ArticleJournal of the American Society for Mass Spectrometry2019
Development and Evaluation of a Reverse-Entry Ion Source Orbitrap Mass Spectrometer.
Article in Journal of the American Society for Mass Spectrometry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Development and Modification of Ion Mobility Mass Spectrometry Instrumentation for Enhanced Analysis of Biological Molecules.Journal of the American Society for Mass Spectrometry · 2025Review
- Improving the Quadrupole to Ion Mobility Region in a Digital Quadrupole/Ion Mobility/Orbitrap Mass Spectrometer.Journal of the American Society for Mass Spectrometry · 2025Article
- Article
- Modified Ion Source for the Improved Collisional Activation of Protein Complexes.Journal of the American Society for Mass Spectrometry · 2023Article
- Optimization of a Digital Mass Filter for the Isolation of Intact Protein Complexes in Stability Zone 1,1.Analytical chemistry · 2023Article
- Surface Activity of Amines Provides Evidence for the Combined ESI Mechanism of Charge Reduction for Protein Complexes.Analytical chemistry · 2022Article
- Investigating the Lipid Selectivity of Membrane Proteins in Heterogeneous Nanodiscs.Analytical chemistry · 2022Article
- Native Mass Spectrometry: Recent Progress and Remaining Challenges.Annual review of biophysics · 2022Review
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Implementing Digital-Waveform Technology for ExtendedJournal of the American Society for Mass Spectrometry · 2021Article
- Variable-Temperature Electrospray Ionization for Temperature-Dependent Folding/Refolding Reactions of Proteins and Ligand Binding.Analytical chemistry · 2021Article
- Native Mass Spectrometry of Membrane Proteins.Analytical chemistry · 2021Review
- Development of Native MS Capabilities on an Extended Mass Range Q-TOF MS.International journal of mass spectrometry · 2020Article
- Discovery of Potent Charge-Reducing Molecules for Native Ion Mobility Mass Spectrometry Studies.Analytical chemistry · 2020Article
- First-Principles Collision Cross Section Measurements of Large Proteins and Protein Complexes.Analytical chemistry · 2020Article
- Native IM-Orbitrap MS: Resolving What Was Hidden.Trends in analytical chemistry : TRAC · 2020Article
- Interpol review of detection and characterization of explosives and explosives residues 2016-2019.Forensic science international. Synergy · 2020Review
- Fundamental Studies of New Ionization Technologies and Insights from IMS-MS.Journal of the American Society for Mass Spectrometry · 2019Article
- Generation of Charge-Reduced Ions of Membrane Protein Complexes for Native Ion Mobility Mass Spectrometry Studies.Journal of the American Society for Mass Spectrometry · 2019Article
- Selective binding of a toxin and phosphatidylinositides to a mammalian potassium channel.Nature communications · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
Abstract
As a step towards development of a high-resolution ion mobility mass spectrometer using the orbitrap mass analyzer platform, we describe herein a novel reverse-entry ion source (REIS) coupled to the higher-energy C-trap dissociation (HCD) cell of an orbitrap mass spectrometer with extended mass range. Development of the REIS is a first step in the development of a drift tube ion mobility-orbitrap MS. The REIS approach retains the functionality of the commercial instrument ion source which permits the uninterrupted use of the instrument during development as well as performance comparisons between the two ion sources. Ubiquitin (8.5 kDa) and lipid binding to the ammonia transport channel (AmtB, 126 kDa) protein complex were used as model soluble and membrane proteins, respectively, to evaluate the performance of the REIS instrument. Mass resolution obtained with the REIS is comparable to that obtained using the commercial ion source. The charge state distributions for ubiquitin and AmtB obtained on the REIS are in agreement with previous studies which suggests that the REIS-orbitrap EMR retains native structure in the gas phase. Graphical Abstract ᅟ.
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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.