Role of oxidative carbonylation in protein quality control and senescence

By T. Nyström. EMBO Journal, 2005

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How researchers see this paper

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Protein carbonylation, cellular dysfunction, and disease progression (2006, background): “Nyström and colleagues have proposed a possible role for protein carbonylation in protein quality control [72].”
Cellular Senescence: Defining a Path Forward. (2019, background): “Protein carbonylation exposes hydrophobic surfaces, leading to unfolding and aggregation, and protein carbonyl residues can be speciﬁcally detected using antibodies (Nystro¨m, 2005).”
Relationship between lipid and protein oxidation in fish (2019, positive): “Due to side chain oxidation of some amino acids (Arg, Lys, His and Pro) or backbone oxidation of Asp, Pro and Glu residues carbonylation can be considered as a per‐ manent and destructive (Hawkins & Davies, 2001) indicator of protein oxidation (Nystrom, 2005).”
A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy (2008, background): “The accumulation of damaged proteins and organelles is believed to be an important aspect of the aging process (22).”
Oxidative Stress Resistance in Deinococcus radiodurans (2011, background): “While there is some evidence that protein oxidation is a cause of cell death in oxidatively stressed bacteria (329), for human cells it is still unclear whether oxidative stress is a cause or a consequence of the primary disease process (117, 337, 465).”