Evidence map›Paper›PMID 19265387›Full record

ArticleAnalytical chemistry2009

Pulsed electron beam water radiolysis for submicrosecond hydroxyl radical protein footprinting.

Caroline Watson, Ireneusz Janik, Tiandi Zhuang, Olga Charvátová, Robert J Woods, Joshua S Sharp

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Fast Protein Footprinting by X-ray Mediated Radical Trifluoromethylation.Journal of the American Society for Mass Spectrometry · 2020
    Article
  11. The Application of Fluorine-Containing Reagents in Structural Proteomics.Angewandte Chemie (International ed. in English) · 2020
    Review
  12. Intrinsic Buffer Hydroxyl Radical Dosimetry Using Tris(hydroxymethyl)aminomethane.Journal of the American Society for Mass Spectrometry · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Variation in FPOP Measurements Is Primarily Caused by Poor Peptide Signal Intensity.Journal of the American Society for Mass Spectrometry · 2018
    Article
  18. Review
  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

6 authors at 2 institutions in 1 country.

Caroline WatsonComplex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA.
Ireneusz Janik
Tiandi Zhuang
Olga Charvátová
Robert J Woods
Joshua S Sharp
University of Notre Dame · USUniversity of Georgia · US

Funding

ZINC DEFICIENCY &PROTEIN EXPRESSION IN RAT OLFACTORY BULBSP41RR005351 · NCRR · UNIVERSITY OF GEORGIA (UGA) · PI VENOT, ANDRE · 1989 to 2011
$18.4M
TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
NCRR NIH HHS P41 RR005351NCRR NIH HHS P41RR005351NIGMS NIH HHS P41 GM103390
6 · The paper itself

Abstract

Hydroxyl radical footprinting is a valuable technique for studying protein structure, but care must be taken to ensure that the protein does not unfold during the labeling process due to oxidative damage. Footprinting methods based on submicrosecond laser photolysis of peroxide that complete the labeling process faster than the protein can unfold have been recently described; however, the mere presence of large amounts of hydrogen peroxide can also cause uncontrolled oxidation and minor conformational changes. We have developed a novel method for submicrosecond hydroxyl radical protein footprinting using a pulsed electron beam from a 2 MeV Van de Graaff electron accelerator to generate a high concentration of hydroxyl radicals by radiolysis of water. The amount of oxidation can be controlled by buffer composition, pulsewidth, dose, and dissolved nitrous oxide gas in the sample. Our results with ubiquitin and beta-lactoglobulin A demonstrate that one submicrosecond electron beam pulse produces extensive protein surface modifications. Highly reactive residues that are buried within the protein structure are not oxidized, indicating that the protein retains its folded structure during the labeling process. Time-resolved spectroscopy indicates that the major part of protein oxidation is complete in a time scale shorter than that of large scale protein motions.

Indexed as

ElectronsAbsorptionChromatography, LiquidFourier AnalysisGalectin 3Hydrogen PeroxideHydroxyl RadicalLactoglobulinsMagnetic Resonance SpectroscopyModels, MolecularOxidation-ReductionProtein ConformationProtein FoldingProtein FootprintingPulse RadiolysisSpectrophotometry, UltravioletGalectin 3Hydrogen PeroxideHydroxyl RadicalLactoglobulinsTrypsinUbiquitinWater

Identifiers

PMID19265387
PMCPMC2733211
OpenAlexW2001857169

What OpenQuestion holds

Textmetadata
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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.