B12 SENGLE

Latent transforming growth factor beta-binding proteins and fibulins compete for fibrillin-1 and exhibit exquisite specificities in binding sites

B12 SENGLEOno, R.N., Sengle, G., Charbonneau, N.L., Carlberg, V., Bächinger, H.P., Sasaki, T., Lee-Arteaga, S., Zilberberg, L., Rifkin, D.B., Ramirez, F., Chu, M.L., and Sakai, L.Y., J Biol Chem. 2009 Jun 19;284(25):16872-81. doi: 10.1074/jbc.M809348200. Epub 2009 Apr 6.

Abstract Latent transforming growth factor (TGF) beta-binding proteins (LTBPs) interact with fibrillin-1. This interaction is important for proper sequestration and extracellular control of TGFbeta....   Read More

A new model for growth factor activation: type II receptors compete with the prodomain for BMP-7

B12 SENGLESengle, G., Ono, R., Lyons, K.M., Bächinger, H.P., and Sakai, L.Y., J Mol Biol. 2008 Sep 12;381(4):1025-39. doi: 10.1016/j.jmb.2008.06.074. Epub 2008 Jul 2.

Abstract Bone morphogenetic proteins (BMPs) are morphogens with long-range signaling activities. BMP-7 is secreted as a stable complex consisting of a growth factor noncovalently...   Read More

Targeting of bone morphogenetic protein growth factor complexes to fibrillin

B12 SENGLE Sengle, G., Charbonneau, N.L., Ono, R.N., Sasaki, T., Alvarez, J., Keene, D.R., Bächinger H.P., and Sakai, L.Y., J Biol Chem. 2008 May 16;283(20):13874-88. doi: 10.1074/jbc.M707820200. Epub 2008 Mar 13.

Abstract Both latent transforming growth factor-beta (TGF-beta)-binding proteins fibrillins are components of microfibril networks, and both interact with members of the TGF-beta family of...   Read More

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