2nd communication: from RERO Explore to swisscovery: Part of RERO's libraries joined the SLSP (Swiss Library Service Platform) network at the beginning of December 2020. See the implications (2nd communication in French / in German) of this change for you as a user.
Haeussler, Dagmar J, Pimentel, David R, Hou, Xiuyun, Burgoyne, Joseph R, Cohen, Richard A, Bachschmid, Markus M
The Journal of biological chemistry, 24 May 2013, Vol.288(21), pp.15380-9
[Peer Reviewed Journal]
MEDLINE/PubMed (U.S. National Library of Medicine)
Checkpoints in Adenoviral Production: Cross-Contamination and E1A (Checkpoints in Adenoviral Production)
Haeussler, Dagmar J, Evangelista, Alicia M, Burgoyne, Joseph R, Cohen, Richard A, Bachschmid, Markus M, Pimental, David R
PLoS ONE, 2011, Vol.6(8), p.e23160
[Peer Reviewed Journal]
Shao, Di, Fry, Jessica L, Han, Jingyan, Hou, Xiuyun, Pimentel, David R, Matsui, Reiko, Cohen, Richard A, Bachschmid, Markus M
The Journal of biological chemistry, 14 March 2014, Vol.289(11), pp.7293-306
[Peer Reviewed Journal]
MEDLINE/PubMed (U.S. National Library of Medicine)
Title: A redox-resistant sirtuin-1 mutant protects against hepatic metabolic and oxidant stress Author:Shao, Di; Fry, Jessica L; Han, Jingyan; Hou, Xiuyun; Pimentel, David R; Matsui, Reiko; Cohen, Richard A; Bachschmid, Markus M Subject:Glutathiolation ; Glutathionylation ; High Fat High Sucrose Diet ; Metabolic Diseases ; Oxidative Stress ; Polyphenols ; Reactive Oxygen and Nitrogen Species ; Resveratrol ; Apoptosis ; Mutation ; Oxidative Stress ; Liver -- Metabolism ; Sirtuin 1 -- Genetics Description:
Sirtuin-1 (SirT1), a member of the NAD(+)-dependent class III histone deacetylase family, is inactivated in vitro by oxidation of critical cysteine thiols. In a model of metabolic syndrome, SirT1 activation attenuated apoptosis of hepatocytes and improved liver function including lipid metabolism. We show in SirT1-overexpressing HepG2 cells that oxidants (nitrosocysteine and hydrogen peroxide) or metabolic stress (high palmitate and high glucose) inactivated SirT1 by reversible oxidative post-translational modifications (OPTMs) on three cysteines. Mutating these oxidation-sensitive cysteines to serine preserved SirT1 activity and abolished reversible OPTMs. Overexpressed mutant SirT1 maintained deacetylase activity and attenuated proapoptotic signaling, whereas overexpressed wild type SirT1 was less protective in metabolically or oxidant-stressed cells. To prove that OPTMs of SirT1 are glutathione (GSH) adducts, glutaredoxin-1 was overexpressed to remove this modification. Glutaredoxin-1...
Is part of:
The Journal of biological chemistry, 14 March 2014, Vol.289(11), pp.7293-306
Identifier:
1083-351X (E-ISSN); 24451382 Version (PMID); 10.1074/jbc.M113.520403 (DOI)