N. A. Burgess-Brown

The paper determines the structure of the SIT1 proline transporter complexed with ACE2 using cryo-EM, revealing substrate specificity and structural changes related to transport and a disease-causing mutation.

The paper reports the structure of the human ELOVL7 elongase, revealing its catalytic mechanism and substrate-binding sites, with implications for inhibiting VLCFA accumulation in diseases.

The paper introduces a method to identify, map, and quantify SARS-CoV-2 Spike glycopeptides using mass-retention time fingerprinting with LC-TOF mass spectrometry.

This study challenges the established order of prelamin A processing by ZMPSTE24, showing that SY^LL cleavage occurs first and independently of C-terminal modifications.

The paper uses a scFv to solve the structure of SP140's PHD-bromodomain and suggests strategies to improve scFvs as crystallization chaperones.

This study identifies TMEM16K as an ER-resident calcium-regulated lipid scramblase and elucidates its structural basis for lipid scrambling and inactivation.

This paper determines the structures of DPAGT1 with substrates and inhibitors, revealing catalytic mechanisms and disease-causing mutations, and designs non-toxic antibiotics for tuberculosis.