Philip M. Remes

This study revisits resonance-excitation collision-induced dissociation (reCID) for DIA proteomics, showing it can achieve performance comparable to HCD with optimized settings and libraries.

The paper develops scalable targeted proteomics assays using the Stellar mass spectrometer for analyzing biofluids, demonstrating high sensitivity and multiplexing capabilities.

This paper evaluates a prototype Orbitrap Astral Zoom mass spectrometer for quantitative proteomics, showing improved performance in ion detection and quantitative precision compared to the standard Orbitrap Astral MS.

The paper develops and evaluates a multiplexed PRM-MS assay for quantifying plasma proteins in an IBD cohort, demonstrating high quantifiability and consistent data acquisition.

The paper introduces a novel hybrid mass spectrometer, Stellar MS, enabling rapid and sensitive clinical biomarker validation using 15N labeled proteins.

This paper demonstrates that a quadrupole-ion trap instrument can perform multiplexed shotgun proteomics with accuracy comparable to a dedicated tribrid instrument, offering a cost-effective alternative.

The paper develops a workflow for targeted proteomics using a hybrid quadrupole-linear ion trap instrument, demonstrating consistent quantification without high-mass accuracy.

The paper introduces a new MS platform with enhanced acquisition rates and real-time chromatogram alignment, enabling high multiplex targeted proteomics with improved sensitivity and throughput.

This paper introduces a dynamic DIA mass spectrometry method that improves quantitative sensitivity by adjusting MS/MS windows during chromatographic separation.