ArticlePLoS biology2020
A widespread family of heat-resistant obscure (Hero) proteins protect against protein instability and aggregation.
Article in PLoS biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- The relationship between coronary artery disease and the heat-resistant obscure chaperone Hero11.Molecular biology reports · 2026Article
- Heterologous expression of heat-resistant obscure (Hero) proteins enhances thermotolerance in plants.iScience · 2025Article
- When Heroes Fall: Reduced Expression of Heat-Resistant Obscure Proteins in Ischemic Stroke.Neuromolecular medicine · 2025Article
- "SERBP1 (Hero45) is a Novel Link with Ischemic Heart Disease Risk: Associations with Coronary Arteries Occlusion, Blood Coagulation and Lipid Profile".Cell biochemistry and biophysics · 2025Article
- SERBP1-PCIF1 complex-controlled m6Am modification in glutamatergic neurons of the primary somatosensory cortex is required for neuropathic pain in mice.Nature communications · 2025Article
- Protein Catalysis Through Structural Dynamics: A Comprehensive Analysis of Energy Conversion in Enzymatic Systems and Its Computational Limitations.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Bioinformatic analysis of the regulatory potential of tagging SNPs provides evidence of the involvement of genes encoding the heat-resistant obscure (Hero) proteins in the pathogenesis of cardiovascular diseases.Journal of integrative bioinformatics · 2025Article
- Translation of zinc finger domains induces ribosome collision and Znf598-dependent mRNA decay in zebrafish.PLoS biology · 2024Article
- Genetic Diversity and Genome-Wide Association Study of Total Phenolics, Flavonoids, and Antioxidant Properties in Potatoes (International journal of molecular sciences · 2024Article
- Article
- DNAJA2 and Hero11 mediate similar conformational extension and aggregation suppression of TDP-43.RNA (New York, N.Y.) · 2024Article
- Innovative Formulation Platform: Paving the Way for Superior Protein Therapeutics with Enhanced Efficacy and Broadened Applications.Advanced materials (Deerfield Beach, Fla.) · 2024Review
- Obesity and Environmental Risk Factors Significantly Modify the Association between Ischemic Stroke and the Hero ChaperoneLife (Basel, Switzerland) · 2024Article
- Calibrated ribosome profiling assesses the dynamics of ribosomal flux on transcripts.Nature communications · 2024Article
- CDCA7 is an evolutionarily conserved hemimethylated DNA sensor in eukaryotes.Science advances · 2024Article
- Protein G-quadruplex interactions and their effects on phase transitions and protein aggregation.Nucleic acids research · 2024Article
- GENESIS CGDYN: large-scale coarse-grained MD simulation with dynamic load balancing for heterogeneous biomolecular systems.Nature communications · 2024Article
- Protein G-quadruplex interactions and their effects on phase transitions and protein aggregation.bioRxiv : the preprint server for biology · 2024Article
- dCas13-mediated translational repression for accurate gene silencing in mammalian cells.Nature communications · 2024Article
- Detecting anomalous proteins using deep representations.NAR genomics and bioinformatics · 2024Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Proteins are typically denatured and aggregated by heating at near-boiling temperature. Exceptions to this principle include highly disordered and heat-resistant proteins found in extremophiles, which help these organisms tolerate extreme conditions such as drying, freezing, and high salinity. In contrast, the functions of heat-soluble proteins in non-extremophilic organisms including humans remain largely unexplored. Here, we report that heat-resistant obscure (Hero) proteins, which remain soluble after boiling at 95°C, are widespread in Drosophila and humans. Hero proteins are hydrophilic and highly charged, and function to stabilize various "client" proteins, protecting them from denaturation even under stress conditions such as heat shock, desiccation, and exposure to organic solvents. Hero proteins can also block several different types of pathological protein aggregations in cells and in Drosophila strains that model neurodegenerative diseases. Moreover, Hero proteins can extend life span of Drosophila. Our study reveals that organisms naturally use Hero proteins as molecular shields to stabilize protein functions, highlighting their biotechnological and therapeutic potential.
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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.