The DOI matches its Crossref record; 242 of the 242 references it cites were found in a registry or an index.
Intrinsically disordered protein regions and phase separation: sequence determinants of assembly or lack thereof
Abstract
Intrinsically disordered protein regions (IDRs) — regions that do not fold into a fixed three-dimensional structure but instead exist in a heterogeneous ensemble of conformations — have recently entered mainstream cell biology in the context of liquid–liquid phase separation (LLPS). IDRs are frequently found to be enriched in phase-separated compartments. Due to this observation, the presence of an IDR in a protein is frequently assumed to be diagnostic of its ability to phase separate. In this review, we clarify the role of IDRs in biological assembly and explore the physical principles through which amino acids can confer the attractive molecular interactions that underlie phase separation. While some disordered regions will robustly drive phase separation, many others will not. We emphasize that rather than ‘disorder' driving phase separation, multivalency drives phase separation. As such, whether or not a disordered region is capable of driving phase separation will depend on the physical chemistry encoded within its amino acid sequence. Consequently, an in-depth understanding of that physical chemistry is a prerequisite to make informed inferences on how and why an IDR may be involved in phase separation or, more generally, in protein-mediated intermolecular interactions.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,843
Biomolecular condensates: organizers of cellular biochemistry
Banani, S. F., Lee, H. O., Hyman, A. A., & Rosen, M. K. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.7 · Cited by 6,100
Liquid phase condensation in cell physiology and disease
Shin, Y., & Brangwynne, C. P. (2017) · Science · doi:10.1126/science.aaf4382 · Cited by 4,152
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
Stereochemistry of polypeptide chain configurations
Ramachandran, G. N., Ramakrishnan, C., & Sasisekharan, V. (1963) · Journal of Molecular Biology · doi:10.1016/s0022-2836(63)80023-6 · Cited by 3,554
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Patel, A., Lee, H. O., Jawerth, L., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 3,282
Germline P Granules Are Liquid Droplets That Localize by Controlled Dissolution/Condensation
Brangwynne, C. P., Eckmann, C. R., Courson, D. S., Rybarska, A., Hoege, C., Gharakhani, J., Jülicher, F., & Hyman, A. A. (2009) · Science · doi:10.1126/science.1172046 · Cited by 3,202
Liquid-Liquid Phase Separation in Biology
Hyman, A. A., Weber, C. A., & Jülicher, F. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013325 · Cited by 3,155
Prediction of the Secondary Structure of Proteins from their Amino Acid Sequence
Chou, P. Y., & Fasman, G. D. (1979) · Advances in Enzymology - and Related Areas of Molecular Biology · doi:10.1002/9780470122921.ch2 · Cited by 2,915
Molliex, A., Temirov, J., Lee, J., Coughlin, M., Kanagaraj, A. P., Kim, H. J., Mittag, T., & Taylor, J. P. (2015) · Cell · doi:10.1016/j.cell.2015.09.015 · Cited by 2,893
Cited by
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
Alderson, T. R., Pritišanac, I., Kolarić, Đ., Moses, A. M., & Forman-Kay, J. D. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2304302120 · Cited by 240
Design principles for creating synthetic underwater adhesives
Narayanan, A., Dhinojwala, A., & Joy, A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00316j · Cited by 193
RNA m6A regulates transcription via DNA demethylation and chromatin accessibility
Deng, S., Zhang, J., Su, J., Zuo, Z., Zeng, L., Liu, K., Zheng, Y., Huang, X., Bai, R., Zhuang, L., et al. (2022) · Nature Genetics · doi:10.1038/s41588-022-01173-1 · Cited by 187
Nuclear Protein Condensates and Their Properties in Regulation of Gene Expression
Li, W., & Jiang, H. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167151 · Cited by 64
(2025) · doi:10.1186/s13059-025-03497-7 · Cited by 45
Metadata
- Authors
- Martin, E. W., & Holehouse, A. S.
- Venue
- Emerging Topics in Life Sciences
- Publisher
- Portland Press Ltd.
- Published
- 2020-10-20
- Volume
- 4
- Issue
- 3
- Pages
- 307-329
- ISSN
- 2397-8554 (ISSN-L)
- 2397-8562
- OpenAlex
- W3093315678
- Cited by
- 281
- References
- 242
- FWCI
- 8.85
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Intrinsically disordered protein regions and phase separation: sequence determinants of assembly or lack thereof. https://app.cochat.ai/papers/10.1042/etls20190164
- The paper
- Martin, E. W., & Holehouse, A. S. (2020). Intrinsically disordered protein regions and phase separation: sequence determinants of assembly or lack thereof. Emerging Topics in Life Sciences. https://doi.org/10.1042/etls20190164
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.
