Mingxing Teng
Baylor College of Medicine, TX·Pharmacology
Most drugs work by blocking a protein's activity, which only helps if the protein has a convenient pocket to block. An alternative is to destroy the protein instead.
- Fields
Pharmacology
Biochemistry
Chemistry
- Topics
cereblon
E3 ubiquitin ligase
molecular glue degraders
- Grants
- 1 known grant, through Jul 2030
What they work on
- Build a comprehensive atlas of the cereblon interactome spanning canonical G-loop degron proteins, mutant G-loop variants and hidden non-G-loop targets, extending bioinformatic predictions already covering 2,458 candidate proteins.
- Validate uncharted predicted proteins as genuine cereblon interactors by testing whether novel molecular glue degraders recruit them to the CRL4CRBN E3 ubiquitin ligase for degradation.
- Develop a degradation-activity-first discovery route in which protein-protein docking guides rational design and screening of candidate molecular glue degraders against prioritized G-loop targets.
- Establish an unbiased, binding-first screening route using a DNA-encoded chemical library to find compounds that stabilize the ternary complex of glue, cereblon and neosubstrate.
More about the research
Certain drugs bind a human protein called cereblon, part of a cellular machine that tags unwanted proteins for disposal, and reshape its surface so it grabs proteins it would never normally touch, sending them to the cell's shredder. Drugs that work by gluing two proteins together this way are called molecular glue degraders. The problem is that no one knows the full list of proteins cereblon can be made to grab, so new ones have mostly turned up by accident.
Why it matters
Many disease-driving proteins, including wild-type proteins without druggable pockets and mutant proteins that resist existing inhibitors, are considered undruggable. A comprehensive map of what cereblon can be induced to degrade, paired with efficient methods for finding the matching molecular glues, could supply chemical tools for studying those proteins and a starting point for designing new degrader drugs.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Jaewon Chang
Emory University, GA·Chemistry
Design and synthesize covalent warheads that react with lysine, tyrosine and serine residues on E3 ubiquitin ligases, the enzymes that tag proteins for destruction, going beyond the cysteine-reactive chemistry used so far.
Qiaobing Xu
Tufts University, MA·Biomedical Engineering
Covalently attach a ligand that binds the target protein onto an E3 ligase-related protein, creating a two-part degrader that avoids the PROTAC hook effect.
Juan Hu
San Diego State University, CA·Chemistry·Early-career
Screen DNA-encoded combinatorial libraries, in which each compound carries an identifying DNA barcode, with a droplet-scale permeation assay to find cyclic peptides that efficiently cross membrane bilayers.
The school
Baylor College of Medicine: 38 labs on PI Pages, $881M a year on research, 115 research doctorates a year.
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