The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
A Million Peptide Motifs for the Molecular Biologist
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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
From molecular to modular cell biology.
Hartwell, L. H., Hopfield, J. J., Leibler, S., & Murray, A. W. (1999) · Nature · doi:10.1038/35011540 · Cited by 3,632
Romero, P. R., Zaidi, S., Fang, Y. Y., Uversky, V. N., Radivojac, P., Oldfield, C. J., Cortese, M. S., Sickmeier, M., LeGall, T., Obradovic, Z., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507916103 · Cited by 480
Tissue-specific alternative splicing remodels protein-protein interaction networks
Ellis, J. D., Barrios-Rodiles, M., Çolak, R., Irimia, M., Kim, T., Calarco, J. A., Wang, X., Pan, Q., O'Hanlon, D., Kim, P. M., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.037 · Cited by 431
Buljan, M., Chalancon, G., Eustermann, S., Wagner, G. P., Fuxreiter, M., Bateman, A., & Babu, M. M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.039 · Cited by 396
Self-citationLinear motifs: Evolutionary interaction switches
Neduva, V., & Russell, R. B. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.04.005 · Cited by 352
Phosphorylation in protein-protein binding: effect on stability and function
Nishi, H., Hashimoto, K., & Panchenko, A. R. (2011) · Structure · doi:10.1016/j.str.2011.09.021 · Cited by 322
Evolution of phosphoregulation: comparison of phosphorylation patterns across yeast species
Beltrao, P., Trinidad, J. C., Fiedler, D., Roguev, A., Lim, W. A., Shokat, K. M., Burlingame, A. L., & Krogan, N. J. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000134 · Cited by 188
Cited by
A reference map of the human binary protein interactome
Luck, K., Kim, D.-K., Lambourne, L., Spirohn, K., Begg, B. E., Bian, W., Brignall, R., Cafarelli, T., Campos-Laborie, F. J., Charloteaux, B., et al. (2020) · Nature · doi:10.1038/s41586-020-2188-x · Cited by 1,197
The molecular basis for cellular function of intrinsically disordered protein regions
Holehouse, A. S., & Kragelund, B. B. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00673-0 · Cited by 696
Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications
Bah, A., & Forman-Kay, J. D. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.695056 · Cited by 566
Bioinks and bioprinting technologies to make heterogeneous and biomimetic tissue constructs
Ashammakhi, N., Ahadian, S., Xu, C., Montazerian, H., Ko, H., Nasiri, R., Barros, N., & Khademhosseini, A. (2019) · Materials Today Bio · doi:10.1016/j.mtbio.2019.100008 · Cited by 549
Dyson, H. J., & Wright, P. E. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.692020 · Cited by 317
Metadata
- Authors
- Tompa, P., Davey, N. E., Gibson, T. J., & Babu, M. M.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2014-07
- Volume
- 55
- Issue
- 2
- Pages
- 161-169
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1992983658
- Cited by
- 525
- References
- 8
- FWCI
- 13.63
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: A Million Peptide Motifs for the Molecular Biologist. https://app.cochat.ai/papers/10.1016/j.molcel.2014.05.032
- The paper
- Tompa, P., Davey, N. E., Gibson, T. J., & Babu, M. M. (2014). A Million Peptide Motifs for the Molecular Biologist. Molecular Cell. https://doi.org/10.1016/j.molcel.2014.05.032
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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.