ArticleGenes & development2024
Protein domains of low sequence complexity-dark matter of the proteome.
Article in Genes & development, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Sequence-encoded conformational biases correlate with self-assembly modes of intrinsically disordered proteins.PNAS nexus · 2026Article
- Biomolecular Condensates in Disease: Decoding the Material State and Engineering Precision Modulators.International journal of molecular sciences · 2026Review
- In-Depth Study of Low-Complexity Domains: From Structural Diversity to Disease Mechanisms.Cells · 2025Review
- Phosphorylation-induced SUMOylation promotes Ulk4 condensation at the ciliary tip to transduce Hedgehog signal.Journal of cell science · 2025Article
- Coincident evolution and functional adaptation of the taxonomically restricted genes ivph-3 and gon-14 in Caenorhabditis nematodes.Biology open · 2025Article
- Insights into Noncanonical and Diversified Functions of ABCF1: From Health to Disease.Journal of molecular biology · 2025Review
- Article
- Direct ionic stress sensing and mitigation by the transcription factor NFAT5.Science advances · 2025Article
- Decoding biomolecular condensate dynamics: an energy landscape approach.PLoS computational biology · 2025Article
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This perspective begins with a speculative consideration of the properties of the earliest proteins to appear during evolution. What did these primitive proteins look like, and how were they of benefit to early forms of life? I proceed to hypothesize that primitive proteins have been preserved through evolution and now serve diverse functions important to the dynamics of cell morphology and biological regulation. The primitive nature of these modern proteins is easy to spot. They are composed of a limited subset of the 20 amino acids used by traditionally evolved proteins and thus are of low sequence complexity. This chemical simplicity limits protein domains of low sequence complexity to forming only a crude and labile type of protein structure currently hidden from the computational powers of machine learning. I conclude by hypothesizing that this structural weakness represents the underlying virtue of proteins that, at least for the moment, constitute the dark matter of the proteome.
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Registered trials
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