Evidence map›Paper›PMID 27184861›Full record

ArticleElectrophoresis2016

Mass spectrometry-based proteomics of oxidative stress: Identification of 4-hydroxy-2-nonenal (HNE) adducts of amino acids using lysozyme and bovine serum albumin as model proteins.

Roshanak Aslebagh, Bruce A Pfeffer, Steven J Fliesler, Costel C Darie

Open access · greenAbstract read
In one paragraph

Article in Electrophoresis, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Mass Spectrometry- and Structural Biology-Based Investigation of Proteins.Advances in experimental medicine and biology · 2026
    Review
  5. Review
  6. Effect of Vitamin E on Transcriptomic Alterations in Alzheimer's Disease.International journal of molecular sciences · 2023
    Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
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  14. Review
  15. Alcohol-induced structural and cellular brain alterations: molecular and histopathological mechanisms.Romanian journal of morphology and embryology = Revue roumaine de morphologie et embryologie
    Review
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 3 institutions in 1 country.

Roshanak AslebaghBiochemistry and Proteomics Group, Department of Chemistry and Biomolecular Science, Clarkson University, Potsdam, NY, USA.
Bruce A PfefferResearch Service, VA Western NY Healthcare System, Buffalo, NY, USA.
Steven J FlieslerResearch Service, VA Western NY Healthcare System, Buffalo, NY, USA.
Costel C DarieBiochemistry and Proteomics Group, Department of Chemistry and Biomolecular Science, Clarkson University, Potsdam, NY, USA. cdarie@clarkson.edu.
Clarkson University · USBuffalo State University · USUniversity at Buffalo, State University of New York · US

Funding

University of Buffalo Clinical and Translational Science Institute - Supplement SchulyerUL1TR001412 · NCATS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI MURPHY, TIMOTHY F · 2015 to 2024
$33.8M
ISOPRENOID METABOLISM IN THE RETINAR01EY007361 · NEI · UNIVERSITY OF SOUTH FLORIDA · PI FLIESLER, STEVEN J. · 1988 to 2015
$4.4M
NCATS NIH HHS UL1 TR001412NEI NIH HHS R01 EY007361
6 · The paper itself

Abstract

Modification of proteins by 4-hydroxy-2-nonenal (HNE), a reactive by-product of ω6 polyunsaturated fatty acid oxidation, on specific amino acid residues is considered a biomarker for oxidative stress, as occurs in many metabolic, hereditary, and age-related diseases. HNE modification of amino acids can occur either via Michael addition or by formation of Schiff-base adducts. These modifications typically occur on cysteine (Cys), histidine (His), and/or lysine (Lys) residues, resulting in an increase of 156 Da (Michael addition) or 138 Da (Schiff-base adducts), respectively, in the mass of the residue. Here, we employed biochemical and mass spectrometry (MS) approaches to determine the MS "signatures" of HNE-modified amino acids, using lysozyme and BSA as model proteins. Using direct infusion of unmodified and HNE-modified lysozyme into an electrospray quadrupole time-of-flight mass spectrometer, we were able to detect up to seven HNE modifications per molecule of lysozyme. Using nanoLC-MS/MS, we found that, in addition to N-terminal amino acids, Cys, His, and Lys residues, HNE modification of arginine (Arg), threonine (Thr), tryptophan (Trp), and histidine (His) residues can also occur. These sensitive and specific methods can be applied to the study of oxidative stress to evaluate HNE modification of proteins in complex mixtures from cells and tissues under diseased versus normal conditions.

Indexed as

Oxidative StressAldehydesAmino AcidsAnimalsCattleChromatography, LiquidModels, ChemicalMuramidaseNanotechnologyProteomicsSensitivity and SpecificitySerum Albumin, BovineTandem Mass Spectrometry4-hydroxy-2-nonenalAldehydesAmino AcidsMuramidaseSerum Albumin, Bovine4-Hydroxy-2-nonenalMass spectrometryMichael additionPeptide modificationProteomicsPyrrole adductsSchiff-base

Identifiers

PMID27184861
PMCPMC5215750
OpenAlexW2406915501

What OpenQuestion holds

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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.