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- W596475673 startingPage "117" @default.
- W596475673 abstract "Type 1 and 2A protein phosphatases (PPases) account for the majority of enzyme activity dephosphorylating phospho-serine and -threonines in living cells. Their action is opposed to that of a large number of serine/threonine protein kinases. In recent years, the enigma of how the action of many protein kinases is reversed by a limited number of protein phosphatases in a regulated manner has been solved by a combination of biochemical and molecular cloning procedures: Both PP1 and PP2A were found to exist as multimeric holoenzymes in vivo, where a limited number of catalytic subunits are complexed to a vast number of regulatory subunits. The latter are now considered to be the determinants of substrate specificity and intracellular localization of the catalytic subunits (1,2)." @default.
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- W596475673 date "1998-01-01" @default.
- W596475673 modified "2023-10-16" @default.
- W596475673 title "Microinjection and Immunological Methods in the Analysis of Type 1 and 2A Protein Phosphatases from Mammalian Cells" @default.
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- W596475673 doi "https://doi.org/10.1385/0-89603-468-2:117" @default.
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