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- W2026494112 endingPage "1392" @default.
- W2026494112 startingPage "1383" @default.
- W2026494112 abstract "Signaling proteins are usually composed of one or more conserved structural domains. These domains are usually regulatory in nature by binding to specific activators or effectors, or species that regulate cellular location, etc. Inositol-specific mammalian phospholipase C (PLC) enzymes are multidomain proteins whose activities are controlled by regulators, such as G proteins, as well as membrane interactions. One of these domains has been found to bind membranes, regulators, and activate the catalytic region. The recently solved structure of a major region of PLC-β2 together with the structure of PLC-δ1 and a wealth of biochemical studies poises the system towards an understanding of the mechanism through which their regulations occurs." @default.
- W2026494112 created "2016-06-24" @default.
- W2026494112 creator A5032136628 @default.
- W2026494112 creator A5078222862 @default.
- W2026494112 date "2007-07-01" @default.
- W2026494112 modified "2023-10-16" @default.
- W2026494112 title "Stimulation of phospholipase Cβ by membrane interactions, interdomain movement, and G protein binding — How many ways can you activate an enzyme?" @default.
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- W2026494112 doi "https://doi.org/10.1016/j.cellsig.2007.04.006" @default.
- W2026494112 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1963342" @default.
- W2026494112 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17524618" @default.
- W2026494112 hasPublicationYear "2007" @default.
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