Academic literature on the topic 'RsEGFP2'

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Journal articles on the topic "RsEGFP2"

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Tuijtel, Maarten W., Abraham J. Koster, Frank G. A. Faas, and Thomas H. Sharp. "Correlated Cryo Super‐Resolution Light and Cryo‐Electron Microscopy on Mammalian Cells Expressing the Fluorescent Protein rsEGFP2." Small Methods 3, no. 12 (2019): 1900425. http://dx.doi.org/10.1002/smtd.201900425.

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Grigorenko, Bella L., Tatiana Domratcheva, Igor V. Polyakov, and Alexander V. Nemukhin. "Protonation States of Molecular Groups in the Chromophore-Binding Site Modulate Properties of the Reversibly Switchable Fluorescent Protein rsEGFP2." Journal of Physical Chemistry Letters 12, no. 34 (2021): 8263–71. http://dx.doi.org/10.1021/acs.jpclett.1c02415.

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Wang, Sheng, Miao Ding, Xuanze Chen, Lei Chang, and Yujie Sun. "Development of bimolecular fluorescence complementation using rsEGFP2 for detection and super-resolution imaging of protein-protein interactions in live cells." Biomedical Optics Express 8, no. 6 (2017): 3119. http://dx.doi.org/10.1364/boe.8.003119.

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Zitter, Elke De, Sam Duwé, Peter Dedecker, and Luc Van Meervelt. "Crystal structures of RSEGFP and RSGREEN0.7 reveal photoswitching in EGFP-derived fluorescent proteins." Acta Crystallographica Section A Foundations and Advances 71, a1 (2015): s228. http://dx.doi.org/10.1107/s2053273315096552.

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Zhang, Xi, Mingshu Zhang, Dong Li, et al. "Highly photostable, reversibly photoswitchable fluorescent protein with high contrast ratio for live-cell superresolution microscopy." Proceedings of the National Academy of Sciences 113, no. 37 (2016): 10364–69. http://dx.doi.org/10.1073/pnas.1611038113.

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Two long-standing problems for superresolution (SR) fluorescence microscopy are high illumination intensity and long acquisition time, which significantly hamper its application for live-cell imaging. Reversibly photoswitchable fluorescent proteins (RSFPs) have made it possible to dramatically lower the illumination intensities in saturated depletion-based SR techniques, such as saturated depletion nonlinear structured illumination microscopy (NL-SIM) and reversible saturable optical fluorescence transition microscopy. The characteristics of RSFPs most critical for SR live-cell imaging include
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Grotjohann, Tim, Ilaria Testa, Matthias Reuss, et al. "rsEGFP2 enables fast RESOLFT nanoscopy of living cells." eLife 1 (December 31, 2012). http://dx.doi.org/10.7554/elife.00248.

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The super-resolution microscopy called RESOLFT relying on fluorophore switching between longlived states, stands out by its coordinate-targeted sequential sample interrogation using low light levels. While RESOLFT has been shown to discern nanostructures in living cells, the reversibly photoswitchable green fluorescent protein (rsEGFP) employed in these experiments was switched rather slowly and recording lasted tens of minutes. We now report on the generation of rsEGFP2 providing faster switching and the use of this protein to demonstrate 25–250 times faster recordings.
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Schnorrenberg, Sebastian, Tim Grotjohann, Gerd Vorbrüggen, Alf Herzig, Stefan W. Hell, and Stefan Jakobs. "In vivo super-resolution RESOLFT microscopy of Drosophila melanogaster." eLife 5 (June 29, 2016). http://dx.doi.org/10.7554/elife.15567.

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Despite remarkable developments in diffraction unlimited super-resolution microscopy, in vivo nanoscopy of tissues and model organisms is still not satisfactorily established and rarely realized. RESOLFT nanoscopy is particularly suited for live cell imaging because it requires relatively low light levels to overcome the diffraction barrier. Previously, we introduced the reversibly switchable fluorescent protein rsEGFP2, which facilitated fast RESOLFT nanoscopy (<xref ref-type="bibr" rid="bib10">Grotjohann et al., 2012</xref>). In that study, as in most other nanoscopy studies, onl
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Dissertations / Theses on the topic "RsEGFP2"

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Grotjohann, Tim. "Generation of Novel Photochromic GFPs: Fluorescent Probes for RESOLFT-type Microscopy at Low Light Intensities." Doctoral thesis, 2012. http://hdl.handle.net/11858/00-1735-0000-000D-EF5C-2.

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