3.8 Article

Experimental methods for dissecting the terraincognita of protein-metabolite interactomes

Journal

CURRENT OPINION IN SYSTEMS BIOLOGY
Volume 28, Issue -, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.coisb.2021.100403

Keywords

ation mass spectrometry; Mass spectrometry

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The interaction between metabolites and proteins is complex and highly dynamic, playing crucial roles in cellular processes. Advances in omics technologies have enabled global profiling of these interactions, but significant challenges remain, including incomplete chemical characterization of metabolomes.
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.

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