1997
DOI: 10.1016/s0305-0491(96)00232-5
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Age- and Radiation-Dependent Changes in Carbonyl Content, Susceptibility to Proteolysis, and Antigenicity of Soluble Rat Liver Proteins

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Cited by 13 publications
(2 citation statements)
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“…Repair processes for proteins modified by carbonylation have not been identified, and, instead, degradation is believed to be the primary mechanism for cellular regulation of proteome carbonylation (201). Increased levels of protein carbonyls have been noted after IR exposure (10 Gy) (310,317), and in addition, have been implicated in the pathophysiology of many human disease states, including chronic lung disease (357), neurodegenerative diseases (133), diabetes (2), and ischemiareperfusion injury [(84) and references therein].…”
Section: Protein Oxidationmentioning
confidence: 99%
“…Repair processes for proteins modified by carbonylation have not been identified, and, instead, degradation is believed to be the primary mechanism for cellular regulation of proteome carbonylation (201). Increased levels of protein carbonyls have been noted after IR exposure (10 Gy) (310,317), and in addition, have been implicated in the pathophysiology of many human disease states, including chronic lung disease (357), neurodegenerative diseases (133), diabetes (2), and ischemiareperfusion injury [(84) and references therein].…”
Section: Protein Oxidationmentioning
confidence: 99%
“…90). In fact, there is an increase in susceptibility to degradation by exogenous proteases of cytosolic proteins from liver of old rats (186), and from senescent fibroblasts (187), and it has been proposed that different age-specific protein modifications must contribute to the increased susceptibility to proteolytic attack (186).…”
Section: Discussionmentioning
confidence: 99%