Evidence map›Paper›PMID 24021887›Full record

ReviewBiochimica et biophysica acta2014

Detection of electrophile-sensitive proteins.

Stephanie B Wall, M Ryan Smith, Karina Ricart, Fen Zhou, Praveen K Vayalil, Joo-Yeun Oh, Aimee Landar

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.2field-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

13 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Proteomic Methods to Evaluate NOX-Mediated Redox Signaling.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

7 authors at 1 institution in 1 country.

Stephanie B WallDepartment of Pathology, Center for Free Radical Biology, University of Alabama at Birmingham, Birmingham, AL, USA.
M Ryan Smith
Karina Ricart
Fen Zhou
Praveen K Vayalil
Joo-Yeun Oh
Aimee Landar
University of Alabama at Birmingham · US

Funding

UAB-UCSD O'Brien Core Center for Acute Kidney Injury ResearchP30DK079337 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI AGARWAL, ANUPAM · 2008 to 2022
$18.3M
Training Program in Cardiovascular PathophysiologyT32HL007918 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BALLINGER, SCOTT W. · 1999 to 2018
$3.6M
The role of the mitochondrial protein thiol modification in endothelial dysfunctiR01HL096638 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI LANDAR, AIMEE LEIGH · 2010 to 2014
$1.8M
NHLBI NIH HHS HL096638NHLBI NIH HHS R01 HL096638NHLBI NIH HHS T32 HL007918NHLBI NIH HHS T32HL007918NIDDK NIH HHS DK079337NIDDK NIH HHS P30 DK079337
6 · The paper itself

Abstract

backgroundRedox signaling is an important emerging mechanism of cellular function. Dysfunctional redox signaling is increasingly implicated in numerous pathologies, including atherosclerosis, diabetes, and cancer. The molecular messengers in this type of signaling are reactive species which can mediate the post-translational modification of specific groups of proteins, thereby effecting functional changes in the modified proteins. Electrophilic compounds comprise one class of reactive species which can participate in redox signaling. Electrophiles modulate cell function via formation of covalent adducts with proteins, particularly cysteine residues. SCOPE OF REVIEW: This review will discuss the commonly used methods of detection for electrophile-sensitive proteins, and will highlight the importance of identifying these proteins for studying redox signaling and developing novel therapeutics. MAJOR

conclusionsThere are several methods which can be used to detect electrophile-sensitive proteins. These include the use of tagged model electrophiles, as well as derivatization of endogenous electrophile-protein adducts. GENERAL SIGNIFICANCE: In order to understand the mechanisms by which electrophiles mediate redox signaling, it is necessary to identify electrophile-sensitive proteins and quantitatively assess adduct formation. Strengths and limitations of these methods will be discussed. This article is part of a Special Issue entitled Current methods to study reactive oxygen species - pros and cons and biophysics of membrane proteins. Guest Editor: Christine Winterbourn.

Indexed as

AnimalsHumansOxidation-ReductionProteinsReactive Oxygen SpeciesProteinsReactive Oxygen Species15-deoxy-Δ(12,14)-prostaglandin J(2)15d-PGJ(2)4-HNE4-hydroxynonenalBD-15d-PGJ(2)biotin 15-deoxy-Δ(12,14)-prostaglandin J(2)BODIPY FL-15-deoxy-Δ(12,14)-prostaglandin J(2)bt-15d-PGJ(2)deoxyribonucleic aciddinitrophenylhydrazineDNADNPHelectrophileElectrophileELISAenzyme-linked immunosorbent assayEpglutathioneglutathione S-transferaseGSHGSTIAMiodoacetamideKeap1Kelch-like enoyl-CoA hydratase-associated protein 1mito-15d-PGJ(2)mitochondrially targeted 15-deoxy-Δ(12,14)-prostaglandin J(2)NACN-acetylcysteineNEMN-ethylmaleimideNrf2nuclear factor-erythroid 2-related factor 2Oxidative post-translational modificationProteomicsReactive speciesRedox signalingThiol

Identifiers

PMID24021887
PMCPMC3858512
OpenAlexW2080906300

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.