The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Relating sequence encoded information to form and function of intrinsically disordered proteins
Open accessAbstract
Intrinsically disordered proteins (IDPs) showcase the importance of conformational plasticity and heterogeneity in protein function. We summarize recent advances that connect information encoded in IDP sequences to their conformational properties and functions. We focus on insights obtained through a combination of atomistic simulations and biophysical measurements that are synthesized into a coherent framework using polymer physics theories.
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Cites
T RANSITION P ATH S AMPLING : Throwing Ropes Over Rough Mountain Passes, in the Dark
Bolhuis, P. G., Chandler, D., Dellago, C., & Geissler, P. L. (2002) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.53.082301.113146 · Cited by 1,972
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
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 · cited 2×
“IDPs are implicated in important cellular processes that include cell division [8,9 ], cell signaling [3 ,10], intracellular transport [11,12 ], bacterial translocation [13 ], cell mechanics [14 ,15], protein degradation [16,17], posttranscriptional regulation [18], and cell cycle control [19].”
BackgroundTemperature-dependent solvation modulates the dimensions of disordered proteins
Wuttke, R., Hofmann, H., Nettels, D., Borgia, M. B., Mittal, J., Best, R. B., & Schuler, B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313006111 · Cited by 192
Describing sequence–ensemble relationships for intrinsically disordered proteins
Mao, A. H., Lyle, N., & Pappu, R. V. (2013) · Biochemical Journal · doi:10.1042/bj20121346 · Cited by 135
Self-citationA quantitative measure for protein conformational heterogeneity
Lyle, N., Das, R. K., & Pappu, R. V. (2013) · The Journal of Chemical Physics · doi:10.1063/1.4812791 · Cited by 85 · cited 2×
“In addition, their ensembles are expected to display significant conformational heterogeneity [39] as characterized by spontaneous conformational fluctuations whose amplitudes are likely to be considerably larger than those of globular proteins.”
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Cited by
Alberti, S., Gladfelter, A., & Mittag, T. (2019) · Cell · doi:10.1016/j.cell.2018.12.035 · Cited by 2,856
Boija, A., Klein, I. A., Sabari, B. R., Dall’Agnese, A., Coffey, E. L., Zamudio, A. V., Li, C. H., Shrinivas, K., Manteiga, J. C., Hannett, N. M., et al. (2018) · Cell · doi:10.1016/j.cell.2018.10.042 · Cited by 1,815
InterPro in 2019: improving coverage, classification and access to protein sequence annotations
Mitchell, A. L., Attwood, T. K., Babbitt, P. C., Blum, M., Bork, P., Bridge, A., Brown, S. D., Chang, H.-Y., El-Gebali, S., Fraser, M. I., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gky1100 · Cited by 1,426
Harmon, T. S., Holehouse, A. S., Rosen, M. K., & Pappu, R. V. (2017) · eLife · doi:10.7554/elife.30294 · Cited by 713
Self-citationAlphaFold and Implications for Intrinsically Disordered Proteins
Ruff, K. M., & Pappu, R. V. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167208 · Cited by 635
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Metadata
- Authors
- Das, R. K., Ruff, K. M., & Pappu, R. V.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2015-06
- Volume
- 32
- Pages
- 102-112
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W1972376083
- Cited by
- 413
- References
- 6
- FWCI
- 2.48
- Type
- journal article
- Language
- en
- Open access
- green
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