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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
Oxidant sensing by reversible disulfide bond formation.
Claudia M Cremers1, Ursula Jakob
1From the Departments of Molecular, Cellular, and Developmental Biology and.
The Journal of Biological Chemistry
|July 18, 2013
Summary
Maintaining cellular redox balance is vital for survival. Reversible protein modifications, like disulfide bonds, help regulate cell function in response to oxidative stress.
Area of Science:
- Biochemistry
- Cell Biology
- Oxidative Stress Research
Background:
- Cellular redox balance is critical for cell survival.
- Oxidative stress, caused by reactive oxygen, nitrogen, or chlorine species, can damage cellular components like DNA, lipids, and proteins.
- Proteins, especially methionine and cysteine residues, are highly susceptible to oxidative modifications.
Purpose of the Study:
- To investigate the regulatory roles of reversible oxidative protein modifications.
- To explore the significance of disulfide bond formation in mediating protein function changes.
- To understand how proteins adapt their activity to varying oxidant levels.
Main Methods:
- Analysis of protein oxidative modifications.
- Investigation of disulfide bond formation dynamics.
- Assessment of protein functional and structural changes in response to oxidative stress.
Main Results:
- Oxidative modifications of proteins, particularly methionine and cysteine, were observed.
- Reversible oxidative modifications were identified as key regulatory mechanisms.
- Disulfide bond formation was shown to induce extensive, reversible structural and functional protein alterations.
Conclusions:
- Reversible protein modifications, especially disulfide bonds, play a crucial role in cellular redox regulation.
- These modifications allow for rapid adjustments in protein activity, adapting to cellular oxidant levels.
- Understanding these mechanisms is vital for comprehending cell survival under oxidative stress.
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