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Recent progress in mass spectrometry and ‘omics’ technologies enable links to be made between the incorporation of proteoforms and their impact upon the structure, function, and cellular location of multiprotein assemblies. We focus this review on two of the most prevalent modifications, namely phosphorylation and glycosylation, and relate these to the properties of protein complexes. In so doing, we highlight how native mass spectrometry serves as a hub to connect ‘omics’ approaches to endogenous protein complexes, thus aiding our understanding of the origin, regulation, and control of multiprotein assemblies.

Original publication




Journal article


Trends in Chemistry

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