Publications
(2023) Cytochrome P460 Cofactor Maturation Proceeds via Peroxide-Dependent Post-translational Modification. J Am Chem Soc. 145, 14404-14416
(2017) The cytotoxic Staphylococcus aureus PSMα3 reveals a cross-α amyloid-like fibril.. Science. 355, 831-833
(2016) Data publication with the structural biology data grid supports live analysis. Nat Commun. 7, 10882
(2023) De novo design of high-affinity binders of bioactive helical peptides. Nature. 10.1038/s41586-023-06953-1
(2021) De novo design of transmembrane β barrels.. Science. 10.1126/science.abc8182
(2023) De novo designed ice-binding proteins from twist-constrained helices. Proc Natl Acad Sci U S A. 120, e2220380120
(2025) De novo designed proteins neutralize lethal snake venom toxins. Nature. 10.1038/s41586-024-08393-x
(2021) De novo protein design by deep network hallucination. Nature. 10.1038/s41586-021-04184-w
(2007) Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex. Cell. 128, 533-46
(2014) Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport. Proc Natl Acad Sci U S A. 111, 4982-7
(2023) Decoupling peptide binding from T cell receptor recognition with engineered chimeric MHC-I molecules. Front Immunol. 14, 1116906
(2020) A defined structural unit enables de novo design of small-molecule-binding proteins. Science. 369, 1227-1233
(2015) Defining the mRNA recognition signature of a bacterial toxin protein. Proc Natl Acad Sci U S A. 112, 13862-7
(2009) Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine. Biochemistry. 48, 9174-84
(2022) Defining the structure-activity relationship for a novel class of allosteric MKP5 inhibitors. Eur J Med Chem. 243, 114712
(2017) Degradation of the BAF Complex Factor BRD9 by Heterobifunctional Ligands. Angew Chem Int Ed Engl. 56, 5738-5743
(2023) Depletion of creatine phosphagen energetics with a covalent creatine kinase inhibitor. Nat Chem Biol. 10.1038/s41589-023-01273-x

