Verdin E, Ott M (2014). Nat Rev Mol Cell Biol.
Archives: Publications
Publications
Evolution of lysine acetylation in the RNA polymerase II C-terminal domain.
Simonti CN, Pollard KS, Schröder S, He D, Bruneau BG, Ott M, Capra JA (2015). BMC Evol Biol 15:35
doi: 10.1186/s12862-015-0327-z. PMID: 25887984; PMCID: PMC4362643.
A combined proteomics/genomics approach links hepatitis C virus infection with nonsense-mediated mRNA decay.
Ramage HR, Kumar GR, Verschueren E, Johnson JR, Von Dollen J, Johnson T, Newton B, Shah P, Horner J, Krogan NJ, Ott M.
doi: 10.1016/j.molcel.2014.12.028.
The hepatitis C virus core protein inhibits adipose triglyceride lipase (ATGL)-mediated lipid mobilization and enhances the ATGL interaction with comparative gene identification 58 (CGI-58) and lipid droplets.
Camus G, Schweiger M, Herker E, Harris C, Kondratowicz AS, Tsou C-L, Farese RV, Herath K, Previs SF, Roddy TP, Pinto S, Zechner R, Ott M (2014). J Biol Chem
doi: 10.1074/jbc.M114.587816. PMID: 25381252; PMCID: PMC4276846.
Evasion of superinfection exclusion and elimination of primary viral RNA by an adapted strain of hepatitis C virus.
Webster B, Ott M, Greene WC (2013). J Virol 87:13354–13369.
Acetylation of RNA Polymerase II Regulates Growth-Factor-Induced Gene Transcription in Mammalian Cells.
Schröder S, Herker E, Itzen F, He D, Thomas S, Gilchrist DA, Kaehlcke K, Cho S, Pollard KS, Capra JA, Schnolzer M, Cole PA, Geyer M, Bruneau BG, Adelman K, Ott M (2013). Mol Cell 52:314–324.
Acetylphosphate: a novel link between lysine acetylation and intermediary metabolism in bacteria.
Verdin E, Ott M (2013). Mol Cell 51:132–134.
Bromodomain Proteins in HIV Infection.
Boehm D, Conrad R, Ott M (2013). Viruses 5:1571–1586. doi: 10.3390/v5061571
Three rules for HIV latency: location, location, and location.
Ott M, Verdin E (2013). Cell Host Microbe 13:625–626.
How the antiviral immune response boosts liver fat.
Camus G, Ott M (2013). Nat Med 19:671–672.