Evidence map›Paper›PMID 24807621›Full record

ArticleAnalytical chemistry2014

Applying label-free quantitation to top down proteomics.

Ioanna Ntai, Kyunggon Kim, Ryan T Fellers, Owen S Skinner, Archer D Smith, Bryan P Early, John P Savaryn, Richard D LeDuc, Paul M Thomas, Neil L Kelleher

Abstract read
In one paragraph

Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. An Improved Top-Down Mass Spectrometry Characterization ofJournal of the American Society for Mass Spectrometry · 2021
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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

10 authors.

Ioanna NtaiDepartments of Chemistry, Molecular Biosciences and the Proteomics Center of Excellence , 2145 N. Sheridan Road, Evanston, Illinois 60208, United States.
Kyunggon Kim
Ryan T Fellers
Owen S Skinner
Archer D Smith
Bryan P Early
John P Savaryn
Richard D LeDuc
Paul M Thomas
Neil L Kelleher

Funding

The UIUC Neuroproteomics Center on Cell-Cell SignalingP30DA018310 · NIDA · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI Elena V Romanova · 2004 to 2026
$24.9M
Eukaryotic Post-Translational ModificationsR01GM067193 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KELLEHER, NEIL L · 2003 to 2015
$4.0M
CCR NIH HHS HHSN261200800001CNCI NIH HHS HHSN261200800001ENIDA NIH HHS P30 DA018310NIGMS NIH HHS R01 GM067193
6 · The paper itself

Abstract

With the prospect of resolving whole protein molecules into their myriad proteoforms on a proteomic scale, the question of their quantitative analysis in discovery mode comes to the fore. Here, we demonstrate a robust pipeline for the identification and stringent scoring of abundance changes of whole protein forms <30 kDa in a complex system. The input is ~100-400 μg of total protein for each biological replicate, and the outputs are graphical displays depicting statistical confidence metrics for each proteoform (i.e., a volcano plot and representations of the technical and biological variation). A key part of the pipeline is the hierarchical linear model that is tailored to the original design of the study. Here, we apply this new pipeline to measure the proteoform-level effects of deleting a histone deacetylase (rpd3) in S. cerevisiae. Over 100 proteoform changes were detected above a 5% false positive threshold in WT vs the Δrpd3 mutant, including the validating observation of hyperacetylation of histone H4 and both H2B isoforms. Ultimately, this approach to label-free top down proteomics in discovery mode is a critical technical advance for testing the hypothesis that whole proteoforms can link more tightly to complex phenotypes in cell and disease biology than do peptides created in shotgun proteomics.

Indexed as

Histone DeacetylasesMutationProteinsProteomicsSaccharomyces cerevisiaeHistone DeacetylasesProteins

Identifiers

PMID24807621
PMCPMC4033644

What OpenQuestion holds

Textmetadata
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.