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1 s in the previously characterized IMPDH from Tritrichomonas foetus ( TfIMPDH).
2  is a sexually transmitted disease caused by Tritrichomonas foetus and characterized by early embryo
3 amine prevalence and risk factors for feline Tritrichomonas foetus and Giardia infection.
4 rmed multiple inhibitor experiments with the Tritrichomonas foetus and human type 2 IMPDHs using tiaz
5 loped to study the cytopathogenic effects of Tritrichomonas foetus and the role of lipophosphoglycan
6 richomonad highly similar to bovine venereal Tritrichomonas foetus but having a unique tropism for th
7 ae) formed one, while Monocercomonas sp. and Tritrichomonas foetus formed the other.
8                Likewise, the bovine parasite Tritrichomonas foetus had no cytotoxic effects on hVECs.
9 e phosphoribosyltransferase (HGXPRTase) from Tritrichomonas foetus has been determined and refined ag
10 e phosphoribosyltransferase (HGXPRTase) from Tritrichomonas foetus has been proven to be a target for
11 mplexes of IMPDH from the protozoan parasite Tritrichomonas foetus have been solved: with its substra
12 with the high K(m) for PPi (165.5 microM) in Tritrichomonas foetus HGXPRTase-catalyzed reverse reacti
13 butane-2,3-dione irreversibly inactivate the Tritrichomonas foetus hypoxanthine-guanine-xanthine phos
14 crystal structures of the protozoan parasite Tritrichomonas foetus IMPDH complexed with the inhibitor
15 al structure of the catalytic core domain of Tritrichomonas foetus IMPDH in complex with IMP and beta
16                An X-ray crystal structure of Tritrichomonas foetus IMPDH with mizoribine monophosphat
17 uctures of IMPDH from the protozoan parasite Tritrichomonas foetus in the apo form at 2.3 A resolutio
18 sferase (HGXPRT) from the protozoan parasite Tritrichomonas foetus is a rational target for antiparas
19                                              Tritrichomonas foetus is a serious veterinary pathogen,
20          One reason is because inhibition of Tritrichomonas foetus ODC results in growth arrest, dest
21 he complete kinetic mechanism for IMPDH from Tritrichomonas foetus using ligand binding, isotope effe
22 ine phosphoribosyltransferase (HGXPRTase) of Tritrichomonas foetus was inactivated by the thiol reage
23                                              Tritrichomonas foetus, a venereal pathogen of cattle, wa
24                                              Tritrichomonas foetus, an anaerobic flagellated protozoa
25 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 ) and its analogue in the protozoan parasite Tritrichomonas foetus.
29 e salvage pathway of the parasitic protozoan Tritrichomonas foetus.
30 ng site of resistant IMPDH from the parasite Tritrichomonas foetuscontains two residues that differ f
31 stinal epithelium via Tamoxifen injection in Tritrichomonas muris (Tm) infected mice, tuft cells, IL-
32                  We identified the protozoan Tritrichomonas muris as the disease-exacerbating element
33             Here, we show that the protozoan Tritrichomonas musculis activates the host epithelial in
34 t al. (2016) identify a commensal protozoan, Tritrichomonas musculis, that can enhance anti-bacterial
35 pitopes with proteins in data banks, such as Tritrichomonas suis, Candida albicans, and Saccharomyces

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