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.

This paper introduces cryoPROS, an AI method to address preferred orientation in cryo-EM, improving resolution without special experimental techniques.

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.

This study identifies two double mutations in SARS-CoV-2 3CLpro that confer resistance to the non-covalent inhibitor WU-04 and reveals trade-offs between catalytic activity, thermostability, and drug resistance.

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.