Evidence map›Paper›PMID 27425180›Full record

ArticleJournal of proteome research2016

193 nm Ultraviolet Photodissociation Mass Spectrometry for Phosphopeptide Characterization in the Positive and Negative Ion Modes.

Michelle R Robinson, Juliana M Taliaferro, Kevin N Dalby, Jennifer S Brodbelt

Abstract read
In one paragraph

Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
  2. Peptide Analysis by Soft X-ray Atmospheric Pressure Photoionization Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025
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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

4 authors.

Michelle R RobinsonDepartment of Chemistry, and ‡Division of Chemical Biology and Medicinal Chemistry College of Pharmacy, The University of Texas Austin, Texas 78712, United States.
Juliana M TaliaferroDepartment of Chemistry, and ‡Division of Chemical Biology and Medicinal Chemistry College of Pharmacy, The University of Texas Austin, Texas 78712, United States.
Kevin N DalbyDepartment of Chemistry, and ‡Division of Chemical Biology and Medicinal Chemistry College of Pharmacy, The University of Texas Austin, Texas 78712, United States.
Jennifer S BrodbeltDepartment of Chemistry, and ‡Division of Chemical Biology and Medicinal Chemistry College of Pharmacy, The University of Texas Austin, Texas 78712, United States.

Funding

Mapping the C Terminal Domain of RNA Polymerase II by UVPD Mass SpectrometryR21EB018391 · NIBIB · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2014 to 2015
$405k
NIBIB NIH HHS R21 EB018391
6 · The paper itself

Abstract

Advances in liquid chromatography tandem mass spectrometry (LC-MS/MS) have permitted phosphoproteomic analysis on a grand scale, but ongoing challenges specifically associated with confident phosphate localization continue to motivate the development of new fragmentation techniques. In the present study, ultraviolet photodissociation (UVPD) at 193 nm is evaluated for the characterization of phosphopeptides in both positive and negative ion modes. Compared to the more standard higher energy collisional dissociation (HCD), UVPD provided more extensive fragmentation with improved phosphate retention on product ions. Negative mode UVPD showed particular merit for detecting and sequencing highly acidic phosphopeptides from alpha and beta casein, but was not as robust for larger scale analysis because of lower ionization efficiencies in the negative mode. HeLa and HCC70 cell lysates were analyzed by both UVPD and HCD. While HCD identified more phosphopeptides and proteins compared to UVPD, the unique matches from UVPD analysis could be combined with the HCD data set to improve the overall depth of coverage compared to either method alone.

Indexed as

Ultraviolet RaysHeLa CellsHumansIonsMass SpectrometryPeptide FragmentsPhosphopeptidesPhotolysisProteinsProteomicsIonsPeptide FragmentsPhosphopeptidesProteinshigher energy collision induced dissociationmass spectrometryphosphoproteomicsultraviolet photodissociation

Identifiers

PMID27425180
PMCPMC5481846

What OpenQuestion holds

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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.