Research

Proteomics methods for structurally- and functionally-resolved biology

My research sits at the intersection of mass spectrometry, structural biology, systems biology, and computational method development. During my Ph.D. I used cross-linking mass spectrometry to map protein structure and interactions directly; as a postdoctoral researcher at Columbia, I’ve moved toward quantitative and clinical proteo(geno)mics to understand disease biology. Throughout, we have continued to develop methods and tailor our approaches to the questions we want to answer — building the analytical tools and software that let a mass spectrometry dataset say more than just “up” or “down.”

Current Research

Splicing Factor Mutations & the Leukemia Proteome

Mapping how SF3B1, U2AF1, and SRSF2 mutations remodel the leukemia cell proteome, down to the specific novel splice-junction peptides responsible, using DIA-MS and a three-tier differential-usage framework I built.

Nuclear RNA Surveillance, Ribotoxic Stress & the Cell Proteome

What happens to the proteome when the RNA exosome’s surveillance cofactor Mtr4 is lost: exosome collapse, translational repression, and an isoform-resolved switch implicating activation of the ribotoxic stress response.

Proteomics for a Multiomic Alzheimer’s Disease Cohort

Documenting the DIA-based quantification methodology behind a 500-participant CSF proteomics dataset and profiling plasma from a cohort subset, within a 1,000-person multiomic Alzheimer’s disease study led by the Mayeux group.

Past Research

Structural Proteomics by Crosslinking Mass Spectrometry

Ph.D. research at the University of Victoria developing and applying cross-linking mass spectrometry to study chaperone mechanism, intrinsically disordered proteins, and pathogen structural biology.

For a complete list of publications, see my Google Scholar profile or ORCID record. A full CV is available as a PDF.