Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease.
By T. Grune, Tobias Jung, K. Merker, K. Davies. International Journal of Biochemistry and Cell Biology, 2004
666 citations recorded by the source corpus.
Subfields: Biochemistry, Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/7061a20c741060fb998c759c3e1a6e4643fbe2f3
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Biochemistry
In Cell Biology
In Molecular Biology
Citations in the corpus
- Role of oxidative carbonylation in protein quality control and senescence (2005, background): “Further, it is argued that this mechanism of inhibition of the proteasome is more dramatic in postmitotic cells, for example, neurons, than dividing cells since the latter can effectively dilute damaged proteins and aggregates by growth and proliferation (Grune et al, 2004).”
- Oxidative Stress Resistance in Deinococcus radiodurans (2011, background): “radiodurans and the age-dependent dramatic increase in the carbonyl content in animals and humans can be attributed to (i) an increased production of ROS (5, 581), (ii) a decline in antioxidant cell defenses (95, 391, 581), (iii) a diminished capacity for the removal of oxidized proteins by the prot”
- Oxidative Stress in Aging Human Skin (2015, background): “has lost efficiency and is even more inhibited by the formation of lipofuscin [230,231].”
- Protein carbonylation, cellular dysfunction, and disease progression (2006, background): “Therefore, heavily oxidized and cross-linked protein aggregates accumulate in cells because they inhibit the proteasome and actually cause a progressive further increase in protein aggregation and cross-linking in nondividing (post-mitotic) cells, and may eventually induce apoptosis, as demonstrated”
- Effect of Oxidation on the Emulsifying Properties of Myofibrillar Proteins (2013, background): “Oxidation may alter the secondary and tertiary structure of proteins, thereby increasing surface hydrophobicity (Grune et al. 2004).”
- Oxidative stress and neurodegeneration: where are we now? (2006, background): “Lowering proteasomal activity (by chemical inhibitors or antisense oligonucleotides) increases levels of oxidized proteins in cells, suggesting that their degradation proceeds via this system (Lee et al. 2001; Grune et al. 2003, 2004).”