ReviewBiomolecules2014
Heavy metals and metalloids as a cause for protein misfolding and aggregation.
Review in Biomolecules, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 164 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
164 citing papers in PubMed, 1 synthesis or guideline pooled it, 461 citations in OpenAlex.
- Toxic heavy metal exposure and heart health: a systematic review and meta-analysis of 324,331 patients.BMC cardiovascular disorders · 2025Pooled it
- Stress granules at the crossroads of the proteostasis network.RNA biology · 2026Review
- PrOMet: Accurate and Robust Metal-Binding Site and Type Prediction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Small molecules rescue pathogenic POLGA aggregation and restore its functions in a mouse model of PEO.EMBO molecular medicine · 2026Article
- Heavy metal toxicity as a driver of endoplasmic reticulum stress and dysfunction.The FEBS journal · 2026Review
- Enzyme-Inspired Design of Redox-Active Molecules for Promotion of Oxidative Protein Folding.Chembiochem : a European journal of chemical biology · 2026Review
- Tracing the threads: How toxic metals contribute to neurodegeneration.IBRO neuroscience reports · 2026Review
- AcrAB-NodT overexpression drives envelope destabilization and metal sensitivity in Caulobacter vibrioides.Archives of microbiology · 2026Review
- Binding of Hg(I) and Hg(II) Ions to Amyloid-Beta (Aβ) Peptide Variants Affect their Structure and Aggregation.Chembiochem : a European journal of chemical biology · 2025Article
- Bioremediation and Recovery of Lead and Cadmium by Spores of Bacillus subtilis C1.MicrobiologyOpen · 2025Article
- Estimating Soil Arsenic Contamination by Integrating Hyperspectral and Geochemical Data with PCA and Optimizing Inversion Models.Sensors (Basel, Switzerland) · 2025Article
- Removal of Toxic Metabolites-Chelation: Manganese Disorders.Journal of inherited metabolic disease · 2025Review
- Metabolic Responses to the Zinc Stress in the Roots and Leaves ofPlants (Basel, Switzerland) · 2025Article
- Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations.Signal transduction and targeted therapy · 2025Review
- Sensing Cellular Damages Induced by Food Safety Hazards Using Bacterial Stress-Responsive Biosensors.Biosensors · 2025Article
- Isolation and pan-genome analysis of Acinetobacter junii SC22, a heavy metal(loid)s resistant and plant growth promoting bacterium, from the Zijin Gold and Copper mine.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025Article
- Pumpkin (Cucurbita moschata Duch.) tolerates high levels of lead and copper by modulating ecophysiological characteristics and antioxidant defense system.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025Article
- Functional Hydrogels: A Promising Platform for Biomedical and Environmental Applications.International journal of molecular sciences · 2025Review
- Metal-Responsive Up-Regulation of Bifunctional Disulfides for Suppressing Protein Misfolding and Promoting Oxidative Folding.Angewandte Chemie (International ed. in English) · 2025Article
- Arsenic binds to nuclear transport factors and disrupts nucleocytoplasmic transport.Journal of cell science · 2025Article
104 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
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While the toxicity of metals and metalloids, like arsenic, cadmium, mercury, lead and chromium, is undisputed, the underlying molecular mechanisms are not entirely clear. General consensus holds that proteins are the prime targets; heavy metals interfere with the physiological activity of specific, particularly susceptible proteins, either by forming a complex with functional side chain groups or by displacing essential metal ions in metalloproteins. Recent studies have revealed an additional mode of metal action targeted at proteins in a non-native state; certain heavy metals and metalloids have been found to inhibit the in vitro refolding of chemically denatured proteins, to interfere with protein folding in vivo and to cause aggregation of nascent proteins in living cells. Apparently, unfolded proteins with motile backbone and side chains are considerably more prone to engage in stable, pluridentate metal complexes than native proteins with their well-defined 3D structure. By interfering with the folding process, heavy metal ions and metalloids profoundly affect protein homeostasis and cell viability. This review describes how heavy metals impede protein folding and promote protein aggregation, how cells regulate quality control systems to protect themselves from metal toxicity and how metals might contribute to protein misfolding disorders.
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.