ArticleACS chemical biology2020
Profiling Cysteine Reactivity and Oxidation in the Endoplasmic Reticulum.
Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
The trial behind it
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
22 citing papers in PubMed, 42 citations in OpenAlex.
- Trans-kingdom coupling of redox signaling to environmental cell stress responses through multiphase partitioning.bioRxiv : the preprint server for biology · 2026Article
- A niche-dependent redox rheostat regulates epithelial stem cell fate.Nature communications · 2025Article
- A Chemoproteomic Approach to Monitor Native Iron-Sulfur Cluster Binding.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Loss of Depalmitoylation Disrupts Homeostatic Plasticity of AMPARs in a Mouse Model of Infantile Neuronal Ceroid Lipofuscinosis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Ultra-rapid Electrophilic Cysteine Arylation.Journal of the American Chemical Society · 2023Article
- Solid-Phase Compatible Silane-Based Cleavable Linker Enables Custom Isobaric Quantitative Chemoproteomics.Journal of the American Chemical Society · 2023Article
- Proximity-labeling chemoproteomics defines the subcellular cysteinome and inflammation-responsive mitochondrial redoxome.Cell chemical biology · 2023Article
- Identifying Redox-Sensitive Cysteine Residues in Mitochondria.Antioxidants (Basel, Switzerland) · 2023Article
- Redox proteomics combined with proximity labeling enables monitoring of localized cysteine oxidation in cells.Cell chemical biology · 2023Article
- Spatial Chemoproteomics for Mapping the Active Proteome.Israel journal of chemistry · 2023Article
- Proximity-labeling chemoproteomics defines the subcellular cysteinome and inflammation-responsive mitochondrial redoxome.bioRxiv : the preprint server for biology · 2023Article
- Divergent Proteome Reactivity Influences Arm-Selective Activation of Pharmacological Endoplasmic Reticulum Proteostasis Regulators.bioRxiv : the preprint server for biology · 2023Article
- The role of s-palmitoylation in neurological diseases: implication for zDHHC family.Frontiers in pharmacology · 2023Review
- Identification of substrates of palmitoyl protein thioesterase 1 highlights roles of depalmitoylation in disulfide bond formation and synaptic function.PLoS biology · 2022Article
- Identifying Interaction Partners of Yeast Protein Disulfide Isomerases Using a Small Thiol-Reactive Cross-Linker: Implications for Secretory Pathway Proteostasis.Chemical research in toxicology · 2022Article
- The novel ER stress inducer Sec C triggers apoptosis by sulfating ER cysteine residues and degrading YAPActa pharmaceutica Sinica. B · 2022Article
- Contemporary proteomic strategies for cysteine redoxome profiling.Plant physiology · 2021Review
- SP3-FAIMS Chemoproteomics for High-Coverage Profiling of the Human Cysteinome*.Chembiochem : a European journal of chemical biology · 2021Article
- Global profiling of distinct cysteine redox forms reveals wide-ranging redox regulation in C. elegans.Nature communications · 2021Article
- Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The endoplasmic reticulum (ER) is the initial site of biogenesis of secretory pathway proteins, including proteins localized to the ER, Golgi, lysosomes, intracellular vesicles, plasma membrane, and extracellular compartments. Proteins within the secretory pathway contain a high abundance of disulfide bonds to protect against the oxidative extracellular environment. These disulfide bonds are typically formed within the ER by a variety of oxidoreductases, including members of the protein disulfide isomerase (PDI) family. Here, we establish chemoproteomic platforms to identify oxidized and reduced cysteine residues within the ER. Subcellular fractionation methods were utilized to enrich for the ER and significantly enhance the coverage of ER-localized cysteine residues. Reactive-cysteine profiling ranked ∼900 secretory pathway cysteines by reactivity with an iodoacetamide-alkyne probe, revealing functional cysteines annotated to participate in disulfide bonds, or
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Registered trials
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.