The DOI matches its Crossref record; 118 of the 118 references it cites were found in a registry or an index.
From Sequence and Forces to Structure, Function, and Evolution of Intrinsically Disordered Proteins
Open accessAbstract
Intrinsically disordered proteins (IDPs), which lack persistent structure, are a challenge to structural biology due to the inapplicability of standard methods for characterization of folded proteins as well as their deviation from the dominant structure/function paradigm. Their widespread presence and involvement in biological function, however, has spurred the growing acceptance of the importance of IDPs and the development of new tools for studying their structure, dynamics and function. The interplay of folded and disordered domains or regions for function and the existence of a continuum of protein states with respect to conformational energetics, motional timescales and compactness is shaping a unified understanding of structure-dynamics-disorder/function relationships. On the 20th anniversary of this journal, Structure, we provide a historical perspective on the investigation of IDPs and summarize the sequence features and physical forces that underlie their unique structural, functional and evolutionary properties.
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Cites
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Cited by
Nott, T. J., Petsalaki, E., Farber, P., Jervis, D., Fussner, E., Plochowietz, A., Craggs, T. D., Bazett-Jones, D. P., Pawson, T., Forman-Kay, J. D., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.013 · Cited by 1,803
Self-citationThe ensemble nature of allostery
Motlagh, H. N., Wrabl, J. O., Li, J., & Hilser, V. J. (2014) · Nature · doi:10.1038/nature13001 · Cited by 1,247
Critical assessment of protein intrinsic disorder prediction
Necci, M., Piovesan, D., Predictors, C., Hoque, M. T., Walsh, I., Iqbal, S., Vendruscolo, M., Sormanni, P., Wang, C., Raimondi, D., et al. (2021) · Nature Methods · doi:10.1038/s41592-021-01117-3 · Cited by 343
Disorder and function: a review of the dehydrin protein family
Graether, S. P., & Boddington, K. F. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00576 · Cited by 326
Metapredict: a fast, accurate, and easy-to-use predictor of consensus disorder and structure
Emenecker, R. J., Griffith, D., & Holehouse, A. S. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.08.039 · Cited by 259
Metadata
- Authors
- Forman-Kay, J. D., & Mittag, T.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 21
- Issue
- 9
- Pages
- 1492-1499
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2052962917
- Cited by
- 261
- References
- 118
- FWCI
- 7.53
- Type
- journal article
- Language
- en
- Open access
- bronze
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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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