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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

prdx-3  -  Protein PRDX-3

Caenorhabditis elegans

 
 
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Disease relevance of prdx-3

 

High impact information on prdx-3

  • The G. rostochiensis peroxiredoxin catalyses the breakdown of hydrogen peroxide, but not cumene or t-butyl hydroperoxide, in a trypanosomatid reducing system comprising trypanothione reductase, trypanothione and tryparedoxin [2].
  • The protein encoded by nDiTPx had a predicted molecular mass of 22.1 kDa and the deduced amino acid sequence was homologous to thioredoxin peroxidase-like sequences described in other filarial nematodes, yeast, bacteria and mammals [3].
  • A Dirofilaria immitis cDNA clone encoding a nucleic acid homolog of thioredoxin peroxidase (nDiTPx) was isolated from a fourth-stage larval cDNA library, using serum from dogs vaccinated by chemotherapeutically-abbreviated D. immitis larval infections [3].
 

Analytical, diagnostic and therapeutic context of prdx-3

References

  1. Removal of hydrogen peroxide by a 1-cysteine peroxiredoxin enzyme of the filarial parasite Dirofilaria immitis. Chandrashekar, R., Tsuji, N., Morales, T.H., Carmody, A.B., Ozols, V.O., Welton, J., Tang, L. Parasitol. Res. (2000) [Pubmed]
  2. Cloning, expression and functional characterisation of a peroxiredoxin from the potato cyst nematode Globodera rostochiensis. Robertson, L., Robertson, W.M., Sobczak, M., Helder, J., Tetaud, E., Ariyanayagam, M.R., Ferguson, M.A., Fairlamb, A., Jones, J.T. Mol. Biochem. Parasitol. (2000) [Pubmed]
  3. Molecular cloning, expression and enzymatic activity of a thioredoxin peroxidase from Dirofilaria immitis. Klimowski, L., Chandrashekar, R., Tripp, C.A. Mol. Biochem. Parasitol. (1997) [Pubmed]
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