???pagination.result.count???
???pagination.result.page???
1
Proteolytic processing of von Willebrand factor by adamts13 and leukocyte proteases. , Lancellotti S, Basso M, De Cristofaro R., Mediterr J Hematol Infect Dis. September 2, 2013; 5 (1): e2013058.
The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains. , Wermter C, Höwel M, Hintze V, Bombosch B, Aufenvenne K, Yiallouros I, Stöcker W., Biol Chem. May 1, 2007; 388 (5): 513-21.
The interaction of recombinant subdomains of the procollagen C-proteinase with procollagen I provides a quantitative explanation for functional differences between the two splice variants, mammalian tolloid and bone morphogenetic protein 1. , Hintze V, Höwel M, Wermter C, Grosse Berkhoff E, Becker-Pauly C, Beermann B, Yiallouros I, Stöcker W., Biochemistry. May 30, 2006; 45 (21): 6741-8.
Characterization of a homolog of human bone morphogenetic protein 1 in the embryo of the sea urchin, Strongylocentrotus purpuratus. , Hwang SP, Partin JS, Lennarz WJ ., Development. March 1, 1994; 120 (3): 559-68.
Spatial and temporal expression pattern during sea urchin embryogenesis of a gene coding for a protease homologous to the human protein BMP-1 and to the product of the Drosophila dorsal-ventral patterning gene tolloid. , Lepage T , Ghiglione C, Gache C., Development. January 1, 1992; 114 (1): 147-63.