Evidence map›Paper›PMID 21826297›Full record

ReviewThe Analyst2011

Top-down mass spectrometry: recent developments, applications and perspectives.

Weidong Cui, Henry W Rohrs, Michael L Gross

Abstract readReview
In one paragraph

Review in The Analyst, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

51 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Multidimensional Separations in Top-Down Proteomics.Analytical science advances · 2023
    Article
  7. Article
  8. Article
  9. Emerging chemistry and biology in protein glutathionylation.Current opinion in chemical biology · 2022
    Review
  10. Article
  11. Article
  12. Novel Strategies to Address the Challenges in Top-Down Proteomics.Journal of the American Society for Mass Spectrometry · 2021
    Review
  13. Article
  14. Using 10,000 Fragment Ions to Inform Scoring in Native Top-down Proteomics.Journal of the American Society for Mass Spectrometry · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. A New Quantification Method Using Electrochemical Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Weidong CuiNIH NCRR Center for Biomedical and Bio-Organic Mass Spectrometry, Department of Chemistry, Washington University, St. Louis, MO 63130, USA. cui@wustl.edu
Henry W Rohrs
Michael L Gross

Funding

YOGA LIFESTYLE INTERVENTION REDUCES BLOOD PRESSURE IN HIV-INFECTED ADULTSP41RR000954 · NCRR · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 1985 to 2011
$16.0M
TrainingP41GM103422 · NIGMS · WASHINGTON UNIVERSITY · PI YARASHESKI, KEVIN E · 2012 to 2019
$12.0M
NCRR NIH HHS P41 RR000954NCRR NIH HHS P41RR000954NIGMS NIH HHS P41 GM103422PHS HHS 1S10025101
6 · The paper itself

Abstract

Top-down mass spectrometry is an emerging approach for the analysis of intact proteins. The term was coined as a contrast with the better-established, bottom-up strategy for analysis of peptide fragments derived from digestion, either enzymatically or chemically, of intact proteins. Although the term top-down originates from proteomics, it can also be applied to mass spectrometric analysis of intact large biomolecules that are constituents of protein assemblies or complexes. Traditionally, mass spectrometry has usually started with intact molecules, and in this regard, top-down approaches reflect the spirit of mass spectrometry. This article provides an overview of the methodologies in top-down mass spectrometry and then reviews applications covering protein posttranslational modifications, protein biophysics, DNAs/RNAs, and protein assemblies. Finally, challenges and future directions are discussed.

Indexed as

Fourier AnalysisMass SpectrometryNucleic AcidsProteinsNucleic AcidsProteins

Identifiers

PMID21826297
PMCPMC3505190

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.