Evidence map›Paper›PMID 32031597›Full record

ReviewEssays in biochemistry2020

Introduction to approaches and tools for the evaluation of protein cysteine oxidation.

Leslie B Poole, Cristina M Furdui, S Bruce King

Open access · greenAbstract readReview
In one paragraph

Review in Essays in biochemistry, 2020. 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
1.3field-weighted citation impact, top 20% 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, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Ten "Cheat Codes" for Measuring Oxidative Stress in Humans.Antioxidants (Basel, Switzerland) · 2024
    Review
  6. The chemical biology of dinitrogen trioxide.Redox biochemistry and chemistry · 2024
    Article
  7. Apigeninidin chloride disruptsFrontiers in cellular and infection microbiology · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Identification of Sulfenylated Cysteines inFrontiers in plant science · 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

3 authors at 1 institution in 1 country.

Leslie B PooleDepartment of Biochemistry, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27157, U.S.A.
Cristina M FurduiCenter for Redox Biology and Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27157, U.S.A.
S Bruce KingCenter for Redox Biology and Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27157, U.S.A.
Wake Forest University · US

Funding

Tumor Tissue CoreP30CA012197 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI Ruben A. Mesa · 1985 to 2026
$55.4M
New Oxidation-Sensing Probes to Evaluate Mitochondrial Dysfunction in Lung InjuryR33ES025645 · NIEHS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI FURDUI, CRISTINA MARIA, KING, S BRUCE · 2017 to 2019
$1.5M
Mechanisms and Regulation of PeroxiredoxinsR01GM119227 · NIGMS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI POOLE, LESLIE B · 2016 to 2019
$1.4M
Proteomic Profiling of Cancer-Related Redox Signaling PathwaysR33CA126659 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI POOLE, LESLIE B · 2008 to 2010
$948k
New Oxidation-Sensing Probes to Evaluate Mitochondrial Dysfunction in Lung InjuryR21ES025645 · NIEHS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI FURDUI, CRISTINA MARIA, KING, S BRUCE · 2015 to 2016
$428k
Profiling of Redox-Sensitive Signaling ProteinsR21CA112145 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI POOLE, LESLIE B · 2005 to 2006
$295k
NCI NIH HHS P30 CA012197NCI NIH HHS R21 CA112145NCI NIH HHS R33 CA126659NIEHS NIH HHS R21 ES025645NIEHS NIH HHS R33 ES025645NIGMS NIH HHS R01 GM119227
6 · The paper itself

Abstract

Oxidative modifications of cysteine thiols in cellular proteins are pivotal to the way signal-stimulated reactive oxygen species are sensed and elicit appropriate or sometimes pathological responses, but the dynamic and often transitory nature of these modifications offer a challenge to the investigator trying to identify such sites and the responses they elicit. A number of reagents and workflows have been developed to identify proteins undergoing oxidation and to query the timing, extent and location of such modifications, as described in this minireview. While no approach is perfect to capture all the redox information in a functioning cell, best practices described herein can enable considerable insights into the "redox world" of cells and organisms.

Indexed as

CysteineElectrophoresis, Polyacrylamide GelFluorescent DyesHumansMolecular ProbesOxidation-ReductionProtein Processing, Post-TranslationalProteinsCysteineFluorescent DyesMolecular ProbesProteinschemical biologycysteine oxidationpost translational modificationproteomicsredox methods

Identifiers

PMID32031597
PMCPMC7477960
OpenAlexW3004989837

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.