Papers associated with LOC105441151 (and LOC582189)

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	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.
	Identification of an astacin-like metallo-proteinase transcript from the infective larvae of Strongyloides stercoralis., Gomez Gallego S, Loukas A, Slade RW, Neva FA, Varatharajalu R, Nutman TB, Brindley PJ., Parasitol Int. June 1, 2005; 54 (2): 123-33.
	Bone morphogenetic protein-1 (BMP-1). Identification of the minimal domain structure for procollagen C-proteinase activity., Hartigan N, Garrigue-Antar L, Kadler KE., J Biol Chem. May 16, 2003; 278 (20): 18045-9.
	Interaction properties of human mannan-binding lectin (MBL)-associated serine proteases-1 and -2, MBL-associated protein 19, and MBL., Thielens NM, Cseh S, Thiel S, Vorup-Jensen T, Rossi V, Jensenius JC, Arlaud GJ., J Immunol. April 15, 2001; 166 (8): 5068-77.

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