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1 ) and its analogue in the protozoan parasite Tritrichomonas foetus.
2 e salvage pathway of the parasitic protozoan Tritrichomonas foetus.
5 is a sexually transmitted disease caused by Tritrichomonas foetus and characterized by early embryo
7 rmed multiple inhibitor experiments with the Tritrichomonas foetus and human type 2 IMPDHs using tiaz
8 loped to study the cytopathogenic effects of Tritrichomonas foetus and the role of lipophosphoglycan
9 richomonad highly similar to bovine venereal Tritrichomonas foetus but having a unique tropism for th
12 e phosphoribosyltransferase (HGXPRTase) from Tritrichomonas foetus has been determined and refined ag
13 e phosphoribosyltransferase (HGXPRTase) from Tritrichomonas foetus has been proven to be a target for
14 mplexes of IMPDH from the protozoan parasite Tritrichomonas foetus have been solved: with its substra
15 with the high K(m) for PPi (165.5 microM) in Tritrichomonas foetus HGXPRTase-catalyzed reverse reacti
16 butane-2,3-dione irreversibly inactivate the Tritrichomonas foetus hypoxanthine-guanine-xanthine phos
17 crystal structures of the protozoan parasite Tritrichomonas foetus IMPDH complexed with the inhibitor
18 al structure of the catalytic core domain of Tritrichomonas foetus IMPDH in complex with IMP and beta
20 uctures of IMPDH from the protozoan parasite Tritrichomonas foetus in the apo form at 2.3 A resolutio
21 sferase (HGXPRT) from the protozoan parasite Tritrichomonas foetus is a rational target for antiparas
23 ansferase (HGXPRTase), a type I PRTase, from Tritrichomonas foetus, is a potential target for antitri
26 thermore, T. vaginalis LPG (but not LPG from Tritrichomonas foetus, the causative agent of bovine tri
27 ed by the genome of the trichomonad parasite Tritrichomonas foetus, this otherwise highly conserved h
28 he complete kinetic mechanism for IMPDH from Tritrichomonas foetus using ligand binding, isotope effe
29 ine phosphoribosyltransferase (HGXPRTase) of Tritrichomonas foetus was inactivated by the thiol reage
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