The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
DALI and the persistence of protein shape
Open accessAbstract
DALI is a popular resource for comparing protein structures. The software is based on distance‐matrix alignment. The associated web server provides tools to navigate, integrate and organize some data pushed out by genomics and structural genomics. The server has been running continuously for the past 25 years. Structural biologists routinely use DALI to compare a new structure against previously known protein structures. If significant similarities are discovered, it may indicate a distant homology, that is, that the structures are of shared origin. This may be significant in determining the molecular mechanisms, as these may remain very similar from a distant predecessor to the present day, for example, from the last common ancestor of humans and bacteria. Meta‐analysis of independent reference‐based evaluations of alignment accuracy and fold discrimination shows DALI at top rank in six out of 12 studies. The web server and standalone software are available from http://ekhidna2.biocenter.helsinki.fi/dali.
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
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
The Pfam protein families database in 2019
El-Gebali, S., Mistry, J., Bateman, A., Eddy, S. R., Luciani, A., Potter, S. C., Qureshi, M., Richardson, L. J., Salazar, G. A., Smart, A., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gky995 · Cited by 4,602
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984 · cited 2×
“20 The heuristics reduce protein structure to ungapped secondary structure elements to simplify the combinatorial search.”
BackgroundMethodSelf-citation
Cited by
Structure, lipid scrambling activity and role in autophagosome formation of ATG9A
Maeda, S., Yamamoto, H., Kinch, L. N., Garza, C. M., Takahashi, S., Otomo, C., Grishin, N. V., Forli, S., Mizushima, N., & Otomo, T. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-00520-2 · Cited by 305
Kunisch, F., Campobasso, C., Wagemans, J., Yildirim, S., Chan, B. K., Schaudinn, C., Lavigne, R., Turner, P. E., Raschke, M. J., Trampuz, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52595-w · Cited by 101
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
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
Structural basis of bacteriophage T5 infection trigger and E. coli cell wall perforation
Linares, R., Arnaud, C.-A., Effantin, G., Darnault, C., Epalle, N. H., Boeri Erba, E., Schoehn, G., & Breyton, C. (2023) · Science Advances · doi:10.1126/sciadv.ade9674 · Cited by 75
Structural basis for placental malaria mediated by Plasmodium falciparum VAR2CSA.
Ma, R., Lian, T., Huang, R., Renn, J. P., Petersen, J. D., Zimmerberg, J., Duffy, P. E., & Tolia, N. H. (2021) · Nature Microbiology · doi:10.1038/s41564-020-00858-9 · Cited by 72
Barbarin-Bocahu, I., & Graille, M. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798322002157 · Cited by 52
Nguyen, D. T., Zhu, L., Gray, D. L., Woods, T. J., Padhi, C., Flatt, K. M., Mitchell, D. A., & van der Donk, W. A. (2024) · ACS Central Science · doi:10.1021/acscentsci.4c00088 · Cited by 51
Deciphering Bacteriophage T5 Host Recognition Mechanism and Infection Trigger
Degroux, S., Effantin, G., Linares, R., Schoehn, G., & Breyton, C. (2023) · Journal of Virology · doi:10.1128/jvi.01584-22 · Cited by 49
Merizo: a rapid and accurate protein domain segmentation method using invariant point attention
Lau, A. M., Kandathil, S. M., & Jones, D. T. (2023) · Nature Communications · doi:10.1038/s41467-023-43934-4 · Cited by 48
Structural atlas of a human gut crassvirus
Bayfield, O. W., Shkoporov, A. N., Yutin, N., Khokhlova, E. V., Smith, J. L. R., Hawkins, D. E. D. P., Koonin, E. V., Hill, C., & Antson, A. A. (2023) · Nature · doi:10.1038/s41586-023-06019-2 · Cited by 48
Structural basis for sterol sensing by Scap and Insig
Yan, R., Cao, P., Song, W., Li, Y., Wang, T., Qian, H., Yan, C., & Yan, N. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109299 · Cited by 43
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
The Diverse Evolutionary Histories of Domesticated Metaviral Capsid Genes in Mammals
Henriques, W. S., Young, J. M., Nemudryi, A., Nemudraia, A., Wiedenheft, B., & Malik, H. S. (2024) · Molecular Biology and Evolution · doi:10.1093/molbev/msae061 · Cited by 31
CRISPR antiphage defence mediated by the cyclic nucleotide-binding membrane protein Csx23
Grüschow, S., McQuarrie, S., Ackermann, K., McMahon, S., Bode, B. E., Gloster, T. M., & White, M. F. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae167 · Cited by 25
Atomic structures of a bacteriocin targeting Gram-positive bacteria
Cai, X., He, Y., Yu, I., Imani, A., Scholl, D., Miller, J. F., & Zhou, Z. H. (2024) · Nature Communications · doi:10.1038/s41467-024-51038-w · Cited by 24
Structure and mechanism of the type I-G CRISPR effector
Shangguan, Q., Graham, S., Sundaramoorthy, R., & White, M. F. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac925 · Cited by 24
DNA-binding mechanism and evolution of replication protein A
(2023) · doi:10.1038/s41467-023-38048-w · Cited by 22
Missense Variants Reveal Functional Insights Into the Human ARID Family of Gene Regulators
Deák, G., & Cook, A. G. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167529 · Cited by 20
They all rock: A systematic comparison of conformational movements in LeuT-fold transporters
Licht, J. A., Berry, S. P., Gutierrez, M. A., & Gaudet, R. (2024) · Structure · doi:10.1016/j.str.2024.06.015 · 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
Liu, J., Yuan, R., Shao, W., Wang, J., Silman, I., & Sussman, J. L. (2023) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26496 · Cited by 18
Kang, H., Han, A.-R., Zhang, A., Jeong, H., Koh, W., Lee, J. M., Lee, H., Jo, H. Y., Maria-Solano, M. A., Bhalla, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49297-8 · Cited by 18
Wichers, J. S., Mesén-Ramírez, P., Fuchs, G., Yu-Strzelczyk, J., Stäcker, J., von Thien, H., Alder, A., Henshall, I., Liffner, B., Nagel, G., et al. (2022) · mBio · doi:10.1128/mbio.00623-22 · Cited by 16
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
Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase
Tanaka, N., Saito, R., Kobayashi, K., Nakai, H., Kamo, S., Kuramochi, K., Taguchi, H., Nakajima, M., & Masaike, T. (2024) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-024-13013-9 · Cited by 13
Fernández, I., Dynesen, L. T., Coquin, Y., Pederzoli, R., Brun, D., Haouz, A., Gessain, A., Rey, F. A., Buseyne, F., & Backovic, M. (2023) · Nature Communications · doi:10.1038/s41467-023-36923-0 · Cited by 11
Sun, W.-S., Lassinantti, L., Järvå, M., Schmitt, A., ter Beek, J., & Berntsson, R. P.-A. (2023) · eLife · doi:10.7554/elife.84427.3 · Cited by 10
Deep-Time Structural Evolution of Retroviral and Filoviral Surface Envelope Proteins
Hötzel, I. (2022) · Journal of Virology · doi:10.1128/jvi.00063-22 · Cited by 9
Integrase-associated niche differentiation of endogenous large DNA viruses in crustaceans
Kawato, S., Nozaki, R., Kondo, H., & Hirono, I. (2024) · Microbiology Spectrum · doi:10.1128/spectrum.00559-23 · Cited by 9
A phage protein screen identifies triggers of the bacterial innate immune system
Nagy, T. A., Gersabeck, G. W., Conte, A. N., & Whiteley, A. T. (2026) · Nature Microbiology · doi:10.1038/s41564-025-02239-6 · Cited by 8
DNA polymerase swapping in Caudoviricetes bacteriophages
Yutin, N., Tolstoy, I., Mutz, P., Wolf, Y. I., Krupovic, M., & Koonin, E. V. (2024) · Virology Journal · doi:10.1186/s12985-024-02482-z · Cited by 8
Dahiya, D., Péter-Szabó, Z., Senanayake, M., Pingali, S. V., Leite, W. C., Byrnes, J., Buchko, G. W., Sivan, P., Vilaplana, F., Master, E. R., et al. (2025) · Biotechnology for Biofuels and Bioproducts · doi:10.1186/s13068-025-02618-5 · Cited by 8
Hötzel, I. (2022) · Journal of Virology · doi:10.1128/jvi.01348-21 · Cited by 5
Ishii, M., Ludzia, P., Marcianò, G., Allen, W., Nerusheva, O. O., & Akiyoshi, B. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e22-07-0269-t · Cited by 5
Minami, A., Nishi, K., Yamada, R., Jinnai, G., Shima, H., Oishi, S., Akagawa, H., Aono, T., Hidaka, M., Masaki, H., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108554 · Cited by 4
Kakoulidis, P., Vlachos, I. S., Thanos, D., Blatch, G. L., Emiris, I. Z., & Anastasiadou, E. (2023) · Communications Biology · doi:10.1038/s42003-023-05076-7 · Cited by 4
An interpretable alphabet for local protein structure search based on amino acid neighborhoods
Zerefa, S., Cool, J., Singh, P., & Petti, S. (2025) · Bioinformatics · doi:10.1093/bioinformatics/btaf458 · 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
Sun, W.-S., Lassinantti, L., Järvå, M., Schmitt, A., Beek, J. T., & Berntsson, R. P.-A. (2022) · doi:10.1101/2022.10.21.513195 · Cited by 1
Molecular dissection of the chromosome partitioning protein RocS and regulation by phosphorylation
Demuysere, M., Ducret, A., & Grangeasse, C. (2024) · Journal of Bacteriology · doi:10.1128/jb.00291-24 · Cited by 1
Synergistic role of CSPBP and SGS1 in sporozoite entry into Aedes aegypti salivary glands
Morvay, A., Araújo, H. R. C., Capurro, M. L., & Burini, B. C. (2026) · Scientific Reports · doi:10.1038/s41598-026-46444-7
Metadata
- Authors
- Holm, L.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2019-11-05
- Volume
- 29
- Issue
- 1
- Pages
- 128-140
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2980170804
- Cited by
- 692
- References
- 4
- FWCI
- 27.57
- Type
- journal article
- Language
- en
- Open access
- green
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.