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- W3113044304 endingPage "261" @default.
- W3113044304 startingPage "248" @default.
- W3113044304 abstract "The set of all intra- and intermolecular interactions, collectively known as the interactome, is currently an unmet challenge for any analytical method, but if measured, could provide unparalleled insight on molecular function in living systems. Developments and applications of chemical cross-linking and high-performance mass spectrometry technologies are beginning to reveal details on how proteins interact in cells and how protein conformations and interactions inside cells change with phenotype or during drug treatment or other perturbations. A major contributor to these advances is Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR-MS) technology and its implementation with accurate mass measurements on cross-linked peptide-pair precursor and fragment ions to enable improved identification methods. However, these applications place increased demands on mass spectrometer performance in terms of high-resolution spectral acquisition rates for on-line MSn experiments. Moreover, FT-ICR-MS also offers unique opportunities to develop and implement parallel ICR cells for multiplexed signal acquisition and the potential to greatly advance accurate mass acquisition rates for interactome studies. This review highlights our efforts to exploit accurate mass FT-ICR-MS technologies with chemical cross-linking and developments being pursued to realize parallel MS array capabilities that will further advance visualization of the interactome." @default.
- W3113044304 created "2020-12-21" @default.
- W3113044304 creator A5008424956 @default.
- W3113044304 creator A5016223830 @default.
- W3113044304 creator A5024181058 @default.
- W3113044304 creator A5080205665 @default.
- W3113044304 date "2020-12-08" @default.
- W3113044304 modified "2023-10-13" @default.
- W3113044304 title "Applications and advancements of FT‐ICR‐MS for interactome studies" @default.
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- W3113044304 doi "https://doi.org/10.1002/mas.21675" @default.