Evidence map›Paper›PMID 24468475›Full record

ArticleFree radical biology & medicine2014

Disulfide bond generation in mammalian blood serum: detection and purification of quiescin-sulfhydryl oxidase.

Benjamin A Israel, Lingxi Jiang, Shawn A Gannon, Colin Thorpe

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Free radical biology & medicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

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  5. Review
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  13. Peripheral Blood RNA Levels ofCirculation. Genomic and precision medicine · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Thiol-Disulfide Exchange Reactions in the Mammalian Extracellular Environment.Annual review of chemical and biomolecular engineering · 2016
    Review
  19. Review
  20. 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.

Benjamin A IsraelDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.
Lingxi JiangDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.
Shawn A GannonDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.
Colin ThorpeDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA. Electronic address: cthorpe@udel.edu.
University of Delaware · US

Funding

Flavoproteins in Oxidative Protein FoldingR01GM026643 · NIGMS · UNIVERSITY OF DELAWARE · PI THORPE, COLIN · 1985 to 2019
$6.6M
CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAININGT32GM008550 · NIGMS · UNIVERSITY OF DELAWARE · PI BAHNSON, BRIAN J · 1994 to 2018
$5.0M
NIGMS NIH HHS 1-T32-GM008550NIGMS NIH HHS GM26642NIGMS NIH HHS R01 GM026643NIGMS NIH HHS T32 GM008550
6 · The paper itself

Abstract

A sensitive new plate-reader assay has been developed showing that adult mammalian blood serum contains circulating soluble sulfhydryl oxidase activity that can introduce disulfide bonds into reduced proteins with the reduction of oxygen to hydrogen peroxide. The activity was purified 5000-fold to >90% homogeneity from bovine serum and found by mass spectrometry to be consistent with the short isoform of quiescin-sulfhydryl oxidase 1 (QSOX1). This FAD-dependent enzyme is present at comparable activity levels in fetal and adult commercial bovine sera. Thus cell culture media that are routinely supplemented with either fetal or adult bovine sera will contain this facile catalyst of protein thiol oxidation. QSOX1 is present at approximately 25 nM in pooled normal adult human serum. Examination of the unusual kinetics of QSOX1 toward cysteine and glutathione at low micromolar concentrations suggests that circulating QSOX1 is unlikely to significantly contribute to the oxidation of these monothiols in plasma. However, the ability of QSOX1 to rapidly oxidize conformationally mobile protein thiols suggests a possible contribution to the redox status of exofacial and soluble proteins in blood plasma. Recent proteomic studies showing that plasma QSOX1 can be utilized in the diagnosis of pancreatic cancer and acute decompensated heart failure, together with the overexpression of this secreted enzyme in a number of solid tumors, suggest that the robust QSOX assay developed here may be useful in the quantitation of enzyme levels in a wide range of biological fluids.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCatalysisCattleDisulfidesHumansKineticsOxidoreductases Acting on Sulfur Group DonorsProtein ConformationProtein IsoformsProteomicsRatsDisulfidesOxidoreductases Acting on Sulfur Group DonorsProtein IsoformsQSOX1 protein, humanAmplex UltraRedAssayBloodCysteineDisulfideDithiothreitolFree radicalsGlutathioneHorseradish peroxidaseHydrogen peroxidePlasmaQSOX1QuiescinRibonucleaseSerumSulfhydryl oxidaseThiol

Identifiers

PMID24468475
PMCPMC3960832
OpenAlexW2054167304

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.