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08:31
Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
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PRESS: PRotEin S-Sulfenylation server.
Marianna Sakka1, Grigorios Tzortzis2, Michalis D Mantzaris3
1Department of Chemistry.
Bioinformatics (Oxford, England)
|May 18, 2016
Summary
Researchers developed the PRotEin S-Sulfenylation (PRESS) web server to predict S-sulfenylation sites on proteins. This tool aids in understanding redox regulation and its role in cell signaling, health, and disease.
Area of Science:
- Biochemistry
- Molecular Biology
- Bioinformatics
Background:
- Reactive oxygen species mediate transient S-sulfenylation of cysteine thiols, impacting cellular processes.
- Understanding S-sulfenylation is crucial for deciphering protein regulation under redox conditions and its role in disease.
Purpose of the Study:
- To develop a computational tool for predicting S-sulfenylation sites in proteins.
- To facilitate the discovery of novel protein functions regulated by redox conditions.
Main Methods:
- Development of the PRotEin S-Sulfenylation (PRESS) web server.
- Utilizing computational approaches to predict S-sulfenylation susceptibility of cysteine thiols.
Main Results:
- The PRESS web server effectively predicts cysteine thiols prone to S-sulfenylation.
- The server is expected to accelerate research into redox-mediated signaling pathways.
Conclusions:
- The PRESS web server provides a valuable resource for studying S-sulfenylation.
- This tool will advance the understanding of S-sulfenylation's role in cell signaling, human health, and disease.
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