Characterization of HSP90 isoforms in transformed bovine leukocytes infected with Theileria annulata

@inproceedings{Kinnaird2017CharacterizationOH,
  title={Characterization of HSP90 isoforms in transformed bovine leukocytes infected with Theileria annulata
},
  author={Jane H. Kinnaird and Meetali Singh and Victoria Gillan and William L. Weir and Ewen D. D. Calder and Isabel Hostettler and Utpal Tatu and Eileen Devaney and Brian R. Shiels},
  booktitle={Cellular microbiology},
  year={2017}
}
HSP90 chaperones are essential regulators of cellular function, as they ensure the appropriate conformation of multiple key client proteins. Four HSP90 isoforms were identified in the protozoan parasite Theileria annulata. Partial characterization was undertaken for three and localization confirmed for cytoplasmic (TA12105), endoplasmic reticulum (TA06470), and apicoplast (TA10720) forms. ATPase activity and binding to the HSP90 inhibitor geldanamycin were demonstrated for recombinant TA12105… CONTINUE READING

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Characterization of HSP90 isoforms in transformed bovine leukocytes infected with Theileria annulata, Cell. Microbiol. 2017;19:e12669

JH Kinnaird, M Singh, V Gillan
  • 2017