Proteomics and glycomics analyses of N-glycosylated structures involved in Toxoplasma gondii--host cell interactions.

@article{Fauquenoy2008ProteomicsAG,
  title={Proteomics and glycomics analyses of N-glycosylated structures involved in Toxoplasma gondii--host cell interactions.},
  author={Sylvain Fauquenoy and Willy Morelle and Agn{\`e}s Hovasse and Audrey Bednarczyk and Christian Slomianny and Christine Schaeffer and Alain van Dorsselaer and Stanislas Tomavo},
  journal={Molecular & cellular proteomics : MCP},
  year={2008},
  volume={7 5},
  pages={891-910}
}
The apicomplexan parasite Toxoplasma gondii recognizes, binds, and penetrates virtually any kind of mammalian cell using a repertoire of proteins released from late secretory organelles and a unique form of gliding motility (also named glideosome) that critically depends on actin filaments and myosin. How T. gondii glycosylated proteins mediate host-parasite interactions remains elusive. To date, only limited evidence is available concerning N-glycosylation in apicomplexans. Here we report… CONTINUE READING

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Guidelines for the next 10 years of proteomics

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