Ryan A. Mehl

This study shows phosphorylation of IGF2BP1 and IGF2BP3 at a conserved serine acts as a configurational switch, altering their RNA binding domain arrangements and affecting mRNA regulation.

This paper introduces a genetic code expansion method to integrate a fluorophore-quencher pair into proteins for monitoring dynamics, demonstrating applications in studying protein function and drug screening.

The paper provides methods for site-specific post-translational modification of alpha-synuclein and tau using genetic code expansion and enzymatic approaches, enabling studies of their structural dynamics and aggregation.

This study develops a highly reactive and stable tetrazine amino acid for site-specific protein labeling, demonstrating improved encoding and ligation efficiency.

This paper introduces an in-cell method to evaluate E3 ligases for targeted protein degradation by conjugating neo-substrates via click chemistry.

This paper develops two orthogonal strategies to label TRPV1 on the cell surface with minimal functional perturbation, enabling tracking of its expression and mobility.

This study uses single-molecule techniques to show that RPA partially wraps ssDNA and that phosphorylation at Ser-384 modulates this wrapping.

The paper develops a system to autonomously produce phosphorylated proteins in E. coli, demonstrating that non-hydrolyzable phosphoserine mimics phosphoserine function in three biological contexts.

This paper introduces a method to site-specifically encode and label two noncanonical amino acids in proteins, enabling dual modification in living cells.