The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins
Open accessAbstract
A significant fraction of every proteome is occupied by biologically active proteins that do not form unique three-dimensional structures. These intrinsically disordered proteins (IDPs) and IDP regions (IDPRs) have essential biological functions and are characterized by extensive structural plasticity. Such structural and functional behavior is encoded in the amino acid sequences of IDPs/IDPRs, which are enriched in disorder-promoting residues and depleted in order-promoting residues. In fact, amino acid residues can be arranged according to their disorder-promoting tendency to form an alphabet of intrinsic disorder that defines the structural complexity and diversity of IDPs/IDPRs. This review is the first in a series of publications dedicated to the roles that different amino acid residues play in defining the phenomenon of protein intrinsic disorder. We start with proline because data suggests that of the 20 common amino acid residues, this one is the most disorder-promoting.
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Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535
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
Blume-Jensen, P., & Hunter, T. (2001) · Nature · doi:10.1038/35077225 · Cited by 3,738
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
Self-citationSerine/threonine phosphatases: mechanism through structure
Shi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.10.006 · Cited by 1,488
Influence of proline residues on protein conformation
MacArthur, M. W., & Thornton, J. M. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90721-h · Cited by 1,189
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
Self-citationYeh, E., Cunningham, M., Arnold, H., Chasse, D., Monteith, T., Ivaldi, G., Hahn, W. C., Stukenberg, P. T., Shenolikar, S., Uchida, T., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1110 · Cited by 791
Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., & Kornfeld, K. (1999) · Genes & Development · doi:10.1101/gad.13.2.163 · Cited by 439
Disorder and Sequence Repeats in Hub Proteins and Their Implications for Network Evolution
Dosztányi, Z., Chen, J., Dunker, A. K., Simon, I., & Tompa, P. (2006) · Journal of Proteome Research · doi:10.1021/pr060171o · Cited by 341
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Oldfield, C. J., & Dunker, A. K. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-164947 · Cited by 1,057
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Wilson, C. J., Choy, W.-Y., & Karttunen, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094591 · Cited by 173
Intrinsically disordered proteins and multicellular organisms
Dunker, A. K., Bondos, S. E., Huang, F., & Oldfield, C. J. (2015) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.09.025 · Cited by 150
Self-citationCasein and casein micelle structures, functions and diversity in 20 species.
Holt, C. (2016) · International Dairy Journal · doi:10.1016/j.idairyj.2016.01.004 · Cited by 95
Urbanek, A., Popovic, M., Morató, A., Estaña, A., Elena-Real, C. A., Mier, P., Fournet, A., Allemand, F., Delbecq, S., Andrade-Navarro, M. A., et al. (2020) · Structure · doi:10.1016/j.str.2020.04.008 · Cited by 66
Intrinsic protein disorder and protein modifications in the processing of biological signals
Phillips, A. H., & Kriwacki, R. W. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.09.003 · Cited by 21
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Metadata
- Authors
- Theillet, F.-X., Kalmar, L., Tompa, P., Han, K.-H., Selenko, P., Dunker, A. K., Daughdrill, G. W., & Uversky, V. N.
- Venue
- Intrinsically Disordered Proteins
- Publisher
- Informa UK Limited
- Published
- 2013-01
- Volume
- 1
- Issue
- 1
- Pages
- e24360
- ISSN
- 2169-0693 (ISSN-L)
- 2169-0707
- OpenAlex
- W1501347866
- Cited by
- 286
- References
- 11
- FWCI
- 5.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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