ArticleACS chemical biology2015
A Chemical Approach for the Detection of Protein Sulfinylation.
Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 70 citations in OpenAlex.
- Profiling the landscape of cysteine posttranslational modifications in brain aging and neurodegeneration.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Review
- Redox regulation by sulfiredoxin-1: bridging cysteine oxidation and liver disease therapeutics.Experimental & molecular medicine · 2025Review
- ROS-mediated regulation of β2AR function: Does oxidation play a meaningful role towards β2-agonist tachyphylaxis in airway obstructive diseases?Biochemical pharmacology · 2024Review
- Agonists and hydrogen peroxide mediate hyperoxidation of β2-adrenergic receptor in airway epithelial cells: Implications for tachyphylaxis to β2-agonists in constrictive airway disorders.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023Article
- Chemical biology approaches to uncovering nuclear ROS control.Current opinion in chemical biology · 2023Review
- Thiol redox proteomics: Characterization of thiol-based post-translational modifications.Proteomics · 2023Review
- Article
- Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs.Redox biology · 2023Article
- Oxidative Stress in Age-Related Neurodegenerative Diseases: An Overview of Recent Tools and Findings.Antioxidants (Basel, Switzerland) · 2023Review
- Oxidative Cysteine Modification of Thiol Isomerases in Thrombotic Disease: A Hypothesis.Antioxidants & redox signaling · 2021Review
- Measuring ROS and redox markers in plant cells.RSC chemical biology · 2021Review
- Irreversible inhibition of BoNT/A protease: proximity-driven reactivity contingent upon a bifunctional approach.RSC medicinal chemistry · 2021Article
- Contemporary proteomic strategies for cysteine redoxome profiling.Plant physiology · 2021Review
- The redox language in neurodegenerative diseases: oxidative post-translational modifications by hydrogen peroxide.Cell death & disease · 2021Review
- Regulation of the Proteolytic Activity of Cysteine Cathepsins by Oxidants.International journal of molecular sciences · 2020Review
- Structural preferences of cysteine sulfinic acid: The sulfinate engages in multiple local interactions with the peptide backbone.Free radical biology & medicine · 2020Article
- Activity-Based Sensing for Site-Specific Proteomic Analysis of Cysteine Oxidation.Accounts of chemical research · 2020Review
- Detection, identification, and quantification of oxidative protein modifications.The Journal of biological chemistry · 2019Review
- The relationship between DJ-1 and S100A8 in human primary alveolar type II cells in emphysema.American journal of physiology. Lung cellular and molecular physiology · 2019Article
- Chemical Probes for Redox Signaling and Oxidative Stress.Antioxidants & redox signaling · 2019Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Protein sulfinic acids are formed by the reaction of reactive oxygen species with protein thiols. Sulfinic acid formation has long been considered an irreversible state of oxidation and is associated with high cellular oxidative stress. Increasing evidence, however, indicates that cysteine is oxidized to sulfinic acid in cells to a greater extent, and is more controlled, than first thought. The discovery of sulfiredoxin has demonstrated that cysteine sulfinic acid can be reversed, pointing to a vast array of potential implications for redox biology. Identification of the site of protein sulfinylation is crucial in clarifying the physiological and pathological effects of post-translational modifications. Currently, the only methods for detection of sulfinic acids involve mass spectroscopy and the use of specific antibodies. However, these methodologies are not suitable for proteomic studies. Herein, we report the first probe for detection of protein sulfinylation, NO-Bio, which combines a C-nitroso warhead for rapid labeling of sulfinic acid with a biotin handle. Based on this new tool, we developed a selective two-step approach. In the first, a sulfhydryl-reactive compound is introduced to selectively block free cysteine residues. Thereafter, the sample is treated with NO-Bio to label sulfinic acids. This new technology represents a rapid, selective, and general technology for sulfinic acid detection in biological samples. As proof of our concept, we also evaluated protein sulfinylation levels in various human lung tumor tissue lysates. Our preliminary results suggest that cancer tissues generally have higher levels of sulfinylation in comparison to matched normal tissues. A new ability to monitor protein sulfinylation directly should greatly expand the impact of sulfinic acid as a post-translational modification.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.