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Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding
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Cited by
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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.”
BackgroundInfluentialPanjkovich, A., & Svergun, D. I. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp04540a · Cited by 204
Sequence‐similar, structure‐dissimilar protein pairs in the PDB
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Folding funnels and conformational transitions via hinge-bending motions
Kumar, S., Ma, B., Tsai, C.-J., Wolfson, H., & Nussinov, R. (1999) · Cell Biochemistry and Biophysics · doi:10.1007/bf02738169 · Cited by 94
Accurate Conformation Sampling via Protein Structural Diffusion
Fan, J., Li, Z., Alcaide, E., Ke, G., Huang, H., & E, W. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c00928 · Cited by 17
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
Wang, B., Wang, C., Chen, J., Liu, D., Sun, C., Zhang, J., Zhang, K., & Li, H. (2026) · Nature Machine Intelligence · doi:10.1038/s42256-026-01198-9 · Cited by 5
eRMSF: A Python Package for Ensemble-Based RMSF Analysis of Biomolecular Systems
Arantes, P. R., Ligabue-Braun, R., & Pedebos, C. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c02413 · Cited by 5
Metadata
- Authors
- Müller, C., Schlauderer, G., Reinstein, J., & Schulz, G.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 1996-02
- Volume
- 4
- Issue
- 2
- Pages
- 147-156
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W1989161865
- Cited by
- 448
- References
- 0
- FWCI
- 2.35
- Type
- journal article
- Language
- en
- Open access
- bronze
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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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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.
