Role of dimerization and substrate exclusion in the regulation of bone morphogenetic protein-1 and mammalian tolloid.

@article{Berry2009RoleOD,
  title={Role of dimerization and substrate exclusion in the regulation of bone morphogenetic protein-1 and mammalian tolloid.},
  author={Richard M. Berry and Thomas Adam Jowitt and Johanna Ferrand and Manfred Roessle and J. G{\"u}nter Grossmann and Elizabeth Gail Canty-Laird and Richard A. Kammerer and Karl E Kadler and Clair Baldock},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 21},
  pages={8561-6}
}
The bone morphogenetic protein (BMP)-1/tolloid metalloproteinases are evolutionarily conserved enzymes that are fundamental to dorsal-ventral patterning and tissue morphogenesis. The lack of knowledge regarding how these proteinases recognize and cleave their substrates represents a major hurdle to understanding tissue assembly and embryonic patterning. Although BMP-1 and mammalian tolloid (mTLD) are splice variants, it is puzzling why BMP-1, which lacks 3 of the 7 noncatalytic domains present… CONTINUE READING
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Bone morphogenetic protein-1/tolloid-related metalloproteinases process osteoglycin and enhance its ability to regulate collagen fibrillogenesis

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