Results 241 to 250 of about 24,797 (285)

Casein kinases

open access: yes
Walter Pyerin, Karin Ackermann
exaly   +2 more sources

Amyloid β-protein stimulates casein kinase I and casein kinase II activities

Brain Research, 1993
Amyloid beta-protein (A beta) is the major protein of cerebrovascular and plaque amyloid in Alzheimer's disease (AD). Extensive evidence has demonstrated abnormal protein phosphorylation in this disease. We investigated the effect of synthetic A beta with the amino-acid sequence corresponding to cerebrovascular A beta and plaque A beta on the ...
A, Chauhan   +4 more
openaire   +2 more sources

Expression analyses of casein kinase 2α and casein kinase 2β in the silkmoth, Bombyx mori

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2008
A period-timeless (per-tim) based feedback loop is considered to be essential in generating circadian rhythms in Drosophila melanogaster. In addition to transcriptional regulation, the post-transcriptional modification is essential to the circadian oscillation of core clock proteins in the circadian system.
Sachio, Iwai   +3 more
openaire   +2 more sources

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
openaire   +2 more sources

Phosphorylation of fibrinogen by casein kinase 1

Biochemical and Biophysical Research Communications, 1983
Casein kinase 1 phosphorylated human fibrinogen, in a reaction that did not use GTP as phosphoryl donor and was neither stimulated by cyclic AMP or Ca2+, nor inhibited by the cyclic AMP-dependent protein kinase inhibitor protein. Maximal incorporation averaged 4 mol of phosphate per mol of fibrinogen, most of it in the largest CNBr-fragment of the ...
E, Itarte   +3 more
openaire   +2 more sources

Subcellular localization of casein kinase I

Biochemical and Biophysical Research Communications, 1990
An anti-yeast CKI antiserum was shown to cross-react with CKI isolated from Krebs II mouse ascites tumour cells. The mammalian CKI showed virtually the same molecular mass (app. 45 kDa) as the yeast enzyme. By immunofluorescence it could be shown that CKI is preferably located in the nucleolus.
N, Grankowski, O G, Issinger
openaire   +2 more sources

Casein kinase: the triple meaning of a misnomer

Biochemical Journal, 2014
The term ‘casein kinase’ has been widely used for decades to denote protein kinases sharing the ability to readily phosphorylate casein in vitro. These fall into three main classes: two of them, later renamed as protein kinases CK1 (casein kinase 1, also known as CKI) and CK2 (also known as CKII), are pleiotropic members of the kinome functionally ...
VENERANDO, ANDREA   +2 more
openaire   +5 more sources

ON THE INTERACTION OF P53 WITH CASEIN KINASE-II

International Journal of Oncology, 1994
Binding of p53 to cellular and viral proteins seems to be implicated in the regulation of its growth suppressor or oncogenic activity. Casein kinase II is among the proteins which tightly associate with p53 and which phosphorylate p53 at a C-terminal amino acid residue.
P, Wagner   +3 more
openaire   +2 more sources

Association of casein kinase II with microtubules

Experimental Cell Research, 1989
A magnesium-dependent heparin-inhibited protein kinase activity associated with brain microtubule preparations has been identified as casein kinase II using a monospecific polyclonal antibody. This enzyme appears enriched in cold-stable microtubule fractions.
Serrano, Luis   +3 more
openaire   +3 more sources

Casein kinase 1: Complexity in the family

The International Journal of Biochemistry & Cell Biology, 2011
The CK1 family of serine/threonine kinases regulates diverse cellular processes, through binding to and phosphorylation a myriad of protein substrates. CK1 prefers substrates primed by prior phosphorylation, and works closely with other kinases in the Wnt pathway. CK1 is itself regulated by posttranslational modification, including autophosphorylation.
Cheong, J.K., Virshup, D.M.
openaire   +2 more sources

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