The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Molecular Principles of the Interactions of Disordered Proteins
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Citations
Cites
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
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
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684
Intrinsic Disorder and Protein Function
Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z. (2002) · Biochemistry · doi:10.1021/bi012159+ · Cited by 1,731
UniRef: comprehensive and non-redundant UniProt reference clusters
Suzek, B. E., Huang, H., McGarvey, P., Mazumder, R., & Wu, C. H. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm098 · Cited by 1,613
Coupling of folding and binding for unstructured proteins
Dyson, H. J., & Wright, P. E. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00289-0 · Cited by 1,327
Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins
Iakoucheva, L. M., Brown, C. J., Lawson, J. D., Obradović, Z., & Dunker, A. K. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00969-5 · Cited by 1,214
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847
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
Self-citationLarge-scale identification of protein–protein interaction of Escherichia coli K-12
Arifuzzaman, M., Maeda, M., Itoh, A., Nishikata, K., Takita, C., Saito, R., Ara, T., Nakahigashi, K., Huang, H.-C., Hirai, A., et al. (2006) · Genome Research · doi:10.1101/gr.4527806 · Cited by 403
Cited by
Wright, P. E., & Dyson, H. J. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.12.003 · Cited by 1,019
The evolutionary origin of orphan genes
Tautz, D., & Domazet-Lošo, T. (2011) · Nature Reviews Genetics · doi:10.1038/nrg3053 · Cited by 764
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
Cryo-EM reveals a phosphorylated R-domain envelops the NBD1 catalytic domain in an ABC transporter
Souza Amado de Carvalho, R., Rasel, M. S. I., Khandelwal, N. K., & Tomasiak, T. M. (2024) · Life Science Alliance · doi:10.26508/lsa.202402779 · Cited by 4
Metadata
- Authors
- Mészáros, B., Tompa, P., Simon, I., & Dosztányi, Z.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2007-09
- Volume
- 372
- Issue
- 2
- Pages
- 549-561
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2084333983
- Cited by
- 278
- References
- 12
- FWCI
- 8.14
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Molecular Principles of the Interactions of Disordered Proteins. https://app.cochat.ai/papers/10.1016/j.jmb.2007.07.004
- The paper
- Mészáros, B., Tompa, P., Simon, I., & Dosztányi, Z. (2007). Molecular Principles of the Interactions of Disordered Proteins. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2007.07.004
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.
