ArticleMethods in molecular biology (Clifton, N.J.)2019
Interrogation of Functional Mitochondrial Cysteine Residues by Quantitative Mass Spectrometry.
Article in Methods in molecular biology (Clifton, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed.
- Superoxide-responsive quinone methide precursors (QMP-SOs) to study superoxide biology by proximity labeling and chemoproteomics.RSC chemical biology · 2024Article
- Predicting cysteine reactivity changes upon phosphorylation using XGBoost.FEBS open bio · 2024Article
- Redox Signaling from Mitochondria: Signal Propagation and Its Targets.Biomolecules · 2020Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Mitochondria are cellular sites of diverse redox biology, including ROS production, iron-sulfur biogenesis, and secondary metabolism, which all rely on proteogenic reactive cysteine residues. Mass spectrometry-based proteomic methods to monitor the reactivity and functionality of cysteine residues across complex proteomes have greatly expanded over the past decade. Here we describe a mitochondrial isolation procedure coupled with cysteine-reactive IA labeling that affords identification and characterization of functional mitochondrial cysteine residues that were heretofore inaccessible to whole-cell proteomic analysis.
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Registered trials
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