Reagents
These reagents are crystallization-quality pure, as used in the following structural studies:
- Allendorph GP et al., Structure of the ternary signaling complex of a TGF-beta superfamily member. Proc Natl Acad Sci U S A. 2006 May 16;103(20):7643-8.
- Allendorph GP et al., BMP-3 and BMP-6 structures illuminate the nature of binding specificity with receptors. Biochemistry. 2007 Oct 30;46(43):12238-47.
- Greenwald J et al., Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase. Nat Struct Biol. 1999 Jan;6(1):18-22.
- Greenwald J et al., The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly. Mol Cell. 2003 Mar;11(3):605-17.
- Greenwald J et al., A flexible activin explains the membrane-dependent cooperative assembly of TGF-beta family receptors. Mol Cell. 2004 Aug 13;15(3):485-9.
- Groppe J et al., Structural basis of BMP signalling inhibition by the cystine knot protein Noggin. Nature. 2002 Dec 12;420(6916):636-42.
- Allendorph GP et al., Designer TGF-beta superfamily ligands with diversified functionality. PLoS One. 2011;6(11):e26402.
- Yoon BH et al., An activin A/BMP2 chimera, AB204, displays bone-healing properties superior to those of BMP2. J Bone Miner Res. 2014 Sep;29(9):1950-9.
- Kuo MM et al., BMP-9 as a potent brown adipogenic inducer with anti-obesity capacity. Biomaterials. 2014 Mar;35(10):3172-9.
- Kuo MM et al., MB109 as bioactive human bone morphogenetic protein-9 refolded and purified from E. coli inclusion bodies. Microb Cell Fact. 2014 Feb 24;13(1):29.
