title: ISG15 uncut: Dissecting enzymatic and non-enzymatic functions of USP18 in vivo.
abstract: Posttranslational protein modification by ISG15 plays an important role in antiviral defense. We selectively inactivated the ISG15 isopeptidase activity of USP18 in mice. Increased ISGylation was accompanied by enhanced viral resistance without causing detrimental side effects suggesting that USP18 protease inhibition might be a suitable antiviral strategy.
authors: R&D LGCR, Sanofi-Aventis Deutschland GmbH, 65926 Frankfurt am Main, Germany.
authors: Lars
authors: L
authors: Ketscher
authors: Institute of Neuropathology, University of Freiburg, 79106 Freiburg, Germany. Electronic address: Klaus-Peter.Knobeloch@uniklinik-freiburg.de.
authors: Klaus-Peter
authors: KP
authors: Knobeloch
mesh_terms: D000818:Animals; D016207:Cytokines / Q000378:metabolism*; D051379:Mice; D011499:Protein Processing, Post-Translational; D043222:Ubiquitin Thiolesterase / Q000378:metabolism*; D014452:Ubiquitins / Q000378:metabolism
chemical_list: D016207:Cytokines; C489550:G1p2 protein, mouse; D014452:Ubiquitins; C118306:Usp18 protein, mouse; D043222:Ubiquitin Thiolesterase
keywords: ISG15; Interferon; Stat1; USP18; Virus