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Translational Medicine / 转化医学E3 Ligase Structures, Ubiquitin Biochemistry

Brenda Schulman

PhD

🏢Max Planck Institute of Biochemistry🌐Germany

Director, Department of Molecular Machines and Signaling

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👥Biography 个人简介

Brenda Schulman is a structural biologist who has revealed the atomic-level mechanisms of E3 ubiquitin ligase function, particularly the cullin-RING ligase (CRL) superfamily that constitutes the largest family of ubiquitin ligases and is frequently co-opted by cancer cells to degrade tumor suppressors. Her cryo-EM and crystallographic studies have shown how NEDD8 modification activates CRLs and how substrate adaptors recruit specific protein targets for ubiquitination. She has elucidated the mechanism of ubiquitin transfer from E2 enzymes to substrates through E3-mediated catalysis. Her structural insights are directly enabling rational design of molecular glues and PROTACs.

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🧪Research Fields 研究领域

E3 ubiquitin ligase structure
cullin-RING ligase mechanism
NEDD8 activation E3
ubiquitin transfer mechanism
structural biology protein degradation

🎓Key Contributions 主要贡献

Representative Works 代表性著作

📄Data Sources 数据来源

Last updated: 2026-04-01 | All information from publicly available academic sources

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