ArticleGenetics2010
Trivalent arsenic inhibits the functions of chaperonin complex.
Article in Genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed, 77 citations in OpenAlex.
- Arsenic binds to nuclear transport factors and disrupts nucleocytoplasmic transport.Journal of cell science · 2025Article
- Direct binding of arsenicals to nuclear transport factors disrupts nucleocytoplasmic transport.bioRxiv : the preprint server for biology · 2025Article
- Mechanisms of genotoxicity and proteotoxicity induced by the metalloids arsenic and antimony.Cellular and molecular life sciences : CMLS · 2023Review
- Prefoldin 2 contributes to mitochondrial morphology and function.BMC biology · 2023Article
- Identification of novel arsenic resistance genes in yeast.MicrobiologyOpen · 2022Article
- Review
- Genome-wide imaging screen uncovers molecular determinants of arsenite-induced protein aggregation and toxicity.Journal of cell science · 2021Article
- Complex Mechanisms of Antimony Genotoxicity in Budding Yeast Involves Replication and Topoisomerase I-Associated DNA Lesions, Telomere Dysfunction and Inhibition of DNA Repair.International journal of molecular sciences · 2021Article
- Prefoldin Function in Cellular Protein Homeostasis and Human Diseases.Frontiers in cell and developmental biology · 2021Review
- Arsenic Exposure and Compromised Protein Quality Control.Chemical research in toxicology · 2020Review
- Article
- Thiol-based direct threat sensing by the stress-activated protein kinase Hog1.Science signaling · 2019Article
- Targeted Degradation of Glucose Transporters Protects against Arsenic Toxicity.Molecular and cellular biology · 2019Article
- YARG: A repository for arsenic-related genes in yeast.PloS one · 2018Article
- Targeting chaperonin containing TCP1 (CCT) as a molecular therapeutic for small cell lung cancer.Oncotarget · 2017Article
- MPSR1 is a cytoplasmic PQC E3 ligase for eliminating emergent misfolded proteins inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Global Fitness Profiling Identifies Arsenic and Cadmium Tolerance Mechanisms in Fission Yeast.G3 (Bethesda, Md.) · 2016Article
- Tmc1 Is a Dynamically Regulated Effector of the Rpn4 Proteotoxic Stress Response.The Journal of biological chemistry · 2016Article
- Defects in Protein Folding Machinery Affect Cell Wall Integrity and Reduce Ethanol Tolerance in S. cerevisiae.Current microbiology · 2016Article
- Computational discovery of pathway-level genetic vulnerabilities in non-small-cell lung cancer.Bioinformatics (Oxford, England) · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 5 institutions in 1 country.
Funding
Abstract
The exact molecular mechanisms by which the environmental pollutant arsenic works in biological systems are not completely understood. Using an unbiased chemogenomics approach in Saccharomyces cerevisiae, we found that mutants of the chaperonin complex TRiC and the functionally related prefoldin complex are all hypersensitive to arsenic compared to a wild-type strain. In contrast, mutants with impaired ribosome functions were highly arsenic resistant. These observations led us to hypothesize that arsenic might inhibit TRiC function, required for folding of actin, tubulin, and other proteins postsynthesis. Consistent with this hypothesis, we found that arsenic treatment distorted morphology of both actin and microtubule filaments. Moreover, arsenic impaired substrate folding by both bovine and archaeal TRiC complexes in vitro. These results together indicate that TRiC is a conserved target of arsenic inhibition in various biological systems.
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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.