Results 191 to 200 of about 30,523 (236)
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Inhibition of Casein Kinase II by Dinucleoside Polyphosphates

Enzyme and Protein, 2017
In our search for potential inhibitors of casein kinase II (CKII) in Artemia, we have shown that dinucleoside polyphosphates are a novel class of effectors for this ubiquitous protein kinase. P^1,P^4-di(guanosine-5')-tetraphosphate (Gp^4G) is a better CKII inhibitor than P^1,P^4-di(adenosine-5')-tetraphosphate (Ap^4A).
Pype, S., Slegers, H.
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Identification of syntaxin‐1A sites of phosphorylation by casein kinase I and casein kinase II

European Journal of Biochemistry, 2002
Casein kinases I (CKI) are serine/threonine protein kinases widely expressed in a range of eukaryotes including yeast, mammals and plants. They have been shown to play a role in diverse physiological events including membrane trafficking. CKIα is associated with synaptic vesicles and phosphorylates some synaptic vesicle associated proteins including ...
Thierry, Dubois   +4 more
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Interaction of polyamines and magnesium with casein kinase II

Archives of Biochemistry and Biophysics, 1984
In reticulocytes, polyamines appear to be physiologically relevant activators of casein kinase II [Hathaway, G. M. and Traugh, J. A. (1984). J. Biol. Chem. 259, 7011-7015]. The mechanism by which polyamines and Mg2+ interact to activate casein kinase II has been investigated. These studies were conducted by holding ionic strength constant at 0.10 M. At
G M, Hathaway, J A, Traugh
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DNA binding activity of casein kinase II

Biochemical and Biophysical Research Communications, 1990
Casein kinase II, an ubiquitous, oligomeric, messenger-independent protein kinase has previously been shown to concentrate in the nuclear compartment when cells are stimulated to proliferate. The present communication reports that purified mammalian CKII interacts with genomic DNA preparations in vitro. This interaction led to an apparent activation of
O, Filhol, C, Cochet, E M, Chambaz
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Aberrant casein kinase II in Alzheimer's disease

Brain Research, 1990
Abnormal protein phosphorylation has been identified in Alzheimer's disease (AD) for several proteins including a Mr 60,000 protein, a Mr 86,000 protein and a microtubule-associated protein tau. The Mr 86,000 protein is phosphorylated by protein kinase C, whereas protein kinases responsible for other aberrant phosphorylation reactions are not known. In
D S, Iimoto   +4 more
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Nucleoplasmin associates with and is phosphorylated by casein kinase ii

Journal of Cell Science, 1995
ABSTRACT Nucleoplasmin is a phosphorylated nuclear-accumulating protein. We report herein that the kinetics of its cytoplasm r nucleus transport are affected by its degree of phosphorylation. Therefore, we sought to identify any protein kinase which specifically associates with nucleoplasmin.
I, Vancurova   +3 more
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Polyamine binding activity of casein kinase II

Biochemical and Biophysical Research Communications, 1991
Protein phosphorylation by the ubiquitous casein kinase II (CKII) is known to be sensitive to naturally occurring polyamines. Using isolated recombinant alpha and beta subunits of the kinase, as well as the alpha 2 beta 2 oligomeric enzyme, it is shown that (i) CKII binds [3H]-spermine with Kds in the micromolar range.
O, Filhol   +3 more
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Identification of calcium-independent myosin kinase with casein kinase II

Archives of Biochemistry and Biophysics, 1983
A crude myosin fraction from bovine brain has been found to contain a Ca2+-independent myosin kinase that catalyzes the phosphorylation of 20,000-Da light chain of gizzard myosin. The myosin kinase has been separated from the myosin by Sepharose CL-4B gel filtration and purified further by chromatography on phosphocellulose, Sephacryl S-300, and ...
S, Matsumura   +4 more
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Detection of casein kinase II by aggregation-induced emission

Talanta, 2019
A novel aggregation-induced emission (AIE) probe comprised of a hydrophilic protein kinase specific peptide and a hydrophobic tetraphenylethene (TPE) unit was synthesized through click reaction. The prepared TPE-peptide probe could be completely degraded by carboxypeptidase Y (CPY) to release hydrophobic TPE part, which aggregated in buffer solution ...
Zhenzhu, Luan   +5 more
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Phosphorylation of caldesmon by smooth-muscle casein kinase II

Journal of Muscle Research and Cell Motility, 1994
A caldesmon kinase activity was partially purified from an extract of chicken gizzard smooth muscle by sequential chromatography on columns of DEAE-Sephacel, MonoQ and Superose 12. This kinase was identified as casein kinase II by Western blotting using peptide-directed antibodies raised against the alpha, alpha' and beta subunits of human casein ...
C, Sutherland   +3 more
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