Evidence map›Paper›PMID 31932818›Full record

ReviewMolecular omics2020

High-throughput quantitative top-down proteomics.

Kellye A Cupp-Sutton, Si Wu

Abstract readReview
In one paragraph

Review in Molecular omics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
7.8field-weighted citation impact, top 1% of its field
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

61 citing papers in PubMed, 115 citations in OpenAlex.

  1. Diagnostic Value of Synovial Fluid Biomarkers for Periprosthetic Joint Infection: A Prospective, Double-blind Trial.Medical science monitor : international medical journal of experimental and clinical research · 2023
    Trial
  2. Review
  3. Article
  4. Article
  5. Review
  6. Vitreous proteomics in rhegmatogenous retinal detachment and proliferative vitreoretinopathy.Biomedical papers of the Medical Faculty of the University Palacky, Olomouc, Czechoslovakia · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Proteomics appending a complementary dimension to precision oncotherapy.Computational and structural biotechnology journal · 2024
    Review
  17. Review
  18. Article
  19. Article
  20. Review

1 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Kellye A Cupp-SuttonDepartment of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Room 2210, Norman, OK 73019-5251, USA. si.wu@ou.edu.
Si Wu
Norman Regional Hospital · US

Funding

Pre-Clinical Studies to Identify SLE Therapeutic TargetsU19AI082714 · NIAID · OKLAHOMA MEDICAL RESEARCH FOUNDATION · PI JAMES, JUDITH A · 2009 to 2018
$6.2M
Quantitative Analysis of Serum Autoantibody Repertories in Systemic Lupus ErythematosusR01AI141625 · NIAID · UNIVERSITY OF OKLAHOMA · PI SINGH, SHANTERI, SMITH, KENNETH MICHAEL · 2019 to 2023
$2.1M
NIAID NIH HHS R01 AI141625NIAID NIH HHS U19 AI082714
6 · The paper itself

Abstract

Top-down mass spectrometry (MS) analyzes intact proteins at the proteoform level, which allows researchers to better understand the functions of protein modifications. Recently, top-down proteomics has increased in popularity due to advancements in high-resolution mass spectrometers, increased efficiency in liquid chromatography (LC) separation, and advances in data analysis software. Some unique protein proteoforms, which have been distinguished using top-down MS, have even been shown to exhibit marked variation in biological function compared to similar proteoforms. However, the qualitative identification of a particular proteoform may not be enough to determine the biological relevance of that proteoform. Quantitative top-down MS methods have been notably applied to the study of the differing biological functions of protein proteoforms and have allowed researchers to explore proteomes at the proteoform, rather than the peptide, level. Here, we review the top-down MS methods that have been used to quantitatively identify intact proteins, discuss current applications of quantitative top-down MS analysis, and present new areas where quantitative top-down MS analysis may be implemented.

Indexed as

AnimalsChromatography, LiquidHumansIsotope LabelingProtein Processing, Post-TranslationalProteomicsSoftwareStaining and LabelingTandem Mass Spectrometry

Identifiers

PMID31932818
PMCPMC7529119
OpenAlexW2998503646

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.