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  • Title: Applications of diagonal chromatography for proteome-wide characterization of protein modifications and activity-based analyses.
    Author: Gevaert K, Impens F, Van Damme P, Ghesquière B, Hanoulle X, Vandekerckhove J.
    Journal: FEBS J; 2007 Dec; 274(24):6277-89. PubMed ID: 18021238.
    Abstract:
    Numerous gel-free proteomics techniques have been reported over the past few years, introducing a move from proteins to peptides as bits of information in qualitative and quantitative proteome studies. Many shotgun proteomics techniques randomly sample thousands of peptides in a qualitative and quantitative manner but overlook the vast majority of protein modifications that are often crucial for proper protein structure and function. Peptide-based proteomic approaches have thus been developed to profile a diverse set of modifications including, but not at all limited, to phosphorylation, glycosylation and ubiquitination. Typical here is that each modification needs a specific, tailor-made analytical procedure. In this minireview, we discuss how one technique - diagonal reverse-phase chromatography - is applied to study two different types of protein modification: protein processing and protein N-glycosylation. Additionally, we discuss an activity-based proteome study in which purine-binding proteins were profiled by diagonal chromatography.
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