The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
A Raf-induced allosteric transition of KSR stimulates phosphorylation of MEK
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Citations
Cites
Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3
Jura, N., Shan, Y., Cao, X., Shaw, D. E., & Kuriyan, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912101106 · Cited by 338
KSR is a scaffold required for activation of the ERK/MAPK module
Roy, F., Laberge, G., Douziech, M., Ferland-McCollough, D., & Therrien, M. (2002) · Genes & Development · doi:10.1101/gad.962902 · Cited by 217
Quantitative Analysis of Synaptic Phosphorylation and Protein Expression
Trinidad, J. C., Thalhammer, A., Specht, C. G., Lynn, A. J., Baker, P. R., Schoepfer, R., & Burlingame, A. L. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700170-mcp200 · Cited by 194
Self-citationSignaling dynamics of the KSR1 scaffold complex
McKay, M. M., Ritt, D. A., & Morrison, D. K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901590106 · Cited by 163
Cited by
Regulation of RAF protein kinases in ERK signalling
Lavoie, H., & Therrien, M. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3979 · Cited by 702
Direct small-molecule inhibitors of KRAS: from structural insights to mechanism-based design
Ostrem, J. M. L., & Shokat, K. M. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.139 · Cited by 641
Self-citationTumor adaptation and resistance to RAF inhibitors
Lito, P., Rosen, N., & Solit, D. B. (2013) · Nature Medicine · doi:10.1038/nm.3392 · Cited by 585
Overcoming mTOR resistance mutations with a new-generation mTOR inhibitor
Rodrik-Outmezguine, V. S., Okaniwa, M., Yao, Z., Novotny, C. J., McWhirter, C., Banaji, A., Won, H., Wong, W., Berger, M., de Stanchina, E., et al. (2016) · Nature · doi:10.1038/nature17963 · Cited by 479
Self-citationGTP-Dependent K-Ras Dimerization
Muratcioglu, S., Chavan, T. S., Freed, B. C., Jang, H., Khavrutskii, L., Freed, R. N., Dyba, M. A., Stefanisko, K., Tarasov, S. G., Gursoy, A., et al. (2015) · Structure · doi:10.1016/j.str.2015.04.019 · Cited by 202
RAS: Striking at the Core of the Oncogenic Circuitry
Gimple, R. C., & Wang, X. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00965 · Cited by 174
Structural basis for the action of the drug trametinib at KSR-bound MEK
Khan, Z. M., Real, A. M., Marsiglia, W. M., Chow, A., Duffy, M. E., Yerabolu, J. R., Scopton, A. P., & Dar, A. C. (2020) · Nature · doi:10.1038/s41586-020-2760-4 · Cited by 178
Self-citationStructure of ERK2 bound to PEA-15 reveals a mechanism for rapid release of activated MAPK
Mace, P. D., Wallez, Y., Egger, M. F., Dobaczewska, M. K., Robinson, H., Pasquale, E. B., & Riedl, S. J. (2013) · Nature Communications · doi:10.1038/ncomms2687 · Cited by 97
BRAF inhibitors suppress apoptosis through off-target inhibition of JNK signaling
Vin, H., Ojeda, S. S., Ching, G., Leung, M. L., Chitsazzadeh, V., Dwyer, D. W., Adelmann, C. H., Restrepo, M., Richards, K. N., Stewart, L. R., et al. (2013) · eLife · doi:10.7554/elife.00969 · Cited by 84
“Pathway drug cocktail”: targeting Ras signaling based on structural pathways
Nussinov, R., Tsai, C.-J., & Mattos, C. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.07.009 · Cited by 62
Exploiting Conformational Ensembles in Modeling Protein–Protein Interactions on the Proteome Scale
Kuzu, G., Gursoy, A., Nussinov, R., & Keskin, O. (2013) · Journal of Proteome Research · doi:10.1021/pr400006k · Cited by 47
Koveal, D., Schuh-Nuhfer, N., Ritt, D., Page, R., Morrison, D. K., & Peti, W. (2012) · Science Signaling · doi:10.1126/scisignal.2003289 · Cited by 36
KSR induces RAS‐independent MAPK pathway activation and modulates the efficacy of KRAS inhibitors
Paniagua, G., Jacob, H. K. C., Brehey, O., García‐Alonso, S., Lechuga, C. G., Pons, T., Musteanu, M., Guerra, C., Drosten, M., & Barbacid, M. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13213 · Cited by 34
Phosphoregulation of the novel hemi-arrestin MAPK scaffold Sms1 prevents untimely mating
Sieber, B., Merlini, L., Li, W., Besomi, M., Michon, L., Gordon-Lennox, S., & Martin, S. G. (2026) · Nature Communications · doi:10.1038/s41467-026-70631-9 · Cited by 5
Metadata
- Authors
- Brennan, D. F., Dar, A. C., Hertz, N. T., Chao, W. C. H., Burlingame, A. L., Shokat, K. M., & Barford, D.
- Venue
- Nature
- Published
- 2011-03-27
- Volume
- 472
- Issue
- 7343
- Pages
- 366-369
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2056924558
- Cited by
- 254
- References
- 4
- FWCI
- 10.11
- 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.
