The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch
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Citations
Cites
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
Variable Control of Ets-1 DNA Binding by Multiple Phosphates in an Unstructured Region
Pufall, M. A., Lee, G. M., Nelson, M. L., Kang, H.-S., Velyvis, A., Kay, L. E., McIntosh, L. P., & Graves, B. J. (2005) · Science · doi:10.1126/science.1111915 · Cited by 246
Self-citation
Cited by
New frontiers in translational control of the cancer genome
Truitt, M. L., & Ruggero, D. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.27 · Cited by 378
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
Alderson, T. R., Pritišanac, I., Kolarić, Đ., Moses, A. M., & Forman-Kay, J. D. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2304302120 · Cited by 240
Self-citationInteractions by disorder – A matter of context
Bugge, K., Brakti, I., Fernandes, C. B., Dreier, J. E., Lundsgaard, J. E., Olsen, J. G., Skriver, K., & Kragelund, B. B. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00110 · Cited by 155
“4EBP2 folds upon phosphorylation of specific sites, and the more folded 4EBP2 becomes, the lower its affinity for eIF4E (Bah et al., 2015).”
BackgroundLiquid–liquid phase separation underpins the formation of replication factories in rotaviruses
Geiger, F., Acker, J., Papa, G., Wang, X., Arter, W. E., Saar, K. L., Erkamp, N. A., Qi, R., Bravo, J. P., Strauss, S., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021107711 · Cited by 130
Finding Our Way in the Dark Proteome
Bhowmick, A., Brookes, D. H., Yost, S. R., Dyson, H. J., Forman-Kay, J. D., Gunter, D., Head-Gordon, M., Hura, G. L., Pande, V. S., Wemmer, D. E., et al. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b06543 · Cited by 128
Self-citationIntrinsically disordered proteins and biomolecular condensates as drug targets
Biesaga, M., Frigolé-Vivas, M., & Salvatella, X. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.02.009 · Cited by 115
Intrinsically disordered proteins and membranes: a marriage of convenience for cell signalling?
Cornish, J., Chamberlain, S. G., Owen, D., & Mott, H. R. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200467 · Cited by 69
Barbarin-Bocahu, I., & Graille, M. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798322002157 · Cited by 52
Warnet, X. L., Bakke Krog, H., Sevillano‐Quispe, O. G., Poulsen, H., & Kjaergaard, M. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.14842 · Cited by 50
ERK2 MAP kinase regulates SUFU binding by multisite phosphorylation of GLI1
Bardwell, A. J., Wu, B., Sarin, K. Y., Waterman, M. L., Atwood, S. X., & Bardwell, L. (2022) · Life Science Alliance · doi:10.26508/lsa.202101353 · Cited by 20
Waszkiewicz, R., Michaś, A., Białobrzewski, M. K., Klepka, B. P., Cieplak-Rotowska, M. K., Staszałek, Z., Cichocki, B., Lisicki, M., Szymczak, P., & Niedzwiecka, A. (2024) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.4c00312 · Cited by 16
Intrinsic Disorder of the Neuronal SNARE Protein SNAP25a in its Pre-fusion Conformation
Stief, T., Gremer, L., Pribicevic, S., Espinueva, D. F., Vormann, K., Biehl, R., Jahn, R., Pérez-Lara, Á., & Lakomek, N.-A. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168069 · Cited by 6
Metadata
- Authors
- Bah, A., Vernon, R. M., Siddiqui, Z., Krzeminski, M., Muhandiram, R., Zhao, C., Sonenberg, N., Kay, L. E., & Forman-Kay, J. D.
- Venue
- Nature
- Published
- 2014-12-22
- Volume
- 519
- Issue
- 7541
- Pages
- 106-109
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2042745266
- Cited by
- 566
- References
- 2
- FWCI
- 18.13
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
