ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026
Affinity-Based Protein Profiling Revealed that HIGD1A is a Direct Target Protein of Aristolochic Acids.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
The trial behind it
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Who cites it
4 citing papers in PubMed.
- Natural Product-Derived Activity-Based and Affinity-Based Probes: Tools for Mechanism of Action Studies.Molecules (Basel, Switzerland) · 2026Review
- Affinity-Based Protein Profiling Revealed that HIGD1A is a Direct Target Protein of Aristolochic Acids.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Integrated analysis of autophagy and ferroptosis mediating aristolochic acid A-induced nephrotoxicity via transcriptome and m6A epigenetic transcriptome in HK-2 cells.Frontiers in genetics · 2026Article
- Oxidative stress mechanisms and potential biomarkers of methyl acetate poisoning: a urinary metabolomics study in rat model and human occupational cohort.Frontiers in molecular biosciences · 2026Article
Corrections and comments
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Authors and funding
16 authors.
Funding
Abstract
Exposure to aristolochic acids (AA) via the ingestion of AA-containing medicine or food is a significant risk factor for severe nephropathy. Despite decades of research, the direct molecular targets underlying AA toxicity remain elusive. In this study, a map of the AA-binding protein atlas in kidney tissues is constructed via the design and synthesis of an AA-based affinity probe. Among the AA-binding proteins, HIGD1A is identified as a high-affinity AA target (SPR: 59.6 nm; ITC: 195 nm) with significant thermostability changes upon AA binding. Furthermore, AA disrupted the HIGD1A-TFAM interaction, triggering TFAM degradation via the autophagy-lysosome pathway. This led to the accumulation of cytosolic mitochondrial DNA. This study also suggested that HIGD1A also contributed to AA-induced inflammation by increasing the cytosolic levels of oxidized mitochondrial DNA to activate the MAPK and NF-κB pathways. This study not only reveals an important target protein of AA but also provides novel inspiration and ideas for toxicology and chemical biology research.
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Registered trials
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