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Zhaomin Liu

Researcher at University of Michigan

Publications -  6
Citations -  706

Zhaomin Liu is an academic researcher from University of Michigan. The author has contributed to research in topics: Protein degradation & Proteolysis targeting chimera. The author has an hindex of 5, co-authored 6 publications receiving 343 citations.

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A Potent and Selective Small-Molecule Degrader of STAT3 Achieves Complete Tumor Regression In Vivo

TL;DR: SD-36 achieves complete and long-lasting tumor regression in multiple xenograft mouse models at well-tolerated dose schedules and is a promising cancer therapeutic strategy.
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Discovery of ERD-308 as a Highly Potent Proteolysis Targeting Chimera (PROTAC) Degrader of Estrogen Receptor (ER).

TL;DR: This work describes the design, synthesis, and extensive structure-activity relationship (SAR) studies of small-molecule ERα degraders based on the proteolysis targeting chimeras (PROTAC) concept, and finds ERD-308 induces more complete ER degradation than fulvestrant, the only approved selective ER degrader (SERD).
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Structure-Based Discovery of SD-36 as a Potent, Selective, and Efficacious PROTAC Degrader of STAT3 Protein.

TL;DR: SD-36 is a potent, selective and efficacious STAT3 degrader based upon the proteolysis targeting chimera (PROTAC) concept and achieves nanomolar cell growth inhibitory activity in leukemia and lymphoma cell lines with high levels of phosphorylated STAT3.
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Simple Structural Modifications Converting a Bona fide MDM2 PROTAC Degrader into a Molecular Glue Molecule: A Cautionary Tale in the Design of PROTAC Degraders.

TL;DR: This study provides the first example that simple structural modifications can convert a bona fide PROTAC degrader into a molecular glue compound, which has a completely different mechanism of action.
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Discovery of M-808 as a Highly Potent, Covalent, Small-Molecule Inhibitor of the Menin–MLL Interaction with Strong In Vivo Antitumor Activity

TL;DR: Determination of the co-crystal structure of M-808 in complex with menin provides a structural basis for their high-affinity, covalent interactions and represents a promising,covalent menin inhibitor for further optimization and evaluation.