Results 171 to 180 of about 25,107 (224)

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, G, Veerman, B J, Braakhuis, J B, Vermorken, E, Boven, A, Leyva, G J, Peters   +6 more
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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, J J, Song, E E, Johnson, E, Chen, J S, Dayton   +4 more
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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 ...
Erika V, Soriano, Valerie C, Clark, Steven E, Ealick   +2 more
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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, Tatiana, Maltseva, András, Földesi, Jyoti, Chattopadhayaya, Staffan, Eriksson   +4 more
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Nucleotide specificity of human deoxycytidine kinase.

Molecular Pharmacology, 1992
The ability of deoxycytidine kinase (dCK) to phosphorylate 2'-deoxycytidine (dCyd) and its analogs in the presence of eight nucleoside triphosphates (NTPs), simulating the cellular milieu, was investigated. Using highly purified dCK from MOLT-4 T lymphoblasts, Km and Vmax values were determined for the phosphorylation of dCyd in the presence of ...
D S, Shewach, K K, Reynolds, L, Hertel
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Unexpected Immunohistochemical Localization of Deoxycytidine Kinase

Clinical Cancer Research, 2006
To the Editor: We read with great interest the April 15, 2006 article by Sebastiani et al. reporting immunohistochemical evaluation of deoxycytidine kinase (dCK) in 44 pancreatic cancer patients, which found that most cases (40 of 44) were positive for dCK ([1][1]).
Lorelei Johnson, Raymond Lai, Cheryl Santos, Laith Dabbagh, John Mackey   +4 more
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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, L, Schulz, R D, Issels, W, Wilmanns   +3 more
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Deoxycytidine kinase is phosphorylated in vitro by protein kinase Cα

Biochimica et Biophysica Acta (BBA) - 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.
L M, Wang, G L, Kucera
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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