{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gong Y"],"funding":["National Natural Science Foundation of China","Shanghai Rising-Star Program","Shanghai Eastern Talent Program"],"pagination":["e13117"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12850329"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(5)"],"pubmed_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 "],"journal":["Advanced science (Weinheim, Baden-Wurttemberg, Germany)"],"pubmed_title":["Affinity-Based Protein Profiling Revealed that HIGD1A is a Direct Target Protein of Aristolochic Acids."],"pmcid":["PMC12850329"],"funding_grant_id":["82271916","23QA1411500","82103885","QNJY2024191","QNWS2024063"],"pubmed_authors":["Wei A","Luo Z","Mao G","Cen J","Zhang S","Gong Y","Sun Z","Zhao X","Yin Z","Sun M","Chong X","Zou Z","Ji X","Zhang X","Pei Z","Meng WQ"],"additional_accession":[]},"is_claimable":false,"name":"Affinity-Based Protein Profiling Revealed that HIGD1A is a Direct Target Protein of Aristolochic Acids.","description":"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 ","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-16T07:22:07.834Z","creation":"2026-06-16T03:09:51.401Z"},"accession":"S-EPMC12850329","cross_references":{"pubmed":["41194492"],"doi":["10.1002/advs.202513117"]}}