ArticleProteomics2013
High throughput screening of disulfide-containing proteins in a complex mixture.
Article in Proteomics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 16 citations in OpenAlex.
- BotCl, the First Chlorotoxin-like Peptide Inhibiting Newcastle Disease Virus: The Emergence of a New Scorpion Venom AMPs Family.Molecules (Basel, Switzerland) · 2023Article
- Top-down mass spectrometry and assigning internal fragments for determining disulfide bond positions in proteins.The Analyst · 2022Article
- Dimerization interface of osteoprotegerin revealed by hydrogen-deuterium exchange mass spectrometry.The Journal of biological chemistry · 2018Article
- Top-Down Characterization of Proteins with Intact Disulfide Bonds Using Activated-Ion Electron Transfer Dissociation.Analytical chemistry · 2018Article
- Custom selenoprotein production enabled by laboratory evolution of recoded bacterial strains.Nature biotechnology · 2018Article
- Small molecule metalloprotease inhibitor with in vitro, ex vivo and in vivo efficacy against botulinum neurotoxin serotype A.Toxicon : official journal of the International Society on Toxinology · 2017Article
- Detection of ROS Induced Proteomic Signatures by Mass Spectrometry.Frontiers in physiology · 2017Review
- Top-down mass spectrometry of cardiac myofilament proteins in health and disease.Proteomics. Clinical applications · 2014Review
- Finding the missing link: disulfide-containing proteins via a high-throughput proteomics approach.Proteomics · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The formation of disulfide bonds between cysteine residues is crucial for the stabilization of native protein structures and, thus, determination of disulfide linkages is an important facet of protein structural characterization. Nonetheless, the identification of disulfide bond linkages remains a significant analytical challenge, particularly in large proteins with complex disulfide patterns. Herein, we have developed a new LC/MS strategy for rapid screening of disulfides in an intact protein mixture after a straightforward reduction step with tris(2-carboxyethyl)phosphine. LC/MS analysis of reduced and nonreduced protein mixtures quickly revealed disulfide-containing proteins owing to a 2 Da mass increase per disulfide reduction and, subsequently, the total number of disulfide bonds in the intact proteins could be determined. We have demonstrated the effectiveness of this method in a protein mixture composed of both disulfide-containing and disulfide-free proteins. Our method is simple (no need for proteolytic digestion, alkylation, or the removal of reducing agents prior to MS analysis), high throughput (fast on-line LC/MS analysis), and reliable (no S-S scrambling), underscoring its potential as a rapid disulfide screening method for proteomics applications.
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What OpenQuestion holds
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.