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Journal articles on the topic 'Total internal reflection fluorescence microscopy'

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Published: 4 June 2021
Last updated: 18 February 2022

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1

Yildiz, Ahmet, and Ronald D. Vale. "Total Internal Reflection Fluorescence Microscopy." Cold Spring Harbor Protocols 2015, no. 9 (2015): pdb.top086348. http://dx.doi.org/10.1101/pdb.top086348.

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2

Denham, Simon, and Deborah Cutchey. "Total Internal Reflection Fluorescence (TIRF) Microscopy." Imaging & Microscopy 11, no. 2 (2009): 54–55. http://dx.doi.org/10.1002/imic.200990043.

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3

Kudalkar, Emily M., Trisha N. Davis, and Charles L. Asbury. "Single-Molecule Total Internal Reflection Fluorescence Microscopy." Cold Spring Harbor Protocols 2016, no. 5 (2016): pdb.top077800. http://dx.doi.org/10.1101/pdb.top077800.

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4

Uchida, Maho, Rosa R. Mouriño-Pérez, and Robert W. Roberson. "Total internal reflection fluorescence microscopy of fungi." Fungal Biology Reviews 24, no. 3-4 (2010): 132–36. http://dx.doi.org/10.1016/j.fbr.2010.12.003.

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5

Schmoranzer, Jan, Mark Goulian, Dan Axelrod, and Sanford M. Simon. "Imaging Constitutive Exocytosis with Total Internal Reflection Fluorescence Microscopy." Journal of Cell Biology 149, no. 1 (2000): 23–32. http://dx.doi.org/10.1083/jcb.149.1.23.

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Total internal reflection fluorescence microscopy has been applied to image the final stage of constitutive exocytosis, which is the fusion of single post-Golgi carriers with the plasma membrane. The use of a membrane protein tagged with green fluorescent protein allowed the kinetics of fusion to be followed with a time resolution of 30 frames/s. Quantitative analysis allowed carriers undergoing fusion to be easily distinguished from carriers moving perpendicularly to the plasma membrane. The flattening of the carriers into the plasma membrane is seen as a simultaneous rise in the total, peak, and width of the fluorescence intensity. The duration of this flattening process depends on the size of the carriers, distinguishing small spherical from large tubular carriers. The spread of the membrane protein into the plasma membrane upon fusion is diffusive. Mapping many fusion sites of a single cell reveals that there are no preferred sites for constitutive exocytosis in this system.
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6

Beaumont, V. "Visualizing membrane trafficking using total internal reflection fluorescence microscopy." Biochemical Society Transactions 31, no. 4 (2003): 819–23. http://dx.doi.org/10.1042/bst0310819.

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There is a dizzying array of fluorescent probes now commercially available to monitor cellular processes, and advances in molecular biology have highlighted the ease with which proteins can now be labelled with fluorophores without loss of functionality. This has led to an explosion in the popularity of fluorescence microscopy techniques. One such specialized technique, total internal reflection fluorescence microscopy (TIR-FM), is ideally suited to gaining insight into events occurring at, or close to, the plasma membrane of live cells with excellent optical resolution. In the last few years, the application of TIR-FM to membrane trafficking events in both non-excitable and excitable cells has been an area of notable expansion and fruition. This review gives a brief overview of that literature, with emphasis on the study of the regulation of exocytosis and endocytosis in excitable cells using TIR-FM. Finally, recent applications of TIR-FM to the study of cellular processes at the molecular level are discussed briefly, providing promise that the future of TIR-FM in cell biology will only get brighter.
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7

Burghardt, Thomas P., Andrew D. Hipp, and Katalin Ajtai. "Around-the-objective total internal reflection fluorescence microscopy." Applied Optics 48, no. 32 (2009): 6120. http://dx.doi.org/10.1364/ao.48.006120.

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8

Axelrod, Daniel. "Total Internal Reflection Fluorescence Microscopy in Cell Biology." Traffic 2, no. 11 (2001): 764–74. http://dx.doi.org/10.1034/j.1600-0854.2001.21104.x.

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9

Kuznetsova, O. B., E. A. Savchenko, A. A. Andryakov, E. Y. Savchenko, and Z. A. Musakulova. "Image processing in total internal reflection fluorescence microscopy." Journal of Physics: Conference Series 1236 (June 2019): 012039. http://dx.doi.org/10.1088/1742-6596/1236/1/012039.

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10

Asbury, Charles L. "Data Analysis for Total Internal Reflection Fluorescence Microscopy." Cold Spring Harbor Protocols 2016, no. 5 (2016): pdb.prot085571. http://dx.doi.org/10.1101/pdb.prot085571.

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11

Leutenegger, Marcel, and Theo Lasser. "Detection efficiency in total internal reflection fluorescence microscopy." Optics Express 16, no. 12 (2008): 8519. http://dx.doi.org/10.1364/oe.16.008519.

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12

Burghardt, Thomas P., Andrew D. Hipp, and Katalin Ajtai. "Around-the-Objective Total Internal Reflection Fluorescence Microscopy." Biophysical Journal 98, no. 3 (2010): 177a—178a. http://dx.doi.org/10.1016/j.bpj.2009.12.949.

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13

Thompson, N. "Total Internal Reflection with Fluorescence Correlation Spectroscopy." Microscopy and Microanalysis 17, S2 (2011): 38–39. http://dx.doi.org/10.1017/s1431927611001061.

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14

Reichert, W. M., and G. A. Truskey. "Total internal reflection fluorescence (TIRF) microscopy. I. Modelling cell contact region fluorescence." Journal of Cell Science 96, no. 2 (1990): 219–30. http://dx.doi.org/10.1242/jcs.96.2.219.

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Total Internal Reflection Fluorescence (TIRF) is a powerful technique for visualizing focal and close contacts between the cell and the surface. Practical application of TIRF has been hampered by the lack of straightforward methods to calculate separation distances. The characteristic matrix theory of thin dielectric films was used to develop simple exponential approximations for the fluorescence excited in the cell-substratum contact region during a TIRF experiment. Two types of fluorescence were examined: fluorescently labeled cell membranes, and a fluorescent water-soluble dye. By neglecting the refractive index of the cell membrane, the fluorescence excited in the cell membrane was modelled by a single exponential function while the fluorescence in the membrane/substratum water gap followed a weighted sum of two exponentials. The error associated with neglecting the cell membrane for an incident angle of 70 degrees never exceeded 2.5%, regardless of the cell-substratum separation distance. Comparisons of approximated fluorescence intensities to more exact solutions of the fluorescence integrals for the three-phase model indicated that the approximations are accurate to about 1% for membrane/substratum gap thicknesses of less than 50 nm if the cytoplasmic and water gap refractive indices are known. The intrinsic error of this model in the determination of membrane/substratum separations was 10% as long as the uncertainties in the water gap and cytoplasmic refractive indices were less than 1%.
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15

Oreopoulos, John, and Christopher M. Yip. "Combined scanning probe and total internal reflection fluorescence microscopy." Methods 46, no. 1 (2008): 2–10. http://dx.doi.org/10.1016/j.ymeth.2008.05.011.

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16

Liu, Qiulan, Youhua Chen, Wenjie Liu, et al. "Total internal reflection fluorescence pattern-illuminated Fourier ptychographic microscopy." Optics and Lasers in Engineering 123 (December 2019): 45–52. http://dx.doi.org/10.1016/j.optlaseng.2019.06.023.

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17

Ross, J., T. Hawkins, and K. Hingorani. "Total Internal Reflection Fluorescence Microscopy to Study Microtubule Dynamics." Microscopy and Microanalysis 17, S2 (2011): 36–37. http://dx.doi.org/10.1017/s143192761100105x.

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18

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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19

Spielmann, Thiemo, Hans Blom, Matthias Geissbuehler, Theo Lasser, and Jerker Widengren. "Transient State Monitoring by Total Internal Reflection Fluorescence Microscopy." Journal of Physical Chemistry B 114, no. 11 (2010): 4035–46. http://dx.doi.org/10.1021/jp911034v.

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20

Knight, Alex E. "Single-molecule fluorescence imaging by total internal reflection fluorescence microscopy (IUPAC Technical Report)." Pure and Applied Chemistry 86, no. 8 (2014): 1303–20. http://dx.doi.org/10.1515/pac-2012-0605.

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AbstractTotal internal reflection fluorescence (TIRF) is a popular illumination technique in microscopy, with many applications in cell and molecular biology and biophysics. The chief advantage of the technique is the high contrast that can be achieved by restricting fluorescent excitation to a thin layer. We summarise the optical theory needed to understand the technique and various aspects required for a practical implementation of it, including the merits of different TIRF geometries. Finally, we discuss a variety of applications including super-resolution microscopy and high-throughput DNA sequencing technologies.
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21

Zheng, Desheng, Leonora Kaldaras, and H. Peter Lu. "Total internal reflection fluorescence microscopy imaging-guided confocal single-molecule fluorescence spectroscopy." Review of Scientific Instruments 83, no. 1 (2012): 013110. http://dx.doi.org/10.1063/1.3677334.

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22

Zheng, Desheng, Leonora Kaldaras, and H. Peter Lu. "Total Internal Reflection Fluorescence Microscopy Imaging-Guided Confocal Single-Molecule Fluorescence Spectroscopy." Biophysical Journal 104, no. 2 (2013): 372a. http://dx.doi.org/10.1016/j.bpj.2012.11.2067.

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23

Burchfield, James G., Jamie A. Lopez, Katarina Mele, Pascal Vallotton, and William E. Hughes. "Exocytotic Vesicle Behaviour Assessed by Total Internal Reflection Fluorescence Microscopy." Traffic 11, no. 4 (2010): 429–39. http://dx.doi.org/10.1111/j.1600-0854.2010.01039.x.

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24

El Arawi, Dalia, Marcelina Cardoso Dos Santos, Cyrille Vézy, and Rodolphe Jaffiol. "Incidence angle calibration for prismless total internal reflection fluorescence microscopy." Optics Letters 44, no. 7 (2019): 1710. http://dx.doi.org/10.1364/ol.44.001710.

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25

Reck-Peterson, S. L., N. D. Derr, and N. Stuurman. "Imaging Single Molecules Using Total Internal Reflection Fluorescence Microscopy (TIRFM)." Cold Spring Harbor Protocols 2010, no. 3 (2010): pdb.top73. http://dx.doi.org/10.1101/pdb.top73.

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26

Lei, Ming, and Andreas Zumbusch. "Total-internal-reflection fluorescence microscopy with W-shaped axicon mirrors." Optics Letters 35, no. 23 (2010): 4057. http://dx.doi.org/10.1364/ol.35.004057.

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27

Dos Santos, Marcelina Cardoso, Régis Déturche, Cyrille Vézy, and Rodolphe Jaffiol. "Axial nanoscale localization by normalized total internal reflection fluorescence microscopy." Optics Letters 39, no. 4 (2014): 869. http://dx.doi.org/10.1364/ol.39.000869.

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28

Sheykhi, Elham, Batool Sajad, Sharareh Tavaddod, Hossein Naderi-Manesh, and Neda Roostaiei. "Tuning fluorophore excitation in a total-internal-reflection-fluorescence microscopy." Applied Optics 58, no. 29 (2019): 8055. http://dx.doi.org/10.1364/ao.58.008055.

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29

Toomre, D. "Generating Live Cell Data Using Total Internal Reflection Fluorescence Microscopy." Cold Spring Harbor Protocols 2012, no. 4 (2012): pdb.ip068676. http://dx.doi.org/10.1101/pdb.ip068676.

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30

BECK, M., M. ASCHWANDEN, and A. STEMMER. "Sub-100-nanometre resolution in total internal reflection fluorescence microscopy." Journal of Microscopy 232, no. 1 (2008): 99–105. http://dx.doi.org/10.1111/j.1365-2818.2008.02075.x.

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31

Chen, Minghan, Natalya V. Zaytseva, Qi Wu, Min Li, and Ye Fang. "Microplate-compatible total internal reflection fluorescence microscopy for receptor pharmacology." Applied Physics Letters 102, no. 19 (2013): 193702. http://dx.doi.org/10.1063/1.4805041.

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32

Toomre, D. "Alignment and Calibration of Total Internal Reflection Fluorescence Microscopy Systems." Cold Spring Harbor Protocols 2012, no. 4 (2012): pdb.prot068668. http://dx.doi.org/10.1101/pdb.prot068668.

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33

Kudalkar, Emily M., Yi Deng, Trisha N. Davis, and Charles L. Asbury. "Coverslip Cleaning and Functionalization for Total Internal Reflection Fluorescence Microscopy." Cold Spring Harbor Protocols 2016, no. 5 (2016): pdb.prot085548. http://dx.doi.org/10.1101/pdb.prot085548.

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34

Ruckstuhl, Thomas, and Stefan Seeger. "Attoliter detection volumes by confocal total-internal-reflection fluorescence microscopy." Optics Letters 29, no. 6 (2004): 569. http://dx.doi.org/10.1364/ol.29.000569.

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35

Fiolka, Reto P., and Andreas Stemmer. "Extending The Resolution In Total Internal Reflection Fluorescence (TIRF) Microscopy." Biophysical Journal 96, no. 3 (2009): 636a. http://dx.doi.org/10.1016/j.bpj.2008.12.3364.

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36

Schneckenburger, Herbert. "Total internal reflection fluorescence microscopy: technical innovations and novel applications." Current Opinion in Biotechnology 16, no. 1 (2005): 13–18. http://dx.doi.org/10.1016/j.copbio.2004.12.004.

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37

Mattheyses, A. L., S. M. Simon, and J. Z. Rappoport. "Imaging with total internal reflection fluorescence microscopy for the cell biologist." Journal of Cell Science 123, no. 21 (2010): 3621–28. http://dx.doi.org/10.1242/jcs.056218.

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38

Toomre, D. "Cellular Imaging Using Total Internal Reflection Fluorescence Microscopy: Theory and Instrumentation." Cold Spring Harbor Protocols 2012, no. 4 (2012): pdb.top068650. http://dx.doi.org/10.1101/pdb.top068650.

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39

Keffer, J. L., C. R. Sabanayagam, M. E. Lee, E. F. DeLong, M. W. Hahn, and J. A. Maresca. "Using Total Internal Reflection Fluorescence Microscopy To Visualize Rhodopsin-Containing Cells." Applied and Environmental Microbiology 81, no. 10 (2015): 3442–50. http://dx.doi.org/10.1128/aem.00230-15.

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ABSTRACTSunlight is captured and converted to chemical energy in illuminated environments. Although (bacterio)chlorophyll-based photosystems have been characterized in detail, retinal-based photosystems, rhodopsins, have only recently been identified as important mediators of light energy capture and conversion. Recent estimates suggest that up to 70% of cells in some environments harbor rhodopsins. However, because rhodopsin autofluorescence is low—comparable to that of carotenoids and significantly less than that of (bacterio)chlorophylls—these estimates are based on metagenomic sequence data, not direct observation. We report here the use of ultrasensitive total internal reflection fluorescence (TIRF) microscopy to distinguish between unpigmented, carotenoid-producing, and rhodopsin-expressing bacteria.Escherichia colicells were engineered to produce lycopene, β-carotene, or retinal. A gene encoding an uncharacterized rhodopsin, actinorhodopsin, was cloned into retinal-producingE. coli. The production of correctly folded and membrane-incorporated actinorhodopsin was confirmed via development of pink color inE. coliand SDS-PAGE. Cells expressing carotenoids or actinorhodopsin were imaged by TIRF microscopy. The 561-nm excitation laser specifically illuminated rhodopsin-containing cells, allowing them to be differentiated from unpigmented and carotenoid-containing cells. Furthermore, water samples collected from the Delaware River were shown by PCR to have rhodopsin-containing organisms and were examined by TIRF microscopy. Individual microorganisms that fluoresced under illumination from the 561-nm laser were identified. These results verify the sensitivity of the TIRF microscopy method for visualizing and distinguishing between different molecules with low autofluorescence, making it useful for analyzing natural samples.
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40

Lee, Eun-Khwang, Jung-Hwan Song, Kwang-Yong Jeong, and Min-Kyo Seo. "Design of plasmonic nano-antenna for total internal reflection fluorescence microscopy." Optics Express 21, no. 20 (2013): 23036. http://dx.doi.org/10.1364/oe.21.023036.

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41

Franken, M. J. Z., C. Poelma, and J. Westerweel. "Nanoscale contact line visualization based on total internal reflection fluorescence microscopy." Optics Express 21, no. 22 (2013): 26093. http://dx.doi.org/10.1364/oe.21.026093.

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42

Fiolka, R., Y. Belyaev, H. Ewers, and A. Stemmer. "Even illumination in total internal reflection fluorescence microscopy using laser light." Microscopy Research and Technique 71, no. 1 (2007): 45–50. http://dx.doi.org/10.1002/jemt.20527.

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43

Thomson, Nancy L., Kenneth H. Pearce, and Helen V. Hsieh. "Total internal reflection fluorescence microscopy: application to substrate-supported planar membranes." European Biophysics Journal 22, no. 5 (1993): 367–78. http://dx.doi.org/10.1007/bf00213560.

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44

Beausang, J. F., Y. Sun, M. E. Quinlan, J. N. Forkey, and Y. E. Goldman. "The Polarized Total Internal Reflection Fluorescence Microscopy (polTIRFM) Twirling Filament Assay." Cold Spring Harbor Protocols 2012, no. 6 (2012): pdb.prot069401. http://dx.doi.org/10.1101/pdb.prot069401.

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45

Kudalkar, Emily M., Trisha N. Davis, and Charles L. Asbury. "Preparation of Reactions for Imaging with Total Internal Reflection Fluorescence Microscopy." Cold Spring Harbor Protocols 2016, no. 5 (2016): pdb.prot085563. http://dx.doi.org/10.1101/pdb.prot085563.

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46

El Arawi, Dalia, Cyrille Vézy, Monique Dontenwill, Maxime Lehmann, and Rodolphe Jaffiol. "Variable-Angle Total Internal Reflection Fluorescence Microscopy: Exploring Integrin-mediated Adhesion." Biophysical Journal 114, no. 3 (2018): 534a—535a. http://dx.doi.org/10.1016/j.bpj.2017.11.2922.

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47

Ohsugi, Yu, and Masataka Kinjo. "Multipoint fluorescence correlation spectroscopy with total internal reflection fluorescence microscope." Journal of Biomedical Optics 14, no. 1 (2009): 014030. http://dx.doi.org/10.1117/1.3080723.

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48

Lin, Jia, and Adam D. Hoppe. "Uniform Total Internal Reflection Fluorescence Illumination Enables Live Cell Fluorescence Resonance Energy Transfer Microscopy." Microscopy and Microanalysis 19, no. 2 (2013): 350–59. http://dx.doi.org/10.1017/s1431927612014420.

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AbstractFluorescence resonance energy transfer (FRET) microscopy is a powerful technique to quantify dynamic protein-protein interactions in live cells. Total internal reflection fluorescence (TIRF) microscopy can selectively excite molecules within about 150 nm of the glass-cell interface. Recently, these two approaches were combined to enable high-resolution FRET imaging on the adherent surface of living cells. Here, we show that interference fringing of the coherent laser excitation used in TIRF creates lateral heterogeneities that impair quantitative TIRF-FRET measurements. We overcome this limitation by using a two-dimensional scan head to rotate laser beams for donor and acceptor excitation around the back focal plane of a high numerical aperture objective. By setting different radii for the circles traced out by each laser in the back focal plane, the penetration depth was corrected for different wavelengths. These modifications quell spatial variations in illumination and permit calibration for quantitative TIRF-FRET microscopy. The capability of TIRF-FRET was demonstrated by imaging assembled cyan and yellow fluorescent protein–tagged HIV-Gag molecules in single virions on the surfaces of living cells. These interactions are shown to be distinct from crowding of HIV-Gag in lipid rafts.
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49

Axelrod, D., L. M. Johns, E. S. Levitan, G. M. Omann, and R. W. Holz. "Submembrane Events In Triggerable Cells Studied by Total Internal Reflection Fluorescence Microscopy." Microscopy and Microanalysis 5, S2 (1999): 1052–53. http://dx.doi.org/10.1017/s1431927600018584.

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We have studied the dynamics of certain key processes near the plasma membrane inside two types of chemically-triggerable living cells using total internal reflection fluorescence microscopy (TIRFM). In TIRFM, a laser beam is incident upon the cell/glass-substrate interface from the glass side at an angle greater than the critical angle for total internal reflection. This creates an exponentially decaying evanescent field in the cell medium (with a characteristic depth of > 100 nm) capable of exciting fluorescence selectively from the membrane-proximal regions at cell/substrate contacts. Various ways of setting up the optics for such a system are discussed, involving the use of either prisms or very high aperture objectives.In one application of TIRFM, the motion of adrenalin-containing secretory granules in the immediate submembrane region of chromaffin cells is examined before and after chemical stimulation that causes the granules to release their contents to the cell exterior.
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50

Forkey, Joseph N., Margot E. Quinlan, and Yale E. Goldman. "Measurement of Single Macromolecule Orientation by Total Internal Reflection Fluorescence Polarization Microscopy." Biophysical Journal 89, no. 2 (2005): 1261–71. http://dx.doi.org/10.1529/biophysj.104.053470.

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