Journal
BIOCHEMICAL JOURNAL
Volume 434, Issue -, Pages 201-210Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20101695
Keywords
actin; iron-sulfur cluster; lipid peroxidation; mistranslation; protein aggregation; protein oxidation
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Funding
- Natural Environment Research Council [NE/E005969/1]
- Biotechnology and Biological Sciences Research Council [BB/I000852/1]
- BBSRC [BB/I000852/1] Funding Source: UKRI
- NERC [NE/E005969/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/I000852/1] Funding Source: researchfish
- Natural Environment Research Council [NE/E005969/1] Funding Source: researchfish
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Aerobic life requires organisms to resist the damaging effects of ROS (reactive oxygen species), particularly during stress. Extensive research has established a detailed picture of how cells respond to oxidative stress. Attention is now focusing on identifying the key molecular targets of ROS, which cause killing when resistance is overwhelmed. Experimental criteria used to establish such targets have differing merits. Depending on the nature of the stress, ROS cause loss of essential cellular functions or gain of toxic functions. Essential targets on which life pivots during ROS stress include membrane lipid integrity and activity of ROS-susceptible proteins, including proteins required for faithful translation of mRNA. Protein oxidation also triggers accumulation of toxic protein aggregates or induction of apoptotic cell death. This burgeoning understanding of the principal ROS targets will offer new possibilities for therapy of ROS related diseases.
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