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Science's STKE, 2005
Ci-VSP, a recently described protein with sequence similarity to both the voltage-sensing domain of a voltage-gated potassium channel and the phosphatase PTEN, functions as a transmembrane phosphoinositide phosphatase that is regulated by changes in voltage across the plasma membrane.
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Ci-VSP, a recently described protein with sequence similarity to both the voltage-sensing domain of a voltage-gated potassium channel and the phosphatase PTEN, functions as a transmembrane phosphoinositide phosphatase that is regulated by changes in voltage across the plasma membrane.
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Current Opinion in Structural Biology, 1995
Protein phosphatases are signal transducing enzymes that dephosphorylate cellular phosphoproteins. The recently determined crystal structures of protein tyrosine and serine/threonine phosphatases reveal that these proteins adopt distinct structures and catalyze dephosphorylation reactions by means of different enzymatic mechanisms.
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Protein phosphatases are signal transducing enzymes that dephosphorylate cellular phosphoproteins. The recently determined crystal structures of protein tyrosine and serine/threonine phosphatases reveal that these proteins adopt distinct structures and catalyze dephosphorylation reactions by means of different enzymatic mechanisms.
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N -Phosphoarginine Phosphatase (17 kDa) and Alkaline Phosphatase as Protein Arginine Phosphatases
Journal of Biochemistry, 1996Seven synthetic polymers, (Glu4, Tyr)n, (Arg)n, (Arg, Pro, Thr)n, (Arg-Gly-Glu)6, (Arg-Gly-Phe)6, (Glu-Arg-Gly-Phe)5, and (Ala-Leu-Arg-Arg-Ile-Arg-Gly-Glu-Arg)2, were treated with phosphoryl chloride to phosphorylate their Tyr, Thr, and Arg residues. Protamines and histones were phosphorylated similarly.
A, Kumon +4 more
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Pathogen protein modularity enables elaborate mimicry of a host phosphatase
Cell, 2023Yi Zhai, Frank L H Menke, Wenbo
exaly

