this new functional nanoscopy to imaging of living mammalian cells. (C) 2008 Optical Society of America"],["dc.identifier.doi","10.1364/OE.16.021093"],["dc.identifier.gro","3143194"],["dc.identifier.isi","000261563100097"],["dc.identifier.pmid","19065250"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/682"],["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","1094-4087"],["dc.title","Nanoscale separation of molecular species based on their rotational mobility"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2009Journal Article Research Paper [["dc.bibliographiccitation.firstpage","1159"],["dc.bibliographiccitation.issue","7233"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","1162"],["dc.bibliographiccitation.volume","457"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Ringemann, Christian"],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Schwarzmann, Günter"],["dc.contributor.author","Sandhoff, Konrad"],["dc.contributor.author","Polyakova, Svetlana"],["dc.contributor.author","Belov, Vladimir N."],["dc.contributor.author","Hein, Birka"],["dc.contributor.author","von Middendorff, Claas"],["dc.contributor.author","Schönle, Andreas"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:47:33Z"],["dc.date.available","2017-09-07T11:47:33Z"],["dc.date.issued","2009"],["dc.description.abstract","Cholesterol-mediated lipid interactions are thought to have a functional role in many membrane-associated processes such as signalling events(1-5). Although several experiments indicate their existence, lipid nanodomains ('rafts') remain controversial owing to the lack of suitable detection techniques in living cells(4,6-9). The controversy is reflected in their putative size of 5-200 nm, spanning the range between the extent of a protein complex and the resolution limit of optical microscopy. Here we demonstrate the ability of stimulated emission depletion (STED) far-field fluorescence nanoscopy(10) to detect single diffusing (lipid) molecules in nanosized areas in the plasma membrane of living cells. Tuning of the probed area to spot sizes similar to 70-fold below the diffraction barrier reveals that unlike phosphoglycerolipids, sphingolipids and glycosylphosphatidylinositol-anchored proteins are transiently (similar to 10-20 ms) trapped in cholesterol-mediated molecular complexes dwelling within <20-nm diameter areas. The non-invasive optical recording of molecular time traces and fluctuation data in tunable nanoscale domains is a powerful new approach to study the dynamics of biomolecules in living cells."],["dc.identifier.doi","10.1038/nature07596"],["dc.identifier.gro","3143149"],["dc.identifier.isi","000263680100047"],["dc.identifier.pmid","19098897"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/631"],["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","Direct observation of the nanoscale dynamics of membrane lipids in a living cell"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS
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