ReviewAnnual review of biophysics2013
Considering protonation as a posttranslational modification regulating protein structure and function.
Review in Annual review of biophysics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
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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
96 citing papers in PubMed.
- Cryo-EM structure of detergent-boundbioRxiv : the preprint server for biology · 2026Article
- Endosome maturation is orchestrated by inside-out proton signaling through a NaNature communications · 2026Article
- Endosome maturation is orchestrated by inside-out proton signaling through a NaResearch square · 2026Article
- TrIPP: a trajectory iterative pKa predictor.Bioinformatics (Oxford, England) · 2026Article
- PKAD-R: curated, redesigned and expanded database of experimental pKa values in proteins.Journal of computational biophysics and chemistry · 2025Article
- Intracellular pH regulates ubiquitin-mediated degradation of the MAP kinase ERK3.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Sensing within: Mitochondrial inside-out signal transduction.Cell chemical biology · 2025Review
- Electromagnetic Field Stimulation Effects on Intrinsically Disordered Proteins and Their Role in Aging and Neurodegeneration.Journal of biomedical science and engineering · 2025Article
- The timing of maternal protein degradation during mammalian preimplantation development is species-specific.Reproduction (Cambridge, England) · 2025Article
- CaBiomolecules · 2025Review
- Real-Time, Continuous Monitoring of Tissue Chips as an Emerging Opportunity for Biosensing.Sensors (Basel, Switzerland) · 2025Review
- Alkaline Amino Acids for Salt Reduction in Surimi: A Review.Foods (Basel, Switzerland) · 2025Review
- A role for pH dynamics regulating transcription factor DNA-binding selectivity.Nucleic acids research · 2025Article
- Molecular and functional profiling of Gαi as an intracellular pH sensor.Nature communications · 2025Article
- Review
- Genesis and regulation of C-terminal cyclic imides from protein damage.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Intracellular pH differentially regulates transcription of metabolic and signaling pathways in normal epithelial cells.The Journal of biological chemistry · 2024Article
- Constitutional adaptation to pChemical science · 2024Article
- pH-regulated single cell migration.Pflugers Archiv : European journal of physiology · 2024Review
- Phenotypic screen of sixty-eight colorectal cancer cell lines identifies CEACAM6 and CEACAM5 as markers of acid resistance.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
36 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
4 authors.
Funding
Abstract
Posttranslational modification is an evolutionarily conserved mechanism for regulating protein activity, binding affinity, and stability. Compared with established posttranslational modifications such as phosphorylation or ubiquitination, posttranslational modification by protons within physiological pH ranges is a less recognized mechanism for regulating protein function. By changing the charge of amino acid side chains, posttranslational modification by protons can drive dynamic changes in protein conformation and function. Addition and removal of a proton is rapid and reversible and, in contrast to most other posttranslational modifications, does not require an enzyme. Signaling specificity is achieved by only a minority of sites in proteins titrating within the physiological pH range. Here, we examine the structural mechanisms and functional consequences of proton posttranslational modification of pH-sensing proteins regulating different cellular processes.
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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.