The Human Nuclear Pore Complex as Revealed by Cryo-Electron Tomography
Open accessAbstract
Nuclear pore complexes (NPCs) are the sole passage through the nuclear envelope, connecting the cytoplasm to the nucleoplasm. These gigantic molecular machines, over 100 MDa in molecular weight, allow free diffusion of small molecules and ions while mediating selective energy-dependent nucleocytoplasmic transport of large macromolecules. Here, we applied cryo-electron tomography to human fibroblast cells, reconstructing their nuclear envelopes without applying any purification steps. From these reconstructions, we extracted subtomograms containing individual NPCs and utilized in silico subtomogram averaging procedures to determine the structure of the mammalian pore complex at a resolution of ∼6.6 nm. Beyond revealing the canonical features of the human NPC, our analysis identified inner lateral channels and fusing bridge-like structures, suggesting alternative routes of peripheral nuclear passage. Finally, we concluded from our structural analysis that the human NPC is structurally distinct from that of lower eukaryotes in terms of dimension and organization but resembles its amphibian (frog) counterpart.
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AlphaFold and RoseTTAfold have demonstrated unprecedented accuracy in predicting structures of monomeric proteins.
“However, AlphaFold and RoseTTAfold have recently demonstrated unprecedented accuracy in predicting structures of monomeric proteins (27,28,(61)(62)(63)(64)(65)(66) and complexes (35,62,67,68).”
From AI-based structure prediction empowers integrative structural analysis of human nuclear pores (2022) · cites this paper as [28]
Intricate structures such as the NPC can now be modeled thanks to in situ and in cellulo cryo-ET and powerful AI-based prediction.
“Thanks to in situ and in cellulo cryo-ET and powerful AI-based prediction (27,28), intricate structures such as the NPC can be now modeled.”
From AI-based structure prediction empowers integrative structural analysis of human nuclear pores (2022) · cites this paper as [28]
AlphaFold and RoseTTAfold accurately assess their confidence at the level of individual residues and interdomain contacts.
“The programs were also shown to accurately assess their confidence at the level of individual residues and interdomain contacts (27,28,62).”
From AI-based structure prediction empowers integrative structural analysis of human nuclear pores (2022) · cites this paper as [28]
Cites
Radiation damage in the TEM and SEM
Egerton, R. F., Li, P., & Malac, M. (2004) · Micron · doi:10.1016/j.micron.2004.02.003 · Cited by 2,137 · see citing works
Transport Between the Cell Nucleus and the Cytoplasm
Görlich, D., & Kutay, U. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.607 · Cited by 2,025 · see citing works
The Yeast Nuclear Pore Complex
Rout, M. P., Aitchison, J. D., Suprapto, A., Hjertaas, K., Zhao, Y., & Chait, B. T. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.4.635 · Cited by 1,403 · see citing works
The molecular architecture of the nuclear pore complex
Alber, F., Dokudovskaya, S., Veenhoff, L. M., Zhang, W., Kipper, J., Devos, D. P., Suprapto, A., Karni-Schmidt, O., Williams, R., Chait, B. T., et al. (2007) · Nature · doi:10.1038/nature06405 · Cited by 1,059 · see citing works
Proteomic analysis of the mammalian nuclear pore complex
Cronshaw, J. M., Krutchinsky, A. N., Zhang, W., Chait, B. T., & Matunis, M. J. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200206106 · Cited by 968 · see citing works
Functional Organization of the Nuclear Envelope
Gerace, L., & Burke, B. E. (1988) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.04.110188.002003 · Cited by 640 · see citing works
The nuclear pore complex: bridging nuclear transport and gene regulation
Strambio‐De‐Castillia, C., Niepel, M., & Rout, M. P. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2928 · Cited by 595 · see citing works
Functional Organization Of The Nuclear Envelope
Gerace, L. (1988) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.4.1.335 · Cited by 595 · see citing works
Numerically Stable Direct Least Squares Fitting of Ellipses
Halíř, R. (1998) · Cited by 549 · see citing works
The Structure of the Nuclear Pore Complex
Hoelz, A., Debler, E., & Blobel, G. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060109-151030 · Cited by 525 · see citing works
Reichelt, R., Holzenburg, A., Buhle, E. L., Jarník, M., Engel, A. H., & Aebi, U. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.4.883 · Cited by 508 · see citing works
Nuclear Pore Complex Structure and Dynamics Revealed by Cryoelectron Tomography
Beck, M., Förster, F. G., Ecke, M., Plitzko, J. M., Melchior, F., Gerisch, G., Baumeister, W. P., & Medalia, O. (2004) · Science · doi:10.1126/science.1104808 · Cited by 501 · see citing works
Self-citationArchitecture and design of the nuclear pore complex
Hinshaw, J. E., Carragher, B. O., & Milligan, R. A. (1992) · Cell · doi:10.1016/0092-8674(92)90635-p · Cited by 454 · see citing works
TOM software toolbox: acquisition and analysis for electron tomography
Nickell, S., Förster, F. G., Linaroudis, A. A., Net, W. D., Beck, F., Hegerl, R., Baumeister, W. P., & Plitzko, J. M. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2004.10.006 · Cited by 449 · see citing works
The nuclear pore complex: nucleocytoplasmic transport and beyond
Fahrenkrog, B., & Aebi, U. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1230 · Cited by 421 · see citing works
Akey, C. W., & Radermacher, M. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.122.1.1 · Cited by 407 · see citing works
Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
Beck, M., Lučić, V., Förster, F. G., Baumeister, W. P., & Medalia, O. (2007) · Nature · doi:10.1038/nature06170 · Cited by 349 · see citing works
Self-citationYang, Q., Rout, M. P., & Akey, C. W. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80023-4 · Cited by 344 · see citing works
Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography
Förster, F. G., Medalia, O., Zauberman, N., Baumeister, W. P., & Fass, D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409178102 · Cited by 302 · see citing works
Self-citationIsolation of the yeast nuclear pore complex.
Rout, M. P., & Blobel, G. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.123.4.771 · Cited by 285 · see citing works
Loïodice, I., Alves, A., Rabut, G. E. E., van Overbeek, M., Ellenberg, J., Sibarita, J., & Doye, V. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-12-0878 · Cited by 266 · see citing works
Rasala, B. A., Orjalo, A. V., Shen, Z., Briggs, S. P., & Forbes, D. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608484103 · Cited by 250 · see citing works
Stoffler, D., Feja, B., Fahrenkrog, B., Walz, J. C., Typke, D., & Aebi, U. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00266-3 · Cited by 240 · see citing works
Dissecting the molecular architecture of integrin adhesion sites by cryo-electron tomography
Patla, I., Volberg, T., Elad, N., Hirschfeld‐Warneken, V. C., Grashoff, C., Fässler, R., Spatz, J. P., Geiger, B., & Medalia, O. (2010) · Nature Cell Biology · doi:10.1038/ncb2095 · Cited by 227 · see citing works
Self-citationWiney, M., Yarar, D., Giddings, T. H., & Mastronarde, D. N. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.11.2119 · Cited by 227 · see citing works
DeGrasse, J. A., DuBois, K. N., Devos, D. P., Siegel, T. N., Šali, A., Field, M. C., Rout, M. P., & Chait, B. T. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900038-mcp200 · Cited by 226 · see citing works
The Nuclear Pore Complex Has Entered the Atomic Age
Brohawn, S. G., Partridge, J. R., Whittle, J. R. R., & Schwartz, T. (2009) · Structure · doi:10.1016/j.str.2009.07.014 · Cited by 184 · see citing works
Gall, J. G. (1967) · The Journal of Cell Biology · doi:10.1083/jcb.32.2.391 · Cited by 176 · see citing works
3-D Ultrastructure of O. tauri: Electron Cryotomography of an Entire Eukaryotic Cell
Henderson, G. P., Gan, L., & Jensen, G. J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000749 · Cited by 142 · see citing works
Role of the Ndc1 interaction network in yeast nuclear pore complex assembly and maintenance
Onischenko, E. A., Stanton, L. H., Madrid, A. S., Kieselbach, T., & Weis, K. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200810030 · Cited by 142 · see citing works
Architecture of a Coat for the Nuclear Pore Membrane
Hsia, K., Stavropoulos, P., Blobel, G., & Hoelz, A. (2007) · Cell · doi:10.1016/j.cell.2007.11.038 · Cited by 134 · see citing works
Goldberg, M. W., & Allen, T. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0206 · Cited by 127 · see citing works
Владимировна, К. Е., Goldberg, M. W., Allen, T., & Akey, C. W. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.2.223 · Cited by 127 · see citing works
Towards reconciling structure and function in the nuclear pore complex
Lim, R. Y. H., Aebi, U., & Fahrenkrog, B. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-007-0371-x · Cited by 122 · see citing works
Structural plasticity of the nuclear pore complex
Akey, C. W. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(95)80050-6 · Cited by 107 · see citing works
Maeshima, K., Iino, H., Hihara, S., Funakoshi, T., Watanabe, A., Nishimura, M., Nakatomi, R., Yahata, K., Imamoto, F., Hashikawa, T., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1878 · Cited by 105 · see citing works
Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments
Владимировна, К. Е., Allen, T., Rutherford, S. A., Bucci, M., Wente, S. R., & Goldberg, M. W. (2003) · Journal of Structural Biology · doi:10.1016/j.jsb.2003.11.010 · Cited by 99 · see citing works
Structural Analysis of a Metazoan Nuclear Pore Complex Reveals a Fused Concentric Ring Architecture
Frenkiel‐Krispin, D., Maco, B., Aebi, U., & Medalia, O. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.11.010 · Cited by 88 · see citing works
Self-citationKampmann, M., Atkinson, C. E., Mattheyses, A. L., & Simon, S. M. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2056 · Cited by 86 · see citing works
Passive and Facilitated Transport in Nuclear Pore Complexes Is Largely Uncoupled
Naim, B., Brumfeld, V., Kapon, R., Kiss, V., Nevo, R., & Reich, Z. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608329200 · Cited by 84 · see citing works
Molecular architecture of the Nup84–Nup145C–Sec13 edge element in the nuclear pore complex lattice
Brohawn, S. G., & Schwartz, T. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1713 · Cited by 82 · see citing works
Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex
Seo, H., Ma, Y., Debler, E., Wacker, D., Kutik, S., Blobel, G., & Hoelz, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907453106 · Cited by 79 · see citing works
Computer Graphic Display Method for Visualizing Three-Dimensional Biological Structures
Jiménez, J., Santisteban, A., Carazo, J. M., & Carrascosa, J. L. (1986) · Science · doi:10.1126/science.3754654 · Cited by 75 · see citing works
Structural analysis of the nuclear pore complex by integrated approaches
Elad, N., Maimon, T., Frenkiel‐Krispin, D., Lim, R. Y. H., & Medalia, O. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.02.009 · Cited by 73 · see citing works
Self-citationCharacterization of the Nuclear Deformation Caused by Changes in Endothelial Cell Shape
Jean, R. P., Gray, D. S., Spector, A. A., & Chen, C. S. (2004) · Journal of Biomechanical Engineering · doi:10.1115/1.1800559 · Cited by 71 · see citing works
Visualizing cellular processes at the molecular level by cryo-electron tomography
Ben‐Harush, K., Maimon, T., Patla, I., Villa, E., & Medalia, O. (2009) · Journal of Cell Science · doi:10.1242/jcs.060111 · Cited by 64 · see citing works
Self-citationFacilitated transport and diffusion take distinct spatial routes through the nuclear pore complex
Fišerová, J., Richards, S. A., Wente, S. R., & Goldberg, M. W. (2010) · Journal of Cell Science · doi:10.1242/jcs.070730 · Cited by 63 · see citing works
Nuclear pore complexes exceeding eightfold rotational symmetry
Hinshaw, J. E., & Milligan, R. A. (2003) · Journal of Structural Biology · doi:10.1016/s1047-8477(02)00626-3 · Cited by 56 · see citing works
Kramer, A., Ludwig, Y., Shahin, V., & Oberleithner, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703720200 · Cited by 40 · see citing works
Danker, T., Schillers, H., Storck, J., Shahin, V., Krämer, B., Wilhelmi, M., & Oberleithner, H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13530 · Cited by 40 · see citing works
On the Octagonal Structure of the Nuclear Pore Complex: Insights from Coarse-Grained Models
Wolf, C. B., & Mofrad, M. R. K. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.130336 · Cited by 35 · see citing works
Isolation and fractionation of rat liver nuclear envelopes and nuclear pore complexes
Matunis, M. J. (2006) · Methods · doi:10.1016/j.ymeth.2006.06.003 · Cited by 33 · see citing works
Cryoelectron Tomography of Eukaryotic Cells
Mader, A., Elad, N., & Medalia, O. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)83012-5 · Cited by 18 · see citing works
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Concepts of nanoparticle cellular uptake, intracellular trafficking, and kinetics in nanomedicine
Donahue, N. D., Acar, H., & Wilhelm, S. (2019) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2019.04.008 · Cited by 962 · see citing works
The nuclear pore complex: understanding its function through structural insight
Beck, M., & Hurt, E. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.147 · Cited by 680 · see citing works
Visualizing the molecular sociology at the HeLa cell nuclear periphery
Mahamid, J., Pfeffer, S., Schaffer, M., Villa, E., Danev, R., Cuellar, L. K., Förster, F. G., Hyman, A. A., Plitzko, J. M., & Baumeister, W. P. (2016) · Science · doi:10.1126/science.aad8857 · Cited by 561 · see citing works
The Structure of the Nuclear Pore Complex (An Update)
Lin, D. H., & Hoelz, A. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-011901 · Cited by 449 · see citing works
Nuclear Pore Scaffold Structure Analyzed by Super-Resolution Microscopy and Particle Averaging
Szymborska, A., de Marco, A., Daigle, N., Cordes, V. C., Briggs, J. A. G., & Ellenberg, J. (2013) · Science · doi:10.1126/science.1240672 · Cited by 434 · see citing works
Transport Selectivity of Nuclear Pores, Phase Separation, and Membraneless Organelles
Schmidt, H. B., & Görlich, D. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.11.001 · Cited by 413 · see citing works
The Nuclear Pore Complex as a Flexible and Dynamic Gate
Knockenhauer, K. E., & Schwartz, T. (2016) · Cell · doi:10.1016/j.cell.2016.01.034 · Cited by 399 · see citing works
Cryo-electron tomography: The challenge of doing structural biology in situ
Lučić, V., Rigort, A., & Baumeister, W. P. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201304193 · Cited by 387 · see citing works
Single-Molecule Localization Microscopy in Eukaryotes
Sauer, M., & Heilemann, M. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00667 · Cited by 387 · see citing works
Nuclear pore complex composition: a new regulator of tissue-specific and developmental functions
Raı́ces, M., & D’Angelo, M. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3461 · Cited by 373 · see citing works
AI-based structure prediction empowers integrative structural analysis of human nuclear pores
Mosalaganti, S., Obarska-Kosinska, A., Siggel, M., Taniguchi, R., Turoňová, B., Zimmerli, C. E., Buczak, K., Schmidt, F. H., Margiotta, E., Mackmull, M.-T., et al. (2022) · Science · doi:10.1126/science.abm9506 · Cited by 355 · see citing works
Integrated Structural Analysis of the Human Nuclear Pore Complex Scaffold
Bui, K. H., von Appen, A., DiGuilio, A. L., Ori, A., Sparks, L., Mackmull, M., Bock, T., Hagen, W. J. H., Andrés‐Pons, A., Glavy, J. S., et al. (2013) · Cell · doi:10.1016/j.cell.2013.10.055 · Cited by 351 · see citing works
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 · see citing works
Cryo-Electron Tomography: Can it Reveal the Molecular Sociology of Cells in Atomic Detail?
Beck, M., & Baumeister, W. P. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.08.006 · Cited by 313 · see citing works
Ori, A., Banterle, N., Iskar, M., Andrés‐Pons, A., Escher, C., Bui, K. H., Sparks, L., Solis‐Mezarino, V., Rinner, O., Peer Bork, B., et al. (2013) · Molecular Systems Biology · doi:10.1038/msb.2013.4 · Cited by 308 · see citing works
Components and regulation of nuclear transport processes
Cautain, B., Hill, R., de Pedro, N., & Link, W. (2014) · FEBS Journal · doi:10.1111/febs.13163 · Cited by 266 · see citing works
Super-Resolution Microscopy: From Single Molecules to Supramolecular Assemblies
Sydor, A. M., Czymmek, K. J., Puchner, E. M., & Mennella, V. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.004 · Cited by 251 · see citing works
Structural biology in situ—the potential of subtomogram averaging
Briggs, J. A. G. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.02.003 · Cited by 246 · see citing works
The cellular environment shapes the nuclear pore complex architecture
Schuller, A. P., Wojtynek, M., Mankus, D. V., Tatlı, M., Kronenberg‐Tenga, R., Regmi, S. G., Dip, P. V., Lytton‐Jean, A. K. R., Brignole, E. J., Dasso, M., et al. (2021) · Nature · doi:10.1038/s41586-021-03985-3 · Cited by 236 · see citing works
Self-citationDynamic Protein Interaction Networks and New Structural Paradigms in Signaling
Csizmók, V., Follis, A. V., Kriwacki, R. W., & Forman-Kay, J. D. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00548 · Cited by 201 · see citing works
The nuclear pore complex – structure and function at a glance
Kabachinski, G., & Schwartz, T. (2015) · Journal of Cell Science · doi:10.1242/jcs.083246 · Cited by 197 · see citing works
Structure and gating of the nuclear pore complex
Eibauer, M., Pellanda, M., Turgay, Y., Dubrovsky-Gaupp, A., Wild, A., & Medalia, O. (2015) · Nature Communications · doi:10.1038/ncomms8532 · Cited by 185 · see citing works
Self-citationResolution doubling in fluorescence microscopy with confocal spinning-disk image scanning microscopy
Schulz, O., Pieper, C., Clever, M., Pfaff, J., Ruhlandt, A., Kehlenbach, R. H., Wouters, F. S., Großhans, J., Bunt, G., & Enderlein, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315858110 · Cited by 169 · see citing works
Cellular Electron Cryotomography: Toward Structural Biology In Situ
Oikonomou, C. M., & Jensen, G. J. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044741 · Cited by 162 · see citing works
Nuclear pore assembly proceeds by an inside-out extrusion of the nuclear envelope
Otsuka, S., Bui, K. H., Schorb, M., Hossain, M. J., Politi, A. Z., Koch, B., Eltsov, M., Beck, M., & Ellenberg, J. (2016) · eLife · doi:10.7554/elife.19071 · Cited by 156 · see citing works
In situ architecture of the algal nuclear pore complex
Mosalaganti, S., Kosiński, J., Albert, S., Schaffer, M., Strenkert, D., Salomé, P. A., Merchant, S., Plitzko, J. M., Baumeister, W. P., Engel, B. D., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04739-y · Cited by 140 · see citing works
Size-dependent leak of soluble and membrane proteins through the yeast nuclear pore complex
Popken, P., Ghavami, A., Onck, P. R., Poolman, B., & Veenhoff, L. M. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-07-1175 · Cited by 135 · see citing works
Diffusion and retention are major determinants of protein targeting to the inner nuclear membrane
Ungricht, R., Klann, M., Horváth, P., & Kutay, U. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201409127 · Cited by 115 · see citing works
Tailoring cryo-electron microscopy grids by photo-micropatterning for in-cell structural studies
Toro‐Nahuelpan, M., Zagoriy, I., Senger, F., Blanchoin, L., Théry, M., & Mahamid, J. (2019) · Nature Methods · doi:10.1038/s41592-019-0630-5 · Cited by 113 · see citing works
Facilitated aggregation of FG nucleoporins under molecular crowding conditions
Milles, S., Bui, K. H., Koehler, C., Eltsov, M., Beck, M., & Lemke, E. A. (2012) · EMBO Reports · doi:10.1038/embor.2012.204 · Cited by 112 · see citing works
Löschberger, A., Franke, C., Krohne, G., van de Linde, S., & Sauer, M. (2014) · Journal of Cell Science · doi:10.1242/jcs.156620 · Cited by 111 · see citing works
Single particle tomography in EMAN2
Galaz-Montoya, J. G., Flanagan, J., Schmid, M. F., & Ludtke, S. J. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.04.016 · Cited by 110 · see citing works
Destination: inner nuclear membrane
Katta, S. S., Smoyer, C. J., & Jaspersen, S. L. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.10.006 · Cited by 104 · see citing works
Schur, F. K. M. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.03.018 · Cited by 101 · see citing works
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Sivan, G., Martin, S. E., Myers, T. G., Buehler, E. C., Szymczyk, K. H., Ormanoglu, P., & Moss, B. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300708110 · Cited by 96 · see citing works
Nuclear Pore Complexes and Nucleocytoplasmic Transport
Dickmanns, A., Kehlenbach, R. H., & Fahrenkrog, B. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.07.010 · Cited by 90 · see citing works
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Plitzko, J. M., Schuler, B., & Selenko, P. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.06.007 · Cited by 90 · see citing works
Uncovering Nuclear Pore Complexity with Innovation
Adams, R. L., & Wente, S. R. (2013) · Cell · doi:10.1016/j.cell.2013.02.042 · Cited by 89 · see citing works
Structure Determination of the Nuclear Pore Complex with Three-Dimensional Cryo electron Microscopy
von Appen, A., & Beck, M. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.01.004 · Cited by 89 · see citing works
Large cargo transport by nuclear pores: implications for the spatial organization of FG‐nucleoporins
Tu, L., Fu, G., Zilman, A., & Musser, S. M. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.239 · Cited by 84 · see citing works
The LINC and NPC relationship – it's complicated!
Jahed, Z., Soheilypour, M., Peyro, M., & Mofrad, M. R. K. (2016) · Journal of Cell Science · doi:10.1242/jcs.184184 · Cited by 84 · see citing works
Toward the atomic structure of the nuclear pore complex: when top down meets bottom up
Hoelz, A., Glavy, J. S., & Beck, M. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3244 · Cited by 81 · see citing works
Gle1 Functions during mRNA Export in an Oligomeric Complex that Is Altered in Human Disease
Folkmann, A. W., Collier, S. E., Zhan, X., Aditi, A., Ohi, M. D., & Wente, S. R. (2013) · Cell · doi:10.1016/j.cell.2013.09.023 · Cited by 81 · see citing works
Photoactivation of silicon rhodamines via a light-induced protonation
Frei, M. S., Hoess, P., Lampe, M., Nijmeijer, B., Kueblbeck, M., Ellenberg, J., Wadepohl, H., Ries, J., Pitsch, S., Reymond, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12480-3 · Cited by 80 · see citing works
Zhu, Y., Liu, T.-W., Madden, Z., Yuzwa, S. A., Murray, K. D., Cecioni, S., Zachara, N. E., & Vocadlo, D. J. (2015) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjv033 · Cited by 77 · see citing works
Boni, A., Politi, A. Z., Strnad, P., Xiang, W., Hossain, M. J., & Ellenberg, J. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201409133 · Cited by 74 · see citing works
Establishment of NE asymmetry — targeting of membrane proteins to the inner nuclear membrane
Ungricht, R., & Kutay, U. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.04.005 · Cited by 70 · see citing works
Molecular architecture of the luminal ring of the Xenopus laevis nuclear pore complex
Zhang, Y., Li, S., Zeng, C., Huang, G., Zhu, X., Wang, Q., Wang, K., Zhou, Q., Yan, C., Zhang, W., et al. (2020) · Cell Research · doi:10.1038/s41422-020-0320-y · Cited by 64 · see citing works
The Nuclear Pore Complex: Birth, Life, and Death of a Cellular Behemoth
Dultz, E., Wojtynek, M., Medalia, O., & Onischenko, E. A. (2022) · Cells · doi:10.3390/cells11091456 · Cited by 63 · see citing works
Self-citationNucleocytoplasmic Transport: Regulatory Mechanisms and the Implications in Neurodegeneration
Ding, B., & Sepehrimanesh, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084165 · Cited by 62 · see citing works
Gated entry into the ciliary compartment
Takao, D., & Verhey, K. J. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2058-0 · Cited by 60 · see citing works
Phase separation of FG-nucleoporins in nuclear pore complexes
Nag, N., Sasidharan, S., Uversky, V. N., Saudagar, P., & Tripathi, T. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119205 · Cited by 59 · see citing works
Fifty Years of Nuclear Pores and Nucleocytoplasmic Transport Studies
Floch, A. G., Palancade, B., & Doye, V. (2014) · Methods in cell biology · doi:10.1016/b978-0-12-417160-2.00001-1 · Cited by 59 · see citing works
Structure and Function of the Nuclear Pore ComplexPreprint
Petrovic, S., Mobbs, G. W., Bley, C. J., Nie, S., Patke, A., & Hoelz, A. (2022) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041264 · Cited by 58 · see citing works
Cellular structural biology as revealed by cryo-electron tomography
Irobalieva, R. N., Martins, B. S., & Medalia, O. (2016) · Journal of Cell Science · doi:10.1242/jcs.171967 · Cited by 57 · see citing works
Self-citationNuclear Delivery of Nanoparticle-Based Drug Delivery Systems by Nuclear Localization Signals
Nie, Y., Fu, G., & Leng, Y. (2023) · Cells · doi:10.3390/cells12121637 · Cited by 56 · see citing works
Pathogen–host reorganization during C hlamydia invasion revealed by cryo‐electron tomography
Nans, A., Saibil, H. R., & Hayward, R. D. (2014) · Cellular Microbiology · doi:10.1111/cmi.12310 · Cited by 56 · see citing works
The structure of lamin filaments in somatic cells as revealed by cryo-electron tomography
Turgay, Y., & Medalia, O. (2017) · Nucleus · doi:10.1080/19491034.2017.1337622 · Cited by 56 · see citing works
Self-citationMoonlighting nuclear pore proteins: tissue-specific nucleoporin function in health and disease
Jühlen, R., & Fahrenkrog, B. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1748-8 · Cited by 52 · see citing works
Youden, B., Jiang, R., Carrier, A. J., Servos, M. R., & Zhang, X. (2022) · ACS Nano · doi:10.1021/acsnano.2c06337 · Cited by 51 · see citing works
The mechanical stability of proteins regulates their translocation rate into the cell nucleus
Infante, E., Stannard, A., Stephanie Board, Rico-Lastres, P., Rostkova, E. V., Beedle, A. E. M., Lezamiz, A., Wang, Y. J., Breen, S. G., Panagaki, F., et al. (2019) · Nature Physics · doi:10.1038/s41567-019-0551-3 · Cited by 51 · see citing works
Liu, H.-F., Zhou, Y., Huang, Q., Piland, J., Jin, W., Mandel, J., Du, X., Martin, J., & Bartesaghi, A. (2023) · Nature Methods · doi:10.1038/s41592-023-02045-0 · Cited by 49 · see citing works
Advances in tomography: probing the molecular architecture of cells
Fridman, K., Mader, A., Zwerger, M., Elia, N., & Medalia, O. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3453 · Cited by 47 · see citing works
Self-citationDistinct roles of nuclear basket proteins in directing the passage of mRNA through the nuclear pore
Li, Y., Aksenova, V., Tingey, M., Yu, J., Ma, P., Arnaoutov, A., Chen, S., Dasso, M., & Yang, W. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2015621118 · Cited by 47 · see citing works
Alignment algorithms and per-particle CTF correction for single particle cryo-electron tomography
Galaz-Montoya, J. G., Hecksel, C. W., Baldwin, P. R., Wang, E., Weaver, S. C., Schmid, M. F., Ludtke, S. J., & Chiu, W. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.03.018 · Cited by 45 · see citing works
Imaging within single NPCs reveals NXF1’s role in mRNA export on the cytoplasmic side of the pore
Ben-Yishay, R., Mor, A., Shraga, A., Ashkenazy-Titelman, A., Kinor, N., Schwed-Gross, A., Jacob, A., Kozer, N., Kumar, P., Garini, Y., et al. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201901127 · Cited by 45 · see citing works
Madni, A., Rehman, S., Sultan, H., Khan, M. M., Ahmad, F., Raza, M. R., Rai, N., & Parveen, F. (2020) · AAPS PharmSciTech · doi:10.1208/s12249-020-01873-z · Cited by 45 · see citing works
On the nuclear pore complex and its emerging role in cellular mechanotransduction
Matsuda, A., & Mofrad, M. R. K. (2022) · APL Bioengineering · doi:10.1063/5.0080480 · Cited by 44 · see citing works
Eisele, N. B., Labokha, A. A., Frey, S., Görlich, D., & Richter, R. P. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.09.006 · Cited by 44 · see citing works
Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Davies, K. M., Daum, B., Gold, V. A. M., Mühleip, A., Brandt, T., Blum, T. B., Mills, D. J., & Kühlbrandt, W. (2014) · Journal of Visualized Experiments · doi:10.3791/51228 · Cited by 43 · see citing works
Duhéron, V., Nilles, N., Pecenko, S., Martinelli, V., & Fahrenkrog, B. (2017) · Journal of Cell Science · doi:10.1242/jcs.198390 · Cited by 43 · see citing works
Structural Analysis of Supramolecular Assemblies by Cryo-Electron Tomography
Harapin, J., Eibauer, M., & Medalia, O. (2013) · Structure · doi:10.1016/j.str.2013.08.003 · Cited by 42 · see citing works
Self-citationSuper-resolved 3D tracking of cargo transport through nuclear pore complexes
Chowdhury, R., Sau, A., & Musser, S. M. (2022) · Nature Cell Biology · doi:10.1038/s41556-021-00815-6 · Cited by 41 · see citing works
Bilokapić, S., & Schwartz, T. (2013) · Structure · doi:10.1016/j.str.2013.02.006 · Cited by 40 · see citing works
The advent of structural biology in situ by single particle cryo-electron tomography
Galaz-Montoya, J. G., & Ludtke, S. J. (2017) · Biophysics Reports · doi:10.1007/s41048-017-0040-0 · Cited by 40 · see citing works
Duhéron, V., Chatel, G., Sauder, U., Oliveri, V., & Fahrenkrog, B. (2014) · Nucleus · doi:10.4161/19491034.2014.990853 · Cited by 39 · see citing works
The role of nuclear Ca2+ in maintaining neuronal homeostasis and brain health
Mozolewski, P., Jeziorek, M., Schuster, C., Bading, H., Frost, B. E., & Dobrowolski, R. (2021) · Journal of Cell Science · doi:10.1242/jcs.254904 · Cited by 39 · see citing works
Modeling the parameters for plasmodesmal sugar filtering in active symplasmic phloem loaders
Liesche, J., & Schulz, A. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00207 · Cited by 36 · see citing works
Biomechanics of the transport barrier in the nuclear pore complex
Stanley, G. J., Fassati, A., & Hoogenboom, B. W. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.05.007 · Cited by 36 · see citing works
Pfaff, J., Rivera‐Monroy, J. E., Jamieson, C., Rajanala, K., Vilardi, F., Schwappach, B., & Kehlenbach, R. H. (2015) · Journal of Cell Science · doi:10.1242/jcs.179333 · Cited by 35 · see citing works
Mudumbi, K. C., Czapiewski, R., Ruba, A., Junod, S. L., Li, Y., Luo, W., Ngo, C., Ospina, V., Schirmer, E. C., & Yang, W. (2020) · Nature Communications · doi:10.1038/s41467-020-16033-x · Cited by 35 · see citing works
Musser, S. M., & Grünwald, D. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.023 · Cited by 33 · see citing works
The Nuclear Pore Complex Is a Key Target of Viral Proteases to Promote Viral Replication
Jesús‐González, L. A. D., Palacios-Rápalo, S. N., Reyes-Ruíz, J. M., Osuna‐Ramos, J. F., Cordero‐Rivera, C. D., Farfán-Morales, C. N., Gutiérrez‐Escolano, A. L., & del Ángel, R. M. (2021) · Viruses · doi:10.3390/v13040706 · Cited by 33 · see citing works
Quantifying Variability of Manual Annotation in Cryo-Electron Tomograms
Hecksel, C. W., Darrow, M. C., Dai, W., Galaz-Montoya, J. G., Chin, J. A., Mitchell, P., Chen, S., Jakana, J., Schmid, M. F., & Chiu, W. (2016) · Microscopy and Microanalysis · doi:10.1017/s1431927616000799 · Cited by 32 · see citing works
Tai, L., Zhu, Y., Ren, H., Huang, X., Zhang, C., & Sun, F. (2022) · Protein & Cell · doi:10.1007/s13238-021-00895-y · Cited by 32 · see citing works
Conserved Spatial Organization of FG Domains in the Nuclear Pore Complex
Atkinson, C. E., Mattheyses, A. L., Kampmann, M., & Simon, S. M. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.3823 · Cited by 32 · see citing works
Nucleocytoplasmic transport inC9orf72-mediated ALS/FTD
Zhang, K., Grima, J. C., Rothstein, J. D., & Lloyd, T. E. (2016) · Nucleus · doi:10.1080/19491034.2016.1172152 · Cited by 32 · see citing works
Nuclear pore targeting of the yeast Pom33 nucleoporin depends on karyopherin- and lipid-binding
Floch, A. G., Tareste, D. C., Fuchs, P., Chadrin, A., Naciri, I., Léger, T., Schlenstedt, G., Palancade, B., & Doye, V. (2014) · Journal of Cell Science · doi:10.1242/jcs.158915 · Cited by 31 · see citing works
Quantifying Nucleoporin Stoichiometry Inside Single Nuclear Pore Complexes In vivo
Mi, L., Goryaynov, A., Lindquist, A., Rexach, M. F., & Yang, W. (2015) · Scientific Reports · doi:10.1038/srep09372 · Cited by 30 · see citing works
Lau, C. H. Y., Hunter, M. J., Stewart, A. G., Perozo, E., & Vandenberg, J. I. (2018) · The Journal of Physiology · doi:10.1113/jp274888 · Cited by 29 · see citing works
Asakawa, H., Kojidani, T., Yang, H.-J., Ohtsuki, C., Osakada, H., Matsuda, A., Iwamoto, M., Chikashige, Y., Nagao, K., Obuse, C., et al. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008061 · Cited by 28 · see citing works
Liu, H., Schneider, H., Recino, A., Richardson, C. A., Goldberg, M. W., & Rudd, C. E. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.015 · Cited by 28 · see citing works
The Hitchhiker’s Guide to Nucleocytoplasmic Trafficking in Neurodegeneration
Moore, S. R., Rabichow, B. E., & Sattler, R. (2020) · Neurochemical Research · doi:10.1007/s11064-020-02989-1 · Cited by 28 · see citing works
Popken, J., Graf, A., Krebs, S., Blum, H., Schmid, V. J., Strauss, A., Guengoer, T., Zakhartchenko, V., Wolf, E., & Cremer, T. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124619 · Cited by 27 · see citing works
The NAE Pathway: Autobahn to the Nucleus for Cell Surface Receptors
Shah, P., Chaumet, A., Royle, S., & Bard, F. (2019) · Cells · doi:10.3390/cells8080915 · Cited by 26 · see citing works
Rush, C., Jiang, Z., Tingey, M., Feng, F., & Yang, W. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1245939 · Cited by 26 · see citing works
The journey of herpesvirus capsids and genomes to the host cell nucleus
Döhner, K., Cornelius, A., Serrero, M. C., & Sodeik, B. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.08.005 · Cited by 25 · see citing works
Goodwin, E. C., Motamedi, N., Lipovsky, A. I., Fernández‐Busnadiego, R., & DiMaio, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094322 · Cited by 25 · see citing works
Regulation and coordination of nuclear envelope and nuclear pore complex assembly
Clever, M., Mimura, Y., Funakoshi, T., & Imamoto, N. (2013) · Nucleus · doi:10.4161/nucl.23796 · Cited by 25 · see citing works
The Effect of Cell Morphology on the Permeability of the Nuclear Envelope to Diffusive Factors
García‐González, A., Jacchetti, E., Marotta, R., Tunesi, M., Matas, J. F. R., & Raimondi, M. T. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00925 · Cited by 24 · see citing works
- Authors
- Maimon, T., Elad, N., Dahan, I., & Medalia, O.
- Affiliations
- Ben-Gurion University of the Negev (IL)
- Corresponding author
- Medalia, Ohad
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2012-06
- Volume
- 20
- Issue
- 6
- Pages
- 998-1006
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2036469447
- Cited by
- 196
- References
- 53
- Citations by year
- 2026: 10 · 2025: 6 · 2024: 4 · 2023: 7 · 2022: 15 · 2021: 14 · 2020: 12 · 2019: 18 · 2018: 16 · 2017: 14 · 2016: 18 · 2015: 19 · 2014: 20 · 2013: 19 · 2012: 4
- FWCI
- 7.96
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
- Zurich Open Repository and Archive (University of Zurich)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- nuclear pore complex, nuclear envelope, nuclear transport, subtomogram averaging, human fibroblasts
- MeSH terms
- Cell Line, Cell Nucleus, Humans, Models, Molecular, Particle Size, Surface Properties, Cryoelectron Microscopy, Protein Structure, Quaternary, Nuclear Pore, Structural Homology, Protein, Electron Microscope Tomography
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