ArticleProceedings of the National Academy of Sciences of the United States of America2020
Frameshifting preserves key physicochemical properties of proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
27 citing papers in PubMed.
- Transcript isoform switching during embryonic and post-hatch development of broiler breast muscle.Poultry science · 2026Article
- Protein tandem repeats that produce frameshifts can generate new structural states and functions.The FEBS journal · 2026Article
- Programmed ribosomal frameshifting duringScience advances · 2025Article
- De novo gene birth and the conundrum of ORFan genes in bacteria.Genome research · 2025Review
- Genetic variation in the bovine heat shock protein gene in Indonesian Bali cattle (Open veterinary journal · 2025Article
- Loss of phytochromobilin synthase activity leads to larger seeds with higher protein content in soybean.BMC plant biology · 2025Article
- Review
- Many purported pseudogenes in bacterial genomes are bona fide genes.BMC genomics · 2024Article
- Alternative Reading Frames are an Underappreciated Source of Protein Sequence Novelty.Journal of molecular evolution · 2023Review
- Selection for immune evasion in SARS-CoV-2 revealed by high-resolution epitope mapping and sequence analysis.iScience · 2023Article
- Rare-event sampling analysis uncovers the fitness landscape of the genetic code.PLoS computational biology · 2023Article
- Cas9-induced large deletions and small indels are controlled in a convergent fashion.Nature communications · 2022Article
- Frameshift and wild-type proteins are often highly similar because the genetic code and genomes were optimized for frameshift tolerance.BMC genomics · 2022Article
- Pairs of Mutually Compensatory Frameshifting Mutations Contribute to Protein Evolution.Molecular biology and evolution · 2022Article
- Overlapping genes in natural and engineered genomes.Nature reviews. Genetics · 2022Review
- Article
- Exploring the Peptide Potential of Genomes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Accurate Prediction of Protein Sequences for Proteogenomics Data Integration.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Biological factors in the synthetic construction of overlapping genes.BMC genomics · 2021Article
- Intergenic ORFs as elementary structural modules of de novo gene birth and protein evolution.Genome research · 2021Article
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
Frameshifts in protein coding sequences are widely perceived as resulting in either nonfunctional or even deleterious protein products. Indeed, frameshifts typically lead to markedly altered protein sequences and premature stop codons. By analyzing complete proteomes from all three domains of life, we demonstrate that, in contrast, several key physicochemical properties of protein sequences exhibit significant robustness against +1 and -1 frameshifts. In particular, we show that hydrophobicity profiles of many protein sequences remain largely invariant upon frameshifting. For example, over 2,900 human proteins exhibit a Pearson's correlation coefficient R between the hydrophobicity profiles of the original and the +1-frameshifted variants greater than 0.7, despite an average sequence identity between the two of only 6.5% in this group. We observe a similar effect for protein sequence profiles of affinity for certain nucleobases as well as protein sequence profiles of intrinsic disorder. Finally, analysis of significance and optimality demonstrates that frameshift stability is embedded in the structure of the universal genetic code and may have contributed to shaping it. Our results suggest that frameshifting may be a powerful evolutionary mechanism for creating new proteins with vastly different sequences, yet similar physicochemical properties to the proteins from which they originate.
Indexed as
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.