Hee‐Chul Ahn
Papers
1
Total Citations
59
H-Index
1
About
Dr. Hee‐Chul Ahn is a structural biologist whose work has fundamentally illuminated the molecular machinery of the ubiquitin-fold modifier 1 (Ufm1) system, a critical but less understood branch of the ubiquitin-like protein family. His landmark 2008 study, "Structural Basis for Ufm1 Processing by UfSP1" (59 citations), provided the first high-resolution view of how the Ufm1-specific protease UfSP1 cleaves the Ufm1 precursor to expose its active C-terminal glycine—a prerequisite for target conjugation. By solving the crystal structure of UfSP1 in complex with Ufm1, Dr. Ahn revealed a novel cysteine-protease fold and a unique substrate-recognition mechanism, establishing a paradigm for how this post-translational modification pathway is activated. This foundational work has been instrumental for subsequent studies linking Ufm1 dysregulation to endoplasmic reticulum stress, cancer, and developmental disorders. Dr. Ahn’s contributions have shaped our understanding of how cells deploy specialized proteases to control ubiquitin-like protein cascades, offering a molecular blueprint for therapeutic targeting in diseases where Ufm1 signaling goes awry.
Research Focus
Key Achievements
Top Papers
- 1Structural Basis for Ufm1 Processing by UfSP159 citations · 2008