UCSF ChimeraX: Structure visualization for researchers, educators, and developers

Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897

UniProt: a worldwide hub of protein knowledge

The UniProt Consortium (2019) · Nucleic Acids Research · doi:10.1093/nar/gky1049 · Cited by 7,698

Announcing the worldwide Protein Data Bank

Berman, H., Henrick, K., & Nakamura, H. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb1203-980 · Cited by 3,093

The chips are down for Moore’s law

Waldrop, M. M. (2016) · Nature · doi:10.1038/530144a · Cited by 2,397

Dense connectomic reconstruction in layer 4 of the somatosensory cortex

Motta, A., Berning, M., Boergens, K. M., Staffler, B., Beining, M., Loomba, S., Hennig, P., Wissler, H., & Helmstaedter, M. (2019) · Science · doi:10.1126/science.aay3134 · Cited by 333

Accurate prediction of protein structures and interactions using a 3-track network

Baek, M., DiMaio, F., Anishchenko, I., Dauparas, J., Ovchinnikov, S., Lee, G. R., Wang, J., Cong, Q., Kinch, L. N., Schaeffer, R. D., et al. (2021) · doi:10.1101/2021.06.14.448402 · Cited by 5,549

SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses

Dejnirattisai, W., Huo, J., Zhou, D., Zahradník, J., Supasa, P., Liu, C., Duyvesteyn, H. M. E., Ginn, H. M., Mentzer, A. J., Tuekprakhon, A., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.046 · Cited by 930

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

Circulating SARS-CoV-2 spike N439K variants maintain fitness while evading antibody-mediated immunity

Thomson, E. C., Rosen, L. E., Shepherd, J. G., Spreafico, R., da Silva Filipe, A., Wojcechowskyj, J. A., Davis, C., Piccoli, L., Pascall, D. J., Dillen, J., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.037 · Cited by 606

Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite

Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.005 · Cited by 519

Mechanisms of Resistance to Noncovalent Bruton’s Tyrosine Kinase Inhibitors

Wang, E., Mi, X., Thompson, M. C., Montoya, S., Notti, R. Q., Afaghani, J., Durham, B. H., Penson, A., Witkowski, M. T., Lu, S. X., et al. (2022) · New England Journal of Medicine · doi:10.1056/nejmoa2114110 · Cited by 272

Molecular basis for redox control by the human cystine/glutamate antiporter system xc−

Parker, J. L., Deme, J. C., Kolokouris, D., Kuteyi, G., Biggin, P. C., Lea, S. M., & Newstead, S. (2021) · Nature Communications · doi:10.1038/s41467-021-27414-1 · Cited by 272

Targeted protein degradation via intramolecular bivalent glues

Hsia, O., Hinterndorfer, M., Cowan, A. D., Iso, K., Ishida, T., Sundaramoorthy, R., Nakasone, M. A., Imrichova, H., Schätz, C., Rukavina, A., et al. (2024) · Nature · doi:10.1038/s41586-024-07089-6 · Cited by 222

Structural basis for Cas9 off-target activity

Pacesa, M., Lin, C.-H., Cléry, A., Saha, A., Arantes, P. R., Bargsten, K., Irby, M. J., Allain, F. H.-T., Palermo, G., Cameron, P., et al. (2022) · Cell · doi:10.1016/j.cell.2022.09.026 · Cited by 198

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

The intrinsic substrate specificity of the human tyrosine kinome

Yaron-Barir, T. M., Joughin, B. A., Huntsman, E. M., Kerelsky, A., Cizin, D. M., Cohen, B. M., Regev, A., Song, J., Vasan, N., Lin, T.-Y., et al. (2024) · Nature · doi:10.1038/s41586-024-07407-y · Cited by 189

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

Targeting cancer with small-molecule pan-KRAS degraders

Popow, J., Farnaby, W., Gollner, A., Kofink, C., Fischer, G., Wurm, M., Zollman, D., Wijaya, A., Mischerikow, N., Hasenoehrl, C., et al. (2024) · Science · doi:10.1126/science.adm8684 · Cited by 198

Cell-free biosynthesis combined with deep learning accelerates de novo-development of antimicrobial peptides

Pandi, A., Adam, D., Zare, A., Trinh, V. T., Schaefer, S. L., Burt, M., Klabunde, B., Bobkova, E., Kushwaha, M., Foroughijabbari, Y., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42434-9 · Cited by 173

Cryo-EM structure of the human cardiac myosin filament

Dutta, D., Nguyen, V., Campbell, K. S., Padrón, R., & Craig, R. (2023) · Nature · doi:10.1038/s41586-023-06691-4 · Cited by 164

Assessment of three‐dimensional RNA structure prediction in CASP15

Das, R., Kretsch, R. C., Simpkin, A. J., Mulvaney, T., Pham, P., Rangan, R., Bu, F., Keegan, R. M., Topf, M., Rigden, D. J., et al. (2023) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26602 · Cited by 139

An atlas of protein homo-oligomerization across domains of life

Schweke, H., Pacesa, M., Levin, T., Goverde, C. A., Kumar, P., Duhoo, Y., Dornfeld, L. J., Dubreuil, B., Georgeon, S., Ovchinnikov, S., et al. (2024) · Cell · doi:10.1016/j.cell.2024.01.022 · Cited by 144

Integrated intracellular organization and its variations in human iPS cells

Viana, M. P., Chen, J., Knijnenburg, T. A., Vasan, R., Yan, C., Arakaki, J. E., Bailey, M., Berry, B., Borensztejn, A., Brown, E. M., et al. (2023) · Nature · doi:10.1038/s41586-022-05563-7 · Cited by 132

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

Structural basis of Gabija anti-phage defence and viral immune evasion

Antine, S. P., Johnson, A. G., Mooney, S. E., Leavitt, A., Mayer, M. L., Yirmiya, E., Amitai, G., Sorek, R., & Kranzusch, P. J. (2024) · Nature · doi:10.1038/s41586-023-06855-2 · Cited by 125

The social and structural architecture of the yeast protein interactome

Michaelis, A. C., Brunner, A.-D., Zwiebel, M., Meier, F., Strauss, M. T., Bludau, I., & Mann, M. (2023) · Nature · doi:10.1038/s41586-023-06739-5 · Cited by 119

A hold-and-feed mechanism drives directional DNA loop extrusion by condensin

Shaltiel, I. A., Datta, S., Lecomte, L., Hassler, M., Kschonsak, M., Bravo, S., Stober, C., Ormanns, J., Eustermann, S., & Haering, C. H. (2022) · Science · doi:10.1126/science.abm4012 · Cited by 112

Mirusviruses link herpesviruses to giant viruses

Gaïa, M., Meng, L., Pelletier, E., Forterre, P., Vanni, C., Fernandez-Guerra, A., Jaillon, O., Wincker, P., Ogata, H., Krupovic, M., et al. (2023) · Nature · doi:10.1038/s41586-023-05962-4 · Cited by 108

Identification of trypsin-degrading commensals in the large intestine

Li, Y., Watanabe, E., Kawashima, Y., Plichta, D. R., Wang, Z., Ujike, M., Ang, Q. Y., Wu, R., Furuichi, M., Takeshita, K., et al. (2022) · Nature · doi:10.1038/s41586-022-05181-3 · Cited by 106

The SMC-family Wadjet complex protects bacteria from plasmid transformation by recognition and cleavage of closed-circular DNA

Deep, A., Gu, Y., Gao, Y.-Q., Ego, K. M., Herzik, M. A., Zhou, H., & Corbett, K. D. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.09.008 · Cited by 106

From interaction networks to interfaces, scanning intrinsically disordered regions using AlphaFold2

Bret, H., Gao, J., Zea, D. J., Andreani, J., & Guerois, R. (2024) · Nature Communications · doi:10.1038/s41467-023-44288-7 · Cited by 103

The molecular architecture of the nuclear basket

(2024) · doi:10.1016/j.cell.2024.07.020 · Cited by 94

In situ architecture of the lipid transport protein VPS13C at ER–lysosome membrane contacts

Cai, S., Wu, Y., Guillén-Samander, A., Hancock-Cerutti, W., Liu, J., & De Camilli, P. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2203769119 · Cited by 93

Native doublet microtubules from Tetrahymena thermophila reveal the importance of outer junction proteins

Kubo, S., Black, C. S., Joachimiak, E., Yang, S. K., Legal, T., Peri, K., Khalifa, A. A. Z., Ghanaeian, A., McCafferty, C. L., Valente-Paterno, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37868-0 · Cited by 93

Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome

Healy, M. D., McNally, K. E., Butkovič, R., Chilton, M., Kato, K., Sacharz, J., McConville, C., Moody, E. R. R., Shaw, S., Planelles-Herrero, V. J., et al. (2023) · Cell · doi:10.1016/j.cell.2023.04.003 · Cited by 91

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

Chromatin remodeling of histone H3 variants by DDM1 underlies epigenetic inheritance of DNA methylation

Lee, S. C., Adams, D. W., Ipsaro, J. J., Cahn, J., Lynn, J., Kim, H.-S., Berube, B., Major, V., Calarco, J. P., LeBlanc, C., et al. (2023) · Cell · doi:10.1016/j.cell.2023.08.001 · Cited by 89

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

Architecture of chloroplast TOC–TIC translocon supercomplex

(2023) · doi:10.1038/s41586-023-05744-y · Cited by 86

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

CombFold: predicting structures of large protein assemblies using a combinatorial assembly algorithm and AlphaFold2

Shor, B., & Schneidman-Duhovny, D. (2024) · Nature Methods · doi:10.1038/s41592-024-02174-0 · Cited by 85

The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state

Lee, K., Thwin, A. C., Nadel, C. M., Tse, E., Gates, S. N., Gestwicki, J. E., & Southworth, D. R. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.023 · Cited by 76

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes

Gupta, M., Azumaya, C. M., Moritz, M., Pourmal, S., Diallo, A., Merz, G. E., Jang, G., Bouhaddou, M., Fossati, A., Brilot, A. F., et al. (2021) · doi:10.1101/2021.05.10.443524 · Cited by 89

IFT-A structure reveals carriages for membrane protein transport into cilia

Hesketh, S. J., Mukhopadhyay, A. G., Nakamura, D., Toropova, K., & Roberts, A. J. (2022) · Cell · doi:10.1016/j.cell.2022.11.010 · Cited by 83

Structures reveal a key mechanism of WAVE regulatory complex activation by Rac1 GTPase

Ding, B., Yang, S., Schaks, M., Liu, Y., Brown, A. J., Rottner, K., Chowdhury, S., & Chen, B. (2022) · Nature Communications · doi:10.1038/s41467-022-33174-3 · Cited by 82

De novo protein identification in mammalian sperm using in situ cryoelectron tomography and AlphaFold2 docking

Chen, Z., Shiozaki, M., Haas, K. M., Skinner, W. M., Zhao, S., Guo, C., Polacco, B. J., Yu, Z., Krogan, N. J., Lishko, P. V., et al. (2023) · Cell · doi:10.1016/j.cell.2023.09.017 · Cited by 82

Posttranslational modification of microtubules by the MATCAP detyrosinase

Landskron, L., Bak, J., Adamopoulos, A., Kaplani, K., Moraiti, M., van den Hengel, L. G., Song, J.-Y., Bleijerveld, O. B., Nieuwenhuis, J., Heidebrecht, T., et al. (2022) · Science · doi:10.1126/science.abn6020 · Cited by 78

Bat genomes illuminate adaptations to viral tolerance and disease resistance

Morales, A. E., Dong, Y., Brown, T., Baid, K., Kontopoulos, D. G., Gonzalez, V., Huang, Z., Ahmed, A.-W., Bhuinya, A., Hilgers, L., et al. (2025) · Nature · doi:10.1038/s41586-024-08471-0 · Cited by 78

Molecular basis of proton sensing by G protein-coupled receptors

Howard, M. K., Hoppe, N., Huang, X.-P., Mitrovic, D., Billesbølle, C. B., Macdonald, C. B., Mehrotra, E., Rockefeller Grimes, P., Trinidad, D. D., Delemotte, L., et al. (2025) · Cell · doi:10.1016/j.cell.2024.11.036 · Cited by 77

De novo-designed pMHC binders facilitate T cell–mediated cytotoxicity toward cancer cells

Johansen, K. H., Wolff, D. S., Scapolo, B., Fernández-Quintero, M. L., Risager Christensen, C., Loeffler, J. R., Rivera-de-Torre, E., Overath, M. D., Kjærgaard Munk, K., Morell, O., et al. (2025) · Science · doi:10.1126/science.adv0422 · Cited by 77

A conserved fertilization complex bridges sperm and egg in vertebrates

Deneke, V. E., Blaha, A., Lu, Y., Suwita, J. P., Draper, J. M., Phan, C. S., Panser, K., Schleiffer, A., Jacob, L., Humer, T., et al. (2024) · Cell · doi:10.1016/j.cell.2024.09.035 · Cited by 78

Structure of a fungal 1,3-β-glucan synthase

Zhao, C.-R., You, Z.-L., Chen, D.-D., Hang, J., Wang, Z.-B., Ji, M., Wang, L.-X., Zhao, P., Qiao, J., Yun, C.-H., et al. (2023) · Science Advances · doi:10.1126/sciadv.adh7820 · Cited by 75

OPA1 helical structures give perspective to mitochondrial dysfunction

(2023) · doi:10.1038/s41586-023-06462-1 · Cited by 75

Discovery and Genomic Characterization of a Novel Henipavirus, Angavokely Virus, from Fruit Bats in Madagascar

Madera, S., Kistler, A., Ranaivoson, H. C., Ahyong, V., Andrianiaina, A., Andry, S., Raharinosy, V., Randriambolamanantsoa, T. H., Ravelomanantsoa, N. A. F., Tato, C. M., et al. (2022) · Journal of Virology · doi:10.1128/jvi.00921-22 · Cited by 74

Conformational control of Cas9 by CRISPR hybrid RNA-DNA guides mitigates off-target activity in T cells

Donohoue, P. D., Pacesa, M., Lau, E., Vidal, B., Irby, M. J., Nyer, D. B., Rotstein, T., Banh, L., Toh, M. S., Gibson, J., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.035 · Cited by 69

Molecular epidemiology of the SARS-CoV-2 variant Omicron BA.2 sub-lineage in Denmark, 29 November 2021 to 2 January 2022

Fonager, J., Bennedbæk, M., Bager, P., Wohlfahrt, J., Ellegaard, K. M., Ingham, A. C., Edslev, S. M., Stegger, M., Sieber, R. N., Lassauniere, R., et al. (2022) · Eurosurveillance · doi:10.2807/1560-7917.es.2022.27.10.2200181 · Cited by 78

Deep learning for reconstructing protein structures from cryo-EM density maps: Recent advances and future directions

Giri, N., Roy, R. S., & Cheng, J. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102536 · Cited by 59

Structure of an endogenous mycobacterial MCE lipid transporter

Chen, J., Fruhauf, A., Fan, C., Ponce, J., Ueberheide, B., Bhabha, G., & Ekiert, D. C. (2023) · Nature · doi:10.1038/s41586-023-06366-0 · Cited by 69

Non-coding 7S RNA inhibits transcription via mitochondrial RNA polymerase dimerization

Zhu, X., Xie, X., Das, H., Tan, B. G., Shi, Y., Al-Behadili, A., Peter, B., Motori, E., Valenzuela, S., Posse, V., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.006 · Cited by 69

Structure of Geobacter OmcZ filaments suggests extracellular cytochrome polymers evolved independently multiple times

Wang, F., Chan, C. H., Suciu, V., Mustafa, K., Ammend, M., Si, D., Hochbaum, A. I., Egelman, E. H., & Bond, D. R. (2022) · eLife · doi:10.7554/elife.81551 · Cited by 69

UBR5 forms ligand-dependent complexes on chromatin to regulate nuclear hormone receptor stability

Tsai, J. M., Aguirre, J. D., Li, Y.-D., Brown, J., Focht, V., Kater, L., Kempf, G., Sandoval, B., Schmitt, S., Rutter, J. C., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.028 · Cited by 68

Evolutionary diversification of methanotrophic ANME-1 archaea and their expansive virome

Laso-Pérez, R., Wu, F., Crémière, A., Speth, D. R., Magyar, J. S., Zhao, K., Krupovic, M., & Orphan, V. J. (2023) · Nature Microbiology · doi:10.1038/s41564-022-01297-4 · Cited by 68

Cryo-EM structure and resistance landscape of M. tuberculosis MmpL3: An emergent therapeutic target

Adams, O., Deme, J. C., Parker, J. L., Fowler, P. W., Lea, S. M., & Newstead, S. (2021) · Structure · doi:10.1016/j.str.2021.06.013 · Cited by 63

Deep contrastive learning enables genome-wide virtual screening

Jia, Y., Gao, B., Tan, J., Zheng, J., Hong, X., Zhu, W., Tan, H., Xiao, Y., Tan, L., Cai, H., et al. (2026) · Science · doi:10.1126/science.ads9530 · Cited by 66

Glucose-sensitive insulin with attenuation of hypoglycaemia

Hoeg-Jensen, T., Kruse, T., Brand, C. L., Sturis, J., Fledelius, C., Nielsen, P. K., Nishimura, E., Madsen, A. R., Lykke, L., Halskov, K. S., et al. (2024) · Nature · doi:10.1038/s41586-024-08042-3 · Cited by 65

Principles of human pre-60 S biogenesis

Vanden Broeck, A., & Klinge, S. (2023) · Science · doi:10.1126/science.adh3892 · Cited by 65

A feed-forward pathway drives LRRK2 kinase membrane recruitment and activation

Vides, E. G., Adhikari, A., Chiang, C. Y., Lis, P., Purlyte, E., Limouse, C., Shumate, J. L., Spínola-Lasso, E., Dhekne, H. S., Alessi, D. R., et al. (2022) · eLife · doi:10.7554/elife.79771 · Cited by 63

Quantifying constraint in the human mitochondrial genome

Lake, N. J., Ma, K., Liu, W., Battle, S. L., Laricchia, K. M., Tiao, G., Puiu, D., Ng, K. K., Cohen, J., Compton, A. G., et al. (2024) · Nature · doi:10.1038/s41586-024-08048-x · Cited by 63

Accelerating crystal structure determination with iterative AlphaFold prediction

Terwilliger, T. C., Afonine, P. V., Liebschner, D., Croll, T. I., McCoy, A. J., Oeffner, R. D., Williams, C. J., Poon, B. K., Richardson, J. S., Read, R. J., et al. (2023) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s205979832300102x · Cited by 62

DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network

(2023) · doi:10.1016/j.molcel.2023.02.009 · Cited by 62

Human senataxin is a bona fide R-loop resolving enzyme and transcription termination factor

Hasanova, Z., Klapstova, V., Porrua, O., Stefl, R., & Sebesta, M. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad092 · Cited by 60

Molecular architecture and dynamics of SARS-CoV-2 envelope by integrative modeling

Pezeshkian, W., Grünewald, F., Narykov, O., Lu, S., Arkhipova, V., Solodovnikov, A., Wassenaar, T. A., Marrink, S. J., & Korkin, D. (2023) · Structure · doi:10.1016/j.str.2023.02.006 · Cited by 60

Three-tiered EGFr domain risk stratification for individualized NOTCH3-small vessel disease prediction

Hack, R. J., Gravesteijn, G., Cerfontaine, M. N., Santcroos, M. A., Gatti, L., Kopczak, A., Bersano, A., Duering, M., Rutten, J. W., & Lesnik Oberstein, S. A. J. (2023) · Brain · doi:10.1093/brain/awac486 · Cited by 60

Disentangling the complex gene interaction networks between rice and the blast fungus identifies a new pathogen effector

Sugihara, Y., Abe, Y., Takagi, H., Abe, A., Shimizu, M., Ito, K., Kanzaki, E., Oikawa, K., Kourelis, J., Langner, T., et al. (2023) · PLOS Biology · doi:10.1371/journal.pbio.3001945 · Cited by 59

Molecular mechanism of agonism and inverse agonism in ghrelin receptor

Qin, J., Cai, Y., Xu, Z., Ming, Q., Ji, S.-Y., Wu, C., Zhang, H., Mao, C., Shen, D.-D., Hirata, K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-27975-9 · Cited by 57

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

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

Snead, D. M., Matyszewski, M., Dickey, A. M., Lin, Y. X., Leschziner, A. E., & Reck-Peterson, S. L. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00863-y · Cited by 54

DNA-measuring Wadjet SMC ATPases restrict smaller circular plasmids by DNA cleavage

Liu, H. W., Roisné-Hamelin, F., Beckert, B., Li, Y., Myasnikov, A., & Gruber, S. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.11.015 · Cited by 53

Reconstitution of BNIP3/NIX-mitophagy initiation reveals hierarchical flexibility of the autophagy machinery

Adriaenssens, E., Schaar, S., Cook, A. S. I., Stuke, J. F. M., Sawa-Makarska, J., Nguyen, T. N., Ren, X., Schuschnig, M., Romanov, J., Khuu, G., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01712-y · Cited by 53

In situ single particle classification reveals distinct 60S maturation intermediates in cells

Lucas, B. A., Zhang, K., Loerch, S., & Grigorieff, N. (2022) · eLife · doi:10.7554/elife.79272 · Cited by 53

Cryo-EM structure of the cytosolic AhR complex.

Wen, Z., Zhang, Y., Zhang, B., Hang, Y., Xu, L., Chen, Y., Xie, Q., Zhao, Q., Zhang, L., Li, G., et al. (2023) · Structure · doi:10.1016/j.str.2022.12.013 · Cited by 51

Structural organization of the retriever–CCC endosomal recycling complex

Boesch, D. J., Singla, A., Han, Y., Kramer, D. A., Liu, Q., Suzuki, K., Juneja, P., Zhao, X., Long, X., Medlyn, M. J., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01184-4 · Cited by 52

Conformational motions and ligand-binding underlying gating and regulation in IP3R channel

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