Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Ralph J. Cisneros"'
Publikováno v:
Journal of Biological Chemistry. 268:10102-10108
The binding of 5-fluorodeoxyuridylate (FdUMP) to carboxypeptidase-inactivated thymidylate synthase obtained from methotrexate-resistant Lactobacillus casei was investigated using [3H]FdUMP in a trichloroacetic acid precipitation assay and by 19F nucl
Autor:
R. Bruce Dunlap, Jerome D. Odom, Ralph J. Cisneros, Mary S. Weir, Jeffrey O. Boles, J. E. Villafranca
Publikováno v:
Biochemistry. 30:11073-11080
Replacement of methionine (Met) residues by selenomethionine (SeMet) was recently shown to facilitate the crystallographic analysis of protein structure through the application of multi-wavelength anomalous diffraction techniques [Yang et al. (1990)
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1077:35-46
Recombinant mouse thymidylate synthase (TS) expressed at high levels in Escherichia coli was purified to homogeneity in greater than 70% yield by a rapid three-step procedure. Both 0.1% Triton X-100 and 10% glycerol were required to stabilize the enz
Publikováno v:
Zurich, Switzerland, September 3–8, 1989
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::96134a49efe0632d4d811ae14681b084
https://doi.org/10.1515/9783110889000-160
https://doi.org/10.1515/9783110889000-160
Autor:
Ralph J. Cisneros, R. Bruce Dunlap
Publikováno v:
Biochimica et biophysica acta. 1039(2)
Covalent binding stoichiometries for both the enzyme:5-fluoro-2'-deoxyuridine 5'-monophosphate (FdUMP) binary complex and the enzyme:FdUMP:5,10-methylenetetrahydrofolate (inhibitory ternary) complex at equilibrium were measured by the trichloroacetic
Autor:
Ralph J. Cisneros, R. Bruce Dunlap
Publikováno v:
Analytical biochemistry. 186(2)
The use of trichloroacetic acid as a protein precipitant and denaturant in the quantitative measurement of covalent complexes of thymidylate synthase is described. Enzyme inactivated with N[3H]ethylmaleimide and inhibitory ternary complex (formed wit
Publikováno v:
Biochemical and biophysical research communications. 167(3)
The arginine located at position 44 of mouse thymidylate synthase is in a highly conserved loop that is in close proximity to the active site cleft of the enzyme. Structural analyses have suggested that this arginine forms hydrogen bonds with the α-
Publikováno v:
Gene. 84:487-491
The coding region of the mouse thymidylate synthase (TS)-encoding cDNA (ts) was inserted downstream from the phage T7 promoter and translation initiation signals of the expression vector, pET-3a, and transformed into Escherichia coli BL21(DE3)[pLysS]
Publikováno v:
Nucleosides, Nucleotides and Nucleic Acids. 8:1135-1140
5-Methylselenenyl and 5-phenyltellurenyldeoxyuridines were constructed via the transmetallation of the corresponding 5-bromo-3′,5′-bis(dimethyl-tert-butyl)silyl deoxyuridine with n-butyllithium followed by electrophilic trapping of the anion with