Biosafety classification is based on U.S. Public Health Service Guidelines, it is the responsibility of the customer to ensure that their facilities comply with biosafety regulations for their own country.
Beach DH, et al. Phospholipid metabolism of cultured Trichomonas vaginalis and Tritrichomonas foetus. Mol. Biochem. Parasitol. 44: 97-108, 1991. PubMed: 2011157
Beach DH, et al. Fatty acid and sterol metabolism of cultured Trichomonas vaginalis and Tritrichomonas foetus. Mol. Biochem. Parasitol. 38: 175-190, 1990. PubMed: 2325705
Kulda J, Honigberg BM. Behavior and pathogenicity of Tritrichomonas foetus in chick liver cell cultures. J. Protozool. 16: 479-495, 1969. PubMed: 5343462
Mertens E, Muller M. Glucokinase and fructokinase of Trichomonas vaginalis and Tritrichomonas foetus. J. Protozool. 37: 384-388, 1990. PubMed: 2213652
Gunderson J, et al. Phylogeny of trichomonads inferred from small-subunit rRNA sequences. J. Eukaryot. Microbiol. 42: 411-415, 1995. PubMed: 7620466
Delgado-Viscogliosi P, et al. Electrophoretic mobility of tubulin subunits as a criterion for testing relationships between trichomonad taxa. Arch. Protistenkd. 146: 191-200, 1995.
Ashton DH. Metronidazole resistant tritrichomonas foetus activities of hydrogenosomal enzymes in course of development of anaerobic resistance. Acta Univ. Carol. Biol. 30: 513-519, 1986.
Yarlett N, et al. Subcellular localization of the enzymes of the arginine dihydrolase pathway in Trichomonas vaginalis and Trtrichomonas foetus. J. Eukaryot. Microbiol. 41: 554-559, 1994. PubMed: 7866382
Mertens E, et al. Presence of a fructose-2,6-bisphosphate-insensitive pyrophosphate: fructose-6-phosphate phosphotransferase in the anaerobic protozoa Tritrichomonas foetus, Trichomonas vaginalis and Isotricha prostoma. Mol. Biochem. Parasitol. 37: 183-190, 1989. PubMed: 2558319
Viscogliosi E, et al. Phylogenetic implication of iron-containing superoxide dismutase genes from trichomonad species. Mol. Biochem. Parasitol. 80: 209-214, 1996. PubMed: 8892298
Felleisen RS. Comparative genetic analysis of tritrichomonadid protozoa by the random amplified polymorphic DNA technique. Parasitol. Res. 84: 153-156, 1998. PubMed: 9493217
Felleisen RS. Comparative sequence analysis of 5.8S rRNA genes and internal transcribed spacer (ITS) regions of trichomonadid protozoa. Parasitology 115: 111-119, 1997. PubMed: 10190167
Vanacova S, et al. Characterization of Trichomonad species and strains by PCR fingerprinting. J. Eukaryot. Microbiol. 44: 545-552, 1997. PubMed: 9435127
Viscogliosi E, Mueller M. Phylogenetic relationships of the glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase, from parabasalid flagellates. J. Mol. Evol. 47: 190-199, 1998. PubMed: 9694668
Brugerolle G, et al. Centrin protein and genes in Trichomonas vaginalis and close relatives. J. Eukaryot. Microbiol. 47: 129-138, 2000. PubMed: 10750840
Mattos A, et al. Fine structure and isozymic characterization of trichomonadid protozoa. Parasitol. Res. 83: 290-295, 1997. PubMed: 9089728
Bouma MJ, et al. Activity of disulfiram (bis(diethylthiocarbamoyl)disulphide) and ditiocarb (diethyldithiocarbamate) against metronidazole-sensitive and -resistant Trichomonas vaginalis and Tritrichomonas foetus. J. Antimicrob. Chemother. 42: 817-820, 1998. PubMed: 10052908
Tachezy J, et al. Cattle pathogen Tritrichomonas foetus (Riedmuller, 1928) and pig commensal Tritrichomonas suis (Gruby & Delafond, 1843) belong to the same species. J. Eukaryot. Microbiol. 49: 154-163, 2002. PubMed: 12046599
Gerbod D, et al. Phylogenetic relationships of class II fumarase genes from trichomonad species. Mol. Biol. Evol. 18: 1574-1584, 2001. PubMed: 11470849
Land KM, et al. Loss of multiple hydrogenosomal proteins associated with organelle metabolism and high-level drug resistance in trichomonads. Exp. Parasitol. 97: 102-110, 2001. PubMed: 11281707
Brugerolle G, et al. Immunolocalization of two hydrogenosomal enzymes of Trichomonas vaginalis. Parasitol. Res. 86: 30-35, 2000. PubMed: 10669133
Singh BN, et al. Immunological and biochemical analysis of glycosylated surface antigens and lipophosphoglycan of Tritrichomonas foetus. J. Parasitol. 87: 770-777, 2001. PubMed: 11534640
Land KM, et al. In vivo expression of ferredoxin in a drug resistant trichomonad increases metronidazole susceptibility. Mol. Biochem. Parasitol. 121: 153-157, 2002. PubMed: 11985873
Nucleotide (GenBank) : Z70668 T.foetus sod1 gene.
Nucleotide (GenBank) : Z70669 T.foetus sod2 gene.
Nucleotide (GenBank) : AJ249457 mRNA for centrin (ce1 gene)
Nucleotide (GenBank) : U17509 Tritrichomonas foetus 16S-like rRNA gene
Nucleotide (GenBank) : AF307994 Tritrichomonas foetus cytosolic malate dehydrogenase 1 (MDH1) mRNA, partial cds
Nucleotide (GenBank) : AF307995 Tritrichomonas foetus cytosolic malate dehydrogenase 2 (MDH2) mRNA, partial cds
Nucleotide (GenBank) : AF022415 Tritrichomonas foetus glyceraldehyde-3-phosphate dehydrogenase (gap1) gene, partial cds.
Nucleotide (GenBank) : AF022416 Tritrichomonas foetus glyceraldehyde-3-phosphate dehydrogenase (gap2) gene, partial cds.
Nucleotide (GenBank) : AF312935 Tritrichomonas foetus ferredoxin mRNA, partial cds; nuclear gene for hydrogenosomal protein
Nucleotide (GenBank) : AF312932 Tritrichomonas foetus hydrogenase mRNA, complete cds; nuclear gene for hydrogenosomal protein
Nucleotide (GenBank) : AF312933 Tritrichomonas foetus malic enzyme mRNA, partial cds; nuclear gene for hydrogenosomal protein
Nucleotide (GenBank) : AF312931 Tritrichomonas foetus succinyl CoA synthetase beta subunit; nuclear gene for hydrogenosomal protein
Nucleotide (GenBank) : AF312930 Tritrichomonas foetus ATP/ADP carrier mRNA, partial sequence; nuclear gene for hydrogenosomal protein
Nucleotide (GenBank) : L08622 Tritrichomonas foetus hypoxanthine-guanine-xanthine phosphoribosyltransferase (hpt) gene, complete cds.
Nucleotide (GenBank) : AF312934 Tritrichomonas foetus pyruvate:ferredoxin oxidoreductase, partial sequence; nuclear gene for hydrogenosomal
Nucleotide (GenBank) : AF312929 Tritrichomonas foetus succinyl CoA synthetase alpha subunit mRNA, partial cds; nuclear gene for hydrogenosomal protein
