A New Generation of the IMAGIC Image Processing System

Structures of Cas9 endonucleases reveal RNA-mediated conformational activation

Jinek, M., Jiang, F., Taylor, D. W., Sternberg, S. H., Kaya, E., Ma, E., Anders, C., Hauer, M., Zhou, K., Lin, S., et al. (2014) · Science · doi:10.1126/science.1247997 · Cited by 1,230

High-Resolution Microtubule Structures Reveal the Structural Transitions in αβ-Tubulin upon GTP Hydrolysis

Alushin, G. M., Lander, G. C., Kellogg, E. H., Zhang, R., Baker, D., & Nogales, E. (2014) · Cell · doi:10.1016/j.cell.2014.03.053 · Cited by 696

Complete subunit architecture of the proteasome regulatory particle

Lander, G. C., Estrin, E., Matyskiela, M. E., Bashore, C., Nogales, E., & Martin, A. (2012) · Nature · doi:10.1038/nature10774 · Cited by 608

Structure of the human transferrin receptor-transferrin complex

Cheng, Y., Zak, O., Aisen, P., Harrison, S. C., & Walz, T. (2004) · Cell · doi:10.1016/s0092-8674(04)00130-8 · Cited by 571

Molecular model for a complete clathrin lattice from electron cryomicroscopy

Fotin, A., Cheng, Y., Sliz, P., Grigorieff, N., Harrison, S. C., Kirchhausen, T., & Walz, T. (2004) · Nature · doi:10.1038/nature03079 · Cited by 541

Structural insight into filament formation by mammalian septins

Sirajuddin, M., Farkasovsky, M., Hauer, F., Kühlmann, D., Macara, I. G., Weyand, M., Stark, H., & Wittinghofer, A. (2007) · Nature · doi:10.1038/nature06052 · Cited by 481

Structural insight into autoinhibition and histone H3-induced activation of DNMT3A

Guo, X., Wang, L., Li, J., Ding, Z., Xiao, J., Yin, X., He, S., Shi, P., Dong, L., Li, G., et al. (2015) · Nature · doi:10.1038/nature13899 · Cited by 361

Cryo-electron microscopy--a primer for the non-microscopist

Milne, J. L. S., Borgnia, M. J., Bartesaghi, A., Tran, E. E. H., Earl, L. A., Schauder, D. M., Lengyel, J., Pierson, J., Patwardhan, A., & Subramaniam, S. (2013) · The FEBS Journal · doi:10.1111/febs.12078 · Cited by 277

High thermodynamic stability of parametrically designed helical bundles

Huang, P.-S., Oberdorfer, G., Xu, C., Pei, X. Y., Nannenga, B. L., Rogers, J. M., DiMaio, F., Gonen, T., Luisi, B., & Baker, D. (2014) · Science · doi:10.1126/science.1257481 · Cited by 277

Conformational switching of the 26S proteasome enables substrate degradation

Matyskiela, M. E., Lander, G. C., & Martin, A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2616 · Cited by 251

A conformational change in the adeno-associated virus type 2 capsid leads to the exposure of hidden VP1 N termini

Kronenberg, S., Böttcher, B., von der Lieth, C. W., Bleker, S., & Kleinschmidt, J. A. (2005) · Journal of Virology · doi:10.1128/jvi.79.9.5296-5303.2005 · Cited by 198

Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase

Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10568 · Cited by 190

Structural Evolution of Glycan Recognition by a Family of Potent HIV Antibodies

Garces, F., Sok, D., Kong, L., McBride, R., Kim, H. J., Saye-Francisco, K. F., Julien, J.-P., Hua, Y., Cupo, A., Moore, J. P., et al. (2014) · Cell · doi:10.1016/j.cell.2014.09.009 · Cited by 178

Structure of the CRISPR Interference Complex CSM Reveals Key Similarities with Cascade

Rouillon, C., Zhou, M., Zhang, J., Politis, A., Beilsten-Edmands, V., Cannone, G., Graham, S., Robinson, C. V., Spagnolo, L., & White, M. F. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.020 · Cited by 188

Molecular Structure of Human TFIIH

Schultz, P., Fribourg, S., Poterszman, A., Mallouh, V., Moras, D., & Egly, J. M. (2000) · Cell · doi:10.1016/s0092-8674(00)00082-9 · Cited by 180

Crystal structure of a soluble CD28-Fab complex

Evans, E. J., Esnouf, R. M., Manso-Sancho, R., Gilbert, R. J. C., James, J. R., Yu, C., Fennelly, J. A., Vowles, C., Hanke, T., Walse, B., et al. (2005) · Nature Immunology · doi:10.1038/ni1170 · Cited by 180

The First Account of a Structurally Persistent Micelle

Kellermann, M., Bauer, W., Hirsch, A., Schade, B., Ludwig, K., & Böttcher, C. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200353510 · Cited by 165

Electron cryo‐microscopy and image reconstruction of adeno‐associated virus type 2 empty capsids

Kronenberg, S., Kleinschmidt, J. A., & Böttcher, B. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve234 · Cited by 161

Molecular Basis of the Rapamycin Insensitivity of Target Of Rapamycin Complex 2

Gaubitz, C., Oliveira, T. M., Prouteau, M., Leitner, A., Karuppasamy, M., Konstantinidou, G., Rispal, D., Eltschinger, S., Robinson, G. C., Thore, S., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.04.031 · Cited by 142

Structural basis for retroviral integration into nucleosomes

Maskell, D. P., Renault, L., Serrao, E., Lesbats, P., Matadeen, R., Hare, S., Lindemann, D., Engelman, A. N., Costa, A., & Cherepanov, P. (2015) · Nature · doi:10.1038/nature14495 · Cited by 138

Computational design of trimeric influenza-neutralizing proteins targeting the hemagglutinin receptor binding site

Strauch, E.-M., Bernard, S. M., La, D., Bohn, A. J., Lee, P. S., Anderson, C. E., Nieusma, T., Holstein, C. A., Garcia, N. K., Hooper, K. A., et al. (2017) · Nature Biotechnology · doi:10.1038/nbt.3907 · Cited by 119

Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity

Nicoll, A. J., Panico, S., Freir, D. B., Wright, D., Terry, C., Risse, E., Herron, C. E., O’Malley, T., Wadsworth, J. D. F., Farrow, M. A., et al. (2013) · Nature Communications · doi:10.1038/ncomms3416 · Cited by 119

An Endoplasmic Reticulum (ER) Membrane Complex Composed of SPFH1 and SPFH2 Mediates the ER-associated Degradation of Inositol 1,4,5-Trisphosphate Receptors

Pearce, M. M. P., Wormer, D. B., Wilkens, S., & Wojcikiewicz, R. J. H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809801200 · Cited by 114

Molecular mechanism of activation-triggered subunit exchange in Ca2+/calmodulin-dependent protein kinase II

Bhattacharyya, M., Stratton, M. M., Going, C. C., McSpadden, E. D., Huang, Y., Susa, A. C., Elleman, A., Cao, Y. M., Pappireddi, N., Burkhardt, P., et al. (2016) · eLife · doi:10.7554/elife.13405 · Cited by 112

Intraflagellar transport dynein is autoinhibited by trapping of its mechanical and track-binding elements

Toropova, K., Mladenov, M., & Roberts, A. J. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3391 · Cited by 85

Microtubule architecture in vitro and in cells revealed by cryo-electron tomography

Atherton, J., Stouffer, M., Francis, F., & Moores, C. A. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798318001948 · Cited by 85

Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ

Malet, H., Canellas, F., Sawa, J., Yan, J., Thalassinos, K., Ehrmann, M., Clausen, T., & Saibil, H. R. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2210 · Cited by 61

Origin of the Reflectin Gene and Hierarchical Assembly of Its Protein

Guan, Z., Cai, T., Liu, Z., Dou, Y., Hu, X., Zhang, P., Sun, X., Li, H., Kuang, Y., Zhai, Q., et al. (2017) · Current Biology · doi:10.1016/j.cub.2017.07.061 · Cited by 52

In Vitro Assembly of Virus-Like Particles of a Gammaretrovirus, the Murine Leukemia Virus XMRV

Hadravová, R., de Marco, A., Ulbrich, P., Štokrová, J., Doležal, M., Pichová, I., Ruml, T., Briggs, J. A. G., & Rumlová, M. (2012) · Journal of Virology · doi:10.1128/jvi.05564-11 · Cited by 26

A multiscale approach reveals the molecular architecture of the autoinhibited kinesin KIF5A

Carrington, G., Fatima, U., Caramujo, I., Lewis, T., Casas-Mao, D., & Peckham, M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105713 · Cited by 26

The Listeria monocytogenes persistence factor ClpL is a potent stand-alone disaggregase

Bohl, V., Hollmann, N. M., Melzer, T., Katikaridis, P., Meins, L., Simon, B., Flemming, D., Sinning, I., Hennig, J., & Mogk, A. (2024) · eLife · doi:10.7554/elife.92746 · Cited by 14