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Correlation Functions Quantify Super-Resolution Images and Estimate Apparent Clustering Due to Over-Counting
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We present an analytical method using correlation functions to quantify clustering in super-resolution fluorescence localization images and electron microscopy images of static surfaces in two dimensions. We use this method to quantify how over-counting of labeled molecules contributes to apparent self-clustering and to calculate the effective lateral resolution of an image. This treatment applies to distributions of proteins and lipids in cell membranes, where there is significant interest in using electron microscopy and super-resolution fluorescence localization techniques to probe membrane heterogeneity. When images are quantified using pair auto-correlation functions, the magnitude of apparent clustering arising from over-counting varies inversely with the surface density of labeled molecules and does not depend on the number of times an average molecule is counted. In contrast, we demonstrate that over-counting does not give rise to apparent co-clustering in double label experiments when pair cross-correlation functions are measured. We apply our analytical method to quantify the distribution of the IgE receptor (FcεRI) on the plasma membranes of chemically fixed RBL-2H3 mast cells from images acquired using stochastic optical reconstruction microscopy (STORM/dSTORM) and scanning electron microscopy (SEM). We find that apparent clustering of FcεRI-bound IgE is dominated by over-counting labels on individual complexes when IgE is directly conjugated to organic fluorophores. We verify this observation by measuring pair cross-correlation functions between two distinguishably labeled pools of IgE-FcεRI on the cell surface using both imaging methods. After correcting for over-counting, we observe weak but significant self-clustering of IgE-FcεRI in fluorescence localization measurements, and no residual self-clustering as detected with SEM. We also apply this method to quantify IgE-FcεRI redistribution after deliberate clustering by crosslinking with two distinct trivalent ligands of defined architectures, and we evaluate contributions from both over-counting of labels and redistribution of proteins.
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“Different from the ACF, overcounting has no effect on the PCF39.”
From A trans-synaptic nanocolumn aligns neurotransmitter release to receptors (2016) · cites this paper as [39]
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“The extent of ga(r) over 1, i.e. r0 for ga(r0) =1, is related to the pattern size of the internal heterogeneity (Extended Data Figure 2b–c)39.”
From A trans-synaptic nanocolumn aligns neurotransmitter release to receptors (2016) · cites this paper as [39]
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Cites
The Fluid Mosaic Model of the Structure of Cell Membranes
Singer, S. J., & Nicolson, G. L. (1972) · Science · doi:10.1126/science.175.4023.720 · Cited by 9,158
Imaging Intracellular Fluorescent Proteins at Nanometer Resolution
Betzig, E., Patterson, G. H., Sougrat, R., Lindwasser, O. W., Olenych, S. G., Bonifacino, J. S., Davidson, M. W., Lippincott‐Schwartz, J., & Hess, H. F. (2006) · Science · doi:10.1126/science.1127344 · Cited by 8,941
Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
Rust, M., Bates, M., & Zhuang, X. (2006) · Nature Methods · doi:10.1038/nmeth929 · Cited by 7,823
Crystal Statistics. I. A Two-Dimensional Model with an Order-Disorder Transition
Onsager, L. (1944) · Physical Review · doi:10.1103/physrev.65.117 · Cited by 6,634
Ultra-High Resolution Imaging by Fluorescence Photoactivation Localization Microscopy
Hess, S. T., Girirajan, T. P. K., & Mason, M. D. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.091116 · Cited by 3,684
Subdiffraction‐Resolution Fluorescence Imaging with Conventional Fluorescent Probes
Heilemann, M., van de Linde, S., Schüttpelz, M., Kasper, R. T., Seefeldt, B., Mukherjee, A., Tinnefeld, P., & Sauer, M. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200802376 · Cited by 1,870
Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission
Klar, T. A., Jakobs, S., Dyba, M., Egner, A., & Hell, S. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.15.8206 · Cited by 1,869
Fast, three-dimensional super-resolution imaging of live cells
Jones, S. A., Shim, S., He, J., & Zhuang, X. (2011) · Nature Methods · doi:10.1038/nmeth.1605 · Cited by 757
Probing protein heterogeneity in the plasma membrane using PALM and pair correlation analysis
Sengupta, P., Jovanović‐Talisman, T., Skoko, D., Renz, M., Veatch, S. L., & Lippincott‐Schwartz, J. (2011) · Nature Methods · doi:10.1038/nmeth.1704 · Cited by 588
Self-citationStatistical Mechanics: Entropy, Order Parameters, and Complexity
Sethna, J. P. (2021) · doi:10.1093/oso/9780198865247.001.0001 · Cited by 495
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Bag, N., Wagenknecht-Wiesner, A., Lee, A., Shi, S. M., Holowka, D. A., & Baird, B. A. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2026583118 · Cited by 46
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Yin, Y., Lee, W. T. C., Gupta, D., Xue, H., Tonzi, P., Borowiec, J. A., Huang, T. T., Modesti, M., & Rothenberg, E. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.08.009 · Cited by 45
Allosteric activation of T cell antigen receptor signaling by quaternary structure relaxation
Lanz, A.-L., Masi, G., Porciello, N., Cohnen, A., Cipria, D., Prakaash, D., Bálint, Š., Raggiaschi, R., Galgano, D., Cole, D. K., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109375 · Cited by 43
Regulation of beta-amyloid production in neurons by astrocyte-derived cholesterolPreprint
Wang, H., Kulas, J. A., Ferris, H. A., & Hansen, S. B. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.18.159632 · Cited by 43
Membrane microdomains: from seeing to understanding
Quang, B. A. T., & Lenne, P. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00018 · Cited by 41
Botulinum neurotoxin type-A enters a non-recycling pool of synaptic vesicles
Harper, C. B., Papadopulos, A., Martin, S., Matthews, D. R., Morgan, G., Nguyen, T. H., Wang, T., Nair, D. K., Choquet, D., & Meunier, F. A. (2016) · Scientific Reports · doi:10.1038/srep19654 · Cited by 41
You, C., Richter, C. P., Löchte, S., Wilmes, S., & Piehler, J. (2014) · Analytical Chemistry · doi:10.1021/ac501127r · Cited by 41
Shelby, S. A., Veatch, S. L., Holowka, D. A., & Baird, B. A. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-06-0425 · Cited by 41
Self-citationHartley, J. M., Chu, T.-W., Peterson, E. M., Zhang, R., Yang, J., Harris, J. M., & Kopec̆ek, J. (2015) · ChemBioChem · doi:10.1002/cbic.201500278 · Cited by 40
Stepwise requirements for polymerases δ and θ in theta-mediated end joining
Stroik, S., Carvajal-Garcia, J., Gupta, D., Edwards, A., Luthman, A. J., Wyatt, D. W., Dannenberg, R. L., Feng, W., Kunkel, T. A., Gupta, G. P., et al. (2023) · Nature · doi:10.1038/s41586-023-06729-7 · Cited by 38
The nanoscale organization of the B lymphocyte membrane
Maity, P. C., Yang, J., Kläsener, K., & Reth, M. G. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.11.010 · Cited by 37
Fluorescence nanoscopy. Methods and applications
Requejo‐Isidro, J. (2013) · Journal of Chemical Biology · doi:10.1007/s12154-013-0096-3 · Cited by 37
Cox, H., Georgiades, P., Xu, H., Waigh, T. A., & Lu, J. R. (2017) · Biomacromolecules · doi:10.1021/acs.biomac.7b00465 · Cited by 37
Zapata, J., Moretto, E., Hannan, S. B., Murru, L., Longatti, A., Mazza, D., Benedetti, L., Fossati, M., Heise, C., Ponzoni, L., et al. (2017) · Nature Communications · doi:10.1038/ncomms14536 · Cited by 38
Quantitative Nanoscale Analysis of IgE-FcεRI Clustering and Coupling to Early Signaling Proteins
Veatch, S. L., Chiang, E. N., Sengupta, P., Holowka, D. A., & Baird, B. A. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp300197p · Cited by 36
Self-citationLin, J., Wester, M. J., Graus, M. S., Lidke, K. A., & Neumann, A. K. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-06-0355 · Cited by 37
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Brandsma, A. M., Schwartz, S. L., Wester, M. J., Valley, C. C., Blezer, G., Vidarsson, G., Lidke, K. A., ten Broeke, T., Lidke, D. S., & Leusen, J. H. W. (2018) · Science Signaling · doi:10.1126/scisignal.aaq0891 · Cited by 39
Grover, J. R., Llewellyn, G. N., Soheilian, F., Nagashima, K., Veatch, S. L., & Ono, A. (2013) · Journal of Virology · doi:10.1128/jvi.03526-12 · Cited by 35
Self-citationGao, L., Chen, J., Gao, J., Wang, H., & Xiong, W. (2016) · Journal of Cell Science · doi:10.1242/jcs.192450 · Cited by 35
Andrews, J. O., Conway, W., Cho, W., Narayanan, A., Spille, J.-H., Jayanth, N., Inoue, T., Mullen, S., Thaler, J., & Cissé, I. I. (2018) · Scientific Reports · doi:10.1038/s41598-018-25454-0 · Cited by 35
Ultrafast single-molecule imaging reveals focal adhesion nano-architecture and molecular dynamics
Fujiwara, T. K., Tsunoyama, T. A., Takeuchi, S., Kalay, Z., Nagai, Y., Kalkbrenner, T., Nemoto, Y. L., Chen, L. H., Shibata, A. C. E., Iwasawa, K., et al. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202110162 · Cited by 36
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Griffié, J., Shlomovich, L., Williamson, D. J., Shannon, M. J., Aaron, J., Khuon, S., Burn, G. L., Boelen, L., Peters, R., Cope, A. P., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-04450-w · Cited by 34
Smith, E. M., Gautier, A., & Puchner, E. M. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00149 · Cited by 34
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Mateos‐Gil, P., Letschert, S., Doose, S., & Sauer, M. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00098 · Cited by 33
Challenges facing quantitative large-scale optical super-resolution, and some simple solutions
Dankovich, T. M., & Rizzoli, S. O. (2021) · iScience · doi:10.1016/j.isci.2021.102134 · Cited by 33
Habuchi, S. (2014) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2014.00020 · Cited by 35
Basic Motifs Target PSGL-1, CD43, and CD44 to Plasma Membrane Sites Where HIV-1 Assembles
Grover, J. R., Veatch, S. L., & Ono, A. (2014) · Journal of Virology · doi:10.1128/jvi.02178-14 · Cited by 32
Self-citationYou, C., Marquez-Lago, T., Richter, C., Wilmes, S., Moraga, I., Garcia, K., Leier, A., & Piehler, J. (2016) · Science Advances · doi:10.1126/sciadv.1600452 · Cited by 35
Ultrafast data mining of molecular assemblies in multiplexed high-density super-resolution images
Yin, Y., Lee, W. T. C., & Rothenberg, E. (2019) · Nature Communications · doi:10.1038/s41467-018-08048-2 · Cited by 32
Towards single molecule biosensors using super-resolution fluorescence microscopy
Lu, X., Nicovich, P. R., Gaus, K., & Gooding, J. J. (2016) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2016.10.048 · Cited by 31
Bermudez‐Hernandez, K., Keegan, S., Whelan, D. R., Reid, D. A., Zagelbaum, J., Yin, Y., Ma, S., Rothenberg, E., & Fenyö, D. (2017) · Scientific Reports · doi:10.1038/s41598-017-14922-8 · Cited by 33
Kim, D., Curthoys, N. M., Parent, M. T., & Hess, S. T. (2013) · Journal of Optics · doi:10.1088/2040-8978/15/9/094011 · Cited by 31
Grußmayer, K. S., Yserentant, K., & Herten, D. (2018) · Methods and Applications in Fluorescence · doi:10.1088/2050-6120/aaf2eb · Cited by 29
A stochastic view on surface inhomogeneity of nanoparticles
Post, R. A. J., van der Zwaag, D., Bet, G., Wijnands, S. P. W., Albertazzi, L., Meijer, E. W., & van der Hofstad, R. (2019) · Nature Communications · doi:10.1038/s41467-019-09595-y · Cited by 31
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Pore, D., Parameswaran, N., Matsui, K., Stone, M. B., Saotome, I., McClatchey, A. I., Veatch, S. L., & Gupta, N. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301315 · Cited by 32
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Valley, C. C., Lidke, K. A., & Lidke, D. S. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a020735 · Cited by 28
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Giliberti, V., Baldassarre, L., Rosa, A., de Turris, V., Ortolani, M., Calvani, P., & Nucara, A. (2016) · Nanoscale · doi:10.1039/c6nr05783g · Cited by 29
Interactions of amyloid-β peptides on lipid bilayer studied by single molecule imaging and tracking
Chang, C., Edwald, E., Veatch, S. L., Steel, D. G., & Gafni, A. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.03.017 · Cited by 31
Self-citationSynthetic and genetic dimers as quantification ruler for single-molecule counting with PALM
Baldering, T. N., Dietz, M. S., Gatterdam, K., Karathanasis, C., Wieneke, R., Tampé, R., & Heilemann, M. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-10-0661 · Cited by 29
Smith, I. F., Swaminathan, D., Dickinson, G. D., & Parker, I. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.05.051 · Cited by 29
Correction of multiple-blinking artifacts in photoactivated localization microscopy
Jensen, L. G., Hoh, T. Y., Williamson, D. J., Griffié, J., Sage, D., Rubin‐Delanchy, P., & Owen, D. M. (2022) · Nature Methods · doi:10.1038/s41592-022-01463-w · Cited by 29
Far‐Red Organic Fluorophores Contain a Fluorescent Impurity
Stone, M. B., & Veatch, S. L. (2014) · ChemPhysChem · doi:10.1002/cphc.201402002 · Cited by 28
Self-citationTopographic prominence as a method for cluster identification in single‐molecule localisation data
Griffié, J., Boelen, L., Burn, G. L., Cope, A. P., & Owen, D. M. (2015) · Journal of Biophotonics · doi:10.1002/jbio.201400127 · Cited by 28
Does PtdIns(4,5)P 2 concentrate so it can multi-task?
Hammond, G. R. V. (2016) · Biochemical Society Transactions · doi:10.1042/bst20150211 · Cited by 28
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Almarza, G., Sánchez, F., & Barrantes, F. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100346 · Cited by 28
Lin, X., Gupta, D., Vaitsiankova, A., Bhandari, S. K., Leung, K. S. K., Menolfi, D., Lee, B. J., Russell, H. R., Gershik, S., Huang, X., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.09.020 · Cited by 27
Itano, M. S., Graus, M. S., Pehlke, C. A., Wester, M. J., Liu, P., Lidke, K. A., Thompson, N. L., Jacobson, K., & Neumann, A. K. (2014) · Frontiers in Physics · doi:10.3389/fphy.2014.00046 · Cited by 27
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Kelly, C. V., Wakefield, D. L., Holowka, D. A., Craighead, H. G., & Baird, B. A. (2014) · ACS Nano · doi:10.1021/nn502593k · Cited by 27
Self-citationHierarchical nanostructure and synergy of multimolecular signalling complexes
Sherman, E., Barr, V. A., Merrill, R. K., Regan, C. K., Sommers, C. L., & Samelson, L. E. (2016) · Nature Communications · doi:10.1038/ncomms12161 · Cited by 25
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Suzuki, K. G. N., Kasai, R. S., Fujiwara, T. K., & Kusumi, A. (2013) · Methods in cell biology · doi:10.1016/b978-0-12-408143-7.00020-7 · Cited by 25
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DeGroot, A. C. M., Busch, D. J., Hayden, C. C., Mihelic, S. A., Alpar, A. T., Behar, M., & Stachowiak, J. C. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.01.036 · Cited by 27
Manzo, C., van Zanten, T. S., Saha, S., Torreno-Pina, J. A., Mayor, S., & Parajo, M. F. G. (2014) · Scientific Reports · doi:10.1038/srep04354 · Cited by 24
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Peterson, E. M., & Harris, J. M. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04512 · Cited by 24
Chen, J., Blanpied, T. A., & Tang, A. (2019) · Methods · doi:10.1016/j.ymeth.2019.07.016 · Cited by 24
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Kim, S., Phan, S., Tran, H. T., Shaw, T. R., Shahmoradian, S. H., Ellisman, M. H., Veatch, S. L., Barmada, S. J., Pappas, S. S., & Dauer, W. T. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01480-1 · Cited by 23
Self-citationPi, J., Jin, H., Yang, F., Chen, Z. W., & Cai, J. (2014) · Nanoscale · doi:10.1039/c4nr04195j · Cited by 23
Pálinkás, H. L., Békési, A., Róna, G., Pongor, L. S., Papp, G., Tihanyi, G., Holub, E., Póti, Á., Gemma, C., Ali, S., et al. (2020) · eLife · doi:10.7554/elife.60498 · Cited by 21
Valley, C. C., Lewis, A. K., & Sachs, J. N. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.01.016 · Cited by 23
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Notelaers, K., Rocha, S., Paesen, R., Swinnen, N., Vangindertael, J., Meier, J. C., Rigo, J., Ameloot, M. M., & Hofkens, J. (2014) · Histochemistry and Cell Biology · doi:10.1007/s00418-014-1197-y · Cited by 22
Ray, P., Raghunathan, K., Ahsan, A., Allam, U. S., Shukla, S., Basrur, V., Veatch, S. L., Lawrence, T. S., Nyati, M. K., & Ray, D. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013519 · Cited by 21
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Metzbower, S. R., Dharmasri, P. A., Levy, A. D., Anderson, M. C., & Blanpied, T. A. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.1715-23.2024 · Cited by 19
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Mund, M., Kaplan, C., & Ries, J. (2014) · Methods in cell biology · doi:10.1016/b978-0-12-420138-5.00014-8 · Cited by 19
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Yin, Y., & Rothenberg, E. (2016) · Scientific Reports · doi:10.1038/srep30819 · Cited by 19
Crowder and surface effects on self-organization of microtubules
Sahu, S., Herbst, L., Quinn, R., & Ross, J. L. (2021) · Physical review. E · doi:10.1103/physreve.103.062408 · Cited by 19
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Szoboszlay, M., Kirizs, T., & Nusser, Z. (2017) · Scientific Reports · doi:10.1038/s41598-017-15695-w · Cited by 18
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Sudha, D. G., Ochoa, J., & Hirst, L. S. (2021) · Soft Matter · doi:10.1039/d1sm00542a · Cited by 17
Peaucelle, A., Wightman, R., & Haas, K. T. (2020) · iScience · doi:10.1016/j.isci.2020.101862 · Cited by 17
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Flores-Tamez, V. A., Baudel, M. A. S. M., Hong, J., Taylor, J. L., Ren, L., Le, T., Syed, A. U., Moustafa, Y., Singhrao, N., Lemus‐Martinez, W. R., et al. (2024) · Journal of the American Heart Association · doi:10.1161/jaha.124.035375 · Cited by 16
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Sun, S.-Y., Li, X.-W., Cao, R., Zhao, Y., Sheng, N., & Tang, A. (2022) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2022.748184 · Cited by 16
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Edwald, E., Stone, M. B., Gray, E. M., Wu, J., & Veatch, S. L. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.08.023 · Cited by 17
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Uphoff, S. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3631-1_16 · Cited by 16
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Böddeker, T. J., Rusch, A., Leeners, K., Murrell, M. P., & Dufresne, E. R. (2023) · PRX Life · doi:10.1103/prxlife.1.023010 · Cited by 18
Nanodomains in early and later phases of FcɛRI signalling
Holowka, D., & Baird, B. A. (2015) · Essays in Biochemistry · doi:10.1042/bse0570147 · Cited by 15
Self-citationXie, X., Cheng, Y., Wen, M., Calindi, A., Yang, K., Chiu, C.-W., & Chen, T. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b10402 · Cited by 15
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Driouchi, A., Gray‐Owen, S. D., & Yip, C. M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102448 · Cited by 14
Zhou, L., Gao, J., Wang, H., Shi, Y., Xu, H., Yan, Q., Jing, Y., Jiang, J., Cai, M., & Wang, H. (2020) · Nanoscale · doi:10.1039/c9nr10931e · Cited by 14
Willems, J., & MacGillavry, H. D. (2022) · Scientific Reports · doi:10.1038/s41598-022-08746-4 · Cited by 14
Fluorescence localization microscopy
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Metadata
- Authors
- Veatch, S. L., Machta, B. B., Shelby, S. A., Chiang, E. N., Holowka, D. A., & Baird, B. A.
- Affiliations
- Cornell University (US)
- Corresponding author
- Veatch, Sarah L.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-02-27
- Volume
- 7
- Issue
- 2
- Pages
- e31457
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3288038
- OpenAlex
- W2073576660
- Cited by
- 290
- References
- 35
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 12 · 2023: 13 · 2022: 19 · 2021: 22 · 2020: 16 · 2019: 24 · 2018: 24 · 2017: 23 · 2016: 33 · 2015: 21 · 2014: 36 · 2013: 23 · 2012: 7
- FWCI
- 12.73
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- arXiv (Cornell University) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- arXiv (Cornell University)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R00GM087810)
- National Institute of Allergy and Infectious Diseases (R01-AI18306, R01AI018306)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Cell Image Analysis Techniques
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- super-resolution imaging, storms, scanning electron microscopy, FcεRI, IgE receptor, mast cells, membrane protein clustering, protein redistribution, crosslinking
- MeSH terms
- Animals, Cell Line, Cell Membrane, Fluorescent Dyes, Fourier Analysis, Immunoglobulin E, Image Processing, Computer-Assisted, Ligands, Microscopy, Electron, Microscopy, Electron, Scanning, Stochastic Processes, Models, Statistical, Cluster Analysis, Normal Distribution, Poisson Distribution, Receptors, IgE, Rats
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