First post from the Wang Lab

We will start a new experiment by asking students and postdocs to write blogs/previews for recent papers. This would be a good practice for their critical thinking and writing skills.

Here is a pretty good eBook "English Communication for Scientists" by Dr. Jean-luc Doumont.

I hope all the trainees in the lab will not only know how to do science but also learn how to communicate their science.

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Multiple Postdoc and Technician Positions Available at Baylor College of Medicine

Multiple postdoc and technician positions are available in Dr. Jin Wang’s group in the Department of Pharmacology and Chemical Biology at Baylor College of Medicine (BCM). BCM is located in the world largest medical center and has access to enormous biomedical resources. The research in the Wang lab is highly interdisciplinary and translational. The Wang lab has both chemistry and biology operations. For chemistry work, we have 17 chemical fume hoods, 4 ISCO combiflash chromatography systems, Agilent analytical LC-MS, Agilent preparative HPLC with auto-purification, and Genevac high throughput solvent evaporation, along with convenient access to 600 and 800 MHz NMR. For biology work, we have common equipment for biochemistry, molecular and cell biology, including tissue culture hoods, RT-PCR, plate reader, and imaging plate reader, and perform animal work to evaluate the efficacy of the experimental therapeutics developed in the group. In addition, we recently acquired a state-...

Lysine-Targeted Covalent Inhibitors Gaining Traction

In the past decade, targeted covalent inhibitors (TCIs) has experienced a resurgence due to its sustained target engagement and improved proteome-wide selectivity. Currently, targeting cysteine residues with acrylamides and other α, β-unsaturated carbonyl compounds is the predominant strategy in TCI development. Although lysine is more prevalent than cysteine and possesses lower mutation rates, lysine has been much less frequently considered and more challenging as a residue targeted by TCIs due to its low nucleophilicity. Recently, Jack Taunton and his colleagues reveled their two related work in JACS . Based on the co-crystal structure of Hsp90 with a reversible inhibitor PU-H71, they designed two arylsulfonyl fluorides 1 and 2 and co-incubated them with Hsp90 protein (Figure 1a, b). Mass spectrometry detected the formation of a 1:1 covalent adduct. Mutation of Lys58 to arginine abrogated the covalent modification, indicating that the TCI selectively modified Lys58 (Fig...

An Unprecedented Covalent Binding Mechanism of ML210 to GPX4

GPX4 is a selenoprotein that plays a critical role in protecting cells against oxidative stress and ferroptosis. The nucleophilic selenocysteine residue (Sec) located in the catalytic center of GPX4 can be exploited to design covalent inhibitors. Previously reported covalent GPX4 inhibitors always contain reactive alkyl chloride groups, conferring poor selectivities. Recently, the Schreiber group reported that ML210 , a direct covalent inhibitor targeting GPX4 in cells, exhibits much more potency and remarkable selectivity compared with chloroacetamide inhibitors. More interestingly, an unprecedented covalent binding mechanism is involved in the ML210 targeting GPX4 in cells. ML210 was previously reported as a ferroptosis inducer. Due to lack of an apparent covalent reactive group and inability to react with small molecule thiols directly, the covalent binding action of ML210 with its target proteins has never been disclosed. To identify that ML210 acts as a direct covalent ...

Quantitative Chemical Biology

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