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Quantitative assessment of post-translational modifications in proteins by mass spectrometry often requires the consideration of the alteration in ionization efficiency of peptides induced by the modification.
MGO is known to induce aggregation and structural modifications in proteins through cross-linking and formation of chemical adducts [7], [8].
Antioxidant redox systems and antioxidant enzymes neutralize ROS, but oxidative stress may induce posttranslational modifications in proteins modulating ROS activities.
Based on the known reactivity of α,β-unsaturated aldehydes, the major modifications in proteins due to these aldehydes are likely through Michael addition, with the main nucleophilic targets being cysteine, histidine, and lysine residues.
The exponential increase in genome sequences and the experimental characterization of a large number of amino acid modifications in proteins has created a bottleneck in connecting known PTMs to the genes catalyzing them (4).
This reactivity has been exploited previously in the chemical modification of thiostrepton, the mapping of Ser/Thr modifications in proteins, the design of solid-phase capture resins, and the identification of lanthipeptides.
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We have developed an integrated bioinformatics resource, which consolidated and mapped all currently available information on genetic modifications in protein kinase genes with sequence, structure and functional data.
The ModFinder module provides new methods to identify and classify protein modifications in protein 3D structures.
Moreover, in contrast to CMV, modifications in protein metabolism were not affected by PSV duration.
Accurately identifying modifications in protein sequences is a critical first step for PTM profiling, and thus our approach may benefit routine proteomic analysis.
Although alterations/ post translational modifications in protein expression have been extensively quantified, complementary analysis of nuclear membrane proteome changes have been limited.
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