All Outputs (3)

Discovery of peptide ligands targeting a specific ubiquitin-like domain– binding site in the deubiquitinase USP11 (2018)
Journal Article
Spiliotopoulos, A., Ferreras, L. B., Densham, R. M., Caulton, S. G., Maddison, B. C., Morris, J. R., …Dreveny, I. (2019). Discovery of peptide ligands targeting a specific ubiquitin-like domain– binding site in the deubiquitinase USP11. Journal of Biological Chemistry, 294(2), 424-436. https://doi.org/10.1074/jbc.RA118.004469

© 2019 Spiliotopoulos et al. Published by The American Society for Biochemistry and Molecular Biology, Inc. Ubiquitin-specific proteases (USPs) reverse ubiquitination and regulate virtually all cellular processes. Defined noncatalytic domains in USP... Read More about Discovery of peptide ligands targeting a specific ubiquitin-like domain– binding site in the deubiquitinase USP11.

The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel (2018)
Journal Article
Ward, S. J., Gratton, H. E., Indrayudha, P., Michavila, C., Mukhopadhyay, R., Maurer, S. K., …Dreveny, I. (2018). The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel. Journal of Biological Chemistry, 293(45), 17362-17374. https://doi.org/10.1074/jbc.RA118.003857

© 2018 Ward et al. Ubiquitin-specific protease 15 (USP15) regulates important cellular processes, including transforming growth factor β (TGF-β) signaling, mitophagy, mRNA processing, and innate immune responses; however, structural information on US... Read More about The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel.

Identification of lipases with activity towards monoacylglycerol by criterion of conserved cap architectures (2018)
Journal Article
Riegler-Berket, L., Leitmeier, A., Aschauer, P., Dreveny, I., & Oberer, M. (in press). Identification of lipases with activity towards monoacylglycerol by criterion of conserved cap architectures. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1863(7),

Monoacylglycerol lipases (MGL) are a subclass of lipases that predominantly hydrolyze monoacylglycerol (MG) into glycerol and fatty acid. MGLs are ubiquitous enzymes across species and play a role in lipid metabolism, affecting energy homeostasis and... Read More about Identification of lipases with activity towards monoacylglycerol by criterion of conserved cap architectures.