ReviewRNA (New York, N.Y.)2022
How do protein domains of low sequence complexity work?
Review in RNA (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
44 citing papers in PubMed.
- Sequence-encoded conformational biases correlate with self-assembly modes of intrinsically disordered proteins.PNAS nexus · 2026Article
- Dysregulation of liquid-liquid phase separation: from molecular mechanisms to targeted therapies in cardiovascular diseases.Journal of nanobiotechnology · 2026Review
- Droplet growth, Ostwald's rule, and emergence of order in Fused in Sarcoma.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Insights into the Structure of Intermediate Filaments.Sub-cellular biochemistry · 2026Review
- Combinatorial protein engineering identifies potent CRISPR activators with reduced toxicity.Nature communications · 2025Article
- How the Extent of Protein Folding and Oligomerization Modulate Condensate Formation and Properties.The journal of physical chemistry letters · 2025Article
- Decoding the interactions and functions of non-coding RNA with artificial intelligence.Nature reviews. Molecular cell biology · 2025Review
- Insights into Noncanonical and Diversified Functions of ABCF1: From Health to Disease.Journal of molecular biology · 2025Review
- CaMKII clusters neuronal LTCCs in biomolecular condensates to gate excitation-transcription coupling.bioRxiv : the preprint server for biology · 2025Article
- A simple method for mapping the location of cross-β-forming regions within protein domains of low sequence complexity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Purification of Low-Complexity Domain Proteins FUS, EWSR1, and Their Fusions.Current protocols · 2025Article
- Conformations of a low-complexity protein in homogeneous and phase-separated frozen solutions.Biophysical journal · 2024Article
- Modular RNA motifs for orthogonal phase separated compartments.Nature communications · 2024Article
- Conformations of a Low-Complexity Protein in Homogeneous and Phase-Separated Frozen Solutions.bioRxiv : the preprint server for biology · 2024Article
- Preserving condensate structure and composition by lowering sequence complexity.Biophysical journal · 2024Article
- The impact of IDR phosphorylation on the RNA binding profiles of proteins.Trends in genetics : TIG · 2024Review
- RNA glues it all.Nature cell biology · 2024Article
- Vimentin filaments integrate low-complexity domains in a complex helical structure.Nature structural & molecular biology · 2024Article
- The Enigma of Tau Protein Aggregation: Mechanistic Insights and Future Challenges.International journal of molecular sciences · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
This review covers research findings reported over the past decade concerning the ability of low complexity (LC) domains to self-associate in a manner leading to their phase separation from aqueous solution. We focus our message upon the reductionist use of two forms of phase separation as biochemical assays to study how LC domains might function in living cells. Cells and their varied compartments represent extreme examples of material condensates. Over the past half century, biochemists, structural biologists, and molecular biologists have resolved the mechanisms driving innumerable forms of macromolecular condensation. In contrast, we remain largely ignorant as to how 10%-20% of our proteins actually work to assist in cell organization. This enigmatic 10%-20% of the proteome corresponds to gibberish-like LC sequences. We contend that many of these LC sequences move in and out of a structurally ordered, self-associated state as a means of offering a combination of organizational specificity and dynamic pliability to living cells. Finally, we speculate that ancient proteins may have behaved similarly, helping to condense, organize, and protect RNA early during evolution.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.