The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
UCSF ChimeraX: Structure visualization for researchers, educators, and developers
Open accessAbstract
UCSF ChimeraX is the next‐generation interactive visualization program from the Resource for Biocomputing, Visualization, and Informatics (RBVI), following UCSF Chimera. ChimeraX brings (a) significant performance and graphics enhancements; (b) new implementations of Chimera's most highly used tools, many with further improvements; (c) several entirely new analysis features; (d) support for new areas such as virtual reality, light‐sheet microscopy, and medical imaging data; (e) major ease‐of‐use advances, including toolbars with icons to perform actions with a single click, basic “undo” capabilities, and more logical and consistent commands; and (f) an app store for researchers to contribute new tools. ChimeraX includes full user documentation and is free for noncommercial use, with downloads available for Windows, Linux, and macOS from https://www.rbvi.ucsf.edu/chimerax.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
Research works printed but not linked: 29
- 10.1038/nmeth.1427 · DOI
- 10.1073/pnas.1309947110 · DOI
- 10.1038/nprot.2010.126 · DOI
- 10.1016/j.str.2015.05.013 · DOI
- 10.1093/nar/gkp302 · DOI
- 10.1093/nar/gkq394 · DOI
- 10.1093/nar/gkq1021 · DOI · Paper page
- 10.1093/nar/gkq1091 · DOI · Paper page
- 10.1093/nar/gkv1126 · DOI · Paper page
- 10.1093/nar/gkv1290 · DOI
- 10.1093/nar/gku1221 · DOI · Paper page
- 10.1093/bioinformatics/btt138 · DOI
- 10.1093/nar/28.1.235 · DOI · Paper page
- 10.1002/jcc.20084 · DOI · Paper page
- 10.1016/j.str.2018.03.011 · DOI
- 10.1002/cpbi.48 · DOI
- 10.1186/1758-2946-3-32 · DOI
- 10.1002/pro.3235 · DOI · Paper page
- Croll TI, 2018, ISOLDE: A physically realistic environment for model building into low‐resolution electron‐density maps, Acta Cryst, 74, 519
- 10.1016/j.cell.2020.04.031 · DOI · Paper page
- 10.1016/j.jmb.2018.06.040 · DOI
- 10.1093/nar/gkw1118 · DOI
- 10.1093/bioinformatics/17.8.700 · DOI
- 10.1002/bip.22074 · DOI
- NakaneT KotechaA SenteA McMullanG MasiulisS Brown Patricia M. G. E. GrigorasIT MalinauskaiteL MalinauskasT MiehlingJ YuL KariaD PechnikovaEV deJongE KeizerJ BischoffM McCormackJ TiemeijerP HardwickSW ChirgadzeDY MurshudovG AricescuAR ScheresSHW(2020).Single‐particle cryo‐EM at atomic resolution.bioRxiv 110189. http://dx.doi.org/10.1101/2020.05.22.110189. · DOI
- 10.7554/eLife.53740 · DOI
- 10.1016/j.str.2008.03.005 · DOI
- 10.1093/nar/gnj031 · DOI
- 10.1093/nar/gku377 · DOI
Cited by
Items 401–494 of 494
The S-component fold: a link between bacterial transporters and receptors
Partipilo, M., & Slotboom, D. J. (2024) · Communications Biology · doi:10.1038/s42003-024-06295-2 · Cited by 4
Accurate predictions of SARS-CoV-2 infectivity from comprehensive analysis
Park, J., Choi, W., Seong, D. Y., Jeong, S., Lee, J. Y., Park, H. J., Chung, D. S., Yi, K., Kim, U., Yoon, G.-Y., et al. (2024) · eLife · doi:10.7554/elife.99833.3 · Cited by 4
Hecquet, T., Arbogast, N., Suhner, D., Goetz, A., Amann, G., Yürekli, S., Marangoni, F., Quintin, S., Greve, J. N., Di Donato, N., et al. (2025) · iScience · doi:10.1016/j.isci.2025.113652 · Cited by 4
Mosebach, L., Ozawa, S.-I., Younas, M., Xue, H., Scholz, M., Takahashi, Y., & Hippler, M. (2024) · Plants · doi:10.3390/plants13121632 · Cited by 4
Macke, A. C., Stump, J. E., Kelly, M. S., Rowley, J., Herath, V., Mullen, S., & Dima, R. I. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01511 · Cited by 4
Architecture and activation of human muscle phosphorylase kinase
Yang, X., Zhu, M., Lu, X., Wang, Y., & Xiao, J. (2024) · Nature Communications · doi:10.1038/s41467-024-47049-2 · Cited by 4
Tippett, D. N., Breen, C., Butler, S. J., Sawicka, M., & Dutzler, R. (2023) · eLife · doi:10.7554/elife.87178.3 · Cited by 3
Wu, W., Gupta, S., Sagan, S. A., Moseley, C. E., Zamvil, S. S., & Pak, J. E. (2024) · Journal of Immunological Methods · doi:10.1016/j.jim.2024.113764 · 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
Effects of residue substitutions on the cellular abundance of proteins
Schulze, T. K., & Lindorff-Larsen, K. (2026) · eLife · doi:10.7554/elife.103721 · Cited by 3
Turvey, S., Muench, S. P., Issad, T., Fishwick, C. W. G., Kearney, M. T., & Simmons, K. J. (2024) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2024.101607 · 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
Structure and post-translational modification of the prostaglandin transporter
Yu, P., Orlando, M. A., & Orlando, B. J. (2025) · Communications Biology · doi:10.1038/s42003-025-08510-0 · Cited by 3
Conserved pathway for homarine catabolism in environmental bacteria
Ferrer-González, F. X., Heal, K. R., Sacks, J. S., Romero-Maysonet, Y., Finch, A. H., Carlson, L. T., Coe, L. S. Y., Bartolek, Z., Luthy, C. B., Gaffney, M. P., et al. (2026) · Nature Microbiology · doi:10.1038/s41564-026-02313-7 · Cited by 3
Allosteric activation of the co-receptor BAK1 by the EFR receptor kinase initiates immune signaling
Mühlenbeck, H., Tsutsui, Y., Lemmon, M. A., Bender, K. W., & Zipfel, C. (2023) · doi:10.1101/2023.08.23.554490 · Cited by 3
Bimai, O., Banerjee, I., Rozman Grinberg, I., Huang, P., Hultgren, L., Ekström, S., Lundin, D., Sjöberg, B.-M., & Logan, D. T. (2024) · eLife · doi:10.7554/elife.89292 · Cited by 3
Dual site targeting of the bacterial 70S ribosome by tetracyclines
Devarkar, S. C., Lomakin, I. B., Wang, J., Grada, A., & Bunick, C. G. (2026) · Nature Communications · doi:10.1038/s41467-026-72788-9 · Cited by 2
Omura, S. N., Nakagawa, R., Kajimoto, S., Okazaki, S., Ishiguro, S., Mori, H., Onishi, K., Kashiwakura, Y., Hiramoto, T., Horinaka, K., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71626-2 · Cited by 2
Extensive natural variation in bacterial ribosomal drug-binding sites
Ekemezie, C. L., Chan, L. I., Brown, C. R., Helena-Bueno, K., Williams, T. A., & Melnikov, S. V. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115878 · Cited by 2
Mechanism of receptor assembly via the pleiotropic adipokine Leptin
Tsirigotaki, A., Dansercoer, A., Verschueren, K. H. G., Marković, I., Pollmann, C., Hafer, M., Felix, J., Birck, C., Van Putte, W., Catteeuw, D., et al. (2022) · doi:10.1101/2022.12.01.518327 · Cited by 2
Leemann, S., & Kleinlogel, S. (2023) · doi:10.1101/2023.01.27.525823 · Cited by 2
Lipophilic modification of salirasib modulates the antiproliferative and antimigratory activity
Ballari, M. S., O. J. Porta, E., Zalazar, E. A., Etichetti, C. M. B., Padrón, J. M., Girardini, J. E., & Labadie, G. R. (2023) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2023.117417 · Cited by 2
Visualizing the mechanism of quinol oxidation and inhibition of a bd -type oxidase using cryo-EM
van der Velden, T. T., Kayastha, K., Pelser, F., Brünle, S., & Jeuken, L. J. C. (2026) · Science Advances · doi:10.1126/sciadv.aec9946 · Cited by 2
Evolutionary Adaptation of an HP1-protein Chromodomain Integrates Chromatin and DNA Sequence Signals
Baumgartner, L., Ipsaro, J. J., Hohmann, U., Handler, D., Schleiffer, A., Duchek, P., & Brennecke, J. (2023) · doi:10.1101/2023.09.29.560096 · Cited by 2
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
Characterization of prevalent genetic variants in the Estonian Biobank body-mass index GWAS
Abner, E., Batool, K., Taba, N., Nikopensius, T., Läll, K., Alekseienko, A., Eriksson, A., Rämö, J., Haapaniemi, H., Kariis, H. M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64006-9 · Cited by 2
BRCA2-HSF2BP oligomeric ring disassembly by BRME1 promotes homologous recombination
Ghouil, R., Miron, S., Sato, K., Ristic, D., van Rossum-Fikkert, S. E., Legrand, P., Ouldali, M., Winter, J.-M., Ropars, V., David, G., et al. (2023) · Science Advances · doi:10.1126/sciadv.adi7352 · Cited by 2
Distribution and molecular evolution of the anti-CRISPR family AcrIF7
Figueroa, W., Cazares, A., Cazares, D., Wu, Y., de la Cruz, A., Welch, M., Kameyama, L., Nobrega, F. L., & Guarneros, G. (2023) · PLOS Biology · doi:10.1371/journal.pbio.3002072 · Cited by 2
Thahsin, N., Khan, K. I., Sarwar, A. N. M. R., Sakib, M. N., & Rahman, M. S. (2025) · Computational and Structural Biotechnology Reports · doi:10.1016/j.csbr.2024.100029 · Cited by 2
Structural insights into Cas9-mediated prespacer selection in CRISPR-Cas adaptation
Gaizauskaite, U., Tamulaitiene, G., Silanskas, A., Gasiunas, G., Siksnys, V., & Sasnauskas, G. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.01.022 · Cited by 2
Hybrid adaptation is hampered by Haldane’s sieve
Bautista, C., Gagnon-Arsenault, I., Utrobina, M., Fijarczyk, A., Bendixsen, D. P., Stelkens, R., & Landry, C. R. (2023) · doi:10.1101/2023.12.15.571924 · Cited by 2
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
Ketaren, N. E., Mast, F. D., Fridy, P. C., Olivier, J. P., Sanyal, T., Sali, A., Chait, B. T., Rout, M. P., & Aitchison, J. D. (2023) · doi:10.1101/2023.07.14.549041 · Cited by 1
Guo, Y., Shukla, S., Minasov, G., Inniss, N. L., Klose, T., Tokars, V. L., Mondragón, A., Otwinowski, Z., Borek, D., & Satchell, K. J. F. (2026) · Protein Science · doi:10.1002/pro.70609 · Cited by 1
Asymmetric horseshoe-like assembly of peroxisomal Yeast Oxalyl-CoA synthetase
Bürgi, J., Lill, P., Giannopoulou, E.-A., Jeffries, C. M., Chojnowski, G., Raunser, S., Gatsogiannis, C., & Wilmanns, M. (2022) · doi:10.1101/2022.08.30.505785 · Cited by 1
Konuma, T., Takai, T., Tsuchiya, C., Nishida, M., Hashiba, M., Yamada, Y., Shirai, H., Motoda, Y., Nagadoi, A., Chikaishi, E., et al. (2024) · Protein Science · doi:10.1002/pro.5002 · Cited by 1
Kunz, L., Bernasconi, Z., Heuberger, M., Isaksson, J., Sotiropoulos, A. G., Stirnemann, U., Jigisha, J., Menardo, F., Wicker, T., Müller, M. C., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-72199-w · Cited by 1
Lolicato, F., Steringer, J., Saleppico, R., Beyer, D., Fernandez-Sobaberas, J., Unger, S., Klein, S., Riegerová, P., Wegehingel, S., Müller, H., et al. (2023) · doi:10.7554/elife.88579.2 · 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
Modeling flexible protein structure with AlphaFold2 and cross-linking mass spectrometry
Manalastas-Cantos, K., Adoni, K. R., Pfeifer, M., Märtens, B., Grünewald, K., Thalassinos, K., & Topf, M. (2023) · doi:10.1101/2023.09.11.557128 · Cited by 1
Characterisation of anhydro-sialic acid transporters from mucosa-associated bacteria
Wu, Y., Bell, A., Thomas, G. H., Bolam, D. N., Sargent, F., Juge, N., Palmer, T., & Severi, E. (2024) · Microbiology · doi:10.1099/mic.0.001448 · Cited by 1
The SSU Processome Component Utp25p is a Pseudohelicase
Helwer, R., & Charette, J. M. (2022) · doi:10.1101/2022.07.08.499361 · Cited by 1
Dodge, G. J., Anderson, A. J., He, Y., Liu, W., Viner, R., & Imperiali, B. (2023) · doi:10.1101/2023.06.16.545297 · Cited by 1
NLRP14 modulates the activity of E3 ubiquitin ligases during the oocyte-to-embryo transition
Liu, S., Qi, Q., Chi, P., Jiao, H., Yan, L., Lu, Y., Zhang, R., Li, J., Ju, S., Han, Z., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71519-4 · Cited by 1
Likelihood-based interactive local docking into cryo-EM maps in ChimeraX
Read, R. J., Pettersen, E. F., McCoy, A. J., Croll, T. I., Terwilliger, T. C., Poon, B. K., Meng, E. C., Liebschner, D., & Adams, P. D. (2024) · doi:10.1101/2024.05.16.594509 · Cited by 1
Self-citationCryo‐EM structures of multiple‐peptide resistance factor ( MprF ) from Pseudomonas aeruginosa
Jha, S., & Vinothkumar, K. R. (2026) · The FEBS Journal · doi:10.1111/febs.70519 · Cited by 1
Remm, S., De Vecchis, D., Schöppe, J., Hutter, C. A. J., Gonda, I., Hohl, M., Newstead, S., Schäfer, L. V., & Seeger, M. A. (2023) · doi:10.1101/2023.01.25.525346 · Cited by 1
Karapanagioti, F., Atlason, Ú. Á., Slotboom, D. J., Poolman, B., & Obermaier, S. (2024) · eLife · doi:10.7554/elife.93971.3 · Cited by 1
2-oxoglutarate triggers assembly of active dodecameric Methanosarcina mazei glutamine synthetase
Herdering, E., Reif-Trauttmansdorff, T., Kumar, A., Habenicht, T., Hochberg, G., Bohn, S., Schuller, J., & Schmitz, R. A. (2024) · doi:10.1101/2024.03.18.585516 · Cited by 1
Bimaï, O., Banerjee, I., Grinberg, I. R., Huang, P., Hultgren, L., Ekström, S., Lundin, D., Sjöberg, B.-M., & Logan, D. T. (2023) · doi:10.1101/2023.06.20.545753 · Cited by 1
PWO proteins are associated with PRC2 since their emergence in vascular plants
Khan, A., Haider, S., Sharaf, A., Kusová, A., Skalák, J., Jourdain, C., Rennie, M., Schrumpfová, P. P., Hejátko, J., Schubert, D., et al. (2025) · doi:10.1101/2025.03.15.643013 · Cited by 1
Jonsson, G., Hofmann, M., Mereiter, S., Hartley‐Tassell, L., Onji, M., Sakic, I., Oliveira, T., Hoffmann, D., Novatchkova, M., Schleiffer, A., et al. (2026) · The FEBS Journal · doi:10.1111/febs.70236 · Cited by 1
Insights from aquaporin structures into drug-resistant sleeping sickness
Matusevicius, M., Corey, R. A., Gragera, M., Yamashita, K., Sprenger, T., Ungogo, M. A., Blaza, J. N., Castro-Hartmann, P., Chirgadze, D. Y., Chaitanya Vedithi, S., et al. (2025) · doi:10.1101/2025.05.15.654314 · Cited by 1
Maturase K forms a plastidial splicing complex with a neofunctionalized branching enzyme
Liang, Y., Gao, Y., Fontana, A., Abt, M., Gicgier, A., Gehring, M., Liu, C., Sharma, M., Zoschke, R., Zeeman, S. C., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-70734-3 · Cited by 1
Structural and mechanistic insights into the constitutive Themis–Grb2 complex in T cell signalling
Clancy, D. M., Sanz-Sanjuan, A., Gilis, E., Tougaard, P., Velghe, I., Van Droogenbroeck, Y., Felix, J., Bloch, Y., Cuadrado, Á. F., Merceron, R., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-73359-8
Lolicato, F., Steringer, J. P., Saleppico, R., Beyer, D., Fernandez-Sobaberas, J., Unger, S., Klein, S., Riegerová, P., Wegehingel, S., Müller, H.-M., et al. (2024) · eLife · doi:10.7554/elife.88579.3
Structural mechanism of FusB-mediated rescue from fusidic acid inhibition of protein synthesis
González-López, A., Ge, X., Larsson, D. S. D., Sanyal, S., & Selmer, M. (2024) · doi:10.1101/2024.08.30.610483
The phage protein paratox is a multifunctional metabolic regulator of Streptococcus
Muna, T. H., Rutbeek, N. R., Horne, J., Lao, Y. W., Krokhin, O. V., & Prehna, G. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkae1200
Graham, C. I., Gierys, A. J., MacMartin, T. L., Penner, T. V., Beck, J. C., Prehna, G., de Kievit, T. R., & Brassinga, A. K. C. (2025) · Microbiology · doi:10.1099/mic.0.001551
Molecular mechanism of complement inhibition by the trypanosome receptor ISG65
Cook, A. D., Carrington, M., & Higgins, M. K. (2024) · doi:10.7554/elife.88960.2
Residues neighboring an SH3-binding motif participate in the interaction in vivo
Jordan, D. F., Dubé, A. K., Dionne, U., Bradley, D., & Landry, C. R. (2025) · GENETICS · doi:10.1093/genetics/iyaf153
TET dioxygenases localize at splicing speckles and promote RNA splicing
Hastert, F. D., Weber, J., Bauer, C., Zhadan, A., Singh, D. N. D., Dix, T. C., Arnold, R., Bessonov, S., Soller, M., Leonhardt, H., et al. (2025) · doi:10.1101/2025.03.07.641893
Ketaren, N. E., Mast, F. D., Fridy, P. C., Olivier, J. P., Sanyal, T., Sali, A., Chait, B. T., Rout, M. P., & Aitchison, J. D. (2024) · doi:10.7554/elife.89423.2
Kumar, P., Saumya, K. U., Bhardwaj, T., & Giri, R. (2025) · Biophysical Chemistry · doi:10.1016/j.bpc.2024.107384
Structural insight into guanylyl cyclase receptor hijacking of the kinase–Hsp90 regulatory mechanism
Caveney, N. A., Tsutsumi, N., & Garcia, K. C. (2023) · doi:10.7554/elife.86784.2
Fitness landscape of substrate-adaptive mutations in evolved APC transporters
Karapanagioti, F., Atlason, Ú. Á., Slotboom, D. J., Poolman, B., & Obermaier, S. (2023) · doi:10.1101/2023.10.12.562049
Structural and dynamic changes in P-Rex1 upon activation by PIP 3 and inhibition by IP 4
Ravala, S. K., Adame-Garcia, S. R., Li, S., Chen, C.-L., Cianfrocco, M. A., Gutkind, J. S., Cash, J. N., & Tesmer, J. J. G. (2023) · doi:10.1101/2023.09.15.557836
Dissecting the Determinants of Domain Insertion Tolerance and Allostery in Proteins
Mathony, J., Aschenbrenner, S., Becker, P., & Niopek, D. (2023) · doi:10.1101/2023.04.11.536407
Lolicato, F., Steringer, J., Saleppico, R., Beyer, D., Fernandez-Sobaberas, J., Unger, S., Klein, S., Riegerová, P., Wegehingel, S., Müller, H., et al. (2023) · doi:10.1101/2023.04.12.536539
Structural analysis of the dynamic ribosome-translocon complex
Lewis, A. J. O., Zhong, F., Keenan, R. J., & Hegde, R. S. (2023) · doi:10.1101/2023.12.22.572959
Targeting PD-1 + T cells with chimeric antigen receptors to reduce the HIV reservoir
Ermellino, L., Banga, R., Georgakis, S., Kadzioch, N. P., Procopio, F., Alcaraz-Serna, A., Alfageme-Abello, O., Porret, R., Cecchin, R., Orfanakis, M., et al. (2026) · Science Advances · doi:10.1126/sciadv.aeb7602
Metadata
- Authors
- Pettersen, E. F., Goddard, T. D., Huang, C. C., Meng, E. C., Couch, G. S., Croll, T. I., Morris, J. H., & Ferrin, T. E.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2020-10-22
- Volume
- 30
- Issue
- 1
- Pages
- 70-82
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W3083406432
- Cited by
- 9,514
- References
- 5
- FWCI
- 328.06
- Type
- journal article
- Language
- en
- Open access
- bronze
- Funders
- National Institute of Allergy and Infectious Diseases
- National Institute of General Medical Sciences (R01‐GM129325)
- Wellcome Trust (209407/Z/17/Z)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.