ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2018
Protein moonlighting: what is it, and why is it important?
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 180 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
180 citing papers in PubMed, 353 citations in OpenAlex.
- Bacterial cell envelope components of gut commensals: effects in host-microbe interaction.Annals of medicine · 2026Review
- SAT1-Induced Spermidine Depletion Potentiates Food Allergy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Peroxisomal Import Stress Drives Cellular Senescence through SCAF1-dependent Suppression of Mitoribosome Biogenesis.bioRxiv : the preprint server for biology · 2026Article
- Protocol for conditional mapping of proximal interactomes of dimeric protein complexes using a BioID-based complementation approach.STAR protocols · 2026Article
- Beyond the gap: moonlighting functions of connexins in cancer.Cell communication and signaling : CCS · 2026Review
- Emergence Biases in Molecular Evolution.Genome biology and evolution · 2026Review
- Review
- Multiomics studies reveal how ambient temperature changes govern cellular responses of Chlamydomonas.The Plant cell · 2026Article
- A comprehensive benchmark of sequence-based subcellular localization predictors for human proteins.Nature methods · 2026Article
- Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026Review
- The Role of the RGD Motif of the IdeC Protein inMicroorganisms · 2026Article
- PurK,Microorganisms · 2026Article
- Dual-Role GH7 Family Proteins From Verticillium dahliae Function as Virulence Factors and Intracellular Effectors Triggering NLR-Mediated Immunity.Plant, cell & environment · 2026Article
- Eukaryote initiation factor 6 modulates small-cell lung carcinoma plasticity via the integrin-FAK signaling axis.Nature communications · 2026Article
- Oxidized MIF is an Alzheimer's disease drug target relaying external risk factors to tau pathology.Cell reports. Medicine · 2026Article
- Cytoplasmic membrane vesicles fromFrontiers in microbiology · 2026Article
- SubCell: Proteome-aware vision foundation models for microscopy capture single-cell biology.bioRxiv : the preprint server for biology · 2025Article
- Review
- Temporal and Spatial Profiling ofProteomes · 2025Article
- Angel wing: a class of alternative splicing regulators in animals.Nucleic acids research · 2025Article
120 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
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the GroEL/HSP60 protein family have been studied for many years because of their critical roles as ATP-dependent molecular chaperones, so it might come as a surprise that some have important functions in ATP-poor conditions, for example, when secreted outside the cell. At least some members of each of the HSP10, HSP70, HSP90, HSP100 and HSP110 heat shock protein families are also 'moonlighting proteins'. Moonlighting proteins exhibit more than one physiologically relevant biochemical or biophysical function within one polypeptide chain. In this class of multifunctional proteins, the multiple functions are not due to gene fusions or multiple proteolytic fragments. Several hundred moonlighting proteins have been identified, and they include a diverse set of proteins with a large variety of functions. Some participate in multiple biochemical processes by using an active site pocket for catalysis and a different part of the protein's surface to interact with other proteins. Moonlighting proteins play a central role in many diseases, and the development of novel treatments would be aided by more information addressing current questions, for example, how some are targeted to multiple cellular locations and how a single function can be targeted by therapeutics without targeting a function not involved in disease.This article is part of the theme issue 'Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective'.
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.