The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 Å resolution
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Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Cited by
GTPase-activating proteins: Helping hands to complement an active site
Scheffzek, K., Ahmadian, M. R., & Wittinghofer, A. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01224-9 · Cited by 410
Scalable emulation of protein equilibrium ensembles with generative deep learning
Lewis, S., Hempel, T., Jiménez-Luna, J., Gastegger, M., Xie, Y., Foong, A. Y. K., Satorras, V. G., Abdin, O., Veeling, B. S., Zaporozhets, I., et al. (2025) · Science · doi:10.1126/science.adv9817 · Cited by 390
SPEACH_AF: Sampling protein ensembles and conformational heterogeneity with Alphafold2
Stein, R. A., & Mchaourab, H. S. (2022) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1010483 · Cited by 258
“At the two extremes, apo AK adopts an open conformation (PDB: 4ake) [8] whereas the inhibitor bound structure adopts a closed conformation (PDB: 1ake) [9] (Fig 2A) that differ by the two ligand binding domains/lids leading to an RMSD of 7.2 Å or TM score of 0.68 between the two crystal structures.”
BackgroundInfluentialLi, W., Wolynes, P. G., & Takada, S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018983108 · Cited by 159
Dougherty, G. W., Mizuno, K., Nöthe-Menchen, T., Ikawa, Y., Boldt, K., Ta-Shma, A., Aprea, I., Minegishi, K., Pang, Y.-P., Pennekamp, P., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19113-0 · Cited by 88
Greives, N., & Zhou, H.-X. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1407545111 · Cited by 82
Francis, B. R. (2013) · Journal of Molecular Evolution · doi:10.1007/s00239-013-9567-y · Cited by 34
Toward the Prediction of Binding Events in Very Flexible, Allosteric, Multidomain Proteins
Basciu, A., Athar, M., Kurt, H., Neville, C., Malloci, G., Muredda, F. C., Bosin, A., Ruggerone, P., Bonvin, A. M. J. J., & Vargiu, A. V. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01810 · Cited by 12
Scalable emulation of protein equilibrium ensembles with generative deep learning
Lewis, S., Hempel, T., Jiménez Luna, J., Gastegger, M., Xie, Y., Foong, A. Y. K., García Satorras, V., Abdin, O., Veeling, B. S., Zaporozhets, I., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.05.626885 · Cited by 349
Metadata
- Authors
- Müller, C. W., & Schulz, G. E.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1992-03
- Volume
- 224
- Issue
- 1
- Pages
- 159-177
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2097294533
- Cited by
- 523
- References
- 1
- FWCI
- 21.18
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
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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.
