MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy

Coot : model-building tools for molecular graphics

Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571

RELION: Implementation of a Bayesian approach to cryo-EM structure determination

Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446

The Resolution Revolution

Kühlbrandt, W. (2014) · Science · doi:10.1126/science.1251652 · Cited by 1,325

Structural basis of mRNA decay by the human exosome–ribosome supercomplex

Kögel, A., Keidel, A., Loukeri, M.-J., Kuhn, C. C., Langer, L. M., Schäfer, I. B., & Conti, E. (2024) · Nature · doi:10.1038/s41586-024-08015-6 · Cited by 25

Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3

Cupo, R. R., Rizo, A. N., Braun, G. A., Tse, E., Chuang, E., Gupta, K., Southworth, D. R., & Shorter, J. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111408 · Cited by 25

Structural basis of the mechanism and inhibition of a human ceramide synthase

Pascoa, T. C., Pike, A. C. W., Tautermann, C. S., Chi, G., Traub, M., Quigley, A., Chalk, R., Štefanić, S., Thamm, S., Pautsch, A., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01414-3 · Cited by 25

Structural basis for lysophosphatidylserine recognition by GPR34

Izume, T., Kawahara, R., Uwamizu, A., Chen, L., Yaginuma, S., Omi, J., Kawana, H., Hou, F., Sano, F. K., Tanaka, T., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45046-z · Cited by 24

Atomic structures of a bacteriocin targeting Gram-positive bacteria

Cai, X., He, Y., Yu, I., Imani, A., Scholl, D., Miller, J. F., & Zhou, Z. H. (2024) · Nature Communications · doi:10.1038/s41467-024-51038-w · Cited by 24

Structure and mechanism of the type I-G CRISPR effector

Shangguan, Q., Graham, S., Sundaramoorthy, R., & White, M. F. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac925 · Cited by 24

Tuning insulin receptor signaling using de novo-designed agonists

Wang, X., Cardoso, S., Cai, K., Venkatesh, P., Hung, A., Ng, M., Hall, C., Coventry, B., Lee, D. S., Chowhan, R., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.09.020 · Cited by 24

Condensin II activation by M18BP1

(2025) · doi:10.1016/j.molcel.2025.06.014 · Cited by 24

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

Structural diversity and clustering of bacterial flagellar outer domains

Fields, J. L., Zhang, H., Bellis, N. F., Petersen, H. A., Halder, S. K., Rich-New, S. T., Krupovic, M., Wu, H., & Wang, F. (2024) · Nature Communications · doi:10.1038/s41467-024-53923-w · Cited by 23

A cereblon-based glue degrader of NEK7 regulates NLRP3 inflammasome in a context-dependent manner

Sylvain, A., Stoehr, N., Ma, F., Cernijenko, A., Schröder, M., Khoshouei, M., Vogelsanger, M., Schoenboerner, M., Burke, A., Rao, P., et al. (2025) · Cell Chemical Biology · doi:10.1016/j.chembiol.2025.06.005 · Cited by 23

Structural insights into human TFIIIC promoter recognition

(2023) · doi:10.1126/sciadv.adh2019 · Cited by 23

Rational exploration of fold atlas for human solute carrier proteins

Xie, T., Chi, X., Huang, B., Ye, F., Zhou, Q., & Huang, J. (2022) · Structure · doi:10.1016/j.str.2022.05.015 · Cited by 23

Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate

Rüttermann, M., Koci, M., Lill, P., Geladas, E. D., Kaschani, F., Klink, B. U., Erdmann, R., & Gatsogiannis, C. (2023) · Nature Communications · doi:10.1038/s41467-023-41640-9 · Cited by 23

Protein–protein interactions in the Mla lipid transport system probed by computational structure prediction and deep mutational scanning

MacRae, M. R., Puvanendran, D., Haase, M. A. B., Coudray, N., Kolich, L., Lam, C., Baek, M., Bhabha, G., & Ekiert, D. C. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104744 · Cited by 23

Tetracenomycin X sequesters peptidyl-tRNA during translation of QK motifs

Leroy, E. C., Perry, T. N., Renault, T. T., & Innis, C. A. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01343-0 · Cited by 22

Polymerization of ZBTB transcription factors regulates chromatin occupancy

Park, P. M. C., Park, J., Brown, J., Hunkeler, M., Roy Burman, S. S., Donovan, K. A., Yoon, H., Nowak, R. P., Słabicki, M., Ebert, B. L., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.06.010 · Cited by 22

Structure and flexibility of the yeast NuA4 histone acetyltransferase complex

Zukin, S. A., Marunde, M. R., Popova, I. K., Soczek, K. M., Nogales, E., & Patel, A. B. (2022) · eLife · doi:10.7554/elife.81400 · Cited by 22

Structural basis underlying specific biochemical activities of non-muscle tropomyosin isoforms

Selvaraj, M., Kokate, S. B., Reggiano, G., Kogan, K., Kotila, T., Kremneva, E., DiMaio, F., Lappalainen, P., & Huiskonen, J. T. (2023) · Cell Reports · doi:10.1016/j.celrep.2022.111900 · Cited by 22

Structural basis for activation of Arf1 at the Golgi complex

(2022) · doi:10.1016/j.celrep.2022.111282 · Cited by 22

Cryo-EM structures of human arachidonate 12S-lipoxygenase bound to endogenous and exogenous inhibitors

Mobbs, J. I., Black, K. A., Tran, M., Burger, W. A. C., Venugopal, H., Holman, T. R., Holinstat, M., Thal, D. M., & Glukhova, A. (2023) · Blood · doi:10.1182/blood.2023020441 · Cited by 22

Structural basis for differential inhibition of eukaryotic ribosomes by tigecycline

Li, X., Wang, M., Denk, T., Buschauer, R., Li, Y., Beckmann, R., & Cheng, J. (2024) · Nature Communications · doi:10.1038/s41467-024-49797-7 · Cited by 21

A Peptide Derived from Lens Epithelium–Derived Growth Factor Stimulates HIV-1 DNA Integration and Facilitates Intasome Structural Studies

Li, M., Chen, X., Wang, H., Jurado, K. A., Engelman, A. N., & Craigie, R. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.040 · Cited by 18

A Potent and Protective Human Neutralizing Antibody Against SARS-CoV-2 Variants

Shan, S., Mok, C. K., Zhang, S., Lan, J., Li, J., Yang, Z., Wang, R., Cheng, L., Fang, M., Aw, Z. Q., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.766821 · Cited by 21

Afadin mediates cadherin-catenin complex clustering on F-actin linked to cooperative binding and filament curvature

Gong, R., Reynolds, M. J., Sun, X., & Alushin, G. M. (2025) · Science Advances · doi:10.1126/sciadv.adu0989 · Cited by 21

Discovery of CRISPR-Cas12a clades using a large language model

Feng, Y., Shi, J., Li, Z., Li, Y., Yang, J., Huang, S., Zheng, J., Han, W., Qiao, Y., Zhang, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63160-4 · Cited by 21

The postsynaptic density in excitatory synapses is composed of clustered, heterogeneous nanoblocks

Sun, R., Allen, J. P., Mao, Z., Wilson, L., Haider, M., Alten, B., Zhou, Z., Wang, X., & Zhou, Q. (2025) · Journal of Cell Biology · doi:10.1083/jcb.202406133 · Cited by 20

Structural insights into the mechanism of phosphate recognition and transport by XPR1

Zhang, W., Chen, Y., Guan, Z., Wang, Y., Tang, M., Du, Z., Zhang, J., Cheng, M., Zuo, J., Liu, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-024-55471-9 · Cited by 20

Molecular mechanism of active Cas7-11 in processing CRISPR RNA and interfering target RNA

Goswami, H. N., Rai, J., Das, A., & Li, H. (2022) · eLife · doi:10.7554/elife.81678 · Cited by 20

Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain

Jojoa-Cruz, S., Burendei, B., Lee, W.-H., & Ward, A. B. (2024) · Structure · doi:10.1016/j.str.2023.11.009 · Cited by 20

Structural basis of a two-antibody cocktail exhibiting highly potent and broadly neutralizing activities against SARS-CoV-2 variants including diverse Omicron sublineages

Li, X., Pan, Y., Yin, Q., Wang, Z., Shan, S., Zhang, L., Yu, J., Qu, Y., Sun, L., Gui, F., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00449-4 · Cited by 20

Cryo-EM structures of the Spo11 core complex bound to DNA

Yu, Y., Wang, J., Liu, K., Zheng, Z., Arter, M., Claeys Bouuaert, C., Pu, S., Patel, D. J., & Keeney, S. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01382-8 · Cited by 20

RNA polymerase drives ribonucleotide excision DNA repair in E. coli

Hao, Z., Gowder, M., Proshkin, S., Bharati, B. K., Epshtein, V., Svetlov, V., Shamovsky, I., & Nudler, E. (2023) · Cell · doi:10.1016/j.cell.2023.04.029 · Cited by 19

The small CRL4CSA ubiquitin ligase component DDA1 regulates transcription-coupled repair dynamics

Llerena Schiffmacher, D. A., Lee, S.-H., Kliza, K. W., Theil, A. F., Akita, M., Helfricht, A., Bezstarosti, K., Gonzalo-Hansen, C., van Attikum, H., Verlaan-de Vries, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50584-7 · Cited by 19

Biochemical profiling and structural basis of ADAR1-mediated RNA editing

Deng, X., Sun, L., Zhang, M., Basavaraj, R., Wang, J., Weng, Y.-L., & Gao, Y. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.02.017 · Cited by 19

Molecular basis of TASL recruitment by the peptide/histidine transporter 1, PHT1

Custódio, T. F., Killer, M., Yu, D., Puente, V., Teufel, D. P., Pautsch, A., Schnapp, G., Grundl, M., Kosinski, J., & Löw, C. (2023) · Nature Communications · doi:10.1038/s41467-023-41420-5 · Cited by 19

Structure of the human Bre1 complex bound to the nucleosome

Onishi, S., Uchiyama, K., Sato, K., Okada, C., Kobayashi, S., Hamada, K., Nishizawa, T., Nureki, O., Ogata, K., & Sengoku, T. (2024) · Nature Communications · doi:10.1038/s41467-024-46910-8 · Cited by 19

HIV-1 Integrase Assembles Multiple Species of Stable Synaptic Complex Intasomes That Are Active for Concerted DNA Integration In vitro

Li, M., Yang, R., Chen, X., Wang, H., Ghirlando, R., Dimitriadis, E. K., & Craigie, R. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168557 · Cited by 18

Tubulin acetyltransferases access and modify the microtubule luminal K40 residue through anchors in taxane-binding pockets

Luo, J., Lam, W. H., Yu, D., Chao, V. C., Zopfi, M. N., Khoo, C. J., Zhao, C., Yan, S., Liu, Z., Li, X. D., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01406-3 · Cited by 18

Nucleic acid mediated activation of a short prokaryotic Argonaute immune system

(2024) · doi:10.1038/s41467-024-49271-4 · Cited by 18

Integrative structural analysis of Pseudomonas phage DEV reveals a genome ejection motor

Lokareddy, R. K., Hou, C.-F. D., Forti, F., Iglesias, S. M., Li, F., Pavlenok, M., Horner, D. S., Niederweis, M., Briani, F., & Cingolani, G. (2024) · Nature Communications · doi:10.1038/s41467-024-52752-1 · Cited by 18

Improved mammalian retromer cryo-EM structures reveal a new assembly interface

Kendall, A. K., Chandra, M., Xie, B., Wan, W., & Jackson, L. P. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102523 · Cited by 18

Cryo-EM structures of apo-APC/C and APC/CCDH1:EMI1 complexes provide insights into APC/C regulation

Höfler, A., Yu, J., Yang, J., Zhang, Z., Chang, L., McLaughlin, S. H., Grime, G. W., Garman, E. F., Boland, A., & Barford, D. (2024) · Nature Communications · doi:10.1038/s41467-024-54398-5 · Cited by 18

Structures of the Mycobacterium tuberculosis efflux pump EfpA reveal the mechanisms of transport and inhibition

Wang, S., Wang, K., Song, K., Lai, Z. W., Li, P., Li, D., Sun, Y., Mei, Y., Xu, C., & Liao, M. (2024) · Nature Communications · doi:10.1038/s41467-024-51948-9 · Cited by 18

Mapping the ultrastructural topology of the corynebacterial cell surface

Isbilir, B., Yeates, A., Alva, V., & Bharat, T. A. M. (2025) · PLOS Biology · doi:10.1371/journal.pbio.3003130 · Cited by 18

Local structural flexibility drives oligomorphism in computationally designed protein assemblies

Khmelinskaia, A., Bethel, N. P., Fatehi, F., Mallik, B. B., Antanasijevic, A., Borst, A. J., Lai, S.-H., Chim, H. Y., Wang, J. Y. ‘., Miranda, M. C., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01490-z · Cited by 18

Structural basis for the transport and regulation mechanism of the multidrug resistance-associated protein 2

Koide, E., Pietz, H. L., Beltran, J., & Chen, J. (2025) · Nature Communications · doi:10.1038/s41467-024-55810-w · Cited by 17

Structural basis for the transport and regulation mechanism of the Multidrug resistance-associated protein 2

Koide, E., Pietz, H. L., Beltran, J., & Chen, J. (2024) · doi:10.1101/2024.06.24.600277 · Cited by 17

Hydrolysis-deficient mosaic microtubules as faithful mimics of the GTP cap

Estévez-Gallego, J., Blum, T. B., Ruhnow, F., Gili, M., Speroni, S., García-Castellanos, R., Steinmetz, M. O., & Surrey, T. (2025) · Nature Communications · doi:10.1038/s41467-025-57555-6 · Cited by 17

Shigella effector IpaH1.4 subverts host E3 ligase RNF213 to evade antibacterial immunity

Zhou, X., Zhang, H., Wang, Y., Wang, D., Lin, Z., Zhang, Y., Tang, Y., Liu, J., Yao, Y.-F., Zhang, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58432-y · Cited by 17

Cryo-EM structure of the human cardiac myosin filament

Dutta, D., Nguyen, V., Campbell, K. S., Padrón, R., & Craig, R. (2023) · doi:10.1101/2023.04.11.536274 · Cited by 17

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

KIDINS220 and InsP8 safeguard the stepwise regulation of phosphate exporter XPR1

(2025) · doi:10.1016/j.molcel.2025.08.003 · Cited by 17

Structural basis for autoinhibition by the dephosphorylated regulatory domain of Ycf1

Khandelwal, N. K., & Tomasiak, T. M. (2024) · Nature Communications · doi:10.1038/s41467-024-46722-w · Cited by 17

Molecular basis for shifted receptor recognition by an encephalitic arbovirus

Fan, X., Li, W., Oros, J., Plante, J. A., Mitchell, B. M., Plung, J. S., Basu, H., Nagappan-Chettiar, S., Boeckers, J. M., Tjang, L. V., et al. (2025) · Cell · doi:10.1016/j.cell.2025.03.029 · Cited by 17

Substrate transport and drug interaction of human thiamine transporters SLC19A2/A3

Li, P., Zhu, Z., Wang, Y., Zhang, X., Yang, C., Zhu, Y., Zhou, Z., Chao, Y., Long, Y., Gao, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-55359-8 · Cited by 17

Cryo-EM structure of the Rous sarcoma virus octameric cleaved synaptic complex intasome

Pandey, K. K., Bera, S., Shi, K., Rau, M. J., Oleru, A. V., Fitzpatrick, J. A. J., Engelman, A. N., Aihara, H., & Grandgenett, D. P. (2021) · Communications Biology · doi:10.1038/s42003-021-01855-2 · Cited by 14

Structural basis for negative regulation of the Escherichia coli maltose system

(2023) · doi:10.1038/s41467-023-40447-y · Cited by 16

The structure of the human LACTB filament reveals the mechanisms of assembly and membrane binding

Bennett, J. A., Steward, L. R., Rudolph, J., Voss, A. P., & Aydin, H. (2022) · PLOS Biology · doi:10.1371/journal.pbio.3001899 · Cited by 16

Structures illustrate step-by-step mitochondrial transcription initiation

Goovaerts, Q., Shen, J., De Wijngaert, B., Basu, U., Patel, S. S., & Das, K. (2023) · Nature · doi:10.1038/s41586-023-06643-y · Cited by 16

Structural recognition and stabilization of tyrosine hydroxylase by the J-domain protein DNAJC12

Tai, M. D. S., Ochoa, L., Flydal, M. I., Velasco-Carneros, L., Muntaner, J., Santiago, C., Gamiz-Arco, G., Moro, F., Jung-KC, K., Gil-Cantero, D., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57733-6 · Cited by 16

CryoEM reveals oligomeric isomers of a multienzyme complex and assembly mechanics

Lee, J. K. J., Liu, Y.-T., Hu, J. J., Aphasizheva, I., Aphasizhev, R., & Zhou, Z. H. (2023) · Journal of Structural Biology: X · doi:10.1016/j.yjsbx.2023.100088 · Cited by 16

Coupling enzymatic activity and gating in an ancient TRPM chanzyme and its molecular evolution

Huang, Y., Kumar, S., Lee, J., Lü, W., & Du, J. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01316-4 · Cited by 16

Structural and functional insights of the human peroxisomal ABC transporter ALDP

Jia, Y., Zhang, Y., Wang, W., Lei, J., Ying, Z., & Yang, G. (2022) · eLife · doi:10.7554/elife.75039 · Cited by 15

EGOC inhibits TOROID polymerization by structurally activating TORC1

Prouteau, M., Bourgoint, C., Felix, J., Bonadei, L., Sadian, Y., Gabus, C., Savvides, S. N., Gutsche, I., Desfosses, A., & Loewith, R. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00912-6 · Cited by 15

McrD binds asymmetrically to methyl-coenzyme M reductase improving active-site accessibility during assembly

(2023) · doi:10.1073/pnas.2302815120 · Cited by 15

Structures of 9-1-1 DNA checkpoint clamp loading at gaps from start to finish and ramification on biology

Zheng, F., Georgescu, R. E., Yao, N. Y., O’Donnell, M. E., & Li, H. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112694 · Cited by 15

Spatial constraints drive amylosome-mediated resistant starch degradation by Ruminococcus bromii in the human colon

Wimmer, B. H., Moraïs, S., Amit, I., Tovar-Herrera, O., Tatli, M., Trautwein-Schult, A., Pfister, B., Zalk, R., Tödtli, P., Simoni, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65800-1 · Cited by 15

Cryo-electron tomography of Birbeck granules reveals the molecular mechanism of langerin lattice formation

Oda, T., Yanagisawa, H., Shinmori, H., Ogawa, Y., & Kawamura, T. (2022) · eLife · doi:10.7554/elife.79990 · Cited by 15

Apo and Aβ46-bound γ-secretase structures provide insights into amyloid-β processing by the APH-1B isoform

Odorčić, I., Hamed, M. B., Lismont, S., Chávez-Gutiérrez, L., & Efremov, R. G. (2024) · Nature Communications · doi:10.1038/s41467-024-48776-2 · Cited by 15

Functional redundancy revealed by the deletion of the mimivirus GMC-oxidoreductase genes

Alempic, J.-M., Bisio, H., Villalta, A., Santini, S., Lartigue, A., Schmitt, A., Bugnot, C., Notaro, A., Belmudes, L., Adrait, A., et al. (2024) · microLife · doi:10.1093/femsml/uqae006 · Cited by 15

Structural basis of microtubule-mediated signal transduction

Choi, S. R., Blum, T. B., Giono, M., Roy, B., Vakonakis, I., Schmid, D., Oelgarth, N., Ranganathan, A., Gossert, A. D., Shivashankar, G. V., et al. (2026) · Cell · doi:10.1016/j.cell.2025.11.011 · Cited by 14

The conserved HIV-1 spacer peptide 2 triggers matrix lattice maturation

(2025) · doi:10.1038/s41586-025-08624-9 · Cited by 14

Saccharibacteria deploy two distinct type IV pili, driving episymbiosis, host competition, and twitching motility

Grossman, A. S., Lei, L., Botting, J. M., Liu, J., Nahar, N., Liu, J., McLean, J. S., He, X., & Bor, B. (2025) · The ISME Journal · doi:10.1093/ismejo/wraf119 · Cited by 14

TopBP1 utilises a bipartite GINS binding mode to support genome replication

Day, M., Tetik, B., Parlak, M., Almeida-Hernández, Y., Räschle, M., Kaschani, F., Siegert, H., Marko, A., Sanchez-Garcia, E., Kaiser, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45946-0 · Cited by 14

Integrated cryoEM structure of a spumaretrovirus reveals cross-kingdom evolutionary relationships and the molecular basis for assembly and virus entry

Calcraft, T., Stanke-Scheffler, N., Nans, A., Lindemann, D., Taylor, I. A., & Rosenthal, P. B. (2024) · Cell · doi:10.1016/j.cell.2024.06.017 · Cited by 14

Structure and dynamics of the pyroglutamylated RF-amide peptide QRFP receptor GPR103

Iwama, A., Kise, R., Akasaka, H., Sano, F. K., Oshima, H. S., Inoue, A., Shihoya, W., & Nureki, O. (2024) · Nature Communications · doi:10.1038/s41467-024-49030-5 · Cited by 14

The filamentous ultrastructure of the PopZ condensate is required for its cellular function

Scholl, D., Boyd, T., Latham, A. P., Salazar, A., Khan, A. M. A. M., Boeynaems, S., Holehouse, A. S., Lander, G. C., Sali, A., Park, D., et al. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01742-y · Cited by 14

Structures of aberrant spliceosome intermediates on their way to disassembly

Soni, K., Horvath, A., Dybkov, O., Schwan, M., Trakansuebkul, S., Flemming, D., Wild, K., Urlaub, H., Fischer, T., & Sinning, I. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01480-7 · Cited by 14

The mitochondrial methylation potential gates mitoribosome assembly

Glasgow, R. I. C., Singh, V., Peña-Pérez, L., Wilhalm, A., Moedas, M. F., Moore, D., Rosenberger, F. A., Li, X., Atanassov, I., Saba, M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60977-x · Cited by 14

Structural insights into the orthosteric inhibition of P2X receptors by non-ATP analog antagonists

(2023) · doi:10.7554/elife.92829 · Cited by 14

Molecular mechanisms of SLC30A10-mediated manganese transport

Shen, X., Zhang, J. K., Sun, P., Zhong, H., He, R., Wang, S., Guo, X., & Yang, H. (2025) · Nature Communications · doi:10.1038/s41467-025-63616-7 · Cited by 14

Phosphorylation-mediated conformational change regulates human SLFN11

Kugler, M., Metzner, F. J., Witte, G., Hopfner, K.-P., & Lammens, K. (2024) · Nature Communications · doi:10.1038/s41467-024-54833-7 · Cited by 13

Synergistic activation of the human phosphate exporter XPR1 by KIDINS220 and inositol pyrophosphate

Zuo, P., Wang, W., Dai, Z., Zheng, J., Yu, S., Wang, G., Yin, Y., Liang, L., & Yin, Y. (2025) · Nature Communications · doi:10.1038/s41467-025-58200-y · Cited by 13

Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase

Bulvas, O., Knejzlík, Z., Sýs, J., Filimoněnko, A., Čížková, M., Clarová, K., Rejman, D., Kouba, T., & Pichová, I. (2024) · Nature Communications · doi:10.1038/s41467-024-50933-6 · Cited by 13

Cryo‐EM structure of the octameric pore of Clostridium perfringens β‐toxin

Bruggisser, J., Iacovache, I., Musson, S. C., Degiacomi, M. T., Posthaus, H., & Zuber, B. (2022) · The EMBO Reports · doi:10.15252/embr.202254856 · Cited by 13

The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking

Pellowe, G. A., Voisin, T. B., Karpauskaite, L., Maslen, S. L., Roeselová, A., Skehel, J. M., Roustan, C., George, R., Nans, A., Kjær, S., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01676-5 · Cited by 13

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

Concurrent remodelling of nucleolar 60S subunit precursors by the Rea1 ATPase and Spb4 RNA helicase

Mitterer, V., Thoms, M., Buschauer, R., Berninghausen, O., Hurt, E., & Beckmann, R. (2023) · eLife · doi:10.7554/elife.84877 · Cited by 13

Spatial N-glycan rearrangement on α5β1 integrin nucleates galectin-3 oligomers to determine endocytic fate

Shafaq-Zadah, M., Dransart, E., Hamitouche, I., Wunder, C., Chambon, V., Valades-Cruz, C. A., Leconte, L., Sarangi, N. K., Robinson, J., Bai, S.-K., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64523-7 · Cited by 12

Cryo-EM structure of the human Asc-1 transporter complex

Li, Y., Guo, Y., Bröer, A., Dai, L., Brӧer, S., & Yan, R. (2024) · Nature Communications · doi:10.1038/s41467-024-47468-1 · Cited by 12

High-affinity PQQ import is widespread in Gram-negative bacteria

Munder, F., Voutsinos, M., Hantke, K., Venugopal, H., & Grinter, R. (2025) · Science Advances · doi:10.1126/sciadv.adr2753 · Cited by 12

HIV-1 Intasomes Assembled with Excess Integrase C-Terminal Domain Protein Facilitate Structural Studies by Cryo-EM and Reveal the Role of the Integrase C-Terminal Tail in HIV-1 Integration

Li, M., Li, Z., Chen, X., Cui, Y., Engelman, A. N., & Craigie, R. (2024) · Viruses · doi:10.3390/v16071166 · Cited by 12

Archaeal type six secretion system mediates contact-dependent antagonism

Zachs, T., Malit, J. J. L., Xu, J., Schürch, A., Sivabalasarma, S., Nußbaum, P., Albers, S.-V., & Pilhofer, M. (2024) · Science Advances · doi:10.1126/sciadv.adp7088 · Cited by 12

The DEAD-box ATPase Dbp10/DDX54 initiates peptidyl transferase center formation during 60S ribosome biogenesis

(2024) · doi:10.1038/s41467-024-47616-7 · Cited by 12

rRNA methylation by Spb1 regulates the GTPase activity of Nog2 during 60S ribosomal subunit assembly

Sekulski, K., Cruz, V. E., Weirich, C. S., & Erzberger, J. P. (2023) · Nature Communications · doi:10.1038/s41467-023-36867-5 · Cited by 12

Cas1 mediates the interference stage in a phage-encoded CRISPR–Cas system

Zhang, L., Wang, H., Zeng, J., Cao, X., Gao, Z., Liu, Z., Li, F., Wang, J., Zhang, Y., Yang, M., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01659-5 · Cited by 12

The Structure of the Drp1 Lattice on Membrane

Peng, R., Rochon, K., Hutson, A. N., Stagg, S. M., & Mears, J. A. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169125 · Cited by 12

Structures of Epstein-Barr virus and Kaposi’s sarcoma-associated herpesvirus virions reveal species-specific tegument and envelope features

Zhen, J., Chen, J., Huang, H., Liao, S., Liu, S., Yuan, Y., Sun, R., Longnecker, R., Wu, T.-T., & Zhou, Z. H. (2024) · Journal of Virology · doi:10.1128/jvi.01194-24 · Cited by 12

Structural basis for excitatory neuropeptide signaling

Kalienkova, V., Dandamudi, M., Paulino, C., & Lynagh, T. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01198-y · Cited by 12