ArticleInternational journal of mass spectrometry2011
Cleavage of Multiple Disulfide Bonds in Insulin via Gold Cationization and Collision-induced Dissociation.
Article in International journal of mass spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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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
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Who cites it
14 citing papers in PubMed.
- Recent Developments in Gas-Phase Ion/Ion Reactions for Analytical Mass Spectrometry.Analytical chemistry · 2020Review
- Gold(I) Cationization Promotes Ring Opening in Lysine-Containing Cyclic Peptides.Journal of the American Society for Mass Spectrometry · 2019Article
- Top-Down Characterization of Proteins with Intact Disulfide Bonds Using Activated-Ion Electron Transfer Dissociation.Analytical chemistry · 2018Article
- In-Source Reduction of Disulfide-Bonded Peptides Monitored by Ion Mobility Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018Article
- Novel Peptide Ion Chemistry Associated with Gold (I) Cationization: Preferential Cleavage at Lysine Residues.International journal of mass spectrometry · 2018Article
- Top-Down Charge Transfer Dissociation (CTD) of Gas-Phase Insulin: Evidence of a One-Step, Two-Electron Oxidation Mechanism.Journal of the American Society for Mass Spectrometry · 2018Article
- Gas-Phase Oxidation via Ion/Ion Reactions: Pathways and Applications.Journal of the American Society for Mass Spectrometry · 2017Article
- Selective Gas-Phase Ion/Ion Reactions: Enabling Disulfide Mapping via Oxidation and Cleavage of Disulfide Bonds in Intermolecularly-Linked Polypeptide Ions.Analytical chemistry · 2016Article
- Enhancing Protein Disulfide Bond Cleavage by UV Excitation and Electron Capture Dissociation for Top-Down Mass Spectrometry.International journal of mass spectrometry · 2015Article
- Mechanisms and energetics of free radical initiated disulfide bond cleavage in model peptides and insulin by mass spectrometry.Chemical science · 2015Article
- Increasing Fragmentation of Disulfide-Bonded Proteins for Top-Down Mass Spectrometry by Supercharging.International journal of mass spectrometry · 2015Article
- Gas-phase transformation of phosphatidylcholine cations to structurally informative anions via ion/ion chemistry.Analytical chemistry · 2013Article
- Gas-phase ion/ion reactions of peptides and proteins: acid/base, redox, and covalent chemistries.Chemical communications (Cambridge, England) · 2013Article
- Electron transfer dissociation (ETD) of peptides containing intrachain disulfide bonds.Journal of the American Society for Mass Spectrometry · 2012Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Intact bovine insulin, with its two chains linked via two disulfide linkages, has been used as a model system to study the incorporation of one or more gold cations as means for facilitating the cleavage of multiple disulfide bonds in a tandem mass spectrometry experiment. Gas-phase ion/ion reactions involving Au(I)Cl(2) (-) or Au(III)Cl(4) (-) were used to incorporate either one or two gold cations into multiply-protonated insulin cations, followed by ion trap collision-induced dissociation (CID) of the products. The incorporation of a single gold cation followed by CID showed little evidence for disulfide bond cleavage. Rather, the CID spectra were similar to those acquired for the same charge state with only excess protons present. However, the incorporation of two gold cations, regardless of oxidation state, resulted in efficient cleavage of the disulfide bonds connecting the two chains of insulin. Furthermore, ion trap CID of the insulin complexes containing two gold cations showed more sequence information compared to the complexes containing only one gold cation or no gold cations. The partitioning of the gold cations between the two chains upon CID proved to be largely asymmetric, as both gold cations tended to stay together. There appeared to be a slight preference for both gold cations to partition into the B-chain. However, the relatively low contribution from single chain ions with only one gold ion suggests a degree of cooperativity in the overall mechanism for separation of the two chains.
Identifiers
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Registered trials
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