ArticleNature structural & molecular biology2017
Constraints and consequences of the emergence of amino acid repeats in eukaryotic proteins.
Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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.
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Who cites it
35 citing papers in PubMed, 76 citations in OpenAlex.
- Article
- The evolution of eukaryotic linear motifs governing the function of androgen receptor from fish to Homo sapiens.Nucleic acids research · 2025Article
- Divergent evolution of low-complexity regions in the vertebrate CPEB protein family.Frontiers in bioinformatics · 2025Article
- Reviewing the Structure-Function Paradigm in Polyglutamine Disorders: A Synergistic Perspective on Theoretical and Experimental Approaches.International journal of molecular sciences · 2024Review
- Homorepeat variability within the human population.NAR genomics and bioinformatics · 2024Article
- Evolution of Transcript Abundance is Influenced by Indels in Protein Low Complexity Regions.Journal of molecular evolution · 2024Article
- Noncanonical usage of stop codons in ciliates expands proteins with structurally flexible Q-rich motifs.eLife · 2024Article
- Mutation and selection processes regulating short tandem repeats give rise to genetic and phenotypic diversity across species.Journal of evolutionary biology · 2023Review
- Lineage-specific protein repeat expansions and contractions reveal malleable regions of immune genes.Genes and immunity · 2022Article
- The sequence context in poly-alanine regions: structure, function and conservation.Bioinformatics (Oxford, England) · 2022Article
- Expansion and functional analysis of the SR-related protein family across the domains of life.RNA (New York, N.Y.) · 2022Article
- Low Complexity Regions in Mammalian Proteins are Associated with Low Protein Abundance and High Transcript Abundance.Molecular biology and evolution · 2022Article
- Article
- Regions with two amino acids in protein sequences: A step forward from homorepeats into the low complexity landscape.Computational and structural biotechnology journal · 2022Article
- Between Interactions and Aggregates: The PolyQ Balance.Genome biology and evolution · 2021Article
- PolyQ length co-evolution in neural proteins.NAR genomics and bioinformatics · 2021Article
- LCD-Composer: an intuitive, composition-centric method enabling the identification and detailed functional mapping of low-complexity domains.NAR genomics and bioinformatics · 2021Article
- Homopeptide and homocodon levels across fungi are coupled to GC/AT-bias and intrinsic disorder, with unique behaviours for some amino acids.Scientific reports · 2021Article
- Mutation-selection balance and compensatory mechanisms in tumour evolution.Nature reviews. Genetics · 2021Review
- A framework for understanding the functions of biomolecular condensates across scales.Nature reviews. Molecular cell biology · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
Proteins with amino acid homorepeats have the potential to be detrimental to cells and are often associated with human diseases. Why, then, are homorepeats prevalent in eukaryotic proteomes? In yeast, homorepeats are enriched in proteins that are essential and pleiotropic and that buffer environmental insults. The presence of homorepeats increases the functional versatility of proteins by mediating protein interactions and facilitating spatial organization in a repeat-dependent manner. During evolution, homorepeats are preferentially retained in proteins with stringent proteostasis, which might minimize repeat-associated detrimental effects such as unregulated phase separation and protein aggregation. Their presence facilitates rapid protein divergence through accumulation of amino acid substitutions, which often affect linear motifs and post-translational-modification sites. These substitutions may result in rewiring protein interaction and signaling networks. Thus, homorepeats are distinct modules that are often retained in stringently regulated proteins. Their presence facilitates rapid exploration of the genotype-phenotype landscape of a population, thereby contributing to adaptation and fitness.
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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.