Evidence map›Paper›PMID 23485913›Full record

ArticleBiochimica et biophysica acta2013

Fast photochemical oxidation of proteins for comparing solvent-accessibility changes accompanying protein folding: data processing and application to barstar.

Brian C Gau, Jiawei Chen, Michael L Gross

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
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  5. Investigation of D76N βJournal of the American Society for Mass Spectrometry · 2021
    Article
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  15. Review
  16. Variation in FPOP Measurements Is Primarily Caused by Poor Peptide Signal Intensity.Journal of the American Society for Mass Spectrometry · 2018
    Article
  17. Review
  18. Article
  19. How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016
    Review
  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

3 authors at 2 institutions in 1 country.

Brian C GauDonald Danforth Plant Science Center, Washington University, St. Louis, MO 63132, USA.
Jiawei Chen
Michael L Gross
Framingham State University · USWashington University in St. Louis · US

Funding

YOGA LIFESTYLE INTERVENTION REDUCES BLOOD PRESSURE IN HIV-INFECTED ADULTSP41RR000954 · NCRR · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 1985 to 2011
$16.0M
TrainingP41GM103422 · NIGMS · WASHINGTON UNIVERSITY · PI YARASHESKI, KEVIN E · 2012 to 2019
$12.0M
A Biomedical Mass Spectrometry Resource: Ongoing Driving Biomedical ProjectsR24GM136766 · NIGMS · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 2020 to 2022
$2.3M
NCRR NIH HHS P41 RR000954NIGMS NIH HHS 8 P41 GM103422-35NIGMS NIH HHS P41 GM103422NIGMS NIH HHS R24 GM136766
6 · The paper itself

Abstract

Mass spectrometry-based protein footprinting reveals regional and even amino-acid structural changes and fills the gap for many proteins and protein interactions that cannot be studied by X-ray crystallography or NMR spectroscopy. Hydroxyl radical-mediated labeling has proven to be particularly informative in this pursuit because many solvent-accessible residues can be labeled by OH in a protein or protein complex, thus providing more coverage than does specific amino-acid modifications. Finding all the OH-labeling sites requires LC/MS/MS analysis of a proteolyzed sample, but data processing is daunting without the help of automated software. We describe here a systematic means for achieving a comprehensive residue-resolved analysis of footprinting data in an efficient manner, utilizing software common to proteomics core laboratories. To demonstrate the method and the utility of OH-mediated labeling, we show that FPOP easily distinguishes the buried and exposed residues of barstar in its folded and unfolded states. This article is part of a Special Issue entitled: Mass spectrometry in structural biology.

Indexed as

Amino AcidsAmino Acid SequenceChromatography, LiquidElectronic Data ProcessingHydroxyl RadicalMass SpectrometryModels, MolecularMolecular Sequence DataOxidation-ReductionPhotochemical ProcessesProtein FoldingProteinsProteomeProteomicsSolventsAmino AcidsHydroxyl RadicalProteinsProteomeSolvents

Identifiers

PMID23485913
PMCPMC3663899
OpenAlexW2017780667

What OpenQuestion holds

Textmetadata
LicenceTDM
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.