Discovery of an enzyme and substrate selective inhibitor of ADAM10 using an exosite-binding glycosylated substrate-Reference-Cited by-同舟云学术

Discovery of an enzyme and substrate selective inhibitor of ADAM10 using an exosite-binding glycosylated substrate

Published:2016-12 Issue:1 Volume:6 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Madoux Franck,Dreymuller Daniela,Pettiloud Jean-Phillipe,Santos Radleigh,Becker-Pauly Christoph,Ludwig Andreas,Fields Gregg B.,Bannister Thomas,Spicer Timothy P.,Cudic Mare,Scampavia Louis D.,Minond Dmitriy

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/s41598-016-0013-4.pdf

Reference58 articles.

1. Ni, S. S., Zhang, J., Zhao, W. L., Dong, X. C. & Wang, J. L. ADAM17 is overexpressed in non-small cell lung cancer and its expression correlates with poor patient survival. Tumour Biol 34, 1813–1818, doi: 10.1007/s13277-013-0721-3 (2013).

2. Ruff, M. et al. The Disintegrin and Metalloprotease ADAM12 Is Associated with TGF-beta-Induced Epithelial to Mesenchymal Transition. PLoS One 10, e0139179, doi: 10.1371/journal.pone.0139179 (2015).

3. Endres, K. & Fahrenholz, F. The Role of the anti-amyloidogenic secretase ADAM10 in shedding the APP-like proteins. Curr Alzheimer Res 9, 157–164 (2012).

4. Feldinger, K. et al. ADAM10 mediates trastuzumab resistance and is correlated with survival in HER2 positive breast cancer. Oncotarget 5, 6633–6646 (2014).

5. Gijsen, M. et al. HER2 phosphorylation is maintained by a PKB negative feedback loop in response to anti-HER2 herceptin in breast cancer. PLoS Biol 8, e1000563, doi: 10.1371/journal.pbio.1000563 (2010).

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