Yigong Shi

This study identifies that phosphoantigen binding causes butyrophilin oligomers to dissociate, enabling Vγ9Vδ2 TCR engagement and activation of γδ T cells.

The paper identifies inhibitor-induced kinase destabilization as a common phenomenon and reveals that it occurs through endogenous proteolytic mechanisms rather than classical ubiquitination.

The paper reports cryo-EM structures of Arabidopsis thaliana AUX1 in IAA-bound and IAA-free states, revealing the molecular mechanism of auxin binding and transport.

The paper reveals a safety latch mechanism in the DNA-unbound MCM2-7 complex that blocks DNA entry and can be disrupted by mutations, leading to replication defects and DNA damage.

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

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

This study shows that Alzheimer's mutations stabilize harmful enzyme-substrate complexes in gamma-secretase, leading to synaptic loss rather than the released Aβ peptides being the primary cause.