ReviewFrontiers in genetics2014
Turnover of protein phosphorylation evolving under stabilizing selection.
Review in Frontiers in genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
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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.
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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
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 54 citations in OpenAlex.
- Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes.GigaScience · 2017Pooled it
- An AI-enabled structural atlas decodes kinase specificity across the human proteome.Nature biotechnology · 2026Article
- Advances in post-translational and epigenetic modification of hyperuricemia-to-gout progression: mechanisms and therapeutic targets.Frontiers in cell and developmental biology · 2026Review
- Most m5C Modifications in Mammalian mRNAs are Nonadaptive.Molecular biology and evolution · 2025Article
- StACS3-mediated drought stress adaptation in potato involves interactions with StPP2C2 and St14-3-3 proteins.Frontiers in plant science · 2025Article
- The fitness cost of spurious phosphorylation.The EMBO journal · 2024Article
- Genetic and selective constraints on the optimization of gene product diversity.bioRxiv : the preprint server for biology · 2024Article
- Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail.Nature communications · 2024Article
- The fitness cost of spurious phosphorylation.bioRxiv : the preprint server for biology · 2023Article
- Evolutionary scaling of maximum growth rate with organism size.Scientific reports · 2022Article
- Phosphorylation and sulfation share a common biosynthetic pathway, but extend biochemical and evolutionary diversity of biological macromolecules in distinct ways.Journal of the Royal Society, Interface · 2022Article
- Enhancing the Discovery of Functional Post-Translational Modification Sites with Machine Learning Models - Development, Validation, and Interpretation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The Case for, and Challenges of, Human Cardiac Tissue in Advancing Phosphoprotein Research.Frontiers in physiology · 2022Review
- A functionally divergent intrinsically disordered region underlying the conservation of stochastic signaling.PLoS genetics · 2021Article
- Natural Selection on the Phase-Separation Properties of FUS during 160 My of Mammalian Evolution.Molecular biology and evolution · 2021Article
- The evolutionary scaling of cellular traits imposed by the drift barrier.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A Theoretical Framework for Evolutionary Cell Biology.Journal of molecular biology · 2020Review
- The sequential phosphorylation of PHF10 subunit of the PBAF chromatin-remodeling complex determines different properties of the PHF10 isoforms.Biology open · 2020Article
- Multiple Site-Specific Phosphorylation of IDPs Monitored by NMR.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Article
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 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most proteins are regulated by posttranslational modifications and changes in these modifications contribute to evolutionary changes as well as to human diseases. Phosphorylation of serines, threonines, and tyrosines are the most common modifications identified to date in eukaryotic proteomes. While the mode of action and the function of most phosphorylation sites remain unknown, functional studies have shown that phosphorylation affects protein stability, localization and ability to interact. Two broad modes of action have been described for protein phosphorylation. The first mode corresponds to the canonical and qualitative view whereby single phosphorylation sites act as molecular switches that either turn on or off specific protein functions through direct or allosteric effects. The second mode is more akin to a rheostat than a switch. In this case, a group of phosphorylation sites in a given protein region contributes collectively to the modification of the protein, irrespective of the precise position of individual sites, through an aggregate property. Here we discuss these two types of regulation and examine how they affect the rate and patterns of protein phosphorylation evolution. We describe how the evolution of clusters of phosphorylation sites can be studied under the framework of complex traits evolution and stabilizing selection.
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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.