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The phosphatase mechanism of bifunctional kinase/phosphatase AceK
Chem. Commun., 2014Through multiple approaches, we identified a novel stepwise mechanism of AceK which is ADP-dependent, enabled by a typical kinase scaffold.
Shu, Wang +5 more
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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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2015
Reversible protein phosphorylation is an essential posttranslational modification mechanism executed by opposing actions of protein phosphatases and protein kinases. About 1,000 predicted kinases in Arabidopsis thaliana kinome predominate the number of protein phosphatases, of which there are only ~150 members in Arabidopsis.
Alois, Schweighofer, Irute, Meskiene
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Reversible protein phosphorylation is an essential posttranslational modification mechanism executed by opposing actions of protein phosphatases and protein kinases. About 1,000 predicted kinases in Arabidopsis thaliana kinome predominate the number of protein phosphatases, of which there are only ~150 members in Arabidopsis.
Alois, Schweighofer, Irute, Meskiene
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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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Phosphatases and tumorigenesis
Current Opinion in Oncology, 1998Phosphatases are regulatory enzymes that antagonize the action of kinases within the cell. An understanding of the contribution of kinases to cancer has emerged during the past two decades; however, our understanding of phosphatases in cancer has lagged behind.
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