Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.11.1 (protein kinase)
 81,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Endogenous protein phosphorylation was studied in extracts of hamster fibroblasts infected with pseudorabies virus. The major phosphorylation was detected quite late in infection and involved an acidic protein of Mr 62,000. It was catalysed by an enzyme activity with the properties of cellular casein kinase II. Two-dimensional gel analysis was used to demonstrate that this same protein was also phosphorylated in vivo. The phosphoprotein was detected in mature virions and is most likely viral in origin.
J Gen Virol 1987 Apr
PMID:A major phosphoprotein of cells infected with pseudorabies virus is phosphorylated by cellular casein kinase II. 303 31

The purified RNA polymerase complex of vesicular stomatitis virus required added thiols for maximal activity, whereas polymerase activity from whole disrupted virions did not. Maximal activity of the purified polymerase complex required greater than or equal to 1 mM added dithiothreitol. The polymerase was inactivated by N-ethylmaleimide (NEM) at 0 degree C, with k2 = 528 +/- 26 M-1 min-1. Activity was recovered by addition of L protein, but not N or NS, to the NEM-inactivated complex, indicating that the NEM-sensitive group was present on the L protein. Nucleoside triphosphates protected the enzyme against inactivation by N-ethylmaleimide. ATP was most effective, with KD = 0.58 +/- 0.07 mM, a value close to the Km of ATP reported previously for initiation of RNA synthesis. dATP was nearly as effective, and GTP was slightly less effective than ATP. Non-hydrolyzable analogs of ATP protected weakly, whereas ADP and pyrimidine triphosphates gave very poor, but still measurable, protection. The ATP binding site thus identified differs from the protein kinase-associated ATP binding site identified on L protein by Sanchez et al. (Sanchez, A., De, B.P., and Banerjee, A. K. (1985) J. Gen. Virol. 66, 1025-1036) in having a substantially lower affinity for ATP. Two putative ATP binding sites were identified in the L protein amino acid sequence, but none were found in the N or NS sequences.
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PMID:Inactivation of the RNA polymerase of vesicular stomatitis virus by N-ethylmaleimide and protection by nucleoside triphosphates. Evidence for a second ATP binding site on L protein. 303 24

Synchronous cultures of Saccharomyces cerevisiae prepared by selection of small unbudded cells from an elutriating rotor were used to measure trehalase activity during the cell cycle. After the small cells had been removed from the rotor, the remainder was used to prepare asynchronous control cultures. Both synchronous and control cultures were studied for two cell cycles. In asynchronous cultures the trehalase activity of crude cell lysates rose continuously. In synchronized populations trehalase activity increased from the beginning of budding onwards. However, around the period of cell division the enzyme activity dropped rapidly but transiently by more than 5-fold. The same changes were found during the second budding cycle. Measurements of invertase and glucose-6-phosphate dehydrogenase activities in the same synchronous and asynchronous cultures revealed a continuous increase for both enzymes. Incubation of cell lysates with cAMP-dependent protein kinase before assaying for trehalase resulted in a 2-fold enhancement of enzyme activity in asynchronous control cultures. In synchronized cells this treatment also led to a significant stimulation of trehalase activity, and largely abolished the cell-cycle-dependent oscillatory pattern of enzyme activity. These results suggest that the activity of trehalase during the cell cycle is regulated, presumably at the post-translational level, by a phosphorylation-dephosphorylation mechanism.
J Gen Microbiol 1988 Mar
PMID:Regulation of trehalase activity during the cell cycle of Saccharomyces cerevisiae. 305 78

The product of the PHO85 gene, which encodes one of the negative regulatory factors of the PHO system in Saccharomyces cerevisiae, shows significant amino acid sequence homology with the CDC28 protein kinase. However, overexpressing PHO85 did not suppress the temperature sensitive phenotype of the cdc28-1 mutation. The nucleotide sequence of the PHO85 gene strongly suggests the presence of an intron near the sequence encoding the N-terminal region.
Mol Gen Genet 1988 Sep
PMID:PHO85, a negative regulator of the PHO system, is a homolog of the protein kinase gene, CDC28, of Saccharomyces cerevisiae. 306 79

Phosphoprotein patterns in two mutants of Saccharomyces cerevisiae, cdc25-20(ts) and cdc25-20(ts) bcy1, were analysed by two-dimensional polyacrylamide gel electrophoresis. Comparison with the phosphoprotein patterns of the mutants cyr1-2(ts) and bcy1, analysed in a previous study, demonstrated not only that the CDC25 gene product is a positive element in the regulation of adenylyl cyclase activity, as suggested by recent studies, but that it is also a negative element in the phosphorylation of a 31 kDa protein (p31c and p31d), a protein whose phosphorylation is correlated with cell cycle arrest, and dephosphorylation with cell cycle initiation, respectively. Moreover, the phosphorylation phenotype of p31c and p31d suggests that the activity of the CDC25 protein is subject to feedback regulation by cAMP-dependent protein kinase, and that the CDC25 protein is a key element in an ammonium (NH+4) signal-response system.
J Gen Microbiol 1988 Sep
PMID:Identification of a 31 kDa protein in Saccharomyces cerevisiae whose phosphorylation is controlled negatively by the CDC25 gene product. 307 84

1. Mefloquine, a phospholipid interacting antimalarial drug, inhibits Ca2+ stimulated phospholipid dependent protein kinase from rat spleen by interfering with the activation process. 2. The type of inhibition was found to be competitive with respect to phosphatidylserine; the apparent Ki-value was determined to be 60 microM.
Gen Pharmacol 1988
PMID:Inhibition by mefloquine of Ca2+ stimulated phospholipid dependent protein kinase from rat spleen. 325 63

A purine analogue, 2-aminopurine, reported to act as an inhibitor of protein kinase, selectively, reversibly and in a dose-dependent manner blocked a very early stage in interferon induction. With chick embryo cells and mouse L cells as hosts, and different viral inducers of interferon, maximal effects of 2-aminopurine were observed during the first 4 h of induction. At 10 mM-2-aminopurine there was a 20-fold reduction in the yield of interferon from both cell types. 2-Aminopurine and actinomycin D both prevented interferon induction with the same time course, indicating a transcriptional block to induction; however, only the action of the former was reversed upon removal of the drug. Addition of 2-aminopurine to an agarose overlay resulted in high efficiency plaque formation by vesicular stomatitis virus New Jersey (Hazelhurst) under conditions where endogenous induction of interferon and its feedback action on aged chick embryo cells normally prevented plaque formation. Two other inducible systems, representing genes involved in interferon action (both its development and activation), and those of heat shock, were not affected by 2-aminopurine. A model is presented implicating the interferon-inducible dsRNA-dependent protein kinase as an interferon induction receptor which, on interaction with dsRNA, generates an amplified signal via phosphorylation that ultimately derepresses the interferon gene(s).
J Gen Virol 1988 Jul
PMID:Interferon induction by viruses. XVI. 2-Aminopurine blocks selectively and reversibly an early stage in interferon induction. 339 21

Treatment of K/Balb cells with IdUrd leads to the expression of endogenous virus and interferon is formed which subsequently can suppress the release of virus into the medium. Under these conditions, a protein kinase activity capable of phosphorylating an endogenous polypeptide of apparent mol. wt. 67000 is detected. This kinase activity is analogous to that induced in K/Balb cells treated with exogenous interferon. The induction of the protein kinase activity in IdUrd-treated K/Balb cells can be blocked by anti-interferon serum, thus providing evidence for the presence and action of interferon.
J Gen Virol 1981 Jan
PMID:Interferon-mediated protein kinase in mouse cells treated with iododeoxyuridine (IdUrd) and induced to express endogenous retroviruses. 616 65

RD-114 is a human sarcoma-derived cell line which is chronically infected with the RD-114 retrovirus. In a previous study, we found that treatment of these cells with human interferon-alpha or human interferon-gamma causes a marked inhibition of RD-114 virus production, but that the replication of exogenous vesicular stomatitis or encephalomyocarditis virus is not impaired. In the present study, we report that neither type of interferon has strong inhibitory effects on DNA synthesis or on multiplication of the cells. We also failed to detect a double-stranded RNA-dependent protein kinase activity in extracts of both interferon-treated and untreated cells. However, a low level of 2',5'-oligoadenylate [2,5(A)] synthetase activity was detectable in extracts of interferon-treated cells. 2,5(A)-dependent endonuclease L activity was detectable in extracts of both untreated and interferon-treated cells. This was probably responsible for the inhibition of protein synthesis observed upon introduction of 2,5(A) to RD-114 cells. In many cells, interferon has been found to induce synthesis of several proteins demonstrable by autoradiographic analysis of slab gels on which extracts of interferon-treated and radiolabelled cells are separated. Using a similar method, no such induced protein synthesis was detectable in interferon-treated RD-114 cells. Our results indicate that RD-114 cells are resistant to most known actions of interferons except for the antiretroviral action to which they are as sensitive as any other cell line.
J Gen Virol 1983 Oct
PMID:Antiviral, anticellular and enzyme-inducing activities of interferons in RD-114 cells. 619 49

The distribution of rabies virus, interferon and interferon-mediated enzymes, pppA(2'p5'A)n synthetase (2-5A synthetase) and poly(rI) . poly(rC)-Sepharose-bound protein kinase, was studied in different regions of the brains of rabies virus-infected rats. A broad range of virus infectivity was found in the brain stem, cerebellum, cortex, hippocampus and striatum. Similarly, the levels of interferon were variable (2500 to 60 000 units/mg protein in tissue extracts) in the different brain regions studied but were unrelated to the corresponding infectivities . The level of 2-5A synthetase and protein kinase was enhanced several-fold in the individual brain regions and the degree of such enhancement was correlated with the level of interferon.
J Gen Virol 1984 May
PMID:Distribution of rabies virus, interferon and interferon-mediated enzymes in the brains of virus-infected rats. 620 34


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