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Phospho-proteins

Dephosphorylation of glycogen phosphorylase is carried out by phospho-protein phosphatase 1. The action of phosphoprotein phosphatase 1 inactivates glycogen phosphorylase. [Pg.478]

PP protein phosphatases PPP phospho protein phosphatases PPM protein phosphatases Mg2+-dependent. [Pg.1013]

Irish JM, Hovland R, Krutzik PO, et al. Single cell profiling of potentiated phospho-protein networks in cancer cells. Cell 2004 118(2) 217-228. [Pg.289]

Beausoleil, S.A., Jedrychowski, M., Schwartz, D., Elias, J.E., Villen, J., Li, J., Cohn, M.A., Cantley, L.C., Gygi, S.P. (2004). Large-scale characterization of HeLa cell nuclear phospho-proteins. Proc. Natl. Acad. Sci. USA 101, 12130-12135. [Pg.255]

Phospho-protein, causes SG assembly Strong signal, robust SG marker... [Pg.101]

Figure 1. Localization of profilin and/or profilin-actin complex into an activated cluster. VASP, Vasodilator-stimulated phospho-protein. Figure 1. Localization of profilin and/or profilin-actin complex into an activated cluster. VASP, Vasodilator-stimulated phospho-protein.
Holzer TR, Fulford AD, Arkins AM et al (2011) Ischemic time impacts biological integrity of phospho-proteins in PI3K/Akt, Erk/ MAPK, and p38 MAPK signaling networks. Anticancer Res 31 2073-2081... [Pg.214]

Ashing must be done if phosphate is at least partially covalentiy bound as, for example, in nucleic acids, nucleotides, or phospho-proteins. [Pg.19]

When the muscle returns to rest, a second enzyme, phosphorylase a phosphatase, also called phospho-protein phosphatase 1 (PP1), removes the phosphoryl groups from phosphorylase a, converting it to the less active form, phosphorylase b. [Pg.584]

With the establishment of the phosphoryl enzyme, the question was whether or not the phosphoryl enzyme was the same as the phospho-protein found by incubating inorganic phosphate with alkaline phosphatase at low pH (35, 114-116, 119, 120). Wilson and Dayan (105) pointed out that the phosphoprotein is thermodynamically very stable It is 105 times more stable than O-phosphorylserine (125) and 0-phosphoryl ethanolamine (105, 126). Alkaline phosphatase, as a true catalyst, must catalyze both the hydrolysis and the formation of phosphate esters. Therefore, if a serine residue existed which was capable of forming a thermodynamically stable phosphate ester, alkaline phosphatase as a nonspecific catalyst would catalyze its formation from both inorganic phosphate and phosphoester substrates. [Pg.398]

Daniel H, Rancillac A, Crepel F (2004) Mechanisms underlying cannabinoid inhibition of presynaptic Ca2+ influx at parallel fibre synapses of the rat cerebellum. J Physiol 557 159-74 Davies CH, Davies SN, Coflingridge GL (1990) Paired-pulse depression of monosynaptic GABA-mediated inhibitory postsynaptic responses in rat hippocampus. J Physiol 424 513-31 De Camilli P, Greengard P (1986a) Synapsin I a synaptic vesicle-associated neuronal phospho-protein. Biochem Pharmacol 35 4349-57... [Pg.246]

De Camilli P, Greengard P (1986b) Synapsin I a synaptic vesicle-associated neuronal phospho-protein. Biochem.Pharmacol 35 4349-57... [Pg.246]

Very recendy a new, physiologic inhibitor of calcineurin has been described by Liu and colleagues at MIT and OriGene (Sun et al., 1998). This protein, called cabin-1 (calcineurin binding protein) is a 2220-residue nuclear protein, which was isolated from a murine T-cell cDNA library in a yeast two-hybrid system with a truncated, catalydcally inac-dve calcineurin used as the bait. Cabin-1 was shown to be a phospho-protein capable of binding to and inhibiting the phosphatase activity of calcineurin, and the interaction between cabin-1 and calcineurin was shown to be sensitive to disruption by FK506 or CsA. In a mammalian... [Pg.272]

Formation and possible roles of specific (phospho)proteins... [Pg.168]

Fig. 1. A model for the pleiotropic effects of LH on functions of Leydig cells. LH interacts with its specific receptor in the plasma membrane of the Leydig cell which results in the activation of several transducing systems and the formation of several second messengers (cyclic AMP, Ca2+, diacylglycerol and arachidonic acid metabolites). Protein kinases (A, C and calmodulin dependent) are activated resulting in the phosphorylation of specific proteins and the synthesis of specific proteins. The (phospho)proteins are involved in the transport of cholesterol to, and the control of, cholesterol metabolism in the inner mitochondrial membrane. Arachidonic acid metabolites (prostaglandins, leukotrienes) may also control steroidogenesis. LH can also regulate the secretion of proteins. The trophic effects of LH are manifested in the growth and differentiation of the Leydig cells. Fig. 1. A model for the pleiotropic effects of LH on functions of Leydig cells. LH interacts with its specific receptor in the plasma membrane of the Leydig cell which results in the activation of several transducing systems and the formation of several second messengers (cyclic AMP, Ca2+, diacylglycerol and arachidonic acid metabolites). Protein kinases (A, C and calmodulin dependent) are activated resulting in the phosphorylation of specific proteins and the synthesis of specific proteins. The (phospho)proteins are involved in the transport of cholesterol to, and the control of, cholesterol metabolism in the inner mitochondrial membrane. Arachidonic acid metabolites (prostaglandins, leukotrienes) may also control steroidogenesis. LH can also regulate the secretion of proteins. The trophic effects of LH are manifested in the growth and differentiation of the Leydig cells.
Riggs, L., Seeley, E. H., Regnier, F. E. (2005). Quantification of phospho-proteins with global internal standard technology. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 817, 89-96. [Pg.86]

M. Kawabuchi, Y. Satomi, T. Takao, Y. Shimonishi, S. Nada, K. Nagai, et al. Transmembrane phospho-protein Cbp regulates the activities of Src-family tyrosine kinases. Nature, 404, 999-1003, 2000. [Pg.54]

Brown, G.C. and Kholodenko, B.N. (1999) Spatial gradients of cellular phospho-proteins. FEBS Lett. 457, 452 54. [Pg.256]

Finally, because this modification occurs on serine and threonine residues, it can also compete directly with an O-phosphory lation event at an identical or nearby site to provide an additional level of regulation on a specific protein. To date, all described O-GlcNAc-modified proteins have been found to be phospho-proteins (28, 29, 30). Such competition between O-GlcNAc and O-phosphate binding occurs with many examples listed above as well as with others. [Pg.316]


See other pages where Phospho-proteins is mentioned: [Pg.413]    [Pg.1013]    [Pg.68]    [Pg.137]    [Pg.419]    [Pg.301]    [Pg.199]    [Pg.122]    [Pg.78]    [Pg.355]    [Pg.49]    [Pg.451]    [Pg.494]    [Pg.466]    [Pg.264]    [Pg.590]    [Pg.485]    [Pg.485]    [Pg.158]    [Pg.271]    [Pg.103]    [Pg.1013]    [Pg.355]    [Pg.210]    [Pg.216]    [Pg.494]    [Pg.396]    [Pg.398]   
See also in sourсe #XX -- [ Pg.398 ]




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