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

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Identification of a peptide fragment of DSCR1 that competitively inhibits calcineurin activity in vitro and in vivo.

Calcineurin phosphatase activity regulates the nuclear localization of the nuclear factor of activated T cells (NFAT) family of transcription factors during immune challenge. Calcineurin inhibitors, such as the cyclosporin A-cyclophilin A and FK506-FKBP12 complexes, regulate this enzymatic activity noncompetitively by binding at a site distinct from the enzyme active site. A family of endogenous protein inhibitors of calcineurin was recently identified and shown to block calcineurin-mediated NFAT nuclear localization and transcriptional activation. One such inhibitor, Down Syndrome Critical Region 1 (DSCR1), functions in T cell activation, cardiac hypertrophy, and angiogenesis. We have identified a small region of DSCR1 that is a potent inhibitor of calcineurin activity in vitro and in vivo.[1]

References

  1. Identification of a peptide fragment of DSCR1 that competitively inhibits calcineurin activity in vitro and in vivo. Chan, B., Greenan, G., McKeon, F., Ellenberger, T. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
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