ArticleJournal of the American Society for Mass Spectrometry2017
Charge Mediated Compaction and Rearrangement of Gas-Phase Proteins: A Case Study Considering Two Proteins at Opposing Ends of the Structure-Disorder Continuum.
Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed.
- Hyphenated Mass Spectrometry-Based Strategies for Characterizing Oligomers of α‑Synuclein in Parkinson's Disease.ACS central science · 2026Article
- Characterization of Gas-Phase Native(-like) Proteins Using Structures for Lossless Ion Manipulations.Analytical chemistry · 2026Article
- Impact of Post-Translational Succination on Small Ubiquitin-Like Modifier 1 Structure: A Dual Approach Combining Gas Phase and Solution Studies.ACS pharmacology & translational science · 2025Article
- Mass spectrometry structural analysis of intrinsically disordered phosphoproteins.International journal of mass spectrometry · 2025Article
- Charging of DNA Complexes in Positive-Mode Native Electrospray Ionization Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Revealing the Fates of Proteins in the Gas Phase.International journal of mass spectrometry · 2024Article
- Exploring the Conformational Landscape of Poly(l-lysine) Dendrimers Using Ion Mobility Mass Spectrometry.Analytical chemistry · 2024Article
- Comparative Structural Analysis of 20S Proteasome Ortholog Protein Complexes by Native Mass Spectrometry.ACS central science · 2020Article
- Recent Developments in Gas-Phase Ion/Ion Reactions for Analytical Mass Spectrometry.Analytical chemistry · 2020Review
- Standard Proteoforms and Their Complexes for Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Determination of Gas-Phase Ion Structures of Locally Polar Homopolymers Through High-Resolution Ion Mobility Spectrometry-Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- The application of ion-mobility mass spectrometry for structure/function investigation of protein complexes.Current opinion in chemical biology · 2018Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Charge reduction in the gas phase provides a direct means of manipulating protein charge state, and when coupled to ion mobility mass spectrometry (IM-MS), it is possible to monitor the effect of charge on protein conformation in the absence of solution. Use of the electron transfer reagent 1,3-dicyanobenzene, coupled with IM-MS, allows us to monitor the effect of charge reduction on the conformation of two proteins deliberately chosen from opposite sides of the order to disorder continuum: bovine pancreatic trypsin inhibitor (BPTI) and beta casein. The ordered BPTI presents compact conformers for each of three charge states accompanied by narrow collision cross-section distributions (
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Registered trials
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