Mechanics and functional consequences of nuclear deformations

Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders

Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174

Nuclear Lamin-A Scales with Tissue Stiffness and Enhances Matrix-Directed Differentiation

Swift, J., Ivanovska, I. L., Buxboim, A., Harada, T., Dingal, P. C. D. P., Pinter, J., Pajerowski, J. D., Spinler, K. R., Shin, J., Tewari, M., et al. (2013) · Science · doi:10.1126/science.1240104 · Cited by 1,998

Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome

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Liquid droplet formation by HP1α suggests a role for phase separation in heterochromatin

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A Mechanical Checkpoint Controls Multicellular Growth through YAP/TAZ Regulation by Actin-Processing Factors

Aragona, M., Panciera, T., Manfrin, A., Giulitti, S., Michielin, F., Elvassore, N., Dupont, S., & Piccolo, S. (2013) · Cell · doi:10.1016/j.cell.2013.07.042 · Cited by 1,651

Chromosomal instability drives metastasis through a cytosolic DNA response

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Force triggers YAP nuclear entry by regulating transport across nuclear pores

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Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy

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Coupling of the nucleus and cytoplasm: Role of the LINC complex

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Physical limits of cell migration: control by ECM space and nuclear deformation and tuning by proteolysis and traction force

Wolf, K., te Lindert, M., Krause, M., Alexander, S., te Riet, J., Willis, A. L., Hoffman, R. M., Figdor, C. G., Weiss, S. J., & Friedl, P. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201210152 · Cited by 1,375

Lamin a truncation in Hutchinson-Gilford progeria

De Sandre-Giovannoli, A., Bernard, R., Cau, P., Navarro, C., Amiel, J., Boccaccio, I., Lyonnet, S., Stewart, C. L., Munnich, A., Le Merrer, M., et al. (2003) · Science · doi:10.1126/science.1084125 · Cited by 1,346

Nuclear envelope rupture and repair during cancer cell migration

Denais, C. M., Gilbert, R. M., Isermann, P., McGregor, A. L., te Lindert, M., Weigelin, B., Davidson, P. M., Friedl, P., Wolf, K., & Lammerding, J. (2016) · Science · doi:10.1126/science.aad7297 · Cited by 1,318

Subdiffraction Multicolor Imaging of the Nuclear Periphery with 3D Structured Illumination Microscopy

Schermelleh, L., Carlton, P. M., Haase, S., Shao, L., Winoto, L., Kner, P., Burke, B. E., Cardoso, M. C., Agard, D. A., Gustafsson, M. G. L., et al. (2008) · Science · doi:10.1126/science.1156947 · Cited by 1,126

Lamin A/C deficiency causes defective nuclear mechanics and mechanotransduction

Lammerding, J., Schulze, P. C., Takahashi, T., Kozlov, S. V., Sullivan, T. L., Kamm, R. D., Stewart, C. L., & Lee, R. T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200419670 · Cited by 1,105

Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson–Gilford progeria syndrome

Goldman, R. D., Shumaker, D. K., Erdos, M. R., Eriksson, M., Goldman, A. E., Gordon, L. B., Gruenbaum, Y., Khuon, S., Mendez, M., Varga, R., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402943101 · Cited by 1,103

Nuclear structure in cancer cells

Zink, D., Fischer, A. H., & Nickerson, J. A. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1430 · Cited by 1,083

Organization of Chromatin by Intrinsic and Regulated Phase Separation

Gibson, B. A., Doolittle, L. K., Schneider, M. W. G., Jensen, L. E., Gamarra, N. I., Henry, L., Gerlich, D. W., Redding, S., & Rosen, M. K. (2019) · Cell · doi:10.1016/j.cell.2019.08.037 · Cited by 1,080

Dilated cardiomyopathy: the complexity of a diverse genetic architecture

Hershberger, R. E., Hedges, D. J., & Morales, A. (2013) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2013.105 · Cited by 1,036

Hippo–YAP/TAZ signalling in organ regeneration and regenerative medicine

Moya, I. M., & Halder, G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0086-y · Cited by 981

Spatiotemporal Control of Intracellular Phase Transitions Using Light-Activated optoDroplets

Shin, Y., Berry, J. M., Pannucci, N. L., Haataja, M., Toettcher, J. E., & Brangwynne, C. P. (2016) · Cell · doi:10.1016/j.cell.2016.11.054 · Cited by 953

ESCRT III repairs nuclear envelope ruptures during cell migration to limit DNA damage and cell death

Raab, M., Gentili, M., Belly, H. D., Thiam, H. R., Vargas, P., Jiménez, A. J., Lautenschläger, F., Voituriez, R., Lennon‐Duménil, A., Manel, N., et al. (2016) · Science · doi:10.1126/science.aad7611 · Cited by 952

Mechanisms of 3D cell migration

Yamada, K. M., & Sixt, M. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0172-9 · Cited by 906

Timing of the brain events underlying access to consciousness during the attentional blink

Sergent, C., Baillet, S., & Dehaene, S. (2005) · Nature Neuroscience · doi:10.1038/nn1549 · Cited by 888

Physical plasticity of the nucleus in stem cell differentiation

Pajerowski, J. D., Dahl, K. N., Zhong, F. L., Sammak, P. J., & Discher, D. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702576104 · Cited by 834

LBR and lamin A/C sequentially tether peripheral heterochromatin and inversely regulate differentiation

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Lamins A and C but Not Lamin B1 Regulate Nuclear Mechanics

Lammerding, J., Fong, L. G., Ji, J. Y., Reue, K., Stewart, C. L., Young, S. G., & Lee, R. T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513511200 · Cited by 721

Liquid Nuclear Condensates Mechanically Sense and Restructure the Genome

Shin, Y., Chang, Y.-C., Lee, D. S. W., Berry, J., Sanders, D. W., Ronceray, P., Wingreen, N. S., Haataja, M., & Brangwynne, C. P. (2018) · Cell · doi:10.1016/j.cell.2018.10.057 · Cited by 676

Heterochromatin-Driven Nuclear Softening Protects the Genome against Mechanical Stress-Induced Damage

Nava, M. M., Miroshnikova, Y. A., Biggs, L. C., Whitefield, D. B., Metge, F., Bouças, J., Vihinen, H., Jokitalo, E., Li, X., ARCOS, J. M. G., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.052 · Cited by 653

Spatial coordination between cell and nuclear shape within micropatterned endothelial cells

Versaevel, M., Grevesse, T., & Gabriele, S. (2012) · Nature Communications · doi:10.1038/ncomms1668 · Cited by 652

Isolated nuclei adapt to force and reveal a mechanotransduction pathway in the nucleus

Guilluy, C., Osborne, L. D., Landeghem, L. V., Sharek, L., Superfine, R., García‐Mata, R., & Burridge, K. (2014) · Nature Cell Biology · doi:10.1038/ncb2927 · Cited by 651

Collagen-based cell migration models in vitro and in vivo

Wolf, K., Alexander, S., Schacht, V., Coussens, L. M., von Andrian, U. H., van Rheenen, J., Deryugina, E., & Friedl, P. (2009) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2009.08.005 · Cited by 637

Transcription upregulation via force-induced direct stretching of chromatin

Tajik, A., Zhang, Y., Wei, F., Sun, J., Jia, Q., Zhou, W., Singh, R., Khanna, N., Belmont, A. S., & Wang, N. (2016) · Nature Materials · doi:10.1038/nmat4729 · Cited by 633

Nuclear lamin stiffness is a barrier to 3D migration, but softness can limit survival

Harada, T., Swift, J., Irianto, J., Shin, J., Spinler, K. R., Athirasala, A., Diegmiller, R., Dingal, P. C. D. P., Ivanovska, I. L., & Discher, D. E. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201308029 · Cited by 611

The nucleus acts as a ruler tailoring cell responses to spatial constraints

Lomakin, A. J., Cattin, C. J., Cuvelier, D., Alraies, Z., Molina, M. S., Nader, G. P. F., Srivastava, N., Sáez, P. J., ARCOS, J. M. G., Zhitnyak, I. Y., et al. (2020) · Science · doi:10.1126/science.aba2894 · Cited by 608

A perinuclear actin cap regulates nuclear shape

Khatau, S. B., Hale, C. M., Stewart-Hutchinson, P. J., Patel, M. S., Stewart, C. L., Searson, P. C., Hodzic, D. M., & Wirtz, D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908686106 · Cited by 607

Emerging views of the nucleus as a cellular mechanosensor

Kirby, T. J., & Lammerding, J. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0038-y · Cited by 594

Viscoelastic Properties of the Cell Nucleus

Guilak, F., Tedrow, J. R., & Burgkart, R. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2360 · Cited by 590

The Interaction between Nesprins and Sun Proteins at the Nuclear Envelope Is Critical for Force Transmission between the Nucleus and Cytoskeleton

Lombardi, M. L., Jaalouk, D. E., Shanahan, C. M., Burke, B. E., Roux, K. J., & Lammerding, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.233700 · Cited by 554

Nuclear Positioning

Gundersen, G. G., & Worman, H. J. (2013) · Cell · doi:10.1016/j.cell.2013.02.031 · Cited by 508

Chromatin and lamin A determine two different mechanical response regimes of the cell nucleus

Stephens, A. D., Banigan, E. J., Adam, S. A., Goldman, R. D., & Marko, J. F. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-09-0653 · Cited by 497

Engineering gene expression and protein synthesis by modulation of nuclear shape

Thomas, C. H., Collier, J. H., Sfeir, C. S., & Healy, K. E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032668799 · Cited by 489

Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin

Wilhelmsen, K., Litjens, S. H. M., Kuikman, I., Tshimbalanga, N., Janssen, H., van den Bout, I., Raymond, K., & Sonnenberg, A. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200506083 · Cited by 483

Mechanical regulation of transcription controls Polycomb-mediated gene silencing during lineage commitment

Le, H. Q., Ghatak, S., Yeung, C. C., Tellkamp, F., Günschmann, C., Dieterich, C., Yeroslaviz, A., Habermann, B. H., Pombo, A., Niessen, C. M., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3387 · Cited by 481

The nucleus measures shape changes for cellular proprioception to control dynamic cell behavior

Venturini, V., Pezzano, F., Català-Castro, F., Häkkinen, H.-M., Jiménez‐Delgado, S., Colomer-Rosell, M., Marro, M., Tolosa-Ramon, Q., Paz-López, S., Valverde, M. A., et al. (2020) · Science · doi:10.1126/science.aba2644 · Cited by 470

Mapping Local and Global Liquid Phase Behavior in Living Cells Using Photo-Oligomerizable Seeds

Bracha, D., Walls, M. T., Wei, M.-T., Zhu, L., Kurian, M., Avalos, J. L., Toettcher, J. E., & Brangwynne, C. P. (2018) · Cell · doi:10.1016/j.cell.2018.10.048 · Cited by 462

Nucleoporins Directly Stimulate Expression of Developmental and Cell-Cycle Genes Inside the Nucleoplasm

Kalverda, B., Pickersgill, H., Shloma, V. V., & Fornerod, M. W. J. (2010) · Cell · doi:10.1016/j.cell.2010.01.011 · Cited by 459

Lamin A/C and emerin regulate MKL1–SRF activity by modulating actin dynamics

Ho, C. Y., Jaalouk, D. E., Vartiainen, M. K., & Lammerding, J. (2013) · Nature · doi:10.1038/nature12105 · Cited by 456

Defects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C–deficient mice

Nikolova-Krstevski, V., Leimena, C., McMahon, A. C., Tan, J. C., Chandar, S., Jogia, D., Kesteven, S. H., Michalicek, J., Otway, R., Verheyen, F., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19448 · Cited by 436

The molecular architecture of lamins in somatic cells

Turgay, Y., Eibauer, M., Goldman, A. E., Shimi, T., Khayat, M., Ben‐Harush, K., Dubrovsky-Gaupp, A., Sapra, K. T., Goldman, R. D., & Medalia, O. (2017) · Nature · doi:10.1038/nature21382 · Cited by 434

LINC Complexes Form by Binding of Three KASH Peptides to Domain Interfaces of Trimeric SUN Proteins

Sosa, B. A., Rothballer, A., Kutay, U., & Schwartz, T. (2012) · Cell · doi:10.1016/j.cell.2012.03.046 · Cited by 426

Lamin B1 duplications cause autosomal dominant leukodystrophy

Padiath, Q. S., Saigoh, K., Schiffmann, R., Asahara, H., Yamada, T., Koeppen, A. H., Hogan, K. J., Ptáček, L. J., & Fu, Y. (2006) · Nature Genetics · doi:10.1038/ng1872 · Cited by 407

Perinuclear Arp2/3-driven actin polymerization enables nuclear deformation to facilitate cell migration through complex environments

Thiam, H. R., Vargas, P., Carpi, N., Crespo, C. L., Raab, M., Terriac, E., King, M. C., Jacobelli, J., Alberts, A. S., Stradal, T. E. B., et al. (2016) · Nature Communications · doi:10.1038/ncomms10997 · Cited by 393

Matrix Elasticity Regulates Lamin-A,C Phosphorylation and Turnover with Feedback to Actomyosin

Buxboim, A., Swift, J., Irianto, J., Spinler, K. R., Dingal, P. C. D. P., Athirasala, A., Kao, Y.-R., Cho, S., Harada, T., Shin, J., et al. (2014) · Current Biology · doi:10.1016/j.cub.2014.07.001 · Cited by 391

Mechanosensing by the nucleus: From pathways to scaling relationships

Cho, S., Irianto, J., & Discher, D. E. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201610042 · Cited by 383

Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells

Lammerding, J., Hsiao, J., Schulze, P. C., Kozlov, S. V., Stewart, C. L., & Lee, R. T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502148 · Cited by 381

Distinct structural and mechanical properties of the nuclear lamina in Hutchinson–Gilford progeria syndrome

Dahl, K. N., Scaffidi, P., Islam, M. F., Yodh, A. G., Wilson, K. L., & Misteli, T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601058103 · Cited by 378

Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization

Roux, K. J., Crisp, M., Liu, Q., Kim, D., Козлов, С. В., Stewart, C. L., & Burke, B. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808602106 · Cited by 376

Nucleokinesis in Neuronal Migration

Tsai, L., & Gleeson, J. G. (2005) · Neuron · doi:10.1016/j.neuron.2005.04.013 · Cited by 374

Defects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C–deficient mice

Nikolova, V., Leimena, C., McMahon, A. C., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200419448 · Cited by 370

Generation of compartmentalized pressure by a nuclear piston governs cell motility in a 3D matrix

Petrie, R. J., Koo, H., & Yamada, K. M. (2014) · Science · doi:10.1126/science.1256965 · Cited by 367

Mechanochemical Feedback Loops in Development and Disease

Hannezo, É., & Heisenberg, C. (2019) · Cell · doi:10.1016/j.cell.2019.05.052 · Cited by 358

Bicaudal D2, Dynein, and Kinesin-1 Associate with Nuclear Pore Complexes and Regulate Centrosome and Nuclear Positioning during Mitotic Entry

Splinter, D., Tanenbaum, M. E., Lindqvist, A., Jaarsma, D., Flotho, A., Yu, K. L., Grigoriev, I., Engelsma, D., Haasdijk, E. D., Keijzer, N., et al. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000350 · Cited by 344

Power-Law Rheology of Isolated Nuclei with Deformation Mapping of Nuclear Substructures

Dahl, K. N., Engler, A. J., Pajerowski, J. D., & Discher, D. E. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.062554 · Cited by 340

The nuclear envelope and the architecture of the nuclear periphery.

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Cytoskeletal to Nuclear Strain Transfer Regulates YAP Signaling in Mesenchymal Stem Cells

Driscoll, T. P., Cosgrove, B. D., Heo, S., Shurden, Z. E., & Mauck, R. L. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.05.010 · Cited by 322

Nuclear Envelope Composition Determines the Ability of Neutrophil-type Cells to Passage through Micron-scale Constrictions

Rowat, A. C., Jaalouk, D. E., Zwerger, M., Ung, W. L., Eydelnant, I. A., Olins, D. E., Olins, A. L., Herrmann, H. O., Weitz, D. A., & Lammerding, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.441535 · Cited by 321

Nuclear Deformability Constitutes a Rate-Limiting Step During Cell Migration in 3-D Environments

Davidson, P. M., Denais, C., Bakshi, M. C., & Lammerding, J. (2014) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-014-0342-y · Cited by 320

Nuclear pores dilate and constrict in cellulo

Zimmerli, C. E., Allegretti, M., Rantos, V., Goetz, S. K., Obarska-Kosińska, A., Zagoriy, I., Halavatyi, A. A., Hummer, G., Mahamid, J., Kosiński, J., et al. (2021) · Science · doi:10.1126/science.abd9776 · Cited by 320

Mechanosensing by the Lamina Protects against Nuclear Rupture, DNA Damage, and Cell-Cycle Arrest

Cho, S., Vashisth, M., Abbas, A. K., Majkut, S., Vogel, K., Xia, Y., Ivanovska, I. L., Irianto, J., Tewari, M., Zhu, K., et al. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.04.020 · Cited by 313

Loss of lamin A function increases chromatin dynamics in the nuclear interior

Bronshtein, I., Kepten, E., Kanter, I., Berezin, S., Lindner, M., Redwood, A. B., Mai, S., Gonzalo, S., Foisner, R., Shav‐Tal, Y., et al. (2015) · Nature Communications · doi:10.1038/ncomms9044 · Cited by 311

Nuclear positioning facilitates amoeboid migration along the path of least resistance

Renkawitz, J., Kopf, A., Stopp, J., de Vries, I., Driscoll, M., Merrin, J., Hauschild, R., Welf, E. S., Danuser, G. M., Fiolka, R. P., et al. (2019) · Nature · doi:10.1038/s41586-019-1087-5 · Cited by 306

Nuclear Lamins: Thin Filaments with Major Functions

de Leeuw, R., Gruenbaum, Y., & Medalia, O. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.08.004 · Cited by 300

Adaptive rheology and ordering of cell cytoskeleton govern matrix rigidity sensing

Gupta, M., Sarangi, B. R., Deschamps, J. R., Nematbakhsh, Y., Callan-Jones, A., Margadant, F., Mège, R., Lim, C. T., Voituriez, R., & Ladoux, B. (2015) · Nature Communications · doi:10.1038/ncomms8525 · Cited by 294

DNA Damage Follows Repair Factor Depletion and Portends Genome Variation in Cancer Cells after Pore Migration

Irianto, J., Xia, Y., Pfeifer, C. R., Athirasala, A., Ji, J., Alvey, C. M., Tewari, M., Bennett, R. R., Harding, S. M., Liu, A. J., et al. (2016) · Current Biology · doi:10.1016/j.cub.2016.11.049 · Cited by 289

Compromised nuclear envelope integrity drives TREX1-dependent DNA damage and tumor cell invasion

Nader, G. P. F., Agüera‐González, S., Routet, F., Gratia, M., Maurin, M., Cancila, V., Cadart, C., Palamidessi, A., Ramos, R. N., Jouve, M. J., et al. (2021) · Cell · doi:10.1016/j.cell.2021.08.035 · Cited by 282

The Cell Nucleus Serves as a Mechanotransducer of Tissue Damage-Induced Inflammation

Enyedi, B., Jelcic, M., & Niethammer, P. (2016) · Cell · doi:10.1016/j.cell.2016.04.016 · Cited by 277

Dynamic Disruptions in Nuclear Envelope Architecture and Integrity Induced by HIV-1 Vpr

de Noronha, C. M. C., Sherman, M. P., Lin, H. W., Cavrois, M., Moir, R. D., Goldman, R. D., & Greene, W. C. (2001) · Science · doi:10.1126/science.1063957 · Cited by 275

Repetitive disruptions of the nuclear envelope invoke temporary loss of cellular compartmentalization in laminopathies

Vos, W. H. D., Houben, F., Kamps, M. A. F., Malhas, A. N., Verheyen, F., Cox, J., Manders, E. M. M., Verstraeten, V. L. R. M., Steensel, M. A. M. V., Marcelis, C., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr344 · Cited by 271

Nuclear envelope rupture is induced by actin-based nucleus confinement

Hatch, E. M., & Hetzer, M. W. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201603053 · Cited by 271

Spatial confinement downsizes the inflammatory response of macrophages

Jain, N., & Vogel, V. (2018) · Nature Materials · doi:10.1038/s41563-018-0190-6 · Cited by 271

Lamina-associated domains: peripheral matters and internal affairs

Briand, N., & Collas, P. (2020) · Genome biology · doi:10.1186/s13059-020-02003-5 · Cited by 269

Mechanics of the Nucleus

Lammerding, J. (2011) · Comprehensive physiology · doi:10.1002/cphy.c100038 · Cited by 267

Transient nuclear envelope rupturing during interphase in human cancer cells

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Mechanical Properties of the Cell Nucleus and the Effect of Emerin Deficiency

Rowat, A. C., Lammerding, J., & Ipsen, J. H. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.086454 · Cited by 257

Actomyosin Is the Main Driver of Interkinetic Nuclear Migration in the Retina

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Nuclear bodies: the emerging biophysics of nucleoplasmic phases

Zhu, L., & Brangwynne, C. P. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.04.003 · Cited by 250

Mutant lamins cause nuclear envelope rupture and DNA damage in skeletal muscle cells

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Structural organization of nuclear lamins A, C, B1, and B2 revealed by superresolution microscopy

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