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

Structure and activation of the human autophagy-initiating ULK1C:PI3KC3-C1 supercomplex

(2025) · doi:10.1038/s41594-025-01557-x · Cited by 40

Molecular basis of Wnt biogenesis, secretion, and Wnt7-specific signaling

Qi, X., Hu, Q., Elghobashi-Meinhardt, N., Long, T., Chen, H., & Li, X. (2023) · Cell · doi:10.1016/j.cell.2023.09.021 · Cited by 40

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

Liu, T., Cao, L., Mladenov, M., Jegou, A., Way, M., & Moores, C. A. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01205-2 · Cited by 40

The PfRCR complex bridges malaria parasite and erythrocyte during invasion

Farrell, B., Alam, N., Hart, M. N., Jamwal, A., Ragotte, R. J., Walters-Morgan, H., Draper, S. J., Knuepfer, E., & Higgins, M. K. (2024) · Nature · doi:10.1038/s41586-023-06856-1 · Cited by 39

The structure of HiSiaQM defines the architecture of tripartite ATP-independent periplasmic (TRAP) transporters

Peter, M. F., Depping, P., Schneberger, N., Severi, E., Gatterdam, K., Tindall, S., Durand, A., Heinz, V., Koenig, P.-A., Geyer, M., et al. (2021) · doi:10.1101/2021.12.03.471092 · Cited by 38

Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter

Peter, M. F., Ruland, J. A., Depping, P., Schneberger, N., Severi, E., Moecking, J., Gatterdam, K., Tindall, S., Durand, A., Heinz, V., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31907-y · Cited by 38

Structural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1

Chen, Z.-P., Xu, D., Wang, L., Mao, Y.-X., Li, Y., Cheng, M.-T., Zhou, C.-Z., Hou, W.-T., & Chen, Y. (2022) · Nature Communications · doi:10.1038/s41467-022-30974-5 · Cited by 37

SSDraw : Software for generating comparative protein secondary structure diagrams

(2023) · doi:10.1002/pro.4836 · Cited by 37

Using AlphaFold Multimer to discover interkingdom protein–protein interactions

Homma, F., Lyu, J., & van der Hoorn, R. A. L. (2024) · The Plant Journal · doi:10.1111/tpj.16969 · Cited by 37

A promiscuous mechanism to phase separate eukaryotic carbon fixation in the green lineage

Barrett, J., Naduthodi, M. I. S., Mao, Y., Dégut, C., Musiał, S., Salter, A., Leake, M. C., Plevin, M. J., McCormick, A. J., Blaza, J. N., et al. (2024) · Nature Plants · doi:10.1038/s41477-024-01812-x · Cited by 37

Oxygen metabolism in descendants of the archaeal-eukaryotic ancestor

Appler, K. E., Lingford, J. P., Gong, X., Panagiotou, K., Leão, P., Langwig, M. V., Greening, C., Ettema, T. J. G., De Anda, V., & Baker, B. J. (2026) · Nature · doi:10.1038/s41586-026-10128-z · Cited by 36

Oxygen metabolism in descendants of the archaeal-eukaryotic ancestor

Appler, K. E., Lingford, J. P., Gong, X., Panagiotou, K., Leão, P., Langwig, M., Greening, C., Ettema, T. J. G., De Anda, V., & Baker, B. J. (2024) · doi:10.1101/2024.07.04.601786 · Cited by 36

Diversity, origin, and evolution of the ESCRT systems

Makarova, K. S., Tobiasson, V., Wolf, Y. I., Lu, Z., Liu, Y., Zhang, S., Krupovic, M., Li, M., & Koonin, E. V. (2024) · mBio · doi:10.1128/mbio.00335-24 · Cited by 36

AlphaFold2 enables accurate deorphanization of ligands to single-pass receptors

Banhos Danneskiold-Samsøe, N., Kavi, D., Jude, K. M., Nissen, S. B., Wat, L. W., Coassolo, L., Zhao, M., Santana-Oikawa, G. A., Broido, B. B., Garcia, K. C., et al. (2024) · Cell Systems · doi:10.1016/j.cels.2024.10.004 · Cited by 35

Cryo-EM structure of the Smc5/6 holo-complex

Hallett, S. T., Campbell Harry, I., Schellenberger, P., Zhou, L., Cronin, N. B., Baxter, J., Etheridge, T. J., Murray, J. M., & Oliver, A. W. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac692 · Cited by 35

Semantic design of functional de novo genes from a genomic language model

(2025) · doi:10.1038/s41586-025-09749-7 · Cited by 35

Cryo-EM structures of an LRRC8 chimera with native functional properties reveal heptameric assembly

Takahashi, H., Yamada, T., Denton, J. S., Strange, K., & Karakas, E. (2023) · eLife · doi:10.7554/elife.82431 · Cited by 35

Pharmacological hallmarks of allostery at the M4 muscarinic receptor elucidated through structure and dynamics

Vuckovic, Z., Wang, J., Pham, V., Mobbs, J. I., Belousoff, M. J., Bhattarai, A., Burger, W. A., Thompson, G., Yeasmin, M., Nawaratne, V., et al. (2023) · eLife · doi:10.7554/elife.83477 · Cited by 34

Structural basis for plasmid restriction by SMC JET nuclease

Roisné-Hamelin, F., Liu, H. W., Taschner, M., Li, Y., & Gruber, S. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.009 · Cited by 34

Structure and mechanism of a tripartite ATP-independent periplasmic TRAP transporter

Davies, J. S., Currie, M. J., North, R. A., Scalise, M., Wright, J. D., Copping, J. M., Remus, D. M., Gulati, A., Morado, D. R., Jamieson, S. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36590-1 · Cited by 34

Structural insight into Tn3 family transposition mechanism

Shkumatov, A. V., Aryanpour, N., Oger, C. A., Goossens, G., Hallet, B. F., & Efremov, R. G. (2022) · Nature Communications · doi:10.1038/s41467-022-33871-z · Cited by 34

Structural pathway for PI3-kinase regulation by VPS15 in autophagy

Cook, A. S. I., Chen, M., Nguyen, T. N., Cabezudo, A. C., Khuu, G., Rao, S., Garcia, S. N., Yang, M., Iavarone, A. T., Ren, X., et al. (2025) · Science · doi:10.1126/science.adl3787 · Cited by 34

Systematic identification of structure-specific protein–protein interactions

(2024) · doi:10.1038/s44320-024-00037-6 · Cited by 34

Double-stranded RNA sequencing reveals distinct riboviruses associated with thermoacidophilic bacteria from hot springs in Japan

Urayama, S.-I., Fukudome, A., Hirai, M., Okumura, T., Nishimura, Y., Takaki, Y., Kurosawa, N., Koonin, E. V., Krupovic, M., & Nunoura, T. (2024) · Nature Microbiology · doi:10.1038/s41564-023-01579-5 · Cited by 34

Genomic screening of 16 UK native bat species through conservationist networks uncovers coronaviruses with zoonotic potential

Tan, C. C. S., Trew, J., Peacock, T. P., Mok, K. Y., Hart, C., Lau, K., Ni, D., Orme, C. D. L., Ransome, E., Pearse, W. D., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38717-w · Cited by 34

Modifying immune responses to adeno-associated virus vectors by capsid engineering

Bentler, M., Hardet, R., Ertelt, M., Rudolf, D., Kaniowska, D., Schneider, A., Vondran, F. W. R., Schoeder, C. T., Delphin, M., Lucifora, J., et al. (2023) · Molecular Therapy - Methods & Clinical Development · doi:10.1016/j.omtm.2023.08.015 · Cited by 34

Using AlphaFold for Rapid and Accurate Fixed Backbone Protein Design

Moffat, L., Greener, J. G., & Jones, D. T. (2021) · doi:10.1101/2021.08.24.457549 · Cited by 33

Molecular architecture of synaptic vesicles

Kravčenko, U., Ruwolt, M., Kroll, J., Yushkevich, A., Zenkner, M., Ruta, J., Lotfy, R., Wanker, E. E., Rosenmund, C., Liu, F., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2407375121 · Cited by 33

Genome expansion by a CRISPR trimmer-integrase

Wang, J. Y., Tuck, O. T., Skopintsev, P., Soczek, K. M., Li, G., Al-Shayeb, B., Zhou, J., & Doudna, J. A. (2023) · Nature · doi:10.1038/s41586-023-06178-2 · Cited by 33

Modeling Flexible Protein Structure With AlphaFold2 and Crosslinking Mass Spectrometry

(2024) · doi:10.1016/j.mcpro.2024.100724 · Cited by 33

Molecular mechanism of substrate recognition by folate transporter SLC19A1

Dang, Y., Zhou, D., Du, X., Zhao, H., Lee, C.-H., Yang, J., Wang, Y., Qin, C., Guo, Z., & Zhang, Z. (2022) · Cell Discovery · doi:10.1038/s41421-022-00508-w · Cited by 33

Rieske head domain dynamics and indazole-derivative inhibition of Candida albicans complex III

Di Trani, J. M., Liu, Z., Whitesell, L., Brzezinski, P., Cowen, L. E., & Rubinstein, J. L. (2022) · Structure · doi:10.1016/j.str.2021.08.006 · Cited by 32

Molecular basis of mRNA delivery to the bacterial ribosome

Webster, M. W., Chauvier, A., Rahil, H., Graziadei, A., Charles, K., Miropolskaya, N., Takacs, M., Saint-André, C., Rappsilber, J., Walter, N. G., et al. (2024) · Science · doi:10.1126/science.ado8476 · Cited by 32

The kidney slit diaphragm resembles a fishnet

Birtasu, A. N., Wieland, K., Ermel, U. H., Arghittu, S. M., Manger, S., Kocylowski, M. K., Fakler, B., Scheffer, M. P., Covino, R., Grahammer, F., et al. (2025) · Kidney International · doi:10.1016/j.kint.2025.08.028 · Cited by 32

Bacterial Shedu immune nucleases share a common enzymatic core regulated by diverse sensor domains

Gu, Y., Li, H., Deep, A., Enustun, E., Zhang, D., & Corbett, K. D. (2025) · Molecular Cell · doi:10.1016/j.molcel.2024.12.004 · Cited by 32

Asymmetrical dose responses shape the evolutionary trade-off between antifungal resistance and nutrient use

Després, P. C., Cisneros, A. F., Alexander, E. M. M., Sonigara, R., Gagné-Thivierge, C., Dubé, A. K., & Landry, C. R. (2022) · Nature Ecology & Evolution · doi:10.1038/s41559-022-01846-4 · Cited by 32

Structural insights into the mechanism of protein transport by the Type 9 Secretion System translocon

(2024) · doi:10.1038/s41564-024-01644-7 · Cited by 32

Molecular insights into human phosphatidylserine synthase 1 reveal its inhibition promotes LDL uptake

Long, T., Li, D., Vale, G., Jiang, Y., Schmiege, P., Yang, Z. J., McDonald, J. G., & Li, X. (2024) · Cell · doi:10.1016/j.cell.2024.08.004 · Cited by 31

Cryo‐EM structures of human ABCA7 provide insights into its phospholipid translocation mechanisms

Le, L. T. M., Thompson, J. R., Dehghani‐Ghahnaviyeh, S., Pant, S., Dang, P. X., French, J. B., Kanikeyo, T., Tajkhorshid, E., & Alam, A. (2023) · The EMBO Journal · doi:10.15252/embj.2022111065 · Cited by 31

Chemical tools to expand the ligandable proteome: Diversity-oriented synthesis-based photoreactive stereoprobes

Ogasawara, D., Konrad, D. B., Tan, Z. Y., Carey, K. L., Luo, J., Won, S. J., Li, H., Carter, T. R., DeMeester, K. E., Njomen, E., et al. (2024) · Cell Chemical Biology · doi:10.1016/j.chembiol.2024.10.005 · Cited by 31

Assessment of three-dimensional RNA structure prediction in CASP15

(2023) · doi:10.1101/2023.04.25.538330 · Cited by 31

Structure and mechanism of NALCN-FAM155A-UNC79-UNC80 channel complex

Kang, Y., & Chen, L. (2022) · Nature Communications · doi:10.1038/s41467-022-30403-7 · Cited by 31

Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane

Park, S. H., Han, J., Jeong, B.-C., Song, J. H., Jang, S. H., Jeong, H., Kim, B. H., Ko, Y.-G., Park, Z.-Y., Lee, K. E., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01111-7 · Cited by 31

Structural basis of peptide recognition and activation of endothelin receptors

(2023) · doi:10.1038/s41467-023-36998-9 · Cited by 31

Proteogenomics reveals sex-biased aging genes and coordinated splicing in cardiac aging

Han, Y., Wennersten, S. A., Wright, J. M., Ludwig, R. W., Lau, E., & Lam, M. P. Y. (2022) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00244.2022 · Cited by 31

Mechanism of orphan subunit recognition during assembly quality control

Yagita, Y., Zavodszky, E., Peak-Chew, S.-Y., & Hegde, R. S. (2023) · Cell · doi:10.1016/j.cell.2023.06.016 · Cited by 30

RNA targeting and cleavage by the type III-Dv CRISPR effector complex

Schwartz, E. A., Bravo, J. P. K., Ahsan, M., Macias, L. A., McCafferty, C. L., Dangerfield, T. L., Walker, J. N., Brodbelt, J. S., Palermo, G., Fineran, P. C., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47506-y · Cited by 30

Clustering of TP53 variants into functional classes correlates with cancer risk and identifies different phenotypes of Li-Fraumeni syndrome

Montellier, E., Lemonnier, N., Penkert, J., Freycon, C., Blanchet, S., Amadou, A., Chuffart, F., Fischer, N. W., Achatz, M.-I., Levine, A. J., et al. (2024) · iScience · doi:10.1016/j.isci.2024.111296 · Cited by 29

Chromatin binding by HORMAD proteins regulates meiotic recombination initiation

Milano, C. R., Ur, S. N., Gu, Y., Zhang, J., Allison, R., Brown, G., Neale, M. J., Tromer, E. C., Corbett, K. D., & Hochwagen, A. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00034-3 · Cited by 29

Extracellular domain of PepT1 interacts with TM1 to facilitate substrate transport

Shen, J., Hu, M., Fan, X., Ren, Z., Portioli, C., Yan, X., Rong, M., & Zhou, M. (2022) · Structure · doi:10.1016/j.str.2022.04.011 · Cited by 29

Phage defence system CBASS is regulated by a prokaryotic E2 enzyme that imitates the ubiquitin pathway

Yan, Y., Xiao, J., Huang, F., Xian, W., Yu, B., Cheng, R., Wu, H., Lu, X., Wang, X., Huang, W., et al. (2024) · Nature Microbiology · doi:10.1038/s41564-024-01684-z · Cited by 29

Foldcomp: a library and format for compressing and indexing large protein structure sets

Kim, H., Mirdita, M., & Steinegger, M. (2023) · Bioinformatics · doi:10.1093/bioinformatics/btad153 · Cited by 29

Modeling the Orthosteric Binding Site of the G Protein-Coupled Odorant Receptor OR5K1

Nicoli, A., Haag, F., Marcinek, P., He, R., Kreißl, J., Stein, J., Marchetto, A., Dunkel, A., Hofmann, T., Krautwurst, D., et al. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c00752 · Cited by 28

Preclinical evaluation of a COVID-19 vaccine candidate based on a recombinant RBD fusion heterodimer of SARS-CoV-2

Barreiro, A., Prenafeta, A., Bech-Sabat, G., Roca, M., Perozo Mur, E., March, R., González-González, L., Madrenas, L., Corominas, J., Fernández, A., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106126 · Cited by 28

The role of metabolism in shaping enzyme structures over 400 million years

(2025) · doi:10.1038/s41586-025-09205-6 · Cited by 28

In situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque

(2025) · doi:10.1038/s41564-025-02012-9 · Cited by 28

The RIX domain defines a class of polymorphic T6SS effectors and secreted adaptors

Kanarek, K., Fridman, C. M., Bosis, E., & Salomon, D. (2023) · Nature Communications · doi:10.1038/s41467-023-40659-2 · Cited by 27

Neurotransmitter release is triggered by a calcium-induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface

Toulmé, E., Salazar Lázaro, A., Trimbuch, T., Rizo, J., & Rosenmund, C. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2409636121 · Cited by 27

Three small partner proteins facilitate the type VII-dependent secretion of an antibacterial nuclease

Yang, Y., Boardman, E., Deme, J., Alcock, F., Lea, S., & Palmer, T. (2023) · mBio · doi:10.1128/mbio.02100-23 · Cited by 27

Conformational changes linked to ADP release from human cardiac myosin bound to actin-tropomyosin

Doran, M. H., Rynkiewicz, M. J., Rasicci, D., Bodt, S. M. L., Barry, M. E., Bullitt, E., Yengo, C. M., Moore, J. R., & Lehman, W. (2023) · Journal of General Physiology · doi:10.1085/jgp.202213267 · Cited by 27

Anti-CRISPR AcrIIC5 is a dsDNA mimic that inhibits type II-C Cas9 effectors by blocking PAM recognition

(2023) · doi:10.1093/nar/gkad052 · Cited by 26

FilamentID reveals the composition and function of metabolic enzyme polymers during gametogenesis

Hugener, J., Xu, J., Wettstein, R., Ioannidi, L., Velikov, D., Wollweber, F., Henggeler, A., Matos, J., & Pilhofer, M. (2024) · Cell · doi:10.1016/j.cell.2024.04.026 · Cited by 26

DdmDE eliminates plasmid invasion by DNA-guided DNA targeting

Yang, X.-Y., Shen, Z., Wang, C., Nakanishi, K., & Fu, T.-M. (2024) · Cell · doi:10.1016/j.cell.2024.07.028 · Cited by 26

Structural basis for an early stage of the photosystem II repair cycle in Chlamydomonas reinhardtii

Li, A., You, T., Pang, X., Wang, Y., Tian, L., Li, X., & Liu, Z. (2024) · Nature Communications · doi:10.1038/s41467-024-49532-2 · Cited by 26

Substrate recognition principles for the PP2A-B55 protein phosphatase

Kruse, T., Garvanska, D. H., Varga, J. K., Garland, W., McEwan, B. C., Hein, J. B., Weisser, M. B., Benavides-Puy, I., Chan, C. B., Sotelo-Parrilla, P., et al. (2024) · Science Advances · doi:10.1126/sciadv.adp5491 · Cited by 26

CryoDRGN-AI: neural ab initio reconstruction of challenging cryo-EM and cryo-ET datasets

Levy, A., Raghu, R., Feathers, J. R., Grzadkowski, M., Poitevin, F., Johnston, J. D., Vallese, F., Clarke, O. B., Wetzstein, G., & Zhong, E. D. (2025) · Nature Methods · doi:10.1038/s41592-025-02720-4 · Cited by 25

A co-transcriptional ribosome assembly checkpoint controls nascent large ribosomal subunit maturation

Sanghai, Z. A., Piwowarczyk, R., Broeck, A. V., & Klinge, S. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-00947-3 · Cited by 25

Structure and dynamics of differential ligand binding in the human ρ-type GABAA receptor

Cowgill, J., Fan, C., Haloi, N., Tobiasson, V., Zhuang, Y., Howard, R. J., & Lindahl, E. (2023) · Neuron · doi:10.1016/j.neuron.2023.08.006 · Cited by 25

Structural insights into binding-site access and ligand recognition by human ABCB1

Kurre, D., Dang, P. X., Le, L. T. M., Gadkari, V. V., & Alam, A. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00361-z · Cited by 25

Design in the DARK: Learning Deep Generative Models for De Novo Protein Design

Moffat, L., Kandathil, S. M., & Jones, D. T. (2022) · doi:10.1101/2022.01.27.478087 · 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

Structure of the ciliary tip central pair reveals the unique role of the microtubule-seam binding protein SPEF1

(2025) · doi:10.1016/j.cub.2025.06.020 · Cited by 25

Structure and host specificity of Staphylococcus epidermidis bacteriophage Andhra

Hawkins, N. C., Kizziah, J. L., Hatoum-Aslan, A., & Dokland, T. (2022) · Science Advances · doi:10.1126/sciadv.ade0459 · 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

Molecular principles of redox-coupled sodium pumping of the ancient Rnf machinery

Kumar, A., Roth, J., Kim, H., Saura, P., Bohn, S., Reif-Trauttmansdorff, T., Schubert, A., Kaila, V. R. I., Schuller, J. M., & Müller, V. (2025) · Nature Communications · doi:10.1038/s41467-025-57375-8 · Cited by 24

Buffering of genetic dominance by allele-specific protein complex assembly

Badonyi, M., & Marsh, J. A. (2023) · Science Advances · doi:10.1126/sciadv.adf9845 · Cited by 24

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

Structural basis for Retriever-SNX17 assembly and endosomal sorting

Singla, A., Boesch, D. J., Fung, H. Y. J., Ngoka, C., Enriquez, A. S., Song, R., Kramer, D. A., Han, Y., Banarer, E., Lemoff, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54583-6 · Cited by 23

Rapid UPF1 depletion illuminates the temporal dynamics of the NMD-regulated human transcriptome

Boehm, V., Wallmeroth, D., Wulf, P. O., Popp, O., Teixeira Alves, L. G., Reinecke, L., Riedel, M., Wyler, E., Franitza, M., Becker, K., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.08.015 · Cited by 23

Structural insights into human TFIIIC promoter recognition

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

Structures of human dynein in complex with the lissencephaly 1 protein, LIS1

Reimer, J. M., DeSantis, M. E., Reck-Peterson, S. L., & Leschziner, A. E. (2023) · eLife · doi:10.7554/elife.84302 · 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

Characterizing glucokinase variant mechanisms using a multiplexed abundance assay

Gersing, S., Schulze, T. K., Cagiada, M., Stein, A., Roth, F. P., Lindorff-Larsen, K., & Hartmann-Petersen, R. (2024) · Genome Biology · doi:10.1186/s13059-024-03238-2 · 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

SUMOylation of the m6A reader YTHDF2 by PIAS1 promotes viral RNA decay to restrict EBV replication

Sugiokto, F. G., Saiada, F., Zhang, K., & Li, R. (2024) · mBio · doi:10.1128/mbio.03168-23 · Cited by 23

Discovery of archaeal Fusexins homologous to eukaryotic HAP2/GCS1 gamete fusion proteins

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