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

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

Secreted ADAMTS-like 2 promotes myoblast differentiation by potentiating WNT signaling

Taye, N., Singh, M., Baldock, C., & Hubmacher, D. (2023) · Matrix Biology · doi:10.1016/j.matbio.2023.05.003 · 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

A suite of designed protein cages using machine learning and protein fragment-based protocols

Meador, K., Castells-Graells, R., Aguirre, R., Sawaya, M. R., Arbing, M. A., Sherman, T., Senarathne, C., & Yeates, T. O. (2024) · Structure · doi:10.1016/j.str.2024.02.017 · 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

Structure of a SARS-CoV-2 spike S2 subunit in a pre-fusion, open conformation

Olmedillas, E., Rajamanickam, R. R., Avalos, R. D., Ana-Sosa-Batiz, F., Zyla, D., Zandonatti, M. A., Harkins, S. S., Shresta, S., Hastie, K. M., & Saphire, E. O. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116052 · Cited by 19

Mriyaviruses: small relatives of giant viruses

Yutin, N., Mutz, P., Krupovic, M., & Koonin, E. V. (2024) · mBio · doi:10.1128/mbio.01035-24 · Cited by 18

CipA mediates complement resistance of Acinetobacter baumannii by formation of a factor I-dependent quadripartite assemblage

(2022) · doi:10.3389/fimmu.2022.942482 · Cited by 18

Filamentation activates bacterial Avs5 antiviral protein

Wang, Y., Tian, Y., Yang, X., Yu, F., & Zheng, J. (2025) · Nature Communications · doi:10.1038/s41467-025-57732-7 · Cited by 18

Computational Insights into Membrane Disruption by Cell-Penetrating Peptides

Catalina-Hernandez, E., Aguilella-Arzo, M., Peralvarez-Marin, A., & Lopez-Martin, M. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01940 · Cited by 18

The palisade layer of the poxvirus core is composed of flexible A10 trimers

(2024) · doi:10.1038/s41594-024-01218-5 · Cited by 18

Breaching the Bacterial Envelope: The Pivotal Role of Perforin-2 (MPEG1) Within Phagocytes

Merselis, L. C., Rivas, Z. P., & Munson, G. P. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.597951 · 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

Conformational space exploration of cryo-EM structures by variability refinement

Afonine, P. V., Gobet, A., Moissonnier, L., Martin, J., Poon, B. K., & Chaptal, V. (2023) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2023.184133 · Cited by 18

Assessing scoring metrics for AlphaFold2 and AlphaFold3 protein complex predictions

Genz, L. R., Nair, S., Nagar, N., & Topf, M. (2025) · Protein Science · doi:10.1002/pro.70327 · Cited by 17

Filament formation activates protease and ring nuclease activities of CRISPR Lon-SAVED

Smalakyte, D., Ruksenaite, A., Sasnauskas, G., Tamulaitiene, G., & Tamulaitis, G. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.09.002 · 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

Nuclear envelope assembly relies on CHMP-7 in the absence of BAF–LEM-mediated hole closure

Barger, S. R., Penfield, L., & Bahmanyar, S. (2023) · Journal of Cell Science · doi:10.1242/jcs.261385 · 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

Architecture of the spinach plastid-encoded RNA polymerase

Wang, T., Wang, G.-L., Fang, Y., Zhang, Y., Peng, W., Zhou, Y., Zhang, A., Yu, L.-J., & Lu, C. (2024) · Nature Communications · doi:10.1038/s41467-024-54266-2 · Cited by 17

A structural model of the iRhom–ADAM17 sheddase complex reveals functional insights into its trafficking and activity

Kahveci-Türköz, S., Bläsius, K., Wozniak, J., Rinkens, C., Seifert, A., Kasparek, P., Ohm, H., Oltzen, S., Nieszporek, M., Schwarz, N., et al. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04783-y · 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 flagellin-induced NAIP5 activation

Paidimuddala, B., Cao, J., & Zhang, L. (2023) · Science Advances · doi:10.1126/sciadv.adi8539 · Cited by 17

Structure and function of the human mitochondrial MRS2 channel

(2024) · doi:10.1038/s41594-024-01420-5 · Cited by 17

Cryo2StructData: A Large Labeled Cryo-EM Density Map Dataset for AI-based Modeling of Protein Structures

Giri, N., Wang, L., & Cheng, J. (2024) · Scientific Data · doi:10.1038/s41597-024-03299-9 · Cited by 17

Structure of SALL4 zinc finger domain reveals link between AT-rich DNA binding and Okihiro syndrome

Watson, J. A., Pantier, R., Jayachandran, U., Chhatbar, K., Alexander-Howden, B., Kruusvee, V., Prendecki, M., Bird, A., & Cook, A. G. (2023) · Life Science Alliance · doi:10.26508/lsa.202201588 · Cited by 14

T cell toxicity induced by tigecycline binding to the mitochondrial ribosome

Shao, Q., Khawaja, A., Nguyen, M. D., Singh, V., Zhang, J., Liu, Y., Nordin, J., Adori, M., Axel Innis, C., Castro Dopico, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59388-9 · Cited by 16

Ecdysterone prevents negative effect of acute immobilization stress on energy metabolism of rat liver mitochondria

Baev, A. Y., Charishnikova, O. S., Khasanov, F. A., Nebesnaya, K. S., Makhmudov, A. R., Rakhmedova, M. T., Khushbaktova, Z. A., Syrov, V. N., & Levitskaya, Y. V. (2022) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2022.106066 · Cited by 16

Dual function of OmpM as outer membrane tether and nutrient uptake channel in diderm Firmicutes

Silale, A., Zhu, Y., Witwinowski, J., Smith, R. E., Newman, K. E., Bhamidimarri, S. P., Baslé, A., Khalid, S., Beloin, C., Gribaldo, S., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42601-y · Cited by 16

CD5L associates with IgM via the J chain

Wang, Y., Su, C., Ji, C., & Xiao, J. (2024) · Nature Communications · doi:10.1038/s41467-024-52175-y · Cited by 16

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

Cryo-EM reveals the conformational epitope of human monoclonal antibody PAM1.4 broadly reacting with polymorphic malarial protein VAR2CSA

Raghavan, S. S. R., Dagil, R., Lopez-Perez, M., Conrad, J., Bassi, M. R., Quintana, M. D. P., Choudhary, S., Gustavsson, T., Wang, Y., Gourdon, P., et al. (2022) · PLOS Pathogens · doi:10.1371/journal.ppat.1010924 · Cited by 14

In silico evolution of globular protein folds from random sequences

Sahakyan, H., Babajanyan, S. G., Wolf, Y. I., & Koonin, E. V. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2509015122 · Cited by 15

Selective cargo and membrane recognition by SNX17 regulates its interaction with Retriever

Martín-González, A., Méndez-Guzmán, I., Zabala-Zearreta, M., Quintanilla, A., García-López, A., Martínez-Lombardía, E., Albesa-Jové, D., Acosta, J. C., & Lucas, M. (2025) · EMBO Reports · doi:10.1038/s44319-024-00340-1 · Cited by 15

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

Self-supervised machine learning methods for protein design improve sampling but not the identification of high-fitness variants

Ertelt, M., Moretti, R., Meiler, J., & Schoeder, C. T. (2025) · Science Advances · doi:10.1126/sciadv.adr7338 · Cited by 15

Hallucination of closed repeat proteins containing central pockets

An, L., Hicks, D. R., Zorine, D., Dauparas, J., Wicky, B. I. M., Milles, L. F., Courbet, A., Bera, A. K., Nguyen, H., Kang, A., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01112-6 · 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

Inhibition of cleavage of human complement component C5 and the R885H C5 variant by two distinct high affinity anti-C5 nanobodies

Struijf, E. M., De la O Becerra, K. I., Ruyken, M., de Haas, C. J. C., van Oosterom, F., Siere, D. Y., van Keulen, J. E., Heesterbeek, D. A. C., Dolk, E., Heukers, R., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104956 · Cited by 15

Missense variants causing Wiedemann-Steiner syndrome preferentially occur in the KMT2A-CXXC domain and are accurately classified using AlphaFold2

Reynisdottir, T., Anderson, K. J., Boukas, L., & Bjornsson, H. T. (2022) · PLOS Genetics · doi:10.1371/journal.pgen.1010278 · 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

Structure of LRRK1 and mechanisms of autoinhibition and activation

(2023) · doi:10.1038/s41594-023-01109-1 · Cited by 15

Quinone extraction drives atmospheric carbon monoxide oxidation in bacteria

(2025) · doi:10.1038/s41589-025-01836-0 · Cited by 15

Molecular Mechanisms of DNMT3A-3L-Mediated de novo DNA Methylation on Chromatin

Yan, Y., Zhou, X. E., Thomas, S. L., Liu, M., Lai, G.-Q., Worden, E. J., Jones, P. A., & Xu, T.-H. (2025) · doi:10.1101/2025.06.10.658647 · Cited by 14

Functional optimization of light-activatable Opto-GPCRs: Illuminating the importance of the proximal C-terminus in G-protein specificity

(2023) · doi:10.3389/fcell.2023.1053022 · Cited by 14

Interaction of PINK1 with nucleotides and kinetin

Gan, Z. Y., Callegari, S., Nguyen, T. N., Kirk, N. S., Leis, A., Lazarou, M., Dewson, G., & Komander, D. (2024) · Science Advances · doi:10.1126/sciadv.adj7408 · 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

Mechanisms of DNMT3A–3L-mediated de novo DNA methylation on chromatin

Yan, Y., Zhou, X. E., Thomas, S. L., Liu, M., Lai, G.-Q., Worden, E. J., Jones, P. A., & Xu, T.-H. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01704-4 · Cited by 14

Structural and functional properties of the transporter SLC26A6 reveal mechanism of coupled anion exchange

Tippett, D. N., Breen, C., Butler, S. J., Sawicka, M., & Dutzler, R. (2023) · eLife · doi:10.7554/elife.87178 · Cited by 14

A genetically tractable non-vertebrate system to study complete camera-type eye regeneration

Accorsi, A., Pardo, B., Ross, E., Corbin, T. J., McClain, M., Weaver, K., Delventhal, K., Gattamraju, A., Morrison, J. A., McKinney, M. C., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61681-6 · Cited by 14

Zinc-finger (ZiF) fold secreted effectors form a functionally diverse family across lineages of the blast fungus Magnaporthe oryzae

(2024) · doi:10.1371/journal.ppat.1012277 · Cited by 14

PICKLUSTER: a protein-interface clustering and analysis plug-in for UCSF ChimeraX

Genz, L. R., Mulvaney, T., Nair, S., & Topf, M. (2023) · Bioinformatics · doi:10.1093/bioinformatics/btad629 · Cited by 14

Chaotic aging: intrinsically disordered proteins in aging-related processes

Manyilov, V. D., Ilyinsky, N. S., Nesterov, S. V., Saqr, B. M. G. A., Dayhoff, G. W., Zinovev, E. V., Matrenok, S. S., Fonin, A. V., Kuznetsova, I. M., Turoverov, K. K., et al. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04897-3 · 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

The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell

Andreas, M. P., & Giessen, T. W. (2024) · Nature Communications · doi:10.1038/s41467-024-54175-4 · 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

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

T and Z , partial seed coat patterning genes in common bean, provide insight into the structure and protein interactions of a plant MBW complex

McClean, P. E., Roy, J., Colbert, C. L., Osborne, C., Lee, R., Miklas, P. N., & Osorno, J. M. (2024) · G3: Genes, Genomes, Genetics · doi:10.1093/g3journal/jkae184 · Cited by 13

DciA Helicase Operators Exhibit Diversity across Bacterial Phyla

Blaine, H. C., Burke, J. T., Ravi, J., & Stallings, C. L. (2022) · Journal of Bacteriology · doi:10.1128/jb.00163-22 · Cited by 13

Mechanism of DNA unwinding by MCM8-9 in complex with HROB

(2024) · doi:10.1038/s41467-024-47936-8 · Cited by 13

Structure of a membrane tethering complex incorporating multiple SNAREs

DAmico, K. A., Stanton, A. E., Shirkey, J. D., Travis, S. M., Jeffrey, P. D., & Hughson, F. M. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01164-8 · 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 insights into the activation of Mre11-Rad50 endonuclease activity by Sae2/CtIP

Nicolas, Y., Bret, H., Cannavo, E., Acharya, A., Cejka, P., Borde, V., & Guerois, R. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.05.019 · Cited by 12

Fitness landscape of substrate-adaptive mutations in evolved amino acid-polyamine-organocation transporters

(2024) · doi:10.7554/elife.93971 · Cited by 12

Extended DNA threading through a dual-engine motor module of the activating signal co-integrator 1 complex

Jia, J., Hilal, T., Bohnsack, K. E., Chernev, A., Tsao, N., Bethmann, J., Arumugam, A., Parmely, L., Holton, N., Loll, B., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37528-3 · Cited by 12

Amino acid sequence encodes protein abundance shaped by protein stability at reduced synthesis cost

(2024) · doi:10.1002/pro.5239 · 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

Pathological mutations reveal the key role of the cytosolic iRhom2 N-terminus for phosphorylation-independent 14-3-3 interaction and ADAM17 binding, stability, and activity

Bläsius, K., Ludwig, L., Knapp, S., Flaßhove, C., Sonnabend, F., Keller, D., Tacken, N., Gao, X., Kahveci-Türköz, S., Grannemann, C., et al. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05132-3 · Cited by 12

ABCFold: easier running and comparison of AlphaFold 3, Boltz-1, and Chai-1

Elliott, L. G., Simpkin, A. J., & Rigden, D. J. (2024) · Bioinformatics Advances · doi:10.1093/bioadv/vbaf153 · 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

A novel fold for acyltransferase-3 (AT3) proteins provides a framework for transmembrane acyl-group transfer

Newman, K. E., Tindall, S. N., Mader, S. L., Khalid, S., Thomas, G. H., & Van Der Woude, M. W. (2023) · eLife · doi:10.7554/elife.81547 · Cited by 12

Four additional natural 7-deazaguanine derivatives in phages and how to make them

(2023) · doi:10.1093/nar/gkad657 · Cited by 12

DMC1 and RAD51 bind FxxA and FxPP motifs of BRCA2 via two separate interfaces

(2024) · doi:10.1093/nar/gkae452 · 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

Signatures of VH1-69-derived hepatitis C virus neutralizing antibody precursors defined by binding to envelope glycoproteins

Capella-Pujol, J., de Gast, M., Radić, L., Zon, I., Chumbe, A., Koekkoek, S., Olijhoek, W., Schinkel, J., van Gils, M. J., Sanders, R. W., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39690-0 · Cited by 12

Structure of full-length ERGIC-53 in complex with MCFD2 for cargo transport

Watanabe, S., Kise, Y., Yonezawa, K., Inoue, M., Shimizu, N., Nureki, O., & Inaba, K. (2024) · Nature Communications · doi:10.1038/s41467-024-46747-1 · Cited by 12

FGF19 and its analog Aldafermin cooperate with MYC to induce aggressive hepatocarcinogenesis

Ursic-Bedoya, J., Desandré, G., Chavey, C., Marie, P., Polizzi, A., Rivière, B., Guillou, H., Assenat, E., Hibner, U., & Gregoire, D. (2024) · EMBO Molecular Medicine · doi:10.1038/s44321-023-00021-x · Cited by 11

Phosphorylation of Rab29 at Ser185 regulates its localization and role in the lysosomal stress response in concert with LRRK2

Komori, T., Kuwahara, T., Fujimoto, T., Sakurai, M., Koyama-Honda, I., Fukuda, M., & Iwatsubo, T. (2023) · Journal of Cell Science · doi:10.1242/jcs.261003 · 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

Pseudomonas aeruginosa AlgF is a protein–protein interaction mediator required for acetylation of the alginate exopolysaccharide

Low, K. E., Gheorghita, A. A., Tammam, S. D., Whitfield, G. B., Li, Y. E., Riley, L. M., Weadge, J. T., Caldwell, S. J., Chong, P. A., Walvoort, M. T. C., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105314 · Cited by 11

Structural basis for a nucleoporin exportin complex between RanBP2, SUMO1-RanGAP1, the E2 Ubc9, Crm1 and the Ran GTPase

Baytshtok, V., DiMattia, M. A., & Lima, C. D. (2025) · Nature Communications · doi:10.1038/s41467-025-61694-1 · Cited by 11

The role of gene duplication and paralog specialisation in the evolution of the mammalian PRPS complex

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