Overall, the future of oncoproteomics holds enormous potential for translating technologies from the bench to the bedside. The proteome encompasses the entire set of proteoforms present at a certain time in a cell, tissue, or individual in a given biological setting. Proteomics includes the assessment of global protein abundance, proteoform levels, spatial conformations, chemical modifications, cellular localization, proteoform functions, cofactors, and interacting partner networks. In the field of proteomics, there has been a paradigm change from protein expression to proteoform abundance from the genome. The variations in protein product may result from genetic changes, mutations, transcriptional variations, RNA splicing, translational error, protein folding, proteolytic cleavage of a signal peptide, or a myriad of post-translational modifications (PTMs). This yields a variety of protein products relative to the canonical form. These diverse molecular forms of a protein product of a single gene are termed ‘proteoforms’. Proteoforms can, therefore, act as the ultimate long-range functional effectors of a gene and increase the structural and functional diversity of the proteome.Įach proteoform has a specific subcellular location, where it interacts with surrounding molecules and may form a complex to carry out a specific biological function, and consequently have important effects at the system level. Further, the extensive temporal dynamic range of the proteoforms adds complexity to proteome analysis. Innovative and progressive proteomic technologies are needed for large-scale analysis of these broad-range processes. The physiological and pathological processes may have a varying abundance of a particular proteoform and may exhibit changes in localization or response to stimuli, which makes them highly relevant to intervention and drug discovery in various diseases.
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