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ProteomicsToward the quantitative characterization of arginine phosphorylations in Staphylococcus aureus
The Gram positive bacterium Staphylococcus aureus plays an important role as an opportunistic pathogen and causative agent of nosocomial infections. As research gained insight into host specific adaptation and a broad range of virulence mechanisms, S. aureus evolved as a model organism for human pat...
ORGANISM(S): Staphylococcus aureus 
2018-10-29 | PXD009874 | Pride
Virulence Silac quantification Staphylococcus aureus Amino acid metabolism Arginine phosphorylation Oxidative stress Phosphopeptide enrichment Hydrogen peroxide Spectral library Quantification 
ProteomicsComprehensive spectral library from the pathogenic bacterium Streptococcus pneumoniae with focus on phosphoproteins
In this study, a comprehensive spectral library for S. pneumoniae with an emphasis on phosphopeptide spectra was compiled. In total, 76% of the theoretical S. pneumoniae proteins were stored in a spectral library. Additionally, in combination with classical database search algorithms and the spectra...
ORGANISM(S): Streptococcus Pneumoniae D39 
MSV000084269 | MassIVE
ProteomicsAnalysis of the effect of ClpC1 directed antibiotics on ClpC1, ClpC2 and ClpC3 protein levels.
Ecumicin and Cyclomarin A (CymA) are known antimicrobial compounds that target the NTD of ClpC1. In proteomics analysis of compound treated M. smegmatis, two novel protein, ClpC2 and ClpC3, have been identified as strong interactors of those compounds in addition to ClpC1. In this study we used PRM ...
ORGANISM(S): Mycolicibacterium Smegmatis 
PXD037198 | panorama
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