Results 131 to 140 of about 14,531 (182)
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Deoxycytidine kinase is phosphorylated in vitro by protein kinase Cα

Biochimica Et Biophysica Acta - Molecular Cell Research, 1994
Deoxycytidine (dCyd) kinase was effectively phosphorylated by protein kinase C. The reaction was rapid, occurring at 4 degrees C as well as at 37 degrees C and approximately 0.7 mol of phosphate could be incorporated per mol of deoxycytidine kinase. Phosphoserine was the primary amino acid to be phosphorylated.
G L Kučera, Gregory L Kučera
exaly   +3 more sources

Structures of human deoxycytidine kinase product complexes

Acta Crystallographica Section D: Biological Crystallography, 2007
Human deoxycytidine kinase (dCK) is involved in the nucleotide-biosynthesis salvage pathway and has also been shown to phosphorylate several antitumor and antiviral prodrugs. The structures of dCK alone and the dead-end complex of dCK with substrate nucleoside and product ADP or UDP have previously been reported; however, there is currently no ...
Ealick S E
exaly   +3 more sources

Deoxycytidine kinase and deoxycytidine deaminase activities in human tumour xenografts

European Journal of Cancer, 1993
Deoxycytidine kinase (dCK) and deaminase (dCDA) are both key enzymes in the activation and inactivation, respectively, of several deoxycytidine antimetabolites. We determined the total dCK and dCDA activities using standard assays, in 28 human solid tumours grown as xenografts in nude mice, and four corresponding cell lines.
V W, Ruiz van Haperen   +6 more
openaire   +2 more sources

Regulation of human deoxycytidine kinase expression

Advances in Enzyme Regulation, 1993
The human deoxycytidine kinase gene is a single copy gene and is comprised of seven exons that are spread over more than 34 kb of the genome. The 5'-flanking region is highly G/C rich and does not contain CAAT or TATA boxes. This region, when cloned into a recorder gene construct containing the chloramphenicol acetyltransferase gene, is capable of ...
B S, Mitchell   +4 more
openaire   +2 more sources

Human Deoxycytidine Kinase as a Deoxyribonucleoside Phosphorylase

Journal of Molecular Biology, 2004
Human deoxycytidine kinase (dCK) is a key enzyme in the 5'-phosphorylation of purine and pyrimidine deoxynucleosides with deoxycytidine as the most efficient substrate. The ability of dCK to degrade 2'-deoxyribonucleosides to free nucleobases and 2-deoxy-alpha-d-ribofuranose-1-phosphate was demonstrated by 1H-31P correlation spectroscopy and by isotope
Elena, Usova   +4 more
openaire   +2 more sources

Regulation of Deoxycytidine Kinase by Deoxycytidine and Deoxycytidine 5′ Triphosphate in Whole Leukemia and Tumor Cells

1998
The clinical importance of the dCTP salvage pathway is given by the fact that deoxycytidine (dCyd) analogs like cytosine arabinoside (ara-C) are activated via the salvage pathway. The non-toxic prodrug ara-C gains its cytotoxic potential by phosphorylation to the 5′-triphosphate ara-CTP. Not only cellular accumulation, but also retention of ara-CTP are
V, Heinemann   +3 more
openaire   +2 more sources

Effect of Phosphorylation on Deoxycytidine Kinase Activity

2006
In contrast to deoxycytidine kinase from leukemic blasts7, the recombinant dCK is a poor substrate for protein kinase C. Protein kinase A effectively phosphorylates the recombinant dCK. However, neither substrate specificity, nor kinetic parameters of dCK were changed upon phosphorylation.
T, Spasokoukotskaja   +6 more
openaire   +2 more sources

Regulation of deoxycytidine kinase activity and inhibition by DFDC

Advances in Enzyme Regulation, 1993
(1) Deoxycytidine kinase activity increased in a transformation- and progression-linked fashion in rat hepatomas of different proliferation rates. The activity also increased and was growth rate-linked in a series of tissue culture cell lines of human and animal tumors.
G, Weber   +7 more
openaire   +2 more sources

Purification and Properties of Human Deoxycytidine Kinase

1986
The purification of deoxycytidine kinase from human leucemic spleen reported here result in a pure protein of molecular weight 28K. The enzyme eluates during gel filtration as a dimer and the same enzyme phosphorylates both deoxycytidine, deoxyguanosine and deoxyadenosine, but with different Km and Vmax values. Our results are in agreement with earlier
C, Bohman, S, Eriksson
openaire   +2 more sources

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