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Journal articles on the topic 'Super-resolution ; dSTORM ; fluorescence microscopy'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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1

Whelan, Donna R., Thorge Holm, Markus Sauer, and Toby D. M. Bell. "Focus on Super-Resolution Imaging with Direct Stochastic Optical Reconstruction Microscopy (dSTORM)." Australian Journal of Chemistry 67, no. 2 (2014): 179. http://dx.doi.org/10.1071/ch13499.

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The last decade has seen the development of several microscopic techniques capable of achieving spatial resolutions that are well below the diffraction limit of light. These techniques, collectively referred to as ‘super-resolution’ microscopy, are now finding wide use, particularly in cell biology, routinely generating fluorescence images with resolutions in the order of tens of nanometres. In this highlight, we focus on direct Stochastic Optical Reconstruction Microscopy or dSTORM, one of the localisation super-resolution fluorescence microscopy techniques that are founded on the detection of fluorescence emissions from single molecules. We detail how, with minimal assemblage, a highly functional and versatile dSTORM set-up can be built from ‘off-the-shelf’ components at quite a modest budget, especially when compared with the current cost of commercial systems. We also present some typical super-resolution images of microtubules and actin filaments within cells and discuss sample preparation and labelling methods.

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2

Khan, Abdullah O., Alessandro Di Maio, Emily J. Guggenheim, et al. "Surface Chemistry-Dependent Evolution of the Nanomaterial Corona on TiO2 Nanomaterials Following Uptake and Sub-Cellular Localization." Nanomaterials 10, no. 3 (2020): 401. http://dx.doi.org/10.3390/nano10030401.

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Nanomaterial (NM) surface chemistry has an established and significant effect on interactions at the nano-bio interface, with important toxicological consequences for manufactured NMs, as well as potent effects on the pharmacokinetics and efficacy of nano-therapies. In this work, the effects of different surface modifications (PVP, Dispex AA4040, and Pluronic F127) on the uptake, cellular distribution, and degradation of titanium dioxide NMs (TiO2 NMs, ~10 nm core size) are assessed and correlated with the localization of fluorescently-labeled serum proteins forming their coronas. Imaging approaches with an increasing spatial resolution, including automated high throughput live cell imaging, correlative confocal fluorescence and reflectance microscopy, and dSTORM super-resolution microscopy, are used to explore the cellular fate of these NMs and their associated serum proteins. Uncoated TiO2 NMs demonstrate a rapid loss of corona proteins, while surface coating results in the retention of the corona signal after internalization for at least 24 h (varying with coating composition). Imaging with two-color super-resolution dSTORM revealed that the apparent TiO2 NM single agglomerates observed in diffraction-limited confocal microscopy are actually adjacent smaller agglomerates, and provides novel insights into the spatial arrangement of the initial and exchanged coronas adsorbed at the NM surfaces.

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3

Danson, Amy E., Alex McStea, Lin Wang, et al. "Super-Resolution Fluorescence Microscopy Reveals Clustering Behaviour of Chlamydia pneumoniae’s Major Outer Membrane Protein." Biology 9, no. 10 (2020): 344. http://dx.doi.org/10.3390/biology9100344.

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Chlamydia pneumoniae is a Gram-negative bacterium responsible for a number of human respiratory diseases and linked to some chronic inflammatory diseases. The major outer membrane protein (MOMP) of Chlamydia is a conserved immunologically dominant protein located in the outer membrane, which, together with its surface exposure and abundance, has led to MOMP being the main focus for vaccine and antimicrobial studies in recent decades. MOMP has a major role in the chlamydial outer membrane complex through the formation of intermolecular disulphide bonds, although the exact interactions formed are currently unknown. Here, it is proposed that due to the large number of cysteines available for disulphide bonding, interactions occur between cysteine-rich pockets as opposed to individual residues. Such pockets were identified using a MOMP homology model with a supporting low-resolution (~4 Å) crystal structure. The localisation of MOMP in the E. coli membrane was assessed using direct stochastic optical reconstruction microscopy (dSTORM), which showed a decrease in membrane clustering with cysteine-rich regions containing two mutations. These results indicate that disulphide bond formation was not disrupted by single mutants located in the cysteine-dense regions and was instead compensated by neighbouring cysteines within the pocket in support of this cysteine-rich pocket hypothesis.

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4

Jayasinghe, Isuru D., Michelle Munro, David Baddeley, Bradley S. Launikonis, and Christian Soeller. "Observation of the molecular organization of calcium release sites in fast- and slow-twitch skeletal muscle with nanoscale imaging." Journal of The Royal Society Interface 11, no. 99 (2014): 20140570. http://dx.doi.org/10.1098/rsif.2014.0570.

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Localization microscopy is a fairly recently introduced super-resolution fluorescence imaging modality capable of achieving nanometre-scale resolution. We have applied the dSTORM variation of this method to image intracellular molecular assemblies in skeletal muscle fibres which are large cells that critically rely on nanoscale signalling domains, the triads. Immunofluorescence staining in fixed adult rat skeletal muscle sections revealed clear differences between fast- and slow-twitch fibres in the molecular organization of ryanodine receptors (RyRs; the primary calcium release channels) within triads. With the improved resolution offered by dSTORM, abutting arrays of RyRs in transverse view of fast fibres were observed in contrast to the fragmented distribution on slow-twitch muscle that were approximately 1.8 times shorter and consisted of approximately 1.6 times fewer receptors. To the best of our knowledge, for the first time, we have quantified the nanometre-scale spatial association between triadic proteins using multi-colour super-resolution, an analysis difficult to conduct with electron microscopy. Our findings confirm that junctophilin-1 (JPH1), which tethers the sarcoplasmic reticulum ((SR) intracellular calcium store) to the tubular (t-) system at triads, was present throughout the RyR array, whereas JPH2 was contained within much smaller nanodomains. Similar imaging of the primary SR calcium buffer, calsequestrin (CSQ), detected less overlap of the triad with CSQ in slow-twitch muscle supporting greater spatial heterogeneity in the luminal Ca 2+ buffering when compared with fast twitch muscle. Taken together, these nanoscale differences can explain the fundamentally different physiologies of fast- and slow-twitch muscle.

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5

Jing, Yingying, Mingjun Cai, Haijiao Xu, et al. "Aptamer-recognized carbohydrates on the cell membrane revealed by super-resolution microscopy." Nanoscale 10, no. 16 (2018): 7457–64. http://dx.doi.org/10.1039/c8nr00089a.

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6

Huang, Bo, Mark Bates, and Xiaowei Zhuang. "Super-Resolution Fluorescence Microscopy." Annual Review of Biochemistry 78, no. 1 (2009): 993–1016. http://dx.doi.org/10.1146/annurev.biochem.77.061906.092014.

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7

Garcia-Guerrero, Estefania, Luis Gerardo Rodríguez-Lobato, Sophia Danhof, et al. "ATRA Augments BCMA Expression on Myeloma Cells and Enhances Recognition By BCMA-CAR T-Cells." Blood 136, Supplement 1 (2020): 13–14. http://dx.doi.org/10.1182/blood-2020-142572.

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Background: B cell maturation antigen (BCMA) is a B-lineage antigen that is retained on malignant plasma cells in multiple myeloma (MM), and is under investigation as a target antigen for humoral and cellular immunotherapy. Targeting BCMA with chimeric antigen receptor (CAR) T-cells, T-cell engaging antibodies and antibody-drug conjugates has resulted in high rates of clinical responses however, the depth and durability of these responses is still not satisfactory and most patients ultimately relapse. This has been attributed at least in part to low or non-uniform BCMA expression on MM cells, as well as MM cell escape after BCMA down-regulation or even loss. Here, we show that epigenetic modulation with all-trans retinoic acid (ATRA) augments BCMA expression at the gene (and protein) level and leads to enhanced BCMA molecule density on the surface of MM cells that translates into increased anti-MM potency of BCMA CAR T-cells. Methods: Primary MM cells and myeloma cell lines were treated with titrated doses of ATRA (25, 50, 100 nM), alone and in combination with the g-secretase inhibitor crenigacestat (10 nM). BCMA expression was analyzed by flow cytometry, RT-qPCR and direct stochastic optical reconstruction microscopy (dSTORM). BCMA CAR T-cells were derived from healthy donors and MM patients (n&gt;6) and their anti-MM function analyzed in vitro and in the NSG/MM.1S murine xenograft model in vivo. Results: By RT-qPCR, we observed a 1.8-fold (MM.1S) and 2.1-fold (OPM-2) increase in BCMA gene expression after treatment with 50 nM ATRA for 72 hours. By flow-cytometry, we confirmed increased BCMA protein expression, with 1.9-fold (MM.1S and OPM-2) increase in mean fluorescence intensity relative to isotype control staining. Super-resolution dSTORM microscopy on MM.1S cells confirmed the increase in BCMA protein expression and showed a homogenous distribution pattern of BCMA molecules across the cell surface without an increase in cluster formation. These data were confirmed with primary MM cells from patients with newly diagnosed (n=7) and relapsed/refractory (n=11) MM. The increase in MFI for BCMA expression on primary MM cells after ATRA treatment was 1.2-fold - 2.2-fold (mean: 1.6-fold; p=.01 at 50 nM ATRA). By ELISA, we did not detect increased levels of soluble BCMA protein in supernatant of MM.1S cells after ATRA treatment. Accordingly, we found superior cytolytic activity, cytokine secretion and proliferation of CD8+ and CD4+BCMA CAR T-cells in response to ATRA-treated vs. non-treated primary MM cells and MM cell lines. In the NSG/MM.1S xenograft model, we confirmed increased BCMA expression on MM.1S after systemic treatment with ATRA, and superior anti-MM activity after adoptive transfer of BCMA CAR T-cells. Further, we confirmed that epigenetic modulation of BCMA-expression with ATRA works synergistically with g-secretase inhibitor treatment that has recently been shown to prevent cleavage of BCMA molecules from the surface of MM cells (Pont Blood 2019). Combination treatment with ATRA and the g-secretase inhibitor crenigacestat led to higher BCMA density on primary MM cells (and cell lines) than each single-agent treatment alone, resulting in maximum reactivity of by BCMA CAR T-cells in vitro and in vivo. Conclusions: Taken together, the data show that BCMA expression on MM cells can be increased by epigenetic modulation with ATRA. After ATRA treatment, MM cells have increased susceptibility to BCMA CAR T-cell treatment in pre-clinical models vitro and in vivo, that can be increased even further by combination treatment of ATRA and g-secretase inhibitors. These data suggest the potential to improve responses (depth and durability) of immunotherapies directed against BCMA. Disclosures Einsele: Takeda: Consultancy, Honoraria, Speakers Bureau; Bristol-Myers Squibb: Consultancy, Honoraria, Research Funding, Speakers Bureau; Amgen: Consultancy, Honoraria, Research Funding, Speakers Bureau; Celgene: Consultancy, Honoraria, Research Funding, Speakers Bureau; Janssen: Consultancy, Honoraria, Research Funding, Speakers Bureau; Novartis: Honoraria, Speakers Bureau; Sanofi: Consultancy, Honoraria, Research Funding, Speakers Bureau; GlaxoSmithKline: Honoraria, Research Funding, Speakers Bureau.

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8

Varga, Dániel, Hajnalka Majoros, Zsuzsanna Ujfaludi, Miklós Erdélyi, and Tibor Pankotai. "Quantification of DNA damage induced repair focus formation via super-resolution dSTORM localization microscopy." Nanoscale 11, no. 30 (2019): 14226–36. http://dx.doi.org/10.1039/c9nr03696b.

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9

Gao, Jing, Ye Wang, Mingjun Cai, et al. "Mechanistic insights into EGFR membrane clustering revealed by super-resolution imaging." Nanoscale 7, no. 6 (2015): 2511–19. http://dx.doi.org/10.1039/c4nr04962d.

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We investigate the distribution of membrane EGFR by direct stochastic optical reconstruction microscopy (dSTORM). Our results illustrate the clustering distribution pattern of EGFR in polarized cells and uncover the essential role of lipid rafts in EGFR cluster maintenance.

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10

Zhanghao, Karl, Juntao Gao, Dayong Jin, Xuedian Zhang, and Peng Xi. "Super-resolution fluorescence polarization microscopy." Journal of Innovative Optical Health Sciences 11, no. 01 (2017): 1730002. http://dx.doi.org/10.1142/s1793545817300026.

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Fluorescence polarization is related to the dipole orientation of chromophores, making fluorescence polarization microscopy possible to reveal structures and functions of tagged cellular organelles and biological macromolecules. Several recent super resolution techniques have been applied to fluorescence polarization microscopy, achieving dipole measurement at nanoscale. In this review, we summarize both diffraction limited and super resolution fluorescence polarization microscopy techniques, as well as their applications in biological imaging.

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11

Zhang, Min, Junling Chen, Zhiyuan Tian, and Hongda Wang. "Reply to the ‘Comment on “Magnetic-field-enabled resolution enhancement in super-resolution imaging”' by Bergmann et al., Physical Chemistry Chemical Physics, 2017, 19, DOI: 10.1039/C6CP05108A." Physical Chemistry Chemical Physics 19, no. 6 (2017): 4891–92. http://dx.doi.org/10.1039/c6cp06510d.

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12

Pastrana, Erika. "Fast 3D super-resolution fluorescence microscopy." Nature Methods 8, no. 1 (2010): 46. http://dx.doi.org/10.1038/nmeth.f.335.

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13

Mishin, A. S., and K. A. Lukyanov. "Live-Cell Super-resolution Fluorescence Microscopy." Biochemistry (Moscow) 84, S1 (2019): 19–31. http://dx.doi.org/10.1134/s0006297919140025.

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14

Mondal, Partha Pratim. "Spatio-temporal Super-resolution Optical Fluorescence Microscopy." iScience Notes 1, no. 1 (2016): 4. http://dx.doi.org/10.22580/2016/iscinote.4.

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15

Mondal, Partha Pratim. "Spatio-temporal Super-resolution Optical Fluorescence Microscopy." iScience Notes 1, no. 1 (2016): 1. http://dx.doi.org/10.22580/2016/iscinotej1.1.4.

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16

FUJITA, Katsumasa. "Recent Developments in Super Resolution Fluorescence Microscopy." Seibutsu Butsuri 50, no. 4 (2010): 174–79. http://dx.doi.org/10.2142/biophys.50.174.

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17

Stöhr, Rainer J., Roman Kolesov, Kangwei Xia, et al. "Super-resolution Fluorescence Quenching Microscopy of Graphene." ACS Nano 6, no. 10 (2012): 9175–81. http://dx.doi.org/10.1021/nn303510p.

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18

Schermelleh, Lothar, Rainer Heintzmann, and Heinrich Leonhardt. "A guide to super-resolution fluorescence microscopy." Journal of Cell Biology 190, no. 2 (2010): 165–75. http://dx.doi.org/10.1083/jcb.201002018.

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For centuries, cell biology has been based on light microscopy and at the same time been limited by its optical resolution. However, several new technologies have been developed recently that bypass this limit. These new super-resolution technologies are either based on tailored illumination, nonlinear fluorophore responses, or the precise localization of single molecules. Overall, these new approaches have created unprecedented new possibilities to investigate the structure and function of cells.

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19

Lin, Youhui, Karin Nienhaus, and Gerd Ulrich Nienhaus. "Nanoparticle Probes for Super-Resolution Fluorescence Microscopy." ChemNanoMat 4, no. 3 (2018): 253–64. http://dx.doi.org/10.1002/cnma.201700375.

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20

McGray, Craig D., Samuel M. Stavis, Joshua Giltinan, et al. "MEMS Kinematics by Super-Resolution Fluorescence Microscopy." Journal of Microelectromechanical Systems 22, no. 1 (2013): 115–23. http://dx.doi.org/10.1109/jmems.2012.2216506.

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21

Lippincott-Schwartz, Jennifer, and Suliana Manley. "Putting super-resolution fluorescence microscopy to work." Nature Methods 6, no. 1 (2008): 21–23. http://dx.doi.org/10.1038/nmeth.f.233.

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22

Mohammadian, Sajjad, Alexandra V. Agronskaia, Gerhard A. Blab, et al. "Integrated super resolution fluorescence microscopy and transmission electron microscopy." Ultramicroscopy 215 (August 2020): 113007. http://dx.doi.org/10.1016/j.ultramic.2020.113007.

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23

Birk. "Super-Resolution Microscopy of Chromatin." Genes 10, no. 7 (2019): 493. http://dx.doi.org/10.3390/genes10070493.

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Since the advent of super-resolution microscopy, countless approaches and studies have been published contributing significantly to our understanding of cellular processes. With the aid of chromatin-specific fluorescence labeling techniques, we are gaining increasing insight into gene regulation and chromatin organization. Combined with super-resolution imaging and data analysis, these labeling techniques enable direct assessment not only of chromatin interactions but also of the function of specific chromatin conformational states.

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24

Mazloom-Farsibaf, Hanieh, Farzin Farzam, Mohamadreza Fazel, Michael J. Wester, Marjolein B. M. Meddens, and Keith A. Lidke. "Comparing lifeact and phalloidin for super-resolution imaging of actin in fixed cells." PLOS ONE 16, no. 1 (2021): e0246138. http://dx.doi.org/10.1371/journal.pone.0246138.

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Visualizing actin filaments in fixed cells is of great interest for a variety of topics in cell biology such as cell division, cell movement, and cell signaling. We investigated the possibility of replacing phalloidin, the standard reagent for super-resolution imaging of F-actin in fixed cells, with the actin binding peptide ‘lifeact’. We compared the labels for use in single molecule based super-resolution microscopy, where AlexaFluor 647 labeled phalloidin was used in a dSTORM modality and Atto 655 labeled lifeact was used in a single molecule imaging, reversible binding modality. We found that imaging with lifeact had a comparable resolution in reconstructed images and provided several advantages over phalloidin including lower costs, the ability to image multiple regions of interest on a coverslip without degradation, simplified sequential super-resolution imaging, and more continuous labeling of thin filaments.

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25

Li, Mengting, and Zhen-Li Huang. "Rethinking resolution estimation in fluorescence microscopy: from theoretical resolution criteria to super-resolution microscopy." Science China Life Sciences 63, no. 12 (2020): 1776–85. http://dx.doi.org/10.1007/s11427-020-1785-4.

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26

DAKE, Fumihiro. "Super-Resolution Fluorescence Microscopy Using Light-Matter Interactions." Journal of the Japan Society for Precision Engineering 86, no. 7 (2020): 524–28. http://dx.doi.org/10.2493/jjspe.86.524.

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27

Wang, Yong, and Jingyi Fei. "Continuous active development of super-resolution fluorescence microscopy." Physical Biology 17, no. 3 (2020): 030401. http://dx.doi.org/10.1088/1478-3975/ab7731.

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28

Hirvonen, Liisa M., and Trevor A. Smith. "Imaging on the Nanoscale: Super-Resolution Fluorescence Microscopy." Australian Journal of Chemistry 64, no. 1 (2011): 41. http://dx.doi.org/10.1071/ch10333.

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Although the resolution of a light microscope is fundamentally limited by diffraction to about half of the wavelength of light, in recent years several techniques have been developed that can overcome this limitation in fluorescence microscopy, allowing imaging with nanometre scale resolution. Many of these techniques are based on photoswitchable molecules that can switch between a bright, fluorescent and a dark, nonfluorescent state. Some of these techniques, as well as their limitations, are discussed.

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29

Deng, Yi, Mingzhai Sun, Pei-Hui Lin, Jianjie Ma, and Joshua W. Shaevitz. "Spatial Covariance Reconstructive (SCORE) Super-Resolution Fluorescence Microscopy." PLoS ONE 9, no. 4 (2014): e94807. http://dx.doi.org/10.1371/journal.pone.0094807.

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30

ZHANG Zhi-min, 张智敏, 匡翠方 KUANG Cui-fang, 王子昂 WANG Zi-ang, et al. "Dual-color fluorescence emission difference super-resolution microscopy." Chinese Optics 11, no. 3 (2018): 329–36. http://dx.doi.org/10.3788/co.20181103.0329.

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31

Klementieva, N. V., E. V. Zagaynova, K. A. Lukyanov, and A. S. Mishin. "The Principles of Super-Resolution Fluorescence Microscopy (Review)." Sovremennye tehnologii v medicine 8, no. 2 (2016): 130–40. http://dx.doi.org/10.17691/stm2016.8.2.17.

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32

Bischak, Connor G., Craig L. Hetherington, Jake T. Precht, et al. "Super Resolution Fluorescence Microscopy by Cathodoluminescence-Activated Excitation." Biophysical Journal 108, no. 2 (2015): 36a. http://dx.doi.org/10.1016/j.bpj.2014.11.223.

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33

van der Velde, Jasper H. M., Jochem H. Smit, Elke Hebisch, Vanessa Trauschke, Michiel Punter, and Thorben Cordes. "Self-healing dyes for super-resolution fluorescence microscopy." Journal of Physics D: Applied Physics 52, no. 3 (2018): 034001. http://dx.doi.org/10.1088/1361-6463/aae752.

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34

Harootunian, A., E. Betzig, M. Isaacson, and A. Lewis. "Super‐resolution fluorescence near‐field scanning optical microscopy." Applied Physics Letters 49, no. 11 (1986): 674–76. http://dx.doi.org/10.1063/1.97565.

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35

Leung, Bonnie O., and Keng C. Chou. "Review of Super-Resolution Fluorescence Microscopy for Biology." Applied Spectroscopy 65, no. 9 (2011): 967–80. http://dx.doi.org/10.1366/11-06398.

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36

Zhang, Yide, Prakash D. Nallathamby, Genevieve D. Vigil, et al. "Super-resolution fluorescence microscopy by stepwise optical saturation." Biomedical Optics Express 9, no. 4 (2018): 1613. http://dx.doi.org/10.1364/boe.9.001613.

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37

Han, Kyu Young, Eva Rittweger, Scott E. Irvine, Christian Eggeling, and Stefan W. Hell. "Optimizing Fluorophores For Super-resolution Fluorescence STED Microscopy." Biophysical Journal 96, no. 3 (2009): 637a. http://dx.doi.org/10.1016/j.bpj.2008.12.3371.

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38

Castelletto, Stefania, and Alberto Boretti. "Viral particle imaging by super-resolution fluorescence microscopy." Chemical Physics Impact 2 (June 2021): 100013. http://dx.doi.org/10.1016/j.chphi.2021.100013.

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39

Gabor, Kristin A., Mudalige S. Gunewardene, David Santucci, and Samuel T. Hess. "Localization-Based Super-Resolution Light Microscopy." Microscopy Today 19, no. 4 (2011): 12–16. http://dx.doi.org/10.1017/s1551929511000435.

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Fluorescence microscopy is an essential and flexible tool for the study of biology, chemistry, and physics. It can provide information on a wide range of spatial and temporal scales. However, since the inception of light microscopy, diffraction has limited the size of the smallest details that could be imaged in any sample using light. Because much of biology occurs on molecular length scales, interest in circumventing the diffraction limit has been high for many years. Recently, several techniques have been introduced that can bend or break the diffraction limit. Localization-based methods introduced in 2006 have reached this goal and are now rapidly growing in popularity.

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40

LEE, Jinwoo, and Sungchul HOHNG. "Super-resolution Fluorescence Microscopy Based on Single-molecule Localization." Physics and High Technology 22, no. 11 (2013): 34. http://dx.doi.org/10.3938/phit.22.053.

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41

Mlodzianoski, Michael J. "Future Considerations for Localization Based Super-Resolution Fluorescence Microscopy." iScience Notes 1, no. 1 (2016): 1. http://dx.doi.org/10.22580/2016/iscinotej1.1.5.

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42

Mlodzianoski, Michael J. "Future Considerations for Localization Based Super-Resolution Fluorescence Microscopy." iScience Notes 2, no. 1 (2017): 1. http://dx.doi.org/10.22580/2017/iscinote.1.

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43

Guo, Min, Panagiotis Chandris, John Paul Giannini, et al. "Single-shot super-resolution total internal reflection fluorescence microscopy." Nature Methods 15, no. 6 (2018): 425–28. http://dx.doi.org/10.1038/s41592-018-0004-4.

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44

Suyama, Taikei, and Yaoju Zhang. "3D SUPER-RESOLUTION FLUORESCENCE MICROSCOPY USING CYLINDRICAL VECTOR BEAMS." Progress In Electromagnetics Research Letters 43 (2013): 73–81. http://dx.doi.org/10.2528/pierl13080205.

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45

Wolff, Georg, Christoph Hagen, Kay Grünewald, and Rainer Kaufmann. "Towards correlative super-resolution fluorescence and electron cryo-microscopy." Biology of the Cell 108, no. 9 (2016): 245–58. http://dx.doi.org/10.1111/boc.201600008.

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46

Flottmann, Benjamin, Manuel Gunkel, Sebastian Malkusch, and Mike Heilemann. "Quantifying Actin mRNA Expression with Super Resolution Fluorescence Microscopy." Biophysical Journal 102, no. 3 (2012): 484a. http://dx.doi.org/10.1016/j.bpj.2011.11.2653.

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47

Mlodzianoski, Michael J., and Joerg Bewersdorf. "Advances in Three Dimensional Super Resolution Fluorescence Localization Microscopy." Biophysical Journal 100, no. 3 (2011): 142a. http://dx.doi.org/10.1016/j.bpj.2010.12.980.

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48

Lindau, Manfred, Qinghua Fang, and Ying Zhao. "Time Super-Resolution Fluorescence Imaging by Event Correlation Microscopy." Biophysical Journal 106, no. 2 (2014): 24a. http://dx.doi.org/10.1016/j.bpj.2013.11.189.

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49

Lu, Xun, Philip R. Nicovich, Katharina Gaus, and J. Justin Gooding. "Towards single molecule biosensors using super-resolution fluorescence microscopy." Biosensors and Bioelectronics 93 (July 2017): 1–8. http://dx.doi.org/10.1016/j.bios.2016.10.048.

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50

Alan, Lukas, Andrea Dlaskova, Tomas Spacek, Jaroslav Zelenka, Tomas Olejar, and Petr Jezek. "Mitochondrial DNA Nucleoid Distribution at Simulated Pathologies as Visualized by 3D Super-Resolution Biplane FPALM / dSTORM Microscopy." Biophysical Journal 106, no. 2 (2014): 203a. http://dx.doi.org/10.1016/j.bpj.2013.11.1194.

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