ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps

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

PHENIX : a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716

MolProbity : all-atom structure validation for macromolecular crystallography

Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115

Overview of the CCP 4 suite and current developments

Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353

Towards automated crystallographic structure refinement with phenix.refine

Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H., & Adams, P. D. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912001308 · Cited by 5,511

OpenMM 7: Rapid development of high performance algorithms for molecular dynamics

Eastman, P., Swails, J., Chodera, J. D., McGibbon, R. T., Zhao, Y., Beauchamp, K. A., Wang, L.-P., Simmonett, A. C., Harrigan, M. P., Stern, C. D., et al. (2017) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1005659 · Cited by 2,748

Iterative model building, structure refinement and density modification with the PHENIX AutoBuild wizard

Terwilliger, T. C., Grosse-Kunstleve, R. W., Afonine, P. V., Moriarty, N. W., Zwart, P. H., Hung, L.-W., Read, R. J., & Adams, P. D. (2008) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744490705024x · Cited by 1,462

Histone divergence in trypanosomes results in unique alterations to nucleosome structure

Deák, G., Wapenaar, H., Sandoval, G., Chen, R., Taylor, M. R. D., Burdett, H., Watson, J. A., Tuijtel, M. W., Webb, S., & Wilson, M. D. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad577 · Cited by 21

Structural and biophysical analysis of a Haemophilus influenzae tripartite ATP-independent periplasmic (TRAP) transporter

Currie, M. J., Davies, J. S., Scalise, M., Gulati, A., Wright, J. D., Newton-Vesty, M. C., Abeysekera, G. S., Subramanian, R., Wahlgren, W. Y., Friemann, R., et al. (2024) · eLife · doi:10.7554/elife.92307.3 · Cited by 20

Plasticity of the binding pocket in peptide transporters underpins promiscuous substrate recognition

Kotov, V., Killer, M., Jungnickel, K. E. J., Lei, J., Finocchio, G., Steinke, J., Bartels, K., Strauss, J., Dupeux, F., Humm, A.-S., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112831 · 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

Sequence-assignment validation in cryo-EM models with checkMySequence

Chojnowski, G. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798322005009 · Cited by 20

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

Structural basis of Pseudomonas biofilm-forming functional amyloid FapC formation

Hansen, K. H., Golcuk, M., Byeon, C. H., Tunc, A., Plechinger, E. B., Dueholm, M. K. D., Conway, J. F., Andreasen, M., Gur, M., & Akbey, Ü. (2025) · Science Advances · doi:10.1126/sciadv.adx7829 · Cited by 18

Structural basis of V-ATPase V O region assembly by Vma12p, 21p, and 22p

Wang, H., Bueler, S. A., & Rubinstein, J. L. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217181120 · Cited by 18

Dynamic inter-domain transformations mediate the allosteric regulation of human 5, 10-methylenetetrahydrofolate reductase

(2024) · doi:10.1038/s41467-024-47174-y · 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

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

Structure of a heteropolymeric type 4 pilus from a monoderm bacterium

Anger, R., Pieulle, L., Shahin, M., Valette, O., Le Guenno, H., Kosta, A., Pelicic, V., & Fronzes, R. (2023) · Nature Communications · doi:10.1038/s41467-023-42872-5 · Cited by 17

Structure and function of the human mitochondrial MRS2 channel

(2024) · doi:10.1038/s41594-024-01420-5 · 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

Structural basis of 5′ splice site recognition by the minor spliceosome

Zhao, J., Peter, D., Brandina, I., Liu, X., & Galej, W. P. (2025) · Molecular Cell · doi:10.1016/j.molcel.2024.12.017 · 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

Structural basis of TFIIIC-dependent RNA polymerase III transcription initiation

Talyzina, A., Han, Y., Banerjee, C., Fishbain, S., Reyes, A., Vafabakhsh, R., & He, Y. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.015 · Cited by 15

Structural basis of eukaryotic transcription termination by the Rat1 exonuclease complex

Yanagisawa, T., Murayama, Y., Ehara, H., Goto, M., Aoki, M., & Sekine, S.-I. (2024) · Nature Communications · doi:10.1038/s41467-024-52157-0 · Cited by 15

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

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

Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410

(2023) · doi:10.1038/s41467-023-42073-0 · Cited by 14

The structure of a Plasmodium vivax Tryptophan Rich Antigen domain suggests a lipid binding function for a pan-Plasmodium multi-gene family

Kundu, P., Naskar, D., McKie, S. J., Dass, S., Kanjee, U., Introini, V., Ferreira, M. U., Cicuta, P., Duraisingh, M., Deane, J. E., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40885-8 · Cited by 14

Structural mechanisms for VMAT2 inhibition by tetrabenazine

Dalton, M. P., Cheng, M. H., Bahar, I., & Coleman, J. A. (2024) · eLife · doi:10.7554/elife.91973.4 · 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

The GATE glycoprotein complex enhances human cytomegalovirus entry in endothelial cells

Norris, M. J., Henderson, L. A., Siddiquey, M. N. A., Yin, J., Yoo, K., Brunel, S., Mor, M., Saphire, E. O., Benedict, C. A., & Kamil, J. P. (2025) · Nature Microbiology · doi:10.1038/s41564-025-02025-4 · Cited by 14

Vibrio cholerae’s ToxRS bile sensing system

Gubensäk, N., Sagmeister, T., Buhlheller, C., Geronimo, B. D., Wagner, G. E., Petrowitsch, L., Gräwert, M. A., Rotzinger, M., Berger, T. M. I., Schäfer, J., et al. (2023) · eLife · doi:10.7554/elife.88721 · Cited by 14

Structure and activation mechanism of a Lamassu phage and plasmid defense system

Li, Y., Adams, D. W., Liu, H. W., Shaw, S. J., Uchikawa, E., Jaskólska, M., Stutzmann, S., Righi, L., Szczelkun, M. D., Blokesch, M., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01677-4 · 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

Structure of Mycobacterial NDH-2 Bound to a 2-Mercapto-Quinazolinone Inhibitor

Liang, Y., Bueler, S. A., Cook, G. M., & Rubinstein, J. L. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00049 · 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

Capturing ribosomal structures in cellular extracts with cryoPRISM: A purification-free cryoEM approach reveals novel structural states

May, M. B., Lopez-Perez, G. S., & Davis, J. H. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2521210123 · 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

Cryo-EM elucidates the uroplakin complex structure within liquid-crystalline lipids in the porcine urothelial membrane

Yanagisawa, H., Kita, Y., Oda, T., & Kikkawa, M. (2023) · Communications Biology · doi:10.1038/s42003-023-05393-x · Cited by 13

Structural basis of Zika virus NS1 multimerization and human antibody recognition

Chew, B. L. A., Ngoh, A. Q., Phoo, W. W., Weng, M. J. G., Sheng, H. J., Chan, K. W. K., Tan, E. Y. J., Gelbart, T., Xu, C., Tan, G. S., et al. (2024) · npj Viruses · doi:10.1038/s44298-024-00024-6 · 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

High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory

Chavali, S. S., Carman, P. J., Shuman, H., Ostap, E. M., & Sindelar, C. V. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2415457122 · Cited by 12

Mechanism of DNA capture by the MukBEF SMC complex and its inhibition by a viral DNA mimic

Bürmann, F., Clifton, B., Koekemoer, S., Wilkinson, O. J., Kimanius, D., Dillingham, M. S., & Löwe, J. (2025) · Cell · doi:10.1016/j.cell.2025.02.032 · 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

Using deep-learning predictions of inter-residue distances for model validation

Sánchez Rodríguez, F., Chojnowski, G., Keegan, R. M., & Rigden, D. J. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798322010415 · Cited by 11

Mechanistic basis of temperature adaptation in microtubule dynamics across frog species

Troman, L., de Gaulejac, E., Biswas, A., Stiens, J., Kuropka, B., Moores, C. A., & Reber, S. (2025) · Current Biology · doi:10.1016/j.cub.2024.12.022 · Cited by 11

Structure of the Staphylococcus aureus bacteriophage 80α neck shows details of the DNA, tail completion protein, and tape measure protein

Kizziah, J. L., Mukherjee, A., Parker, L. K., & Dokland, T. (2025) · Structure · doi:10.1016/j.str.2025.03.007 · Cited by 11

Building molecular model series from heterogeneous CryoEM structures using Gaussian mixture models and deep neural networks

Chen, M. (2025) · Communications Biology · doi:10.1038/s42003-025-08202-9 · Cited by 11

Molecular basis of SARS-CoV-2 Omicron variant evasion from shared neutralizing antibody response

(2023) · doi:10.1016/j.str.2023.04.010 · Cited by 11

Mouse radial spoke 3 is a metabolic and regulatory hub in cilia

(2025) · doi:10.1038/s41594-025-01594-6 · Cited by 11

The structure of the Orm2-containing serine palmitoyltransferase complex reveals distinct inhibitory potentials of yeast Orm proteins

Körner, C., Schäfer, J.-H., Esch, B. M., Parey, K., Walter, S., Teis, D., Januliene, D., Schmidt, O., Moeller, A., & Fröhlich, F. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114627 · Cited by 10

Distinct pathways for evolution of enhanced receptor binding and cell entry in SARS-like bat coronaviruses

(2024) · doi:10.1371/journal.ppat.1012704 · Cited by 10

Structure of the yeast ceramide synthase

Schäfer, J.-H., Clausmeyer, L., Körner, C., Esch, B. M., Wolf, V. N., Sapia, J., Ahmed, Y., Walter, S., Vanni, S., Januliene, D., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01415-2 · Cited by 10

Structural journey of an insecticidal protein against western corn rootworm

Marini, G., Poland, B., Leininger, C., Lukoyanova, N., Spielbauer, D., Barry, J. K., Altier, D., Lum, A., Scolaro, E., Ortega, C. P., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39891-7 · Cited by 9

Structural analysis of the dynamic ribosome-translocon complex

Lewis, A. J., Zhong, F., Keenan, R. J., & Hegde, R. S. (2024) · eLife · doi:10.7554/elife.95814.3 · Cited by 9

Structure of the F-tractin–F-actin complex

Shatskiy, D., Sivan, A., Wedlich-Söldner, R., & Belyy, A. (2025) · Journal of Cell Biology · doi:10.1083/jcb.202409192 · Cited by 9

SNARE disassembly requires Sec18/NSF side loading

(2025) · doi:10.1038/s41594-025-01590-w · Cited by 9

Molecular mechanism of bacteriophage contraction structure of an S-layer–penetrating bacteriophage

Wilson, J. S., Fortier, L.-C., Fagan, R. P., & Bullough, P. A. (2025) · Life Science Alliance · doi:10.26508/lsa.202403088 · Cited by 9

Structure of yeast RAVE bound to a partial V 1 complex

(2024) · doi:10.1073/pnas.2414511121 · Cited by 9

End-to-end cryo-EM complex structure determination with high accuracy and ultra-fast speed

Wang, J., Tan, C., Gao, Z., Zhang, G., Zhang, Y., & Li, S. Z. (2025) · Nature Machine Intelligence · doi:10.1038/s42256-025-01056-0 · Cited by 8

Molecular mechanism of complement inhibition by the trypanosome receptor ISG65

(2023) · doi:10.7554/elife.88960 · Cited by 8

Cryo-EM reveals the structure and dynamics of a 723-residue malate synthase G

Ho, M.-R., Wu, Y.-M., Lu, Y.-C., Ko, T.-P., & Wu, K.-P. (2023) · Journal of Structural Biology · doi:10.1016/j.jsb.2023.107958 · Cited by 8

CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply

Jeong, T.-K., Frater, R. C. M., Yoon, J., Groth, A., & Song, J.-J. (2025) · Nature Communications · doi:10.1038/s41467-025-56976-7 · Cited by 8

Microtubules in the axon are GDP bound but adopt a stable GTP-like expanded state

Zehr, E. A., Sun, S., Sarbanes, S. L., & Roll-Mecak, A. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01787-7 · Cited by 8

Likelihood-based interactive local docking into cryo-EM maps in ChimeraX

(2024) · doi:10.1107/s2059798324006776 · Cited by 8

The crystal structure of vaccinia virus protein E2 and perspectives on the prediction of novel viral protein folds

(2022) · doi:10.1099/jgv.0.001716 · Cited by 8

Structure of transmembrane AMPA receptor regulatory protein subunit γ2

(2025) · doi:10.1038/s41467-025-56027-1 · Cited by 8

Molecular mechanism of PP2A/B55α phosphatase inhibition by IER5

Cao, R., Jones, D. T. D., Pan, L., Yang, A., Wang, S., Padi, S. K. R., Rawson, S., Aster, J. C., & Blacklow, S. C. (2025) · Cell Chemical Biology · doi:10.1016/j.chembiol.2025.03.004 · Cited by 7

Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains

Hay, I. M., Shamin, M., Caroe, E. R., Mohammed, A. S. A., Svergun, D. I., Jeffries, C. M., Graham, S. C., Sharpe, H. J., & Deane, J. E. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102750 · Cited by 7

Scavenger receptor CD163 multimerises to allow uptake of diverse ligands

Zhou, R. X., & Higgins, M. K. (2025) · Nature Communications · doi:10.1038/s41467-025-62054-9 · Cited by 7

AcrVIB1 inhibits CRISPR-Cas13b immunity by promoting unproductive crRNA binding accessible to RNase attack

(2025) · doi:10.1016/j.molcel.2025.01.020 · Cited by 7

4D structural biology–quantitative dynamics in the eukaryotic RNA exosome complex

Liebau, J., Lazzaretti, D., Fürtges, T., Bichler, A., Pilsl, M., Rudack, T., & Sprangers, R. (2025) · Nature Communications · doi:10.1038/s41467-025-62982-6 · Cited by 7

Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP

Azinas, S., Wallden, K., Katikaridis, P., Jenne, T., Schahl, A., Mogk, A., & Carroni, M. (2025) · Communications Biology · doi:10.1038/s42003-025-08908-w · Cited by 7

Automated simulation-based membrane protein refinement into cryo-EM data

Yvonnesdotter, L., Rovšnik, U., Blau, C., Lycksell, M., Howard, R. J., & Lindahl, E. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.05.033 · Cited by 6

SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features

Gewehr, L., Junglas, B., Jilly, R., Franz, J., Zhu, W. E., Weidner, T., Bonn, M., Sachse, C., & Schneider, D. (2023) · Nature Communications · doi:10.1038/s41467-023-37746-9 · Cited by 6

Structural mechanisms for VMAT2 inhibition by tetrabenazine

Dalton, M. P., Cheng, M. H., Bahar, I., & Coleman, J. A. (2023) · doi:10.1101/2023.09.05.556211 · Cited by 6

Cryo-EM Structure of the relaxosome, a complex essential for bacterial mating and the spread of antibiotic resistance genes

Williams, S. M., Raffl, S., Kienesberger, S., Ilangovan, A., Zechner, E. L., & Waksman, G. (2025) · Nature Communications · doi:10.1038/s41467-025-60116-6 · Cited by 6

Structure of a new capsid form and comparison with A-, B-, and C-capsids clarify herpesvirus assembly

Stevens, A., Kashyap, S., Crofut, E., Alvarez-Cabrera, A. L., Jih, J., Liu, Y.-T., & Zhou, Z. H. (2025) · Journal of Virology · doi:10.1128/jvi.00504-25 · Cited by 5

Comparative characterization of Cas12f orthologs reveals mechanistic features underlying enhanced genome editing efficiency

Guan, K., Ocampo, R. F., Matheus Carnevali, P. B., Castelle, C. J., Gonzalez-Osorio, L., Castanzo, D. T., Thomas, N. C., Brothers, M., Dangerfield, T. L., Hooper, M. M., et al. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01788-6 · Cited by 5

Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery

Drobnič, T., Salzer, R., Nierhaus, T., Jiang, M. K. X., Bellini, D., Steindorf, A., Albers, S.-V., Baum, B., & Löwe, J. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2525941123 · Cited by 5

Molecular mechanism of complement inhibition by the trypanosome receptor ISG65

Cook, A. D., Carrington, M., & Higgins, M. K. (2023) · doi:10.1101/2023.04.27.538609 · Cited by 5

Structural basis of a dual-function type II-B CRISPR–Cas9

Hibshman, G. N., & Taylor, D. W. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf585 · Cited by 4

Molecular exaptation by the integrin αI domain

Hollis, J. A., Chan, M. C., Malik, H. S., & Campbell, M. G. (2025) · Science Advances · doi:10.1126/sciadv.adx9567 · Cited by 4

Structural basis for ACT1 oligomerization induced by IL-17 receptor hetero-tetramer

Zhang, H., Bai, X.-C., & Zhang, X. (2025) · Nature Communications · doi:10.1038/s41467-025-67536-4 · Cited by 4

Structural basis of nearest-neighbor cooperativity in the ring-shaped gene regulatory protein TRAP from protein engineering and cryo-EM

Li, W., Yang, H., Stachowski, K., Norris, A. S., Lichtenthal, K., Kelly, S., Gollnick, P., Wysocki, V. H., & Foster, M. P. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2409030121 · Cited by 4

Structures of Native Doublet Microtubules from Trichomonas vaginalis Reveal Parasite-Specific Proteins

Stevens, A., Kashyap, S., Crofut, E. H., Wang, S. E., Muratore, K. A., Johnson, P. J., & Zhou, Z. H. (2025) · Nature Communications · doi:10.1038/s41467-025-59369-y · Cited by 4

Cortactin stabilizes actin branches by bridging activated Arp2/3 to its nucleated actin filament

(2023) · doi:10.1101/2023.08.16.553490 · Cited by 4

Structure of a type II SMC Wadjet complex from Neobacillus vireti

(2025) · doi:10.1016/j.str.2025.06.004 · Cited by 4

Cryo-EM reveals a phosphorylated R-domain envelops the NBD1 catalytic domain in an ABC transporter

Souza Amado de Carvalho, R., Rasel, M. S. I., Khandelwal, N. K., & Tomasiak, T. M. (2024) · Life Science Alliance · doi:10.26508/lsa.202402779 · Cited by 4

A lipoprotein partner for the Escherichia coli outer membrane protein TolC

Horne, J., Kaplan, E., Jin, B., Abbott, K., Flores, V., Petsolari, E., Gradon, J., Ntsogo, Y., Harris, A., Yu, D., et al. (2026) · eLife · doi:10.7554/elife.110666.3 · Cited by 3

Structural insights into cobalamin loading and reactivation of human methionine synthase

Ferreira, D. S. M., McLennan, K., Diamond, C., Vollmar, M., Kiyani, W., Froese, D. S., Kopec, J., Bailey, H. J., Chalk, R., Baslé, A., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-72899-3 · Cited by 3

Cryo-electron tomography reveals the microtubule-bound form of inactive LRRK2

Chen, S., Basiashvili, T., Hutchings, J., Sanz Murillo, M., Villagran Suarez, A., Xiong, E., Alegrio Louro, J., Leschziner, A. E., & Villa, E. (2025) · eLife · doi:10.7554/elife.100799.3 · Cited by 3

Structural basis for selective inhibition of human GABA transporter GAT3

Mortensen, J. S., Bavo, F., Jensen, M. H., Pedersen, A. P. S., Storm, J. P., Pape, T., Frølund, B., Wellendorph, P., & Shahsavar, A. (2026) · Nature Communications · doi:10.1038/s41467-026-68479-0 · Cited by 3

The bile acid-sensitive ion channel is gated by Ca2+-dependent conformational changes in the transmembrane domain

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Structural insights into Cir-mediated killing by the antimicrobial protein Microcin V

Maurakis, S. A., O’Donnell, A. C., Botos, I., Ghirlando, R., Davies, B. W., & Buchanan, S. K. (2025) · Communications Biology · doi:10.1038/s42003-025-08846-7 · Cited by 3

Cryo-EM structure and B-factor refinement with ensemble representation

(2022) · doi:10.1101/2022.06.08.495259 · Cited by 3

Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape

(2026) · doi:10.1126/science.aea6343 · Cited by 3

Broad substrate scope C-C oxidation in cyclodipeptides catalysed by a flavin-dependent filament

Sutherland, E., Harding, C. J., du Monceau de Bergendal, T., Florence, G. J., Ackermann, K., Bode, B. E., Synowsky, S., Sundaramoorthy, R., & Czekster, C. M. (2025) · Nature Communications · doi:10.1038/s41467-025-56127-y · Cited by 2

X-Ray Structure and enzymatic study of a Bacterial NADPH oxidase highlight the activation mechanism of eukaryotic NOX

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Structure of the human CTF18−RFC clamp loader bound to PCNA

Briola, G. R., Tehseen, M., Al-Amodi, A., Young, G., Danazumi, A. U., Nguyen, P. Q., Savva, C. G., Hedglin, M., Hamdan, S. M., & De Biasio, A. (2026) · eLife · doi:10.7554/elife.103493 · Cited by 2

Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1

Susorov, D., Miścicka, A., Golovenko, D., Loveland, A. B., Zinoviev, A., Pestova, T. V., & Korostelev, A. A. (2025) · Nature Communications · doi:10.1038/s41467-025-66833-2 · Cited by 1

A model for drug transport across two membranes of Gram-negative bacteria by an MFS tripartite assembly

(2026) · doi:10.1038/s41467-026-70500-5 · Cited by 1

Molecular mechanism of complement inhibition by the trypanosome receptor ISG65

Cook, A. D., Carrington, M., & Higgins, M. K. (2024) · eLife · doi:10.7554/elife.88960.3 · Cited by 1

Structural basis for EtfD-mediated coupling of β-oxidation and the respiratory chain in mycobacteria

Courbon, G. M., Makarov, V., Cole, S. T., Schnapinger, D., Ehrt, S., & Rubinstein, J. L. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00726-y · Cited by 1

Cryo-electron tomography reveals the microtubule-bound form of inactive LRRK2

Chen, S., Basiashvili, T., Hutchings, J., Sanz Murillo, M., Villagran Suarez, A., Xiong, E., Alegrio Louro, J., Leschziner, A. E., & Villa, E. (2025) · eLife · doi:10.7554/elife.100799 · Cited by 1

Structure of the human CTF18−RFC clamp loader bound to PCNA

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Structure and catalytic mechanism of methylisocitrate lyase, a potential drug target against Coxiella burnetii

Stuart, W. S., Jenkins, C. H., Ireland, P. M., Isupov, M. N., Norville, I. H., & Harmer, N. J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108517 · Cited by 1