Evidence map›Paper›PMID 18160050›Full record

ArticleFree radical biology & medicine2008

Identifying the site of spin trapping in proteins by a combination of liquid chromatography, ELISA, and off-line tandem mass spectrometry.

Olivier M Lardinois, Charles D Detweiler, Kenneth B Tomer, Ronald P Mason, Leesa J Deterding

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In one paragraph

Article in Free radical biology & medicine, 2008. 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
3.5field-weighted citation impact, top 8% 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, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Ferryl Hemoglobin and Heme Induce AInternational journal of molecular sciences · 2021
    Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Regulation of Ras proteins by reactive nitrogen species.Free radical biology & medicine · 2011
    Review
  12. Article
  13. Article
  14. Article
  15. Nitrones as therapeutics.Free radical biology & medicine · 2008
    Review
  16. 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

5 authors at 1 institution in 1 country.

Olivier M LardinoisLaboratory of Pharmacology and Chemistry, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USA.
Charles D Detweiler
Kenneth B Tomer
Ronald P Mason
Leesa J Deterding
National Institute of Environmental Health Sciences · US

Funding

PROTEIN DERIVED RADICALSZ01ES050139 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI MASON, RONALD P · 1995 to 2008
$4.7M
Protein Characterization By Mass SpectrometryZ01ES050171 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI TOMER, KENNETH · 2000 to 2008
$1.1M
MASS SPECTROMETRY AND OXIDATIVE STRESSZ01ES050153 · NIEHS · ENVIRONMENTAL HEALTH SCIENCES · PI TOMER, KENNETH · 1996 to 2006
–
Intramural NIH HHS Z01 ES050153Intramural NIH HHS Z99 ES999999
6 · The paper itself

Abstract

An off-line mass spectrometry method that combines immuno-spin trapping and chromatographic procedures has been developed for selective detection of the nitrone spin trap 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) covalently attached to proteins, an attachment which occurs only subsequent to DMPO trapping of free radicals. In this technique, the protein-DMPO nitrone adducts are digested to peptides with proteolytic agents, peptides from the enzymatic digest are separated by HPLC, and enzyme-linked immunosorbent assays (ELISA) using polyclonal anti-DMPO nitrone antiserum are used to detect the eluted HPLC fractions that contain DMPO nitrone adducts. The fractions showing positive ELISA signals are then concentrated and characterized by tandem mass spectrometry (MS/MS). This method, which constitutes the first liquid chromatography-ELISA-mass spectrometry (LC-ELISA-MS)-based strategy for selective identification of DMPO-trapped protein residues in complex peptide mixtures, facilitates location and preparative fractionation of DMPO nitrone adducts for further structural characterization. The strategy is demonstrated for human hemoglobin, horse heart myoglobin, and sperm whale myoglobin, three globin proteins known to form DMPO-trappable protein radicals on treatment with H(2)O(2). The results demonstrate the power of the new experimental strategy to select DMPO-labeled peptides and identify sites of DMPO covalent attachments.

Indexed as

Chromatography, LiquidEnzyme-Linked Immunosorbent AssaySpin TrappingTandem Mass SpectrometryAnimalsChromatography, High Pressure LiquidFree RadicalsHeartHemoglobinsHorsesHumansMetmyoglobinMyoglobinNitrogen OxidesSpectrometry, Mass, Electrospray IonizationSperm WhaleFree RadicalsHemoglobinsMetmyoglobinMyoglobinNitrogen Oxidesnitrones

Identifiers

PMID18160050
PMCPMC2268891
OpenAlexW2055287511

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.