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Overproduction, purification, and biochemical characterization of the dual specificity H1 protein phosphatase encoded by variola major virus

  1. Author:
    Tropea, J. E.
    Phan, J.
    Waugh, D. S.
  2. Author Address

    NCI, Ctr Canc Res, Macromol Crystallog Lab, Frederick, MD 21701 USA.;Waugh, DS, NCI, Ctr Canc Res, Macromol Crystallog Lab, POB B, Frederick, MD 21701 USA.;waughd@ncifcrf.gov
    1. Year: 2006
    2. Date: Nov
  1. Journal: Protein Expression and Purification
    1. 50
    2. 1
    3. Pages: 31-36
  2. Type of Article: Article
  3. ISSN: 1046-5928
  1. Abstract:

    Smallpox, a highly contagious infectious disease caused by the variola major virus, has an overall mortality rate of about 30%. Because there currently is no specific treatment for smallpox, and the only prevention is vaccination, there is an urgent need for the development of effective antiviral drugs. The dual specificity protein phosphatase encoded by the smallpox virus (H1) is essential for the production of infectious viral particles, making it a promising molecular target for antiviral therapeutics. Here, we report the molecular cloning, overproduction, purification, and initial biochemical characterization of H1 phosphatase, thereby paving the way for the discovery of small molecule inhibitors. (c) 2006 Elsevier Inc. All rights reserved.

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External Sources

  1. DOI: 10.1016/j.pep.2006.05.007
  2. PMID: 16793284
  3. WOS: 000242260700005

Library Notes

  1. No notes added.
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