Evidence map›Paper›PMID 23567800›Full record

ReviewBiochimica et biophysica acta2014

Quantification of thiols and disulfides.

Jakob R Winther, Colin Thorpe

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 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
7.7field-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

123 citing papers in PubMed, 380 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
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  7. HBiochemistry · 2026
    Article
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  9. Advancing QuantitativeACS macro letters · 2026
    Article
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  18. Review
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63 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

2 authors at 2 institutions in 2 countries.

Jakob R WintherSection for Biomolecular Sciences, Department of Biology, University of Copenhagen, Copenhagen Biocenter, DK-2200 Copenhagen, Denmark. Electronic address: jrwinther@bio.ku.dk.
Colin Thorpe
University of Copenhagen · DKUniversity of Delaware · US

Funding

Flavoproteins in Oxidative Protein FoldingR01GM026643 · NIGMS · UNIVERSITY OF DELAWARE · PI THORPE, COLIN · 1985 to 2019
$6.6M
NIGMS NIH HHS GM26643NIGMS NIH HHS R01 GM026643
6 · The paper itself

Abstract

backgroundDisulfide bond formation is a key posttranslational modification, with implications for structure, function and stability of numerous proteins. While disulfide bond formation is a necessary and essential process for many proteins, it is deleterious and disruptive for others. Cells go to great lengths to regulate thiol-disulfide bond homeostasis, typically with several, apparently redundant, systems working in parallel. Dissecting the extent of oxidation and reduction of disulfides is an ongoing challenge due, in part, to the facility of thiol/disulfide exchange reactions. SCOPE OF REVIEW: In the present account, we briefly survey the toolbox available to the experimentalist for the chemical determination of thiols and disulfides. We have chosen to focus on the key chemical aspects of current methodology, together with identifying potential difficulties inherent in their experimental implementation. MAJOR

conclusionsWhile many reagents have been described for the measurement and manipulation of the redox status of thiols and disulfides, a number of these methods remain underutilized. The ability to effectively quantify changes in redox conditions in living cells presents a continuing challenge. GENERAL SIGNIFICANCE: Many unresolved questions in the metabolic interconversion of thiols and disulfides remain. For example, while pool sizes of redox pairs and their intracellular distribution are being uncovered, very little is known about the flux in thiol-disulfide exchange pathways. New tools are needed to address this important aspect of cellular metabolism. 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

AnimalsDisulfidesHumansOxidation-ReductionProteinsSulfhydryl CompoundsDisulfidesProteinsSulfhydryl Compounds1-cyano-4-dimethylamino-pyridinium2-mercato ethanol4,4′-dithiodipyridine4-acetamido-4′-maleimidylstilbene-2,2′-disulfonic acid4-(aminosulfonyl)-7-fluoro-2,1,3-benzoxadiazole4-DPS5,5′-dithiobis-(2-nitrobenzoic) acid5-thio-2-nitrobenzoic acid7-fluorobenzo-2-oxa-1,3-diazole-4-sulfonateABD-FAMSCDAPDetectionDTNBEDTAendoplasmic reticulumERethylenediamine tetraacetic acidExchangeglutathioneglutathione disulfideGSHGSSGheavy maleimide derivativeHMDMBBrMEMMTSModificationMonobromobimaneNucleophilePAGEPEGpolyacrylamide gel electrophoresispolyethyleneglycolRedoxSBD-FSDSS-methyl methanethiosulfonatesodium dodecylsulfateTCEPTHPTNBtris(2-carboxyethyl) phosphinetris(2-hydroxyethyl) phosphine

Identifiers

PMID23567800
PMCPMC3766385
OpenAlexW1988536671

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.