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Serine kinase

A more recently introduced format is the AlphaScreen assay. The assay principal behind this technology has previously been described above. In the kinase format a biotinylated peptide is bound to a streptavidin donor bead, and a phopshospecific antibody is bound to the acceptor bead. When the substrate is phosphorylated, the beads come in close proximity and a signal is generated. An example using the assay for the detection of inhibitors of serine kinases is presented by Von Leo-prechting [26]. [Pg.42]

Featherstone, C., and Russell, P. (1991). Fission yeast p mitotic inhibitor is a tyrosine/serine kinase. Nature 349 808-811. [Pg.39]

These authors identified novel serine kinases activated by cytokines and chemokines in T cells using PAP-1, and verified MAP kinase dependent IL-16 secretion in T-cell receptor-activated T cells. [Pg.90]

Von, L.A., Kumpf, R., Menzel, S., Reulle, D., Griebel, R., Valler, M.J., and Buttner, F.H., Miniaturization and validation of a high-throughput serine kinase assay using the alpha screen platform, /. Biomol. Screen., 9, 719, 2004. [Pg.100]

Deans JP, Sehieven GL, Shu GL et al. Association of tyrosine and serine kinases with the B-cell sur-faee antigen CD20 induetion via CD20 of tyrosine phosphorylation and activation of phospholipase C-gamma 1 and PLC phospholipase C-gamma 2. JImmunol 1993 151 4494 504. [Pg.226]

Heesom, K.J. Moule, S.K. Denton, R.M. Purification and characterisation of an insulin-stimulated protein-serine kinase which phosphorylates acetyl-CoA carboxylase. FEBS Lett., 422, 43-46 (1998)... [Pg.128]

Jiao, J. Chollet, R. (1990). Regulatory phosphorylation of serine-15 in maize phosphoeno/pyruvate carboxylase by a C4-leaf protein-serine kinase. Archives of Biochemistry and Biophysics 283, 300-5. [Pg.134]

Astoul, E., Laurence, A. D., Totty, N., Beer, S., Alexander, D. R., and Cantrell, D. A. (2003) Approaches to define antigen receptor-induced serine kinase signal transduction pathways. J. Biol. Chem. 278,9267-9275. [Pg.18]

In most cases the NADH oxidase activates the Na+/H+ exchanger in animal cells. In plant cells, it appears to activate the H+-ATPase. The mechanism for channel activation is analogous to channel activation by ligand receptors. Since the oxidase can control tyrosine kinase, activation of the exchanger is most likely through the MAP tyrosine kinase-activated serine kinase which phosphorylates the antiport. [Pg.184]

Borthwick, A.C., Edged, N.J., Denton, R.M. 1990 Protein-serine kinase from rat epididymal adipose tissue which phosphorylates and activates acetyl-CoA carboxylase. Possible role in insulin action. Biochem. J. 270, 795-801. [Pg.82]

Von Leoprechting, A. et al. 2004. Miniaturization and validation of a high-throughput serine kinase assay using the AlphaScreen platform. J. Biomol. Screen. 9, 719-725. [Pg.24]

Girault JA, Hemmings HC, Jr, Zorn SH, Gustafson EL, Greengard P (1990b) Characterization in mammalian brain of a DARPP-32 serine kinase identical to casein kinase II. J Neurochem 55 1772-1783. [Pg.142]

Serine Kinases Modulating the Insulin Receptor Functions. 39... [Pg.25]

IRS-1 Couples the Insulin Receptor Tyrosine Kinase to a Ras-activated Signalling Cascade of Serine Kinases... [Pg.37]

It has been known for a long time that a number of enzymes are regulated by insulin through phosphorylation and dephosphorylation at serine residues (Kahn, 1985). Therefore, a signal transduction from the tyrosine-specific insulin receptor kinase to a serine-specific kinase must occur. The serine kinase that might fulfil both functions in the insulin signal-transduction chain has not yet been identified however, there are several possible candidates for these so called switch kinases (Fig. 10). [Pg.37]


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