Evidence map›Paper›PMID 24447299›Full record

ArticleAnalytical chemistry2014

Ultraviolet photodissociation for characterization of whole proteins on a chromatographic time scale.

Joe R Cannon, Michael B Cammarata, Scott A Robotham, Victoria C Cotham, Jared B Shaw, Ryan T Fellers, Bryan P Early, Paul M Thomas, Neil L Kelleher, Jennifer S Brodbelt

Open access · greenAbstract 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 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

40 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Top-Down Analysis of Proteins in Low Charge States.Journal of the American Society for Mass Spectrometry · 2019
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  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

10 authors at 2 institutions in 1 country.

Joe R CannonDepartment of Chemistry, University of Texas at Austin , 1 University Station A5300, Austin, Texas 78712, United States.
Michael B Cammarata
Scott A Robotham
Victoria C Cotham
Jared B Shaw
Ryan T Fellers
Bryan P Early
Paul M Thomas
Neil L Kelleher
Jennifer S Brodbelt
The University of Texas at Austin · USNorthwestern University · US

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
UV Photodissociation for Acidic and Basic Proteome CharacterizationR21GM099028 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2011 to 2012
$384k
NIDA NIH HHS P30 DA018310NIGMS NIH HHS R01 GM067193NIGMS NIH HHS R21 GM099028
6 · The paper itself

Abstract

Intact protein characterization using mass spectrometry thus far has been achieved at the cost of throughput. Presented here is the application of 193 nm ultraviolet photodissociation (UVPD) for top down identification and characterization of proteins in complex mixtures in an online fashion. Liquid chromatographic separation at the intact protein level coupled with fast UVPD and high-resolution detection resulted in confident identification of 46 unique sequences compared to 44 using HCD from prepared Escherichia coli ribosomes. Importantly, nearly all proteins identified in both the UVPD and optimized HCD analyses demonstrated a substantial increase in confidence in identification (as defined by an average decrease in E value of ∼40 orders of magnitude) due to the higher number of matched fragment ions. Also shown is the potential for high-throughput characterization of intact proteins via liquid chromatography (LC)-UVPD-MS of molecular weight-based fractions of a Saccharomyces cerevisiae lysate. In total, protein products from 215 genes were identified and found in 292 distinct proteoforms, 168 of which contained some type of post-translational modification.

Indexed as

Amino Acid SequenceAnimalsChromatography, LiquidHorsesMolecular Sequence DataPhotoelectron SpectroscopyProtein Structure, TertiarySaccharomyces cerevisiae ProteinsTime FactorsSaccharomyces cerevisiae Proteins

Identifiers

PMID24447299
PMCPMC3958131
OpenAlexW2032372830

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.