Jason A. McAlister

Adaptive Focused Acoustics-integrated proteome profiling of macrophages uncovers low abundant proteins associated with immune homeostasis, inflammatory response, and transport

This study evaluates adaptive focused acoustics (AFA) technology for macrophage lysis and proteomics, showing improved proteome coverage, reproducibility, and detection of low-abundance immune proteins.

Recently emerged Fusarium chemotypes reprogram wheat defence and detoxification networks during Fusarium head blight development

This study shows that new Fusarium chemotypes reprogram wheat defense networks, altering detoxification and defense responses, and identifies chemotype-specific evasion of host defenses.

Mycotoxin-driven proteome remodeling reveals limited activation of Triticum aestivum responses to emerging chemotypes integrated with fungal modulation of ergosterols

This study examines proteome changes in wheat and Fusarium graminearum in response to 15ADON/3ANX mycotoxins, identifying chemotype-specific proteins and fungal virulence factors.

Whole blood proteome dynamics defines predictive diagnostic and prognostic signatures of cryptococcal infection

Global proteomic analysis of Cryptococcus neoformans clinical strains reveals significant differences between latent and lethal infection

This study compares proteomic profiles of Cryptococcus neoformans clinical strains to identify differences between latent and lethal infections.

Spatiotemporal dynamics of cryptococcal infection reveal novel immune modulatory mechanisms and antifungal targets

This study uses mass spectrometry to analyze proteome changes in three organs during Cryptococcus neoformans infection, identifying new immune modulatory mechanisms and antifungal targets.

ProteoPlotter: an executable proteomics visualization tool compatible with Perseus

ProteoPlotter is a visualization tool for proteomics data that complements Perseus, offering enhanced features for data analysis and interpretation.

HEPN-AbiV is an RNase in the antiphage system AbiV

This study identifies AbiV as an RNase in the bacterial antiphage system AbiV, revealing its structure, function, and mechanism of action.