Results 221 to 230 of about 94,811 (247)
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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.
Hongwei Tan +6 more
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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.
Irute Meskiene, Alois Schweighofer
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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.
Irute Meskiene, Alois Schweighofer
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Cold Spring Harbor Protocols, 2020
Several types of alkaline phosphatases (or alkaline phosphomonoesterase) are commonly used in molecular cloning, including bacterial alkaline phosphatase (BAP) and calf intestinal alkaline phosphatase (CIP, CIAP, or CAP). Similar enzymes isolated from more esoteric cold-blooded organisms (e.g., SAP from shrimp) have become available in recent years and
Michael R, Green, Joseph, Sambrook
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Several types of alkaline phosphatases (or alkaline phosphomonoesterase) are commonly used in molecular cloning, including bacterial alkaline phosphatase (BAP) and calf intestinal alkaline phosphatase (CIP, CIAP, or CAP). Similar enzymes isolated from more esoteric cold-blooded organisms (e.g., SAP from shrimp) have become available in recent years and
Michael R, Green, Joseph, Sambrook
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Urologic Clinics of North America, 1979
Acid phosphatase is a ubiquitous lysosomal enzyme that hydrolyses organic phosphates at an acid pH. Although the postpuberteral prostatic epithelial cell contains a uniquely high concentration of acid phosphatase, cellular components of bone, spleen, kidney, liver, intestine, and blood also contain this enzyme.
M O, Henneberry, G, Engel, J T, Grayhack
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Acid phosphatase is a ubiquitous lysosomal enzyme that hydrolyses organic phosphates at an acid pH. Although the postpuberteral prostatic epithelial cell contains a uniquely high concentration of acid phosphatase, cellular components of bone, spleen, kidney, liver, intestine, and blood also contain this enzyme.
M O, Henneberry, G, Engel, J T, Grayhack
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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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In Vitro Phosphatase Assays for the Eya2 Tyrosine Phosphatase
2023Protein tyrosine phosphatases (PTP), such as the Eyes Absent (Eya) family of proteins, play important roles in diverse biological processes. In vitro phosphatase assays are essential tools for characterizing the enzymatic activity as well as discovering inhibitors and regulators of these phosphatases. Two common types of in vitro phosphatase assays use
Christopher, Alderman +4 more
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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.
Michio Kondo +4 more
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A plant oncogene as a phosphatase
Nature, 1996The plant oncogene rolB from Agrobacterium rhizogenes elicits differentiation and growth of neoplastic roots (hairy roots) in dicotyledonous plants. rolB-transformed plant cells show a sensitivity to auxin several order of magnitude higher than normal, and an increased binding capability to this most studied plant growth regulator.
FILIPPINI, FRANCESCO +7 more
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