Evidence map›Paper›PMID 24723542›Full record

ArticleProteomics2014

Ultraviolet photodissociation enhances top-down mass spectrometry as demonstrated on green fluorescent protein variants.

Xibei Dang, Nicolas L Young

Abstract readComment
PubMed Publisher
In one paragraph

Article in Proteomics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Progress in Top-Down Proteomics and the Analysis of Proteoforms.Annual review of analytical chemistry (Palo Alto, Calif.) · 2016
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Xibei DangIon Cyclotron Resonance Program, National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL, USA; Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL, USA.
Nicolas L Young
Florida State University · USNational High Magnetic Field Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ultraviolet photodissociation (UVPD) is a compelling fragmentation technique with great potential to enhance proteomics generally and top-down MS specifically. In this issue, Cannon et al. (Proteomics 2014, 14, XXXX-XXXX) use UVPD to perform top-down MS on several sequence variants of green fluorescent protein and compare the results to CID, higher energy collision induced dissociation, and electron transfer dissociation. As compared to the other techniques UVPD produces a wider variety of fragment ion types that are relatively evenly distributed across the protein sequences. Overall, their results demonstrate enhanced sequence coverage and higher confidence in sequence assignment via UVPD MS. Based on these and other recent results UVPD is certain to become an increasingly widespread and valuable tool for top-down proteomics.

Indexed as

Green Fluorescent ProteinsProteomicsTandem Mass SpectrometryGreen Fluorescent ProteinsGreen fluorescent proteinTechnologyTop-down proteomicsUltraviolet photodissociation

Identifiers

PMID24723542
OpenAlexW2165791581

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.