ReviewNature reviews. Chemistry2020
Amino acid homorepeats in proteins.
Review in Nature reviews. Chemistry, 2020. 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 74 citations in OpenAlex.
- Variation in multiple classes of simple sequence repeats can alter drug susceptibility inbioRxiv : the preprint server for biology · 2026Article
- Amino acid homorepeats in tape measure proteins correlate with bacteriophage tail length.The Journal of general virology · 2026Article
- Article
- Improving the Thermostability of the Qβ Bacteriophage Coat Protein Through Single-Site Mutation Based on Molecular Dynamics.International journal of molecular sciences · 2026Article
- Seeking Precise Protein-like Functions from Random Heteropolymer Ensemble and through Dimensionality Reduction.ACS central science · 2025Review
- Protein language model identifies disordered, conserved motifs implicated in phase separation.eLife · 2025Article
- The evolution of eukaryotic linear motifs governing the function of androgen receptor from fish to Homo sapiens.Nucleic acids research · 2025Article
- Chromosomal localization of PHOX2B during M-phase is disrupted in disease-associated mutants.Development, growth & differentiation · 2025Article
- Low-complexity regions in fungi display functional groups and are depleted in positively charged amino acids.NAR genomics and bioinformatics · 2025Article
- Divergent evolution of low-complexity regions in the vertebrate CPEB protein family.Frontiers in bioinformatics · 2025Article
- Identification of Protein Hydrolysates from Sesame Meal and In Vivo Study of Their Gastric Mucosal Protective Effects.Foods (Basel, Switzerland) · 2024Article
- Predicting the involvement of polyQ- and polyA in protein-protein interactions by their amino acid context.Heliyon · 2024Article
- Cellular localization of a variant RAPGEF5 protein associated with idiopathic epilepsy risk in the Belgian shepherd.Canine medicine and genetics · 2024Article
- 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
- Alternative low-populated conformations prompt phase transitions in polyalanine repeat expansions.Nature communications · 2024Article
- Interpretable feature extraction and dimensionality reduction in ESM2 for protein localization prediction.Briefings in bioinformatics · 2024Article
- Prediction of folding patterns for intrinsic disordered protein.Scientific reports · 2023Article
- Article
- Pathogen-specific structural features ofmBio · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
Amino acid homorepeats, or homorepeats, are polypeptide segments found in proteins that contain stretches of identical amino acid residues. Although abnormal homorepeat expansions are linked to pathologies such as neurodegenerative diseases, homorepeats are prevalent in eukaryotic proteomes, suggesting that they are important for normal physiology. In this Review, we discuss recent advances in our understanding of the biological functions of homorepeats, which range from facilitating subcellular protein localization to mediating interactions between proteins across diverse cellular pathways. We explore how the functional diversity of homorepeat-containing proteins could be linked to the ability of homorepeats to adopt different structural conformations, an ability influenced by repeat composition, repeat length and the nature of flanking sequences. We conclude by highlighting how an understanding of homorepeats will help us better characterize and develop therapeutics against the human diseases to which they contribute.
Identifiers
What OpenQuestion holds
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.