ArticleCell chemical biology2016
Chemoproteomic Strategy to Quantitatively Monitor Transnitrosation Uncovers Functionally Relevant S-Nitrosation Sites on Cathepsin D and HADH2.
Article in Cell chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- Identification of Protein Targets ofACS chemical biology · 2024Article
- S-Nitrosylation of cathepsin B affects autophagic flux and accumulation of protein aggregates in neurodegenerative disorders.Cell death and differentiation · 2022Article
- An infection-induced oxidation site regulates legumain processing and tumor growth.Nature chemical biology · 2022Article
- SP3-Enabled Rapid and High Coverage Chemoproteomic Identification of Cell-State-Dependent Redox-Sensitive Cysteines.Molecular & cellular proteomics : MCP · 2022Article
- Chemoproteomic interrogation of selenocysteine by low-pH isoTOP-ABPP.Methods in enzymology · 2022Article
- Protein S-nitrosylation and oxidation contribute to protein misfolding in neurodegeneration.Free radical biology & medicine · 2021Review
- Nitric Oxide-Dependent Protein Post-Translational Modifications Impair Mitochondrial Function and Metabolism to Contribute to Neurodegenerative Diseases.Antioxidants & redox signaling · 2020Review
- Profiling Cysteine Reactivity and Oxidation in the Endoplasmic Reticulum.ACS chemical biology · 2020Article
- Chemical Biology Approaches to Interrogate the Selenoproteome.Accounts of chemical research · 2019Review
- Reactive-cysteine profiling for drug discovery.Current opinion in chemical biology · 2019Review
- Chemical Probes for Redox Signaling and Oxidative Stress.Antioxidants & redox signaling · 2019Review
- A chemoproteomic portrait of the oncometabolite fumarate.Nature chemical biology · 2019Article
- Interrogation of Functional Mitochondrial Cysteine Residues by Quantitative Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Redox Signaling by Reactive Electrophiles and Oxidants.Chemical reviews · 2018Review
- A Quantitative Chemoproteomic Platform to Monitor Selenocysteine Reactivity within a Complex Proteome.Cell chemical biology · 2018Article
- Redox regulation of cell proliferation: Bioinformatics and redox proteomics approaches to identify redox-sensitive cell cycle regulators.Free radical biology & medicine · 2018Review
- Isotopically-Labeled Iodoacetamide-Alkyne Probes for Quantitative Cysteine-Reactivity Profiling.Molecular pharmaceutics · 2018Article
- Global profiling of lysine reactivity and ligandability in the human proteome.Nature chemistry · 2017Article
- Systematic and Quantitative Assessment of Hydrogen Peroxide Reactivity With Cysteines Across Human Proteomes.Molecular & cellular proteomics : MCP · 2017Article
- Identifying Functional Cysteine Residues in the Mitochondria.ACS chemical biology · 2017Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
S-Nitrosoglutathione (GSNO) is an endogenous transnitrosation donor involved in S-nitrosation of a variety of cellular proteins, thereby regulating diverse protein functions. Quantitative proteomic methods are necessary to establish which cysteine residues are most sensitive to GSNO-mediated transnitrosation. Here, a competitive cysteine-reactivity profiling strategy was implemented to quantitatively measure the sensitivity of >600 cysteine residues to transnitrosation by GSNO. This platform identified a subset of cysteine residues with a high propensity for GSNO-mediated transnitrosation. Functional characterization of previously unannotated S-nitrosation sites revealed that S-nitrosation of a cysteine residue distal to the 3-hydroxyacyl-CoA dehydrogenase type 2 (HADH2) active site impaired catalytic activity. Similarly, S-nitrosation of a non-catalytic cysteine residue in the lysosomal aspartyl protease cathepsin D (CTSD) inhibited proteolytic activation. Together, these studies revealed two previously uncharacterized cysteine residues that regulate protein function, and established a chemical-proteomic platform with capabilities to determine substrate specificity of other cellular transnitrosation agents.
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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.