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una/phosphatase
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Protein-tyrosine phosphatase alpha, RPTP alpha, is a Helicobacter pylori VacA receptor.
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Helicobacter pylori vacuolating cytotoxin, VacA, induces vacuolation, mitochondrial damage, cytochrome c release, and apoptosis of gastric epithelial cells. To detect gastric proteins that serve as VacA receptors, we used VacA co-immunoprecipitation techniques following biotinylation of the cell
Naphthalenebis[alpha,alpha-difluoromethylenephosphonates] as potent inhibitors of protein tyrosine phosphatases.
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A series of naphthalenebis(difluoromethylenephosphonates) were prepared and compared to their monosubstituted counterparts as inhibitors of the protein phosphatases, PTP1B, CD45 and PP2A. In general, the bissubstituted compounds were better inhibitors than the mono derivatives and some of these are
Alpha,alpha-difluoro-beta-ketophosphonates as potent inhibitors of protein tyrosine phosphatase 1B.
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A novel series of inhibitors that contain an aryl alpha,alpha-difluoro-beta-ketophosphonate group has been synthesized and evaluated against protein tyrosine phosphatase 1B. These compounds exhibit strong inhibitory activity, the best of which has a K(i) value of 0.17 microM. These results
Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1.
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Functional studies of the protein phosphatase-1 (PP1) regulator Sds22 suggest that it is indirectly and/or directly involved in one of the most ancient functions of PP1, i.e. reversing phosphorylation by the Aurora-related protein kinases. We predict that the conserved portion of Sds22 folds into a
Crystallization of the A alpha subunit of protein phosphatase 2A.
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The A alpha subunit of human protein phosphatase 2A forms crystals in space group P2(1) with cell dimensions a = 104.0, b = 174.9, c = 168.2 A, and beta angle = 90.2 degrees. At cryogenic temperatures, the crystals diffracted to a resolution limit of approximately 3.0 A. Based on the unit cell
Phosphorylation of Mg(2+)-dependent protein phosphatase alpha (type 2C alpha) by casein kinase II.
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In this study we show that rat Mg(2+)-dependent protein phosphatase alpha (MPP alpha) expressed in Saccharomyces cerevisiae cells was phosphorylated on serine residues in vivo. The recombinant rat MPP alpha purified from Escherichia coli cells harboring an expression vector was phosphorylated in
Screening of alpha-helical peptide ligands controlling a calcineurin-phosphatase activity.
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In this paper, we describe an application of 202-membered fluorescently labeled peptide library designed to take an alpha-helix secondary structure. As a proof-of-concept experiment, a calmodulin (CaM)/calcineurin (Cn) pair was chosen to screen alpha-helical peptide ligands that tightly bind to CaM
Multiple forms and glycoprotein nature of acid phosphatase, alpha-fucosidase and alpha-mannosidase of psoriatic scales.
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Isoelectric focusing and concanavalin A-Sepharose chromatography were used to study the multiple forms and glycoprotein natures of so-called lysosomal hydrolases from psoriatic scales. Acid phosphatase appeared as 5 different forms with pI values of 6.5, 6.1, 5.8, 5.6 and 5.45. Seven isoenzymes of
[Diphosphoric acid ester of 4, 4-dihydroxy-alpha, alpha-diethylstilbene as the substrate of prostatic phosphatase].
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Serum acid alpha-naphthyl phosphatase activity.
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Serum acid alpha-naphthyl phosphatase activity.
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A new colorimetric method for alkaline phosphatase activity using alpha-naphthyl phosphate as a substrate.
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Protein phosphatase inhibitors enhance the expression of an alpha-amylase gene, alpha Amy3, in cultured rice cells.
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A rice (Oryza sativa L.) gene for alpha-amylase, alpha Amy3, was strongly and rapidly induced by treatment of suspension-cultured cells with okadaic acid (OA), a potent and specific inhibitor of protein serine/threonine phosphatases 1 and 2A. The massive accumulation of alpha Amy3 mRNA in response
[ALPHA-NAPHTHYLPHOSPHATE AS A SUBSTRATE FOR MEASURING ACID PHOSPHATASE OF PROSTATIC ORIGIN].
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Regulatory proteins of eukaryotic initiation factor 2-alpha subunit (eIF2 alpha) phosphatase, under ischemic reperfusion and tolerance.
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Phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 (eIF2alpha), which is one of the substrates of protein phosphatase 1 (PP1), occurs rapidly during the first minutes of post-ischemic reperfusion after an episode of cerebral ischemia. In the present work, two
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