Evidence map›Paper›PMID 24014150›Full record

ArticleJournal of the American Society for Mass Spectrometry2013

Improved identification and relative quantification of sites of peptide and protein oxidation for hydroxyl radical footprinting.

Xiaoyan Li, Zixuan Li, Boer Xie, Joshua S Sharp

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

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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 at 1 institution in 1 country.

Xiaoyan LiComplex Carbohydrate Research Center, University of Georgia, Athens, GA, 30602, USA.
Zixuan Li
Boer Xie
Joshua S Sharp
University of Georgia · US

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
Improved Hydroxyl Radical Footprinting for Modeling Protein StructureR01GM096049 · NIGMS · UNIVERSITY OF MISSISSIPPI · PI SHARP, JOSHUA S · 2012 to 2016
$1.4M
NIGMS NIH HHS 1R01GM096049-01A1NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R01 GM096049
6 · The paper itself

Abstract

Protein oxidation is typically associated with oxidative stress and aging and affects protein function in normal and pathological processes. Additionally, deliberate oxidative labeling is used to probe protein structure and protein-ligand interactions in hydroxyl radical protein footprinting (HRPF). Oxidation often occurs at multiple sites, leading to mixtures of oxidation isomers that differ only by the site of modification. We utilized sets of synthetic, isomeric "oxidized" peptides to test and compare the ability of electron-transfer dissociation (ETD) and collision-induced dissociation (CID), as well as nano-ultra high performance liquid chromatography (nanoUPLC) separation, to quantitate oxidation isomers with one oxidation at multiple adjacent sites in mixtures of peptides. Tandem mass spectrometry by ETD generates fragment ion ratios that accurately report on relative oxidative modification extent on specific sites, regardless of the charge state of the precursor ion. Conversely, CID was found to generate quantitative MS/MS product ions only at the higher precursor charge state. Oxidized isomers having multiple sites of oxidation in each of two peptide sequences in HRPF product of protein Robo-1 Ig1-2, a protein involved in nervous system axon guidance, were also identified and the oxidation extent at each residue was quantified by ETD without prior liquid chromatography (LC) separation. ETD has proven to be a reliable technique for simultaneous identification and relative quantification of a variety of functionally different oxidation isomers, and is a valuable tool for the study of oxidative stress, as well as for improving spatial resolution for HRPF studies.

Indexed as

Hydroxyl RadicalAmino Acid SequenceChromatography, High Pressure LiquidElectronsHumansNerve Tissue ProteinsOxidation-ReductionPeptidesProtein FootprintingProteinsReceptors, ImmunologicRoundabout ProteinsTandem Mass SpectrometryHydroxyl RadicalNerve Tissue ProteinsPeptidesProteinsReceptors, ImmunologicRoundabout Proteins

Identifiers

PMID24014150
PMCPMC3814024
OpenAlexW2031601633

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.