| Literature DB >> 34311404 |
Timothy B Ware1, Ku-Lung Hsu2.
Abstract
Advancements in chemical proteomics and mass spectrometry lipidomics are providing new opportunities to understand lipid kinase activity, specificity, and regulation on a global cellular scale. Here, we describe recent developments in chemical biology of lipid kinases with a focus on those members that phosphorylate diacylglycerols. We further discuss future implications of how these mass spectrometry-based approaches can be adapted for studies of additional lipid kinase members with the aim of bridging the gap between protein and lipid kinase-focused investigations.Entities:
Keywords: Activity-based protein profiling; Chemical proteomics; Diacylglycerol; Kinase; Kinome; Lipid; Lipidomics; Mass spectrometry; Phosphatidic acid; Phosphoinositide; Phosphorylation; Signaling; SuFEx; SuTEx; Sulfonyl fluorides; Sulfonyl triazoles
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Year: 2021 PMID: 34311404 PMCID: PMC8671151 DOI: 10.1016/j.cbpa.2021.06.007
Source DB: PubMed Journal: Curr Opin Chem Biol ISSN: 1367-5931 Impact factor: 8.822