TOM software toolbox: acquisition and analysis for electron tomography

Disclosure of the mycobacterial outer membrane: Cryo-electron tomography and vitreous sections reveal the lipid bilayer structure

Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J. M., & Engelhardt, H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709530105 · Cited by 596

Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans

Malmström, J., Beck, M., Schmidt, A., Lange, V., Deutsch, E. W., & Aebersold, R. (2009) · Nature · doi:10.1038/nature08184 · Cited by 421

Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution

Schur, F. K. M., Hagen, W. J. H., Rumlová, M., Ruml, T., Müller, B., Kräusslich, H.-G., & Briggs, J. A. G. (2015) · Nature · doi:10.1038/nature13838 · Cited by 296

In-cell architecture of an actively transcribing-translating expressome

O’Reilly, F. J., Xue, L., Graziadei, A., Sinn, L., Lenz, S., Tegunov, D., Blötz, C., Singh, N., Hagen, W. J. H., Cramer, P., et al. (2020) · Science · doi:10.1126/science.abb3758 · Cited by 284

The native 3D organization of bacterial polysomes

Brandt, F., Etchells, S. A., Ortiz, J. O., Elcock, A. H., Hartl, F. U., & Baumeister, W. (2009) · Cell · doi:10.1016/j.cell.2008.11.016 · Cited by 258

Quantitative analysis of the native presynaptic cytomatrix by cryoelectron tomography

Fernández-Busnadiego, R., Zuber, B., Maurer, U. E., Cyrklaff, M., Baumeister, W., & Lučić, V. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200908082 · Cited by 267

Structure of the membrane-assembled retromer coat determined by cryo-electron tomography

Kovtun, O., Leneva, N., Bykov, Y. S., Ariotti, N., Teasdale, R. D., Schaffer, M., Engel, B. D., Owen, D. J., Briggs, J. A. G., & Collins, B. M. (2018) · Nature · doi:10.1038/s41586-018-0526-z · Cited by 247

Three-Dimensional Analysis of Budding Sites and Released Virus Suggests a Revised Model for HIV-1 Morphogenesis

Carlson, L.-A., Briggs, J. A. G., Glass, B., Riches, J. D., Simon, M. N., Johnson, M. C., Müller, B., Grünewald, K., & Kräusslich, H.-G. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.10.013 · Cited by 230

Three-dimensional architecture of murine rod outer segments determined by cryoelectron tomography

Nickell, S., Park, P. S.-H., Baumeister, W., & Palczewski, K. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200612010 · Cited by 209

The Human Nuclear Pore Complex as Revealed by Cryo-Electron Tomography

Maimon, T., Elad, N., Dahan, I., & Medalia, O. (2012) · Structure · doi:10.1016/j.str.2012.03.025 · Cited by 196

Visualizing translation dynamics at atomic detail inside a bacterial cell

Xue, L., Lenz, S., Zimmermann-Kogadeeva, M., Tegunov, D., Cramer, P., Bork, P., Rappsilber, J., & Mahamid, J. (2022) · Nature · doi:10.1038/s41586-022-05255-2 · Cited by 184

In situ architecture of the ER–mitochondria encounter structure

Wozny, M. R., Di Luca, A., Morado, D. R., Picco, A., Khaddaj, R., Campomanes, P., Ivanović, L., Hoffmann, P. C., Miller, E. A., Vanni, S., et al. (2023) · Nature · doi:10.1038/s41586-023-06050-3 · Cited by 134

Cryo Electron Tomography of Native HIV-1 Budding Sites

Carlson, L.-A., de Marco, A., Oberwinkler, H., Habermann, A., Briggs, J. A. G., Kräusslich, H.-G., & Grünewald, K. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001173 · Cited by 133

Determination of protein structure at 8.5 Å resolution using cryo-electron tomography and sub-tomogram averaging

Schur, F. K. M., Hagen, W. J. H., de Marco, A., & Briggs, J. A. G. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.10.015 · Cited by 90

Architecture and mechanism of metazoan retromer:SNX3 tubular coat assembly

Leneva, N., Kovtun, O., Morado, D. R., Briggs, J. A. G., & Owen, D. J. (2021) · Science Advances · doi:10.1126/sciadv.abf8598 · Cited by 90

Vimentin filaments integrate low-complexity domains in a complex helical structure

Eibauer, M., Weber, M. S., Kronenberg-Tenga, R., Beales, C. T., Boujemaa-Paterski, R., Turgay, Y., Sivagurunathan, S., Kraxner, J., Köster, S., Goldman, R. D., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01261-2 · Cited by 87

A cryo-ET survey of microtubules and intracellular compartments in mammalian axons

Foster, H. E., Ventura Santos, C., & Carter, A. P. (2022) · Journal of Cell Biology · doi:10.1083/jcb.202103154 · Cited by 69

Implementation and performance evaluation of reconstruction algorithms on graphics processors

Castaño Díez, D., Mueller, H., & Frangakis, A. S. (2007) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.08.010 · Cited by 68

Molecular-scale visualization of sarcomere contraction within native cardiomyocytes

Burbaum, L., Schneider, J., Scholze, S., Böttcher, R. T., Baumeister, W., Schwille, P., Plitzko, J. M., & Jasnin, M. (2021) · Nature Communications · doi:10.1038/s41467-021-24049-0 · Cited by 67

The Structure of Immature Virus-Like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the p10 Domain in Assembly

Schur, F. K. M., Dick, R. A., Hagen, W. J. H., Vogt, V. M., & Briggs, J. A. G. (2015) · Journal of Virology · doi:10.1128/jvi.01502-15 · Cited by 61

Autophagy preferentially degrades non-fibrillar polyQ aggregates

(2024) · doi:10.1016/j.molcel.2024.04.018 · Cited by 51

Determinants shaping the nanoscale architecture of the mouse rod outer segment

Pöge, M., Mahamid, J., Imanishi, S. S., Plitzko, J. M., Palczewski, K., & Baumeister, W. (2021) · eLife · doi:10.7554/elife.72817 · Cited by 50

An amphipathic helix in Brl1 is required for nuclear pore complex biogenesis in S. cerevisiae

(2022) · doi:10.7554/elife.78385 · Cited by 29

Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer

Obr, M., Ricana, C. L., Nikulin, N., Feathers, J.-P. R., Klanschnig, M., Thader, A., Johnson, M. C., Vogt, V. M., Schur, F. K. M., & Dick, R. A. (2021) · Nature Communications · doi:10.1038/s41467-021-23506-0 · Cited by 23

Structure and organization of full-length epidermal growth factor receptor in extracellular vesicles by cryo-electron tomography

Gonzalez-Magaldi, M., Gullapalli, A., Papoulas, O., Liu, C., Leung, A. Y.-H., Guo, L., Brilot, A. F., Marcotte, E. M., Ke, Z., & Leahy, D. J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2424678122 · Cited by 17

Molecular mechanisms of flotillin complexes in organizing membrane microdomains

Lu, M.-A., Qian, Y., Ma, L., Hong, J., Li, X., Yu, L., Guo, Q., & Gao, N. (2026) · Nature Communications · doi:10.1038/s41467-026-69197-3 · Cited by 13

Anti-Ebola virus mAb 3A6 protects highly viremic animals from fatal outcome via binding GP(1,2) in a position elevated from the virion membrane

Hastie, K. M., Salie, Z. L., Ke, Z., Halfmann, P. J., DeWald, L. E., McArdle, S., Grinyó, A., Davidson, E., Schendel, S. L., Hariharan, C., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56452-2 · Cited by 9

Autophagy preferentially degrades non-fibrillar polyQ aggregates

Zhao, D. Y., Bäuerlein, F. J. B., Saha, I., Hartl, F. U., Baumeister, W., & Wilfling, F. (2023) · doi:10.1101/2023.08.08.552291 · Cited by 3