| First Author | Lorenzen I | Year | 2011 |
| Journal | Biochem Biophys Res Commun | Volume | 415 |
| Issue | 2 | Pages | 330-6 |
| PubMed ID | 22033402 | Mgi Jnum | J:178752 |
| Mgi Id | MGI:5300094 | Doi | 10.1016/j.bbrc.2011.10.056 |
| Citation | Lorenzen I, et al. (2011) Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain. Biochem Biophys Res Commun 415(2):330-6 |
| abstractText | A disintegrin and metalloprotease protein 17 (ADAM17) is a transmembrane zinc dependent metalloprotease. The catalytic activity of the enzyme results in the shedding of a broad range of membrane proteins. The release of the corresponding ectodomains induces a switch in various physiological and pathophysiological processes. So far there is not much information about the molecular mechanism of ADAM17 activation available. As for other transmembrane proteases, multimerisation may play a critical role in the activation and function of ADAM17. The present work demonstrates that ADAM17 indeed exists as a multimer in the cell membrane and that this multimerisation is mediated by its EGF-like domain. |
