J. V. Olsen

The paper uses multi-layered proteomics to show insulin increases EphA2 via ERK pathway, independent of insulin resistance, and dependent on low IGF1R levels.

One-Tip provides a proteomics method for high-depth protein identification from minimal cell samples and single zygotes with high throughput.

This study uses enamel proteomics to determine biological sex and assess intraspecific variation in Paranthropus robustus from South Africa, supporting the idea that morphological variation may reflect taxonomic diversity.

This study identifies Matrix Gla Protein (MGP) as a driver of stemness and tumor initiation in ovarian cancer by promoting Hedgehog signaling and enhancing tumor-initiating capacity.

This study optimizes linear ion trap data independent acquisition for single-cell proteomics, showing quantitative accuracy down to 0.5 ng on column using LIT-based libraries from as few as 40 cells.

The paper shows that loss of Nt-acetylation in yeast leads to unstable ribosomal proteins and increased turnover.

This study identifies Amisulpride as a potential therapeutic for arthritis by reducing synovial fibroblast activation, independent of its known targets.

This study identifies PRMT5-mediated arginine methylation of RIPK3 as a feedback mechanism regulating RIPK1 activity and function in cell death pathways.

SPIN is a proteomics workflow that rapidly identifies over 150 mammalian species from samples using mass spectrometry, demonstrating effectiveness on degraded archaeological materials.

This study shows that GHB stabilizes the CaMKII hub domain, providing neuroprotection in cellular and mouse models.

This study identifies proteome and phosphoproteome changes associated with AML relapse using patient samples and validates them with kinase inhibitors.

This paper introduces a DIA-based phosphoproteomics method that achieves high sensitivity and reproducibility without spectral libraries, demonstrating its scalability in analyzing kinase inhibitor effects on EGF signaling.

The paper introduces a proteomics sample preparation method using protein aggregation on microparticles, demonstrating its applicability to various proteomic analyses.

The paper determines the mass resolution limits for resolving TMT reporter ions with 0.0063 Da mass differences using an Orbitrap mass spectrometer.

The paper introduces a novel LC system for proteomics that enables rapid, high-throughput, and robust analysis with deep proteome coverage.