The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Weak functional constraints on phosphoproteomes
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Citations
Cites
PAML 4: Phylogenetic Analysis by Maximum Likelihood
Yang, Z. (2007) · Molecular Biology and Evolution · doi:10.1093/molbev/msm088 · Cited by 13,879
Mechanisms of specificity in protein phosphorylation
Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451
The regulation of protein function by multisite phosphorylation – a 25 year update
Cohen, P. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01712-6 · Cited by 1,136
Evolution of protein kinase signaling from yeast to man
Manning, G., Plowman, G. D., Hunter, T., & Sudarsanam, S. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02179-5 · Cited by 979
The interplay between structure and function in intrinsically unstructured proteins
Tompa, P. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.072 · Cited by 717
Reproducible isolation of distinct, overlapping segments of the phosphoproteome
Bodenmiller, B., Mueller, L. N., Mueller, M., Domon, B., & Aebersold, R. (2007) · Nature Methods · doi:10.1038/nmeth1005 · Cited by 563
Phosphoproteomics of the Arabidopsis Plasma Membrane and a New Phosphorylation Site Database[W]
Nühse, T. S., Stensballe, A., Jensen, O. N., & Peck, S. C. (2004) · The Plant Cell · doi:10.1105/tpc.104.023150 · Cited by 478
Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation
Gsponer, J., Futschik, M. E., Teichmann, S. A., & Babu, M. M. (2008) · Science · doi:10.1126/science.1163581 · Cited by 466
Gnad, F., Ren, S., Cox, J., Olsen, J. V., Macek, B., Oroshi, M., & Mann, M. (2007) · Genome Biology · doi:10.1186/gb-2007-8-11-r250 · Cited by 454
Mayrose, I. (2004) · Molecular Biology and Evolution · doi:10.1093/molbev/msh194 · Cited by 447
Cited by
Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes
Vlastaridis, P., Kyriakidou, P., Chaliotis, A., Van de Peer, Y., Oliver, S. G., & Amoutzias, G. D. (2017) · GigaScience · doi:10.1093/gigascience/giw015 · Cited by 733
Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation
Swaney, D. L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N. J., & Villén, J. (2013) · Nature Methods · doi:10.1038/nmeth.2519 · Cited by 599
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 503
The functional landscape of the human phosphoproteome
Ochoa, D., Jarnuczak, A. F., Viéitez, C., Gehre, M., Soucheray, M., Mateus, A., Kleefeldt, A. A., Hill, A., Garcia-Alonso, L., Stein, F., et al. (2020) · Nature Biotechnology · doi:10.1038/s41587-019-0344-3 · Cited by 491
Mechanisms and Consequences of Macromolecular Phase Separation
Bergeron-Sandoval, L.-P., Safaee, N., & Michnick, S. W. (2016) · Cell · doi:10.1016/j.cell.2016.05.026 · Cited by 355
Self-citation
Metadata
- Authors
- Landry, C. R., Levy, E. D., & Michnick, S. W.
- Venue
- Trends in Genetics
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 25
- Issue
- 5
- Pages
- 193-197
- ISSN
- 0168-9525 (ISSN-L)
- OpenAlex
- W2078964925
- Cited by
- 272
- References
- 23
- FWCI
- 1.00
- Type
- journal article
- Language
- en
- Open access
- closed
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- Landry, C. R., Levy, E. D., & Michnick, S. W. (2009). Weak functional constraints on phosphoproteomes. Trends in Genetics. https://doi.org/10.1016/j.tig.2009.03.003
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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.