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Despite decades of research, the direct molecular targets underlying AA toxicity remain elusive. In this study, a map of the AA\u2010binding protein atlas in kidney tissues is constructed via the design and synthesis of an AA\u2010based affinity probe. Among the AA\u2010binding proteins, HIGD1A is identified as a high\u2010affinity AA target (SPR: 59.6 n\n                    <jats:sc>m<\/jats:sc>\n                    ; ITC: 195 n\n                    <jats:sc>m<\/jats:sc>\n                    ) with significant thermostability changes upon AA binding. Furthermore, AA disrupted the HIGD1A\u2010TFAM interaction, triggering TFAM degradation via the autophagy\u2010lysosome pathway. This led to the accumulation of cytosolic mitochondrial DNA. This study also suggested that HIGD1A also contributed to AA\u2010induced inflammation by increasing the cytosolic levels of oxidized mitochondrial DNA to activate the MAPK and NF\u2010\u03baB 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.\n                  <\/jats:p>","DOI":"10.1002\/advs.202513117","type":"journal-article","created":{"date-parts":[[2025,11,6]],"date-time":"2025-11-06T06:50:23Z","timestamp":1762411823000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Affinity\u2010Based Protein Profiling Revealed that HIGD1A is a Direct Target Protein of Aristolochic Acids"],"prefix":"10.1002","volume":"13","author":[{"given":"Yin","family":"Gong","sequence":"first","affiliation":[{"name":"Faculty of Naval Medicine Naval Military Medical University  Shanghai China"},{"name":"College of Life Sciences Jiangxi Normal University  Nanchang 330022 China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shanshan","family":"Zhang","sequence":"additional","affiliation":[{"name":"Faculty of 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