ArticleCell2011
A mechanism for the evolution of phosphorylation sites.
Article in Cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 163 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
163 citing papers in PubMed, 267 citations in OpenAlex.
- Mechanisms of Phenotypic Evolution from Molecules to Organisms: Integrating Evolutionary Biochemistry and Evolutionary Developmental Biology.Annual review of ecology, evolution, and systematics · 2026Article
- PP2A and CDK16 antagonistically regulate WIPI2B phosphorylation and neuronal autophagosome biogenesis.iScience · 2026Article
- Evolutionary tuning of the molecular charge state of UBP24 shapes responses to high temperature.Nature plants · 2026Article
- Are Sulfates of the Hydroxyl Amino Acids Threonine and Serine Truly Extremely Rare or Do They Simply Escape Detection?Life (Basel, Switzerland) · 2026Article
- Origins of allostery in vertebrate hemoglobin evolution.bioRxiv : the preprint server for biology · 2026Article
- Disruption of the human cystin-1 myristoyl-electrostatic switch causes polycystic kidney disease that phenocopies autosomal recessive polycystic kidney disease.Kidney international · 2026Article
- Impact of Ser81 phosphorylation on alanine: glyoxylate aminotransferase associated with Primary hyperoxaluria type I.Molecular biomedicine · 2026Article
- Methods for studying the effects of phosphorylation patterns in proteins.Biochemical Society transactions · 2026Review
- Modulation of succinyl-CoA:3-ketoacid CoA transferase activity by a single amino acid residue in acetate:succinate CoA transferase from Trypanosoma brucei, the causative agent of African sleeping sickness.Protein science : a publication of the Protein Society · 2026Article
- Phosphovariants of the canonical heterotrimeric Gα protein, GPA1, differentially affect G protein activity and Arabidopsis development.bioRxiv : the preprint server for biology · 2026Article
- Acidosis promotes exon skipping through sequestering SR-rich splicing factors in nuclear speckles.Frontiers in molecular biosciences · 2026Article
- Phosphoproteomics Protocol for the Identification of Novel Biomarkers from Extracellular Vesicles of Cancerous Cells.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Molecular response to the non-lytic peptide bac7 (1-35) triggers disruption of Klebsiella pneumoniae biofilm.PLoS pathogens · 2025Article
- Impact of C-Terminal PKC Phosphorylation on TRPC6 Current Kinetics.International journal of molecular sciences · 2025Article
- Phosphomimetic Experiments Do Not Support a Causal Role for TFAM Phosphorylation in mtDNA Elimination in Sperm.Journal of molecular biology · 2025Article
- Phosphorylation-mimicking histone H3.3 rescues exercise-induced gene responses in an epigenetic aging model of mouse skeletal muscle.Laboratory animal research · 2025Article
- Optimum level of NEDD4 and its interaction with nsP3 are crucial to facilitate efficient Chikungunya virus (CHIKV) infection.The Journal of general virology · 2025Article
- HDAC3 Serine 424 Phospho-mimic and Phospho-null Mutants Bidirectionally Modulate Long-Term Memory Formation and Synaptic Plasticity in the Adult and Aging Mouse Brain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- EPSD 2.0: An Updated Database of Protein Phosphorylation Sites Across Eukaryotic Species.Genomics, proteomics & bioinformatics · 2025Article
- Differential Role of Phosphorylation in Glucagon Family Receptor Signaling Revealed by Mass Spectrometry.Journal of proteome research · 2025Article
103 more citing papers are in PubMed but not listed here.
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 at 1 institution in 1 country.
Funding
Abstract
Protein phosphorylation provides a mechanism for the rapid, reversible control of protein function. Phosphorylation adds negative charge to amino acid side chains, and negatively charged amino acids (Asp/Glu) can sometimes mimic the phosphorylated state of a protein. Using a comparative genomics approach, we show that nature also employs this trick in reverse by evolving serine, threonine, and tyrosine phosphorylation sites from Asp/Glu residues. Structures of three proteins where phosphosites evolved from acidic residues (DNA topoisomerase II, enolase, and C-Raf) show that the relevant acidic residues are present in salt bridges with conserved basic residues, and that phosphorylation has the potential to conditionally restore the salt bridges. The evolution of phosphorylation sites from glutamate and aspartate provides a rationale for why phosphorylation sometimes activates proteins, and helps explain the origins of this important and complex process.
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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.