Yu Feng

This study uses AlphaFold 3 to identify and characterize phage proteins that inhibit bacterial transcription, revealing novel mechanisms of action.

This study determines the cryo-EM structure of the DosR-dependent transcriptional activation complex in Mtb and identifies its molecular mechanism for dormancy regulation.

This study presents cryo-EM structures of Mor-TAC and C-TAC complexes, revealing a tetrameric binding mode and interactions with RNAP, elucidating the transcription activation mechanism of phage Mor/C family activators.

This study determines cryo-EM structures of PhoP-dependent transcription complexes in Mtb to elucidate its dual role as activator and repressor in stress adaptation.

The paper reports cryo-EM structures of E. coli intrinsic termination complexes to define the structural mechanism of bacterial transcription termination.

This study reports crystal structures of ECF-sigma-factor-dependent transcription initiation complexes in Mycobacterium tuberculosis, revealing conserved interactions with RNAP and promoter DNA.

This study reports crystal structures of Mycobacterium tuberculosis RNA polymerase with and without antituberculosis drugs, revealing a new class of inhibitors and their binding mechanisms.