Evidence map›Paper›PMID 25654326›Full record

ArticleAnalytical chemistry2015

Quantitative chemoproteomics for site-specific analysis of protein alkylation by 4-hydroxy-2-nonenal in cells.

Jing Yang, Keri A Tallman, Ned A Porter, Daniel C Liebler

Open access · hybridAbstract read
In one paragraph

Article in Analytical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

46 citing papers in PubMed, 96 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Protein Haptenation and Its Role in Allergy.Chemical research in toxicology · 2024
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Profiling of Protein Carbonylations in Ferroptosis by Chemical Proteomics.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Dienone Compounds: Targets and Pharmacological Responses.Journal of medicinal chemistry · 2020
    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

4 authors at 1 institution in 1 country.

Jing YangDepartment of Biochemistry, Vanderbilt University School of Medicine , 465 21st Avenue South, U1213 MRB III, Nashville, Tennessee 37232, United States.
Keri A Tallman
Ned A Porter
Daniel C Liebler
Vanderbilt University · US

Funding

Vanderbilt Proteome Characterization CenterU24CA159988 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI LIEBLER, DANIEL C · 2011 to 2016
$13.9M
ASK signalosomes and environmental sensingR01ES022936 · NIEHS · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MCLAUGHLIN, BETHANN M · 2014 to 2018
$1.8M
NCI NIH HHS U24 CA159988NCI NIH HHS U24CA159988NIEHS NIH HHS R01 ES022936NIEHS NIH HHS R01ES022936
6 · The paper itself

Abstract

Protein alkylation by 4-hydroxy-2-nonenal (HNE), an endogenous lipid derived electrophile, contributes to stress signaling and cellular toxicity. Although previous work has identified protein targets for HNE alkylation, the sequence specificity of alkylation and dynamics in a cellular context remain largely unexplored. We developed a new quantitative chemoproteomic platform, which uses isotopically tagged, photocleavable azido-biotin reagents to selectively capture and quantify the cellular targets labeled by the alkynyl analogue of HNE (aHNE). Our analyses site-specifically identified and quantified 398 aHNE protein alkylation events (386 cysteine sites and 12 histidine sites) in intact cells. This data set expands by at least an order of magnitude the number of such modification sites previously reported. Although adducts formed by Michael addition are thought to be largely irreversible, we found that most aHNE modifications are lost rapidly in situ. Moreover, aHNE adduct turnover occurs only in intact cells and loss rates are site-selective. This quantitative chemoproteomics platform provides a versatile general approach to map bioorthogonal-chemically engineered post-translational modifications and their cellular dynamics in a site-specific and unbiased manner.

Indexed as

AldehydesAlkylationChromatography, LiquidColorectal NeoplasmsCross-Linking ReagentsHumansNeoplasm ProteinsProtein Processing, Post-TranslationalTandem Mass SpectrometryTumor Cells, Cultured4-hydroxy-2-nonenalAldehydesCross-Linking ReagentsNeoplasm Proteins

Identifiers

PMID25654326
PMCPMC4350606
OpenAlexW1978104803

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.