Two domains unique to osteoblast-specific transcription factor Osf2/Cbfa1 contribute to its transactivation function and its inability to heterodimerize with Cbfbeta.

@article{Thirunavukkarasu1998TwoDU,
  title={Two domains unique to osteoblast-specific transcription factor Osf2/Cbfa1 contribute to its transactivation function and its inability to heterodimerize with Cbfbeta.},
  author={Kannan Thirunavukkarasu and Meenakshi Mahajan and Keith W McLarren and Stefano Stifani and Gerard Karsenty},
  journal={Molecular and cellular biology},
  year={1998},
  volume={18 7},
  pages={4197-208}
}
Osf2/Cbfa1, hereafter called Osf2, is a member of the Runt-related family of transcription factors that plays a critical role during osteoblast differentiation. Like all Runt-related proteins, it contains a runt domain, which is the DNA-binding domain, and a C-terminal proline-serine-threonine-rich (PST) domain thought to be the transcription activation domain. Additionally, Osf2 has two amino-terminal domains distinct from any other Runt-related protein. To understand the mechanisms of… CONTINUE READING
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STRUCTURE-FUNCTION ANALYSIS OF Osf2/Cbfa1 4207 on F ebuary 23

  • M. Kurokawa, T. Tanaka, K. Tanaka, N. Hirano, S. Ogawa, Y. K. Mitani
  • J. Biol. Chem
  • 1998
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