ReviewProteomics2012
Electron transfer dissociation mass spectrometry in proteomics.
Review in Proteomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
48 citing papers in PubMed.
- Deep Proteoform Sequencing with Top-Down Direct Mass Technology.bioRxiv : the preprint server for biology · 2026Article
- Integration of alternative fragmentation techniques into standard LC-MS workflows using a single deep learning model enhances proteome coverage.Nature methods · 2026Article
- Review
- Linker H1 Histone Direct Top-Down Proteoform Analysis.Journal of proteome research · 2025Article
- Electron Capture Dissociation for Discovery Top-Down Proteomics of Peptides and Small Proteins on Chromatographic Time Scales.Journal of the American Society for Mass Spectrometry · 2025Article
- Histone Analysis Using Mobility- and Mass-Selected Ultraviolet Photodissociation in Tandem with Ultra-High-Resolution Mass Spectrometry.Analytical chemistry · 2025Article
- Capillary Zone Electrophoresis-Mass Spectrometry of Intact G Protein-Coupled Receptors Enables Proteoform Profiling.Analytical chemistry · 2025Article
- Emerging opportunities for intact and native protein analysis using chemical proteomics.Analytica chimica acta · 2025Review
- The Accurate Prediction of Antibody Deamidations by Combining High-Throughput Automated Peptide Mapping and Protein Language Model-Based Deep Learning.Antibodies (Basel, Switzerland) · 2024Article
- Top/Middle-Down Characterization of α-Synuclein Glycoforms.Analytical chemistry · 2023Article
- Review
- Top-"Double-Down" Mass Spectrometry of Histone H4 Proteoforms: Tandem Ultraviolet-Photon and Mobility/Mass-Selected Electron Capture Dissociations.Analytical chemistry · 2022Article
- Recent Advances in Mass Spectrometry-Based Structural Elucidation Techniques.Molecules (Basel, Switzerland) · 2022Review
- New free radical-initiated peptide sequencing (FRIPS) mass spectrometry reagent with high conjugation efficiency enabling single-step peptide sequencing.Scientific reports · 2022Article
- What's all the phos about? Insights into the phosphorylation state of the RNA polymerase II C-terminal domainRSC chemical biology · 2021Review
- Glycoproteogenomics: Setting the Course for Next-generation Cancer Neoantigen Discovery for Cancer Vaccines.Genomics, proteomics & bioinformatics · 2021Review
- Mass Spectrometry-Based Methods for Immunoglobulin G N-Glycosylation Analysis.Experientia supplementum (2012) · 2021Article
- Recent advances in the mass spectrometric analysis of glycosphingolipidome - A review.Analytica chimica acta · 2020Review
- Recent Developments in Gas-Phase Ion/Ion Reactions for Analytical Mass Spectrometry.Analytical chemistry · 2020Review
- Electron Transfer/Higher Energy Collisional Dissociation of Doubly Charged Peptide Ions: Identification of Labile Protein Phosphorylations.Journal of the American Society for Mass Spectrometry · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Mass spectrometry has rapidly evolved to become the platform of choice for proteomic analysis. While CID remains the major fragmentation method for peptide sequencing, electron transfer dissociation (ETD) is emerging as a complementary method for the characterization of peptides and post-translational modifications (PTMs). Here, we review the evolution of ETD and some of its newer applications including characterization of PTMs, non-tryptic peptides and intact proteins. We will also discuss some of the unique features of ETD such as its complementarity with CID and the use of alternating CID/ETD along with issues pertaining to analysis of ETD data. The potential of ETD for applications such as multiple reaction monitoring and proteogenomics in the future will also be discussed.
Indexed as
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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.