ReviewJournal of the American Society for Mass Spectrometry2008
Top-down identification and characterization of biomolecules by mass spectrometry.
Review in Journal of the American Society for Mass Spectrometry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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
42 citing papers in PubMed.
- Top-Down Characterization of Yeast tRNA by Gas-Phase Fractionation and Collisionally Activated Dissociation Informed by Electron Photodetachment Charge Reduction Mass Spectrometry.Analytical chemistry · 2025Article
- A Review of Readout Circuit Schemes Using Silicon Nanowire Ion-Sensitive Field-Effect Transistors for pH-Sensing Applications.Biosensors · 2025Review
- Fourier-transform ion cyclotron resonance mass spectrometry for characterizing proteoforms.Mass spectrometry reviews · 2022Review
- Thermal Analysis of a Mixture of Ribosomal Proteins by vT-ESI-MS: Toward a Parallel Approach for Characterizing theAnalytical chemistry · 2021Article
- Mapping Microproteins and ncRNA-Encoded Polypeptides in Different Mouse Tissues.Frontiers in cell and developmental biology · 2021Article
- 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
- Small Packages, Big Returns: Uncovering the Venom Diversity of Small Invertebrate Conoidean Snails.Integrative and comparative biology · 2016Article
- A Structures for Lossless Ion Manipulations (SLIM) Module for Collision Induced Dissociation.Journal of the American Society for Mass Spectrometry · 2016Article
- Enhanced Dissociation of Intact Proteins with High Capacity Electron Transfer Dissociation.Journal of the American Society for Mass Spectrometry · 2016Article
- Enhancing Protein Disulfide Bond Cleavage by UV Excitation and Electron Capture Dissociation for Top-Down Mass Spectrometry.International journal of mass spectrometry · 2015Article
- Current strategies and findings in clinically relevant post-translational modification-specific proteomics.Expert review of proteomics · 2015Review
- Analyzing internal fragmentation of electrosprayed ubiquitin ions during beam-type collisional dissociation.Journal of the American Society for Mass Spectrometry · 2015Article
- Supercharging with m-nitrobenzyl alcohol and propylene carbonate: forming highly charged ions with extended, near-linear conformations.Analytical chemistry · 2015Article
- Revealing ligand binding sites and quantifying subunit variants of noncovalent protein complexes in a single native top-down FTICR MS experiment.Journal of the American Society for Mass Spectrometry · 2014Article
- Top-down MS for rapid methionine oxidation site assignment in filgrastim.Analytical and bioanalytical chemistry · 2013Article
- Deciphering post-translational modification codes.FEBS letters · 2013Review
- Competitive binding sites of a ruthenium arene anticancer complex on oligonucleotides studied by mass spectrometry: ladder-sequencing versus top-down.Journal of the American Society for Mass Spectrometry · 2013Article
- Characterization of modified RNA by top-down mass spectrometry.Angewandte Chemie (International ed. in English) · 2012Article
- The proteomics big challenge for biomarkers and new drug-targets discovery.International journal of molecular sciences · 2012Review
- Analysis of protein isoforms: can we do it better?Proteomics · 2012Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The most widely used modern mass spectrometers face severe performance limitations with molecules larger than a few kDa. For far larger biomolecules, a common practice has been to break these up chemically or enzymatically into fragments that are sufficiently small for the instrumentation available. With its many sophisticated recent enhancements, this "bottom-up" approach has proved highly valuable, such as for the rapid, routine identification and quantitation of DNA-predicted proteins in complex mixtures. Characterization of smaller molecules, however, has always measured the mass of the molecule and then that of its fragments. This "top-down" approach has been made possible for direct analysis of large biomolecules by the uniquely high (>10(5)) mass resolving power and accuracy ( approximately 1 ppm) of the Fourier-transform mass spectrometer. For complex mixtures, isolation of a single component's molecular ions for MS/MS not only gives biomolecule identifications of far higher reliability, but directly characterizes sequence errors and post-translational modifications. Protein sizes amenable for current MS/MS instrumentation are increased by a "middle-down" approach in which limited proteolysis forms large (e.g., 10 kDa) polypeptides that are then subjected to the top-down approach, or by "prefolding dissociation." The latter, which extends characterization to proteins >200 kDa, was made possible by greater understanding of how molecular ion tertiary structure evolves in the gas phase.
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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.