The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Intrinsically disordered proteins as crucial constituents of cellular aqueous two phase systems and coacervates
Open accessAbstract
Here, we hypothesize that intrinsically disordered proteins (IDPs) serve as important drivers of the intracellular liquid–liquid phase separations that generate various membrane‐less organelles. This hypothesis is supported by the overwhelming abundance of IDPs in these organelles. Assembly and disassembly of these organelles are controlled by changes in the concentrations of IDPs, their posttranslational modifications, binding of specific partners, and changes in the pH and/or temperature of the solution. Each resulting phase provides a distinct solvent environment for other solutes leading to their unequal distribution within phases. The specificity and efficiency of such partitioning is determined by the nature of the IDP(s) and defines “targeted” enrichment of specific molecules in the resulting membrane‐less organelles that determines their specific activities.
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
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
Macromolecular crowding: obvious but underappreciated
Ellis, R. J. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01938-7 · Cited by 2,309
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
Zimmerman, S. B., & Trach, S. O. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90499-v · Cited by 1,337
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
Implications of macromolecular crowding for protein assembly
Minton, A. P. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00045-7 · Cited by 649
Influence of excluded volume upon macromolecular structure and associations in ‘crowded” media
Minton, A. P. (1997) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(97)80159-0 · Cited by 212
Cited by
Elbaum-Garfinkle, S., Kim, Y., Szczepaniak, K., Chen, C. C.-H., Eckmann, C. R., Myong, S., & Brangwynne, C. P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504822112 · Cited by 1,278
Uversky, V. N. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.10.015 · Cited by 707
Self-citationAumiller, W. M., Pir Cakmak, F., Davis, B. W., & Keating, C. D. (2016) · Langmuir · doi:10.1021/acs.langmuir.6b02499 · Cited by 325
Active coacervate droplets as a model for membraneless organelles and protocells
Donau, C., Späth, F., Sosson, M., Kriebisch, B. A. K., Schnitter, F., Tena-Solsona, M., Kang, H.-S., Salibi, E., Sattler, M., Mutschler, H., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18815-9 · Cited by 309
Disentangling the complexity of low complexity proteins
Mier, P., Paladin, L., Tamana, S., Petrosian, S., Hajdu-Soltész, B., Urbanek, A., Gruca, A., Plewczynski, D., Grynberg, M., Bernadó, P., et al. (2020) · Briefings in Bioinformatics · doi:10.1093/bib/bbz007 · Cited by 104
Metadata
- Authors
- Uversky, V. N., Kuznetsova, I. M., Turoverov, K. K., & Zaslavsky, B.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2014-11-29
- Volume
- 589
- Issue
- 1
- Pages
- 15-22
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2031787395
- Cited by
- 277
- References
- 7
- FWCI
- 5.72
- Type
- journal article
- Language
- en
- Open access
- bronze
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
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.
