Evidence map›Paper›PMID 18052106›Full record

ReviewChemical research in toxicology2008

Protein damage by reactive electrophiles: targets and consequences.

Daniel C Liebler

Open access · bronzeAbstract readReview
In one paragraph

Review in Chemical research in toxicology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed, 1 pooled it
6.8field-weighted citation impact, top 2% 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

97 citing papers in PubMed, 1 synthesis or guideline pooled it, 236 citations in OpenAlex.

  1. Pooled it
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  12. Observational
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  17. Potential Applications of NRF2 Inhibitors in Cancer Therapy.Oxidative medicine and cellular longevity · 2019
    Review
  18. Article
  19. Review
  20. Review

37 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Daniel C LieblerDepartment of Biochemistry, Vanderbilt University School of Medicine,, Nashville, Tennessee 37232, USA. daniel.liebler@vanderbilt.edu
Vanderbilt University · US

Funding

Structural Biology Facility CoreP30ES000267 · NIEHS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1985 to 2014
$20.3M
TRAINING PROGRAM IN ENVIRONMENTAL TOXICOLOGYT32ES007028 · NIEHS · VANDERBILT UNIVERSITY · PI F PETER Guengerich, Fiona Edith Harrison · 1985 to 2026
$15.7M
Protein Adducts and Proteome Profiles in Oxidative StressP01ES013125 · NIEHS · VANDERBILT UNIVERSITY · PI PORTER, NED ALLEN · 2005 to 2012
$12.6M
PROTEIN TARGETS OF ENVIRONMENTAL CHEMICALSR01ES010056 · NIEHS · VANDERBILT UNIVERSITY · PI LIEBLER, DANIEL C · 1999 to 2008
$1.9M
Regulation of Nrf2 SignalingR01CA104590 · NCI · VANDERBILT UNIVERSITY · PI FREEMAN, MICHAEL L. · 2005 to 2009
$1.5M
Proteomic Analysis of Alkylation Stress ResponsesR01ES011811 · NIEHS · VANDERBILT UNIVERSITY · PI LIEBLER, DANIEL C · 2002 to 2005
$1.3M
NCI NIH HHS CA104590NCI NIH HHS R01 CA104590NIEHS NIH HHS ES000267NIEHS NIH HHS ES001811NIEHS NIH HHS ES007028NIEHS NIH HHS ES010056NIEHS NIH HHS ES013125NIEHS NIH HHS P01 ES013125NIEHS NIH HHS P30 ES000267NIEHS NIH HHS R01 ES010056NIEHS NIH HHS R01 ES011811NIEHS NIH HHS T32 ES007028
6 · The paper itself

Abstract

It has been 60 years since the Millers first described the covalent binding of carcinogens to tissue proteins. Protein covalent binding was gradually overshadowed by the emergence of DNA adduct formation as the dominant paradigm in chemical carcinogenesis but re-emerged in the early 1970s as a critical mechanism of drug and chemical toxicity. Technology limitations hampered the characterization of protein adducts until the emergence of mass spectrometry-based proteomics in the late 1990s. The time since then has seen rapid progress in the characterization of the protein targets of electrophiles and the consequences of protein damage. Recent integration of novel affinity chemistries for electrophile probes, shotgun proteomics methods, and systems modeling tools has led to the identification of hundreds of protein targets of electrophiles in mammalian systems. The technology now exists to map the targets of damage to critical components of signaling pathways and metabolic networks and to understand mechanisms of damage at a systems level. The implementation of sensitive, specific analyses for protein adducts from both xenobiotic-derived and endogenous electrophiles offers a means to link protein damage to clinically relevant health effects of both chemical exposures and disease processes.

Indexed as

AnimalsElectrophoresis, Polyacrylamide GelHumansImmunochemistryProteinsProteomicsSignal TransductionXenobioticsProteinsXenobiotics

Identifiers

PMID18052106
PMCPMC2533766
OpenAlexW1974332498

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.