Qi Hu

This study reveals the molecular mechanism of MEK1/2-catalyzed dual phosphorylation of ERK1/2 through cryo-EM structures and crosslinked complexes.

The paper introduces REAL-SWIT, a generative framework for ultra-large virtual screening that efficiently explores chemical space by generating molecules with favorable docking scores.

This paper introduces AFEX, a geometry-constrained framework for predicting active kinase domains, achieving high accuracy across the human kinome.

This paper develops a method to control RAS protein signaling by modulating palmitoylation through fusion with APT1 and the inhibitor ML348, enabling reversible subcellular localization changes.

This paper introduces ErePOC, a contrastive learning model for representing protein binding pockets, which improves DEL target selection by identifying shared characteristics and functional similarities.

The paper determines cryo-EM structures of human ACC1 in inactive and activated states, revealing structural dynamics and regulatory mechanisms.

This study uses an ABA-induced proximity system to reversibly control kinase signaling by recruiting phosphatases, revealing how phosphatases regulate oncogenic kinases like BCR::ABL1, BRAF(V600E), and MEK1.

The paper reports high-resolution cryo-EM structures of human PCC and MCC, revealing substrate binding modes and biotin coordination mechanisms.

The paper reports cryo-EM structures of DHHC9-GCP16 and Erf2-Erf4 complexes, revealing that GCP16 stabilizes DHHC9 and that phospholipid binding and specific palmitoylation are essential for catalytic activity.

The paper develops BRET-based biosensors for evaluating SARS-CoV-2 3CLpro inhibitors in BSL-2 labs, showing they correlate with known inhibitor activities.