CTFFIND4: Fast and accurate defocus estimation from electron micrographs

SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies

Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599

Distinct conformational states of SARS-CoV-2 spike protein

Cai, Y., Zhang, J., Xiao, T., Peng, H., Sterling, S. M., Walsh, R. M., Rawson, S., Rits-Volloch, S., & Chen, B. (2020) · Science · doi:10.1126/science.abd4251 · Cited by 1,221

Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies

Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795

Structure-based classification of tauopathies

Shi, Y., Zhang, W., Yang, Y., Murzin, A. G., Falcon, B., Kotecha, A., van Beers, M., Tarutani, A., Kametani, F., Garringer, H. J., et al. (2021) · Nature · doi:10.1038/s41586-021-03911-7 · Cited by 878

Structural mechanism for NEK7-licensed activation of NLRP3 inflammasome

Sharif, H., Wang, L., Wang, W. L., Magupalli, V. G., Andreeva, L., Qiao, Q., Hauenstein, A. V., Wu, Z., Núñez, G., Mao, Y., et al. (2019) · Nature · doi:10.1038/s41586-019-1295-z · Cited by 824

BNT162b vaccines protect rhesus macaques from SARS-CoV-2

Vogel, A. B., Kanevsky, I., Che, Y., Swanson, K. A., Muik, A., Vormehr, M., Kranz, L. M., Walzer, K. C., Hein, S., Güler, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03275-y · Cited by 694

SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects

Wrobel, A. G., Benton, D. J., Xu, P., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0468-7 · Cited by 544

Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40

Yang, H., Jiang, X., Li, B., Yang, H. J., Miller, M., Yang, A., Dhar, A., & Pavletich, N. P. (2017) · Nature · doi:10.1038/nature25023 · Cited by 548

Structure-based membrane dome mechanism for Piezo mechanosensitivity

Guo, Y. R., & MacKinnon, R. (2017) · eLife · doi:10.7554/elife.33660 · Cited by 446

Force-induced conformational changes in PIEZO1

Lin, Y.-C., Guo, Y. R., Miyagi, A., Levring, J., MacKinnon, R., & Scheuring, S. (2019) · Nature · doi:10.1038/s41586-019-1499-2 · Cited by 433

Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase

Verba, K. A., Wang, R. Y.-R., Arakawa, A., Liu, Y., Shirouzu, M., Yokoyama, S., & Agard, D. A. (2016) · Science · doi:10.1126/science.aaf5023 · Cited by 424

Near-atomic model of microtubule-tau interactions

Kellogg, E. H., Hejab, N. M. A., Poepsel, S., Downing, K. H., DiMaio, F., & Nogales, E. (2018) · Science · doi:10.1126/science.aat1780 · Cited by 416

Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms

Billesbølle, C. B., Azumaya, C. M., Kretsch, R. C., Powers, A. S., Gonen, S., Schneider, S., Arvedson, T., Dror, R. O., Cheng, Y., & Manglik, A. (2020) · Nature · doi:10.1038/s41586-020-2668-z · Cited by 344

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

Cryo-EM structures of the TMEM16A calcium-activated chloride channel

Dang, S., Feng, S., Tien, J., Peters, C. J., Bulkley, D., Lolicato, M., Zhao, J., Zuberbühler, K., Ye, W., Qi, L., et al. (2017) · Nature · doi:10.1038/nature25024 · Cited by 333

A thermostable, closed SARS-CoV-2 spike protein trimer

Xiong, X., Qu, K., Ciazynska, K. A., Hosmillo, M., Carter, A. P., Ebrahimi, S., Ke, Z., Scheres, S. H. W., Bergamaschi, L., Grice, G. L., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0478-5 · Cited by 313

Structure deformation and curvature sensing of PIEZO1 in lipid membranes

Yang, X., Lin, C., Chen, X., Li, S., Li, X., & Xiao, B. (2022) · Nature · doi:10.1038/s41586-022-04574-8 · Cited by 305

Structure, lipid scrambling activity and role in autophagosome formation of ATG9A

Maeda, S., Yamamoto, H., Kinch, L. N., Garza, C. M., Takahashi, S., Otomo, C., Grishin, N. V., Forli, S., Mizushima, N., & Otomo, T. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-00520-2 · Cited by 305

Structural Basis for the RNA-Guided Ribonuclease Activity of CRISPR-Cas13d

Zhang, C., Konermann, S., Brideau, N. J., Lotfy, P., Wu, X., Novick, S. J., Strutzenberg, T., Griffin, P. R., Hsu, P. D., & Lyumkis, D. (2018) · Cell · doi:10.1016/j.cell.2018.09.001 · Cited by 276

NLRP3 cages revealed by full-length mouse NLRP3 structure control pathway activation

Andreeva, L., David, L., Rawson, S., Shen, C., Pasricha, T., Pelegrin, P., & Wu, H. (2021) · Cell · doi:10.1016/j.cell.2021.11.011 · Cited by 292

NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly

Baek, K., Krist, D. T., Prabu, J. R., Hill, S., Klügel, M., Neumaier, L.-M., von Gronau, S., Kleiger, G., & Schulman, B. A. (2020) · Nature · doi:10.1038/s41586-020-2000-y · Cited by 270

Hallucinating symmetric protein assemblies

Wicky, B. I. M., Milles, L. F., Courbet, A., Ragotte, R. J., Dauparas, J., Kinfu, E., Tipps, S., Kibler, R. D., Baek, M., DiMaio, F., et al. (2022) · Science · doi:10.1126/science.add1964 · Cited by 240

Small-molecule-induced polymerization triggers degradation of BCL6

Słabicki, M., Yoon, H., Koeppel, J., Nitsch, L., Roy Burman, S. S., Di Genua, C., Donovan, K. A., Sperling, A. S., Hunkeler, M., Tsai, J. M., et al. (2020) · Nature · doi:10.1038/s41586-020-2925-1 · Cited by 270

Structure of the bacterial ribosome at 2 Å resolution

Watson, Z. L., Ward, F. R., Méheust, R., Ad, O., Schepartz, A., Banfield, J. F., & Cate, J. H. (2020) · eLife · doi:10.7554/elife.60482 · Cited by 263

Structural basis for sequestration and autoinhibition of cGAS by chromatin

Michalski, S., de Oliveira Mann, C. C., Stafford, C. A., Witte, G., Bartho, J., Lammens, K., Hornung, V., & Hopfner, K.-P. (2020) · Nature · doi:10.1038/s41586-020-2748-0 · Cited by 256

Structure of a Pancreatic ATP-Sensitive Potassium Channel

Li, N., Wu, J.-X., Ding, D., Cheng, J., Gao, N., & Chen, L. (2017) · Cell · doi:10.1016/j.cell.2016.12.028 · Cited by 252

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

Structural basis of nucleosome-dependent cGAS inhibition

Boyer, J. A., Spangler, C. J., Strauss, J. D., Cesmat, A. P., Liu, P., McGinty, R. K., & Zhang, Q. (2020) · Science · doi:10.1126/science.abd0609 · Cited by 238

Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and substrate-bound states

Manolaridis, I., Jackson, S. M., Taylor, N. M. I., Kowal, J., Stahlberg, H., & Locher, K. P. (2018) · Nature · doi:10.1038/s41586-018-0680-3 · Cited by 228

Structural basis for regulation of human acetyl-CoA carboxylase

Hunkeler, M., Hagmann, A., Stuttfeld, E., Chami, M., Guri, Y., Stahlberg, H., & Maier, T. (2018) · Nature · doi:10.1038/s41586-018-0201-4 · Cited by 229

Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism

Wang, R. Y.-R., Noddings, C. M., Kirschke, E., Myasnikov, A. G., Johnson, J. L., & Agard, D. A. (2022) · Nature · doi:10.1038/s41586-021-04252-1 · Cited by 220

Atomic model for the dimeric F O region of mitochondrial ATP synthase

Guo, H., Bueler, S. A., & Rubinstein, J. L. (2017) · Science · doi:10.1126/science.aao4815 · Cited by 225

Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15

Faust, T. B., Yoon, H., Nowak, R. P., Donovan, K. A., Li, Z., Cai, Q., Eleuteri, N. A., Zhang, T., Gray, N. S., & Fischer, E. S. (2020) · Nature Chemical Biology · doi:10.1038/s41589-019-0378-3 · Cited by 218

De novo protein design enables the precise induction of RSV-neutralizing antibodies

Sesterhenn, F., Yang, C., Bonet, J., Cramer, J. T., Wen, X., Wang, Y., Chiang, C.-I., Abriata, L. A., Kucharska, I., Castoro, G., et al. (2020) · Science · doi:10.1126/science.aay5051 · Cited by 191

Structural and mechanistic insights into fungal β-1,3-glucan synthase FKS1

Hu, X., Yang, P., Chai, C., Liu, J., Sun, H., Wu, Y., Zhang, M., Zhang, M., Liu, X., & Yu, H. (2023) · Nature · doi:10.1038/s41586-023-05856-5 · Cited by 213

Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold

Fontana, P., Dong, Y., Pi, X., Tong, A. B., Hecksel, C. W., Wang, L., Fu, T.-M., Bustamante, C., & Wu, H. (2022) · Science · doi:10.1126/science.abm9326 · Cited by 195

ABCG2 transports anticancer drugs via a closed-to-open switch

Orlando, B. J., & Liao, M. (2020) · Nature Communications · doi:10.1038/s41467-020-16155-2 · Cited by 198

Structural mechanism of a Rag GTPase activation checkpoint by the lysosomal folliculin complex

Lawrence, R. E., Fromm, S. A., Fu, Y., Yokom, A. L., Kim, D. J., Thelen, A. M., Young, L. N., Lim, C.-Y., Samelson, A. J., Hurley, J. H., et al. (2019) · Science · doi:10.1126/science.aax0364 · Cited by 192

Cryo-EM and antisense targeting of the 28-kDa frameshift stimulation element from the SARS-CoV-2 RNA genome

Zhang, K., Zheludev, I. N., Hagey, R. J., Haslecker, R., Hou, Y. J., Kretsch, R., Pintilie, G. D., Rangan, R., Kladwang, W., Li, S., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00653-y · Cited by 189

Cryo-EM structures capture the transport cycle of the P4-ATPase flippase

Hiraizumi, M., Yamashita, K., Nishizawa, T., & Nureki, O. (2019) · Science · doi:10.1126/science.aay3353 · Cited by 185

Structural basis for IL-12 and IL-23 receptor sharing reveals a gateway for shaping actions on T versus NK cells

Glassman, C. R., Mathiharan, Y. K., Jude, K. M., Su, L., Panova, O., Lupardus, P. J., Spangler, J. B., Ely, L. K., Thomas, C., Skiniotis, G., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.018 · Cited by 181

Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils

Röder, C., Kupreichyk, T., Gremer, L., Schäfer, L. U., Pothula, K. R., Ravelli, R. B. G., Willbold, D., Hoyer, W., & Schröder, G. F. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0442-4 · Cited by 180

The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure

Boyer, D. R., Li, B., Sun, C., Fan, W., Zhou, K., Hughes, M. P., Sawaya, M. R., Jiang, L., & Eisenberg, D. S. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917914117 · Cited by 179

Structures of human Patched and its complex with native palmitoylated sonic hedgehog

Qi, X., Schmiege, P., Coutavas, E., Wang, J., & Li, X. (2018) · Nature · doi:10.1038/s41586-018-0308-7 · Cited by 178

Structure of a CLC chloride ion channel by cryo-electron microscopy

Park, E., Campbell, E. B., & MacKinnon, R. (2017) · Nature · doi:10.1038/nature20812 · Cited by 164

Structure of Human ATG9A, the Only Transmembrane Protein of the Core Autophagy Machinery

Guardia, C. M., Tan, X.-F., Lian, T., Rana, M. S., Zhou, W., Christenson, E. T., Lowry, A. J., Faraldo-Gómez, J. D., Bonifacino, J. S., Jiang, J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107837 · Cited by 163

Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism

Noddings, C. M., Wang, R. Y.-R., Johnson, J. L., & Agard, D. A. (2022) · Nature · doi:10.1038/s41586-021-04236-1 · Cited by 164

Structural transitions in influenza haemagglutinin at membrane fusion pH

Benton, D. J., Gamblin, S. J., Rosenthal, P. B., & Skehel, J. J. (2020) · Nature · doi:10.1038/s41586-020-2333-6 · Cited by 161

Selective activation of PFKL suppresses the phagocytic oxidative burst

Amara, N., Cooper, M. P., Voronkova, M. A., Webb, B. A., Lynch, E. M., Kollman, J. M., Ma, T., Yu, K., Lai, Z., Sangaraju, D., et al. (2021) · Cell · doi:10.1016/j.cell.2021.07.004 · Cited by 158

Structural insights into integrin α 5 β 1 opening by fibronectin ligand

Schumacher, S., Dedden, D., Nunez, R. V., Matoba, K., Takagi, J., Biertümpfel, C., & Mizuno, N. (2021) · Science Advances · doi:10.1126/sciadv.abe9716 · Cited by 150

Structural basis for channel conduction in the pump-like channelrhodopsin ChRmine

Kishi, K. E., Kim, Y. S., Fukuda, M., Inoue, M., Kusakizako, T., Wang, P. Y., Ramakrishnan, C., Byrne, E. F. X., Thadhani, E., Paggi, J. M., et al. (2022) · Cell · doi:10.1016/j.cell.2022.01.007 · Cited by 149

Asymmetric Molecular Architecture of the Human γ-Tubulin Ring Complex

Wieczorek, M., Urnavicius, L., Ti, S.-C., Molloy, K. R., Chait, B. T., & Kapoor, T. M. (2020) · Cell · doi:10.1016/j.cell.2019.12.007 · Cited by 136

Cryo-EM structure of the agonist-bound Hsp90-XAP2-AHR cytosolic complex

Gruszczyk, J., Grandvuillemin, L., Lai-Kee-Him, J., Paloni, M., Savva, C. G., Germain, P., Grimaldi, M., Boulahtouf, A., Kwong, H.-S., Bous, J., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34773-w · Cited by 137

Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme

Sui, X., Wang, K., Gluchowski, N. L., Elliott, S. D., Liao, M., Walther, T. C., & Farese, R. V. (2020) · Nature · doi:10.1038/s41586-020-2289-6 · Cited by 120

Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage

(2021) · doi:10.1016/j.molcel.2021.07.031 · Cited by 120

A supramolecular assembly mediates lentiviral DNA integration

Ballandras-Colas, A., Maskell, D. P., Serrao, E., Locke, J., Swuec, P., Jónsson, S. R., Kotecha, A., Cook, N. J., Pye, V. E., Taylor, I. A., et al. (2017) · Science · doi:10.1126/science.aah7002 · Cited by 107

Structure of the CLC-1 chloride channel from Homo sapiens

Park, E., & MacKinnon, R. (2018) · eLife · doi:10.7554/elife.36629 · Cited by 109

Structural transitions in the GTP cap visualized by cryo-electron microscopy of catalytically inactive microtubules

LaFrance, B. J., Roostalu, J., Henkin, G., Greber, B. J., Zhang, R., Normanno, D., McCollum, C. O., Surrey, T., & Nogales, E. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2114994119 · Cited by 100

One-step nanoscale expansion microscopy reveals individual protein shapes

Shaib, A. H., Chouaib, A. A., Chowdhury, R., Altendorf, J., Mihaylov, D., Zhang, C., Krah, D., Imani, V., Spencer, R. K. W., Georgiev, S. V., et al. (2025) · Nature Biotechnology · doi:10.1038/s41587-024-02431-9 · Cited by 104

Membrane-anchored HDCR nanowires drive hydrogen-powered CO2 fixation

Dietrich, H. M., Righetto, R. D., Kumar, A., Wietrzynski, W., Trischler, R., Schuller, S. K., Wagner, J., Schwarz, F. M., Engel, B. D., Müller, V., et al. (2022) · Nature · doi:10.1038/s41586-022-04971-z · Cited by 99

In-cell architecture of the mitochondrial respiratory chain

Waltz, F., Righetto, R. D., Lamm, L., Salinas-Giegé, T., Kelley, R., Zhang, X., Obr, M., Khavnekar, S., Kotecha, A., & Engel, B. D. (2025) · Science · doi:10.1126/science.ads8738 · Cited by 95

Structural conservation of antibiotic interaction with ribosomes

Paternoga, H., Crowe-McAuliffe, C., Bock, L. V., Koller, T. O., Morici, M., Beckert, B., Myasnikov, A. G., Grubmüller, H., Nováček, J., & Wilson, D. N. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01047-y · Cited by 94

Bottom-up de novo design of functional proteins with complex structural features

Yang, C., Sesterhenn, F., Bonet, J., van Aalen, E. A., Scheller, L., Abriata, L. A., Cramer, J. T., Wen, X., Rosset, S., Georgeon, S., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-020-00699-x · Cited by 84

Decreased lipidated ApoE‐receptor interactions confer protection against pathogenicity of ApoE and its lipid cargoes in lysosomes

Guo, J. L., Braun, D., Fitzgerald, G. A., Hsieh, Y.-T., Rougé, L., Litvinchuk, A., Steffek, M., Propson, N. E., Heffner, C. M., Discenza, C., et al. (2025) · Cell · doi:10.1016/j.cell.2024.10.027 · Cited by 91

Donor-strand exchange drives assembly of the TasA scaffold in Bacillus subtilis biofilms

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Abundant Aβ fibrils in ultracentrifugal supernatants of aqueous extracts from Alzheimer’s disease brains

Stern, A. M., Yang, Y., Jin, S., Yamashita, K., Meunier, A. L., Liu, W., Cai, Y., Ericsson, M., Liu, L., Goedert, M., et al. (2023) · Neuron · doi:10.1016/j.neuron.2023.04.007 · Cited by 91

Structural differences between yeast and mammalian microtubules revealed by cryo-EM

Howes, S. C., Geyer, E. A., LaFrance, B., Zhang, R., Kellogg, E. H., Westermann, S., Rice, L. M., & Nogales, E. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201612195 · Cited by 89

Structure of PDE3A-SLFN12 complex reveals requirements for activation of SLFN12 RNase

Garvie, C. W., Wu, X., Papanastasiou, M., Lee, S., Fuller, J., Schnitzler, G. R., Horner, S. W., Baker, A., Zhang, T., Mullahoo, J. P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24495-w · Cited by 85

How Pol α-primase is targeted to replisomes to prime eukaryotic DNA replication

Jones, M. L., Aria, V., Baris, Y., & Yeeles, J. T. P. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.035 · Cited by 86

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

Structural basis for membrane attack complex inhibition by CD59

Couves, E. C., Gardner, S., Voisin, T. B., Bickel, J. K., Stansfeld, P. J., Tate, E. W., & Bubeck, D. (2023) · Nature Communications · doi:10.1038/s41467-023-36441-z · Cited by 85

eIF5B and eIF1A reorient initiator tRNA to allow ribosomal subunit joining

Lapointe, C. P., Grosely, R., Sokabe, M., Alvarado, C., Wang, J., Montabana, E., Villa, N., Shin, B.-S., Dever, T. E., Fraser, C. S., et al. (2022) · Nature · doi:10.1038/s41586-022-04858-z · Cited by 80

Tetracenomycin X inhibits translation by binding within the ribosomal exit tunnel

Osterman, I. A., Wieland, M., Maviza, T. P., Lashkevich, K. A., Lukianov, D. A., Komarova, E. S., Zakalyukina, Y. V., Buschauer, R., Shiriaev, D. I., Leyn, S. A., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0578-x · Cited by 75

Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor

Noddings, C. M., Johnson, J. L., & Agard, D. A. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01128-y · Cited by 75

Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface

Jenni, S., & Harrison, S. C. (2018) · Science · doi:10.1126/science.aar6436 · Cited by 72

Albumin-binding adenoviruses circumvent pre-existing neutralizing antibodies upon systemic delivery

Rojas, L. A., Condezo, G. N., Moreno, R., Fajardo, C. A., Arias-Badia, M., San Martín, C., & Alemany, R. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.07.004 · Cited by 66

Comparative Structural Analysis of 20S Proteasome Ortholog Protein Complexes by Native Mass Spectrometry

Vimer, S., Ben-Nissan, G., Morgenstern, D., Kumar-Deshmukh, F., Polkinghorn, C., Quintyn, R. S., Vasil’ev, Y. V., Beckman, J. S., Elad, N., Wysocki, V. H., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00080 · Cited by 63

Structural basis of microRNA biogenesis by Dicer-1 and its partner protein Loqs-PB

Jouravleva, K., Golovenko, D., Demo, G., Dutcher, R. C., Hall, T. M. T., Zamore, P. D., & Korostelev, A. A. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.09.002 · Cited by 57

Cryo-EM reveals the architecture of placental malaria VAR2CSA and provides molecular insight into chondroitin sulfate binding

Wang, K., Dagil, R., Lavstsen, T., Misra, S. K., Spliid, C. B., Wang, Y., Gustavsson, T., Sandoval, D. R., Vidal-Calvo, E. E., Choudhary, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23254-1 · Cited by 52

Substrate and product complexes reveal mechanisms of Hedgehog acylation by HHAT

Jiang, Y., Benz, T. L., & Long, S. B. (2021) · Science · doi:10.1126/science.abg4998 · Cited by 55

Structure and regulation of the nuclear exosome targeting complex guides RNA substrates to the exosome

Gerlach, P., Garland, W., Lingaraju, M., Salerno-Kochan, A., Bonneau, F., Basquin, J., Jensen, T. H., & Conti, E. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.011 · Cited by 55

The final step of 40S ribosomal subunit maturation is controlled by a dual key lock

Plassart, L., Shayan, R., Montellese, C., Rinaldi, D., Larburu, N., Pichereaux, C., Froment, C., Lebaron, S., O'Donohue, M.-F., Kutay, U., et al. (2021) · eLife · doi:10.7554/elife.61254 · Cited by 55

Structural basis for Parkinson’s disease-linked LRRK2’s binding to microtubules

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Structural basis for regulation of the opposing (p)ppGpp synthetase and hydrolase within the stringent response Orchestrator Rel.

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