Zobrazeno 1 - 10
of 50
pro vyhledávání: '"G. F. Maley"'
Autor:
E, Chu, D M, Voeller, P F, Morrison, K L, Jones, T, Takechi, G F, Maley, F, Maley, C J, Allegra
Publikováno v:
The Journal of biological chemistry. 269(32)
Human thymidylate synthase (TS) protein specifically binds to its own TS mRNA and functions as a translational repressor. In the presence of reducing agents, the RNA binding activity of TS protein is significantly enhanced. In contrast, treatment of
Publikováno v:
The Journal of biological chemistry. 268(17)
The cDNA encoding human dCMP deaminase was isolated from a lambda ZAPII expression library using an antibody generated against highly purified HeLa cell dCMP deaminase. The cloned cDNA consists of 1856 base pairs and encodes a protein of 178 amino ac
Publikováno v:
The Journal of biological chemistry. 268(4)
Deoxycytidylate (dCMP) deaminase, a hexameric allosteric enzyme induced on infection of Escherichia coli by bacteriophage T4, was shown to contain two atoms of zinc per subunit by atomic absorption spectroscopy. One zinc appears to be involved in cat
Publikováno v:
Zurich, Switzerland, September 3–8, 1989
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::152fe8bc564c5ec7ad1ee00fcb38cf41
https://doi.org/10.1515/9783110889000-152
https://doi.org/10.1515/9783110889000-152
Publikováno v:
Cancer research. 50(13)
The effects of the lipid-soluble dihydrofolate reductase inhibitor, trimetrexate, on the inhibition of thymidylate biosynthesis as a result of perturbation in cellular folate pools in H35 hepatoma cells in vitro has been investigated. Exposure of the
Publikováno v:
Molecular microbiology. 4(6)
Group I introns are present in at least three bacteriophage T4 genes: td, nrdB and sunY. The transcription products of these three genes have similar intron consensus regions and secondary structures, which render them capable of guanosine-mediated i
Publikováno v:
The Journal of biological chemistry. 265(1)
The cd gene of bacteriophage T4, which encodes the enzyme deoxycytidylate deaminase, was isolated as a 1.9-kilobase DNA fragment and completely sequenced. The deduced amino acid sequence was found to be 193 residues long compared with 188 for the cor
Autor:
F, Maley, G F, Maley
Publikováno v:
Progress in nucleic acid research and molecular biology. 39
Publikováno v:
Journal of Biological Chemistry. 257:11876-11878
Thymidine triphosphate, a negative regulator of deoxycytidylate deaminase, was found to bind covalently to this enzyme on exposure to UV light at 254 nM. The rate of half-maximal fixation was extremely rapid, occurring within 30 s and probably attain
Publikováno v:
The Journal of biological chemistry. 258(13)
The amino acid sequence of deoxycytidylate deaminase isolated from T2 phage-infected Escherichia coli has been determined. The enzyme is a hexamer, consisting of identical polypeptide subunits, each composed of 188 amino acids with a calculated Mr =