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Using a quantitative proteome approach based on isobaric tagging, we obtained protein profiles from cells grown on each carbon source.
The purpose of this study is to understand the comprehensive proteome responses occurring during natural interactions between C. albicans and macrophages using a quantitative proteome analysis.
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Here we have used a quantitative proteomics approach to compare the proteomes of healthy and P. larvae-infected A. mellifera larvae, leading to the discovery that the infected state is associated with an elevated expression of immunity proteins, chaperones, certain metabolic proteins with an accelerated consumption of energy stores.
Using a quantitative whole cell proteomics approach combined with multidimensional protein identification technology (MuDPIT) mass spectrometry), we found that σ32-I54N σ32-I54Non producexpressionike transcriproducedy remodeled proteostasis network without perturbing the majoritranscriptionallyous cellularemodelede.
We analyzed an ex vivo model of in situ aged human dermal fibroblasts, obtained from 15 adult healthy donors from three different age groups using an unbiased quantitative proteome-wide approach applying label-free mass spectrometry.
Triplicate analyses were performed for each sample in three independent experiments, and the collected data were reviewed for protein identification and quantification in a quantitative proteome analysis.
To clarify the mechanisms of hemicelluloses and pectin recognition and metabolism, we carried out a quantitative proteome analysis of C. cellulovorans cultured with these substrates.
In total, we identified 734 proteins using our "intracellular" quantitative proteome analysis, and we were able to identify substrate-specific proteins using statistical analysis.
We used the quantitative proteome set that was reported recently [ 15].
PBM total proteins were extracted using a complete proteome extraction mammalian kit (Calbiochem Catalog No. 539779).
Five different proteomes were analyzed and compared using a MS-based quantitative proteomics approach by 18O/16O stable isotope labeling.
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