The emerging process of Top Down mass spectrometry for protein analysis: biomarkers, protein-therapeutics, and achieving high throughput
Open accessAbstract
Top Down mass spectrometry (MS) has emerged as an alternative to common Bottom Up strategies for protein analysis. In the Top Down approach, intact proteins are fragmented directly in the mass spectrometer to achieve both protein identification and characterization, even capturing information on combinatorial post-translational modifications. Just in the past two years, Top Down MS has seen incremental advances in instrumentation and dedicated software, and has also experienced a major boost from refined separations of whole proteins in complex mixtures that have both high recovery and reproducibility. Combined with steadily advancing commercial MS instrumentation and data processing, a high-throughput workflow covering intact proteins and polypeptides up to 70 kDa is directly visible in the near future.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
The citation lists haven’t been fetched yet
References 52 · Cited by 99
- Authors
- Kellie, J. F., Tran, J. C., Lee, J. E., Ahlf, D. R., Thomas, H. M., Ntai, I., Catherman, A. D., Durbin, K. R., Zamdborg, L., Vellaichamy, A., Thomas, P. M., & Kelleher, N. L.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- Corresponding author
- Kelleher, Neil L
- ORCID
- Venue
- Molecular BioSystems
- Publisher
- Oxford University Press (OUP)
- Published
- 2010-03-29
- Volume
- 6
- Issue
- 9
- Pages
- 1532-1539
- ISSN
- 1742-2051 (ISSN-L)
- 1742-206X
- PMC
- PMC3115741
- OpenAlex
- W2119425965
- Cited by
- 99
- References
- 52
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 1 · 2023: 4 · 2022: 3 · 2021: 5 · 2020: 3 · 2019: 2 · 2018: 4 · 2017: 11 · 2016: 4 · 2015: 9 · 2014: 14 · 2013: 14 · 2012: 10
- FWCI
- 5.28
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular BioSystems (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- David and Lucile Packard Foundation
- National Institute of General Medical Sciences (R01GM067193, GM 067193)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Keywords
- top-down mass spectrometry, protein analysis, biomarkers, therapeutic proteins, post-translational modification, high-throughput proteomics, protein separation, polypeptides
- MeSH terms
- HeLa Cells, Humans, Proteins, Mass Spectrometry, Biomarkers, Proteomics
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review