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- W3208282133 abstract "A single metabolite can have diverse biological functions, from biosynthetic intermediates to signaling molecules that binds to one or more proteins. Similarly, a single protein can interact with one or many different metabolites. The extensive and highly dynamic protein-metabolite interaction network affects and shapes all cellular processes. Recent progress in omics technologies has made global profiling of protein-metabolite interaction feasible. Herein, we aim to highlight experimental approaches developed to characterize protein-metabolite interactomes, with particular emphasis on co-fractionation mass spectrometry. We will also discuss remaining grand challenges, including the largely incomplete chemical characterization of metabolomes." @default.
- W3208282133 created "2021-11-08" @default.
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- W3208282133 date "2021-12-01" @default.
- W3208282133 modified "2023-10-14" @default.
- W3208282133 title "Experimental methods for dissecting the terraincognita of protein-metabolite interactomes" @default.
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- W3208282133 doi "https://doi.org/10.1016/j.coisb.2021.100403" @default.
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