bioRxivBioinformaticsPreprint
ELiAH2: update of the atlas of E3 ligases in human tissues by integrating tissue-specificity and docking properties of ligands for targeted protein degradation
서상재, Seunghun Song, Younghoon Kim, Moon Ki KimiD, Hyeonjae LeeiD, Hyojung PaikiD
Abstract
Targeted protein degradation (TPD), including proteolysis-targeting chimeras (PROTACs), requires coordinated selection of E3 ligases, target proteins, and ligands to achieve efficient and tissue-selective degradation. However, current TPD resources provide limited support for integrating tissue-specific transcriptomic evidence with structural compatibility during early candidate prioritization. Here, we present ELiAH2, an expanded database for transcriptome- and structure-guided prioritization of TPD candidates. ELiAH2 integrates GTEx RNA-seq profiles across 24 human tissues to characterize tissue-specific expression patterns of E3 ligases and target genes. Compared with the previous version, ELiAH, current update presented over 200% of expansion for the number of covered tissues and samples. Previously, E3 ligase-target gene associations were inferred using mutual information-based network analysis, enabling users to explore transcriptomic relationships. To further support structural evaluation, ELiAH2 provides large-scale docking datasets comprising 827,385 E3 ligase-target protein pairs and 7,800,521 protein-ligand docking models, including E3 ligase-ligand and target protein-ligand interactions. Docking scores, ranked interaction tables, gene and ligand identifiers, and downloadable PDB structures are incorporated into the web interface. By combining tissue specificity, E3-target association, protein-protein docking, and protein-ligand docking, ELiAH2 provides a comprehensive resource for narrowing the TPD search space and supporting rational degrader design. ELiAH2 is freely available at https://eliahdb.org.
- Citations
- 0
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- ELITE: E3 Ligase Inference for Tissue specific Elimination: A LLM Based E3 Ligase Prediction System for Precise Targeted Protein Degradation
Sabyasachi Patjoshi, Sumit Madan, Holger Fröhlich·bioRxiv·Nov 5, 2025
- E3-specific degrader discovery by dynamic tracing of substrate receptor abundance
Alexander Hanzl, Eleonora Barone, … Georg E. Winter·Journal of the American Chemical SocietyPeer-reviewed·Jan 5, 2023
- Identification of actionable targeted protein degradation effector sites through Site-specific Ligand Incorporation-induced Proximity (SLIP)
Zhangping Xiao, Efthymios-Spyridon Gavriil, … Edward W. Tate·Journal of the American Chemical SocietyPeer-reviewed·Jun 10, 2025
- Targeted Protein Degradation by KLHDC2 Ligands Identified by High Throughput Screening
Han Zhou, Tonglian Zhou, … Michael J. Bollong·bioRxiv·Mar 31, 2025
- An in-cell approach to evaluate E3 ligases for use in targeted protein degradation.
Yunan Zheng, Anamika Singh, … Ryan A. Mehl·Journal of the American Chemical SocietyPeer-reviewed·Jun 10, 2025
- A CRISPR activation screen identifies FBXO22 as an E3 ligase supporting targeted protein degradation
A. A. Basu, C. Zhang, … X. Zhang·bioRxiv·Sep 15, 2023